|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
2-463 |
0e+00 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 741.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 2 AWLDTQDRCLGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAE 81
Cdd:cd07111 13 AWLDAHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 82 VIQKHQRLLWTLESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 161
Cdd:cd07111 93 HIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 162 AVGCTVVALVPPA-SPAPLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGECAEL 240
Cdd:cd07111 173 AMGNTVVLKPAEYtPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 241 GLALGTESLLLLTDTADVDSAVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARG 317
Cdd:cd07111 253 SLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGqvcCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 318 AAACDLVQRFVREAQ-SQGAQVFQAGDV-PSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPR 395
Cdd:cd07111 333 DPAQLKRIRELVEEGrAEGADVFQPGADlPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPY 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006441 396 GGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRPSGTPA 463
Cdd:cd07111 413 GLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWEPA 480
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
58-459 |
1.54e-126 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 384.64 E-value: 1.54e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 58 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAIQAST----------- 126
Cdd:cd07078 8 RAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRlhgevipspdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 127 QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASP-APLLLAQLAGELGPFPGILNVLSGPASLV 205
Cdd:cd07078 87 GELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPlTALLLAELLAEAGLPPGVLNVVTGDGDEV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 206 -PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLL 281
Cdd:cd07078 167 gAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQvctAASRLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 282 IQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSN 358
Cdd:cd07078 247 VHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLiSAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKgyFVPPTVLTD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 359 LPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGL-RDPSVPTGG 437
Cdd:cd07078 327 VDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAEPSAPFGG 406
|
410 420
....*....|....*....|..
gi 768006441 438 CKESGCSWHGGPDGLYEYLRPS 459
Cdd:cd07078 407 VKQSGIGREGGPYGLEEYTEPK 428
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
58-459 |
1.28e-92 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 294.14 E-value: 1.28e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 58 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAIQA-----------ST 126
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLAdklggpelpspDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 127 QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAP-LLLAQLAGELGPFPGILNVLSGPASLV 205
Cdd:cd06534 83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTaLALAELLQEAGLPPGVVNVVPGGGDEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 206 -PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLL 281
Cdd:cd06534 163 gAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQictAASRLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 282 IQESVWDEAMRRLQermgrlrsgrgldgavdmgargaaacdlvqrfvreaqsqgaqvfqagdvpserpfyppTLVSNLPP 361
Cdd:cd06534 243 VHESIYDEFVEKLV----------------------------------------------------------TVLVDVDP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 362 ASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGL-RDPSVPTGGCKE 440
Cdd:cd06534 265 DMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGVKN 344
|
410
....*....|....*....
gi 768006441 441 SGCSWHGGPDGLYEYLRPS 459
Cdd:cd06534 345 SGIGREGGPYGLEEYTRTK 363
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
11-458 |
2.03e-82 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 270.84 E-value: 2.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 11 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLL 90
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 91 WTLESLVTGRAVREVRdGDVQLAQQLLHYHA-----IQASTQEEALAG------WEPMGVIGLILPPTFSFLEMMWRICP 159
Cdd:COG1012 86 AALLTLETGKPLAEAR-GEVDRAADFLRYYAgearrLYGETIPSDAPGtrayvrREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 160 ALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPAS-LVPILASQPGIRKVAFCGAPEEGRALRRSLAG 235
Cdd:COG1012 165 ALAAGNTVV--LKPAEQTPLsalLLAELLEEAGLPAGVLNVVTGDGSeVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 236 ECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVD 312
Cdd:COG1012 243 NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQrctAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 313 MGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLV 389
Cdd:COG1012 323 MGPLiSEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGgyFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIAL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 390 ANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGL-RDPSVPTGGCKESGCSWHGGPDGLYEYLRP 458
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTET 472
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
19-457 |
1.59e-81 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 267.86 E-value: 1.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 19 WLKPEHRnSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVT 98
Cdd:pfam00171 1 WVDSESE-TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 99 GRAVREVRdGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVV 168
Cdd:pfam00171 80 GKPLAEAR-GEVDRAIDVLRYYAglarrldgetLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 169 alVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLAL 244
Cdd:pfam00171 159 --LKPSELTPLtalLLAELFEEAGLPAGVLNVVTGSGAEVgEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 245 GTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAA 320
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQvctATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPlISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 321 CDLVQRFVREAQSQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSA 399
Cdd:pfam00171 317 LERVLKYVEDAKEEGAKLLTGGEAGLDNGyFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 768006441 400 SVWSERLGQALELGYGLQVGTVWINAHGLRDP-SVPTGGCKESGCSWHGGPDGLYEYLR 457
Cdd:pfam00171 397 GVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTE 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
32-458 |
1.94e-79 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 262.38 E-value: 1.94e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 111
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 112 LAQQLLHYHAIQASTQEEAL----AGW------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPLL- 180
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVipvrGPFlnytvrEPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVV--LKPAELTPLSa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 181 --LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTAD 257
Cdd:cd07115 161 lrIAELMAEAGFPAGVLNVVTGFGEVAgAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 258 VDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQS 333
Cdd:cd07115 241 LDAAVRAAATGIFYNQGQmctAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLvSQAQFDRVLDYVDVGRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 334 QGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALEL 412
Cdd:cd07115 321 EGARLLTGGKRPGARGFFvEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 768006441 413 GYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 458
Cdd:cd07115 401 AAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEV 446
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
32-458 |
1.98e-77 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 257.09 E-value: 1.98e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGD 109
Cdd:cd07114 3 NPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR-AQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 110 VQLAQQLLHYHAIQASTQEEALAG-----------WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAP 178
Cdd:cd07114 82 VRYLAEWYRYYAGLADKIEGAVIPvdkgdylnftrREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 179 LL-LAQLAGELGPFPGILNVLSGPASLVPI-LASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTA 256
Cdd:cd07114 162 TLeLAKLAEEAGFPPGVVNVVTGFGPETGEaLVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 257 DVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQ 332
Cdd:cd07114 242 DLDAAVNGVVAGIFAAAGQtcvAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGpLATERQLEKVERYVARAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 333 SQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLG 407
Cdd:cd07114 322 EEGARVLTGGERPSGADlgagyFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 768006441 408 QALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 458
Cdd:cd07114 402 RAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQT 452
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
14-456 |
9.54e-72 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 242.60 E-value: 9.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAF--KGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 91
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 92 TLESLVTGRAVREVRdGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 161
Cdd:cd07119 81 RLETLNTGKTLRESE-IDIDDVANCFRYYAglatketgevYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 162 AVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGEC 237
Cdd:cd07119 160 AAGNTVV--IKPSEVTPLTtiaLFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTATGRSIMRAAAGNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 238 AELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 314
Cdd:cd07119 238 KKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGqvcSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 315 A-RGAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALL 388
Cdd:cd07119 318 PlVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDElakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006441 389 VANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 456
Cdd:cd07119 398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
32-458 |
2.43e-69 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 235.12 E-value: 2.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 111
Cdd:cd07106 3 NPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 112 LAQQLLHYHA--------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASP-APLLLA 182
Cdd:cd07106 82 GAVAWLRYTAsldlpdevIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPlCTLKLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 183 QLAGELGPfPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAV 262
Cdd:cd07106 162 ELAQEVLP-PGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 263 EGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQSQGAQV 338
Cdd:cd07106 241 PKLFWGAFINSGQvcaAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGpVQNKMQYDKVKELVEDAKAKGAKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 339 FQAGDVPsERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGL 416
Cdd:cd07106 321 LAGGEPL-DGPgyFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 768006441 417 QVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 458
Cdd:cd07106 400 EAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQT 441
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
32-442 |
2.49e-69 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 235.15 E-value: 2.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 111
Cdd:cd07093 3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 112 LAQQLLHYHAIQASTQE----EALAGW------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL-- 179
Cdd:cd07093 83 RAAANFRFFADYILQLDgesyPQDGGAlnyvlrQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVV--LKPSEWTPLta 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 180 -LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTAD 257
Cdd:cd07093 161 wLLAELANEAGLPPGVVNVVHGFGPEAgAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 258 VDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARGAAA-CDLVQRFVREAQS 333
Cdd:cd07093 241 LDRAVDAAVRSSFSNNGEvclAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEhLEKVLGYVELARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 334 QGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQ 408
Cdd:cd07093 321 EGATILTGGGRPELPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGR 400
|
410 420 430
....*....|....*....|....*....|....
gi 768006441 409 ALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 442
Cdd:cd07093 401 AHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASG 434
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
12-442 |
3.02e-67 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 230.31 E-value: 3.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 12 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 91
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 92 TLESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQEE----------ALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 161
Cdd:cd07559 82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGslseidedtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 162 AVGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGEC 237
Cdd:cd07559 162 AAGNTVV--LKPASQTPlsiLVLMELIGDLLP-KGVVNVVTGFGSEAgKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 238 AELGLALGTESL-LLLTDTAD-----VDSAVEGVVDAAWsDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLD 308
Cdd:cd07559 239 IPVTLELGGKSPnIFFDDAMDadddfDDKAEEGQLGFAF-NQGEvctCPSRALVQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 309 GAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRT 382
Cdd:cd07559 318 PETMMGAQvSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGldkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 383 AKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 442
Cdd:cd07559 398 EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
12-455 |
8.06e-67 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 229.25 E-value: 8.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 12 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG-WSAHPGVVRAQHLTRLAEVIQKHQRLL 90
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 91 WTLESLVTGRAVREVRDGDVQLAQQLLHYHAIQA-------------STQEEALAGW---EPMGVIGLILPPTFSFLEMM 154
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWAtkingetlapsipSMQGERYTAFtrrEPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 155 WRICPALAVGCTVValVPPASPAPLLL---AQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRR 231
Cdd:cd07113 161 WKIGAALATGCTIV--IKPSEFTPLTLlrvAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 232 SLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLD 308
Cdd:cd07113 239 QAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGqvcAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 309 GAVDMGA-RGAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEA 386
Cdd:cd07113 319 ESVMFGPlANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFvQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006441 387 LLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEY 455
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDY 467
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
12-457 |
2.57e-66 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 227.86 E-value: 2.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 12 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAH--PGVVRAQHLTRLAEVIQKHQRL 89
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRkmDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 90 LWTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICP 159
Cdd:cd07091 85 LAALESLDNGKPLEESAKGDVALSIKCLRYYAgwadkiqgktIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 160 ALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSlag 235
Cdd:cd07091 165 ALAAGNTVV--LKPAEQTPLsalYLAELIKEAGFPPGVVNIVPGFGPTAgAAISSHMDVDKIAFTGSTAVGRTIMEA--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 236 eCAE-----LGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGL 307
Cdd:cd07091 240 -AAKsnlkkVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQcccAGSRIFVQESIYDEFVEKFKARAEKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 308 DGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKE 385
Cdd:cd07091 319 DPDTFQGPQvSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFiQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768006441 386 ALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 457
Cdd:cd07091 399 VIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQ 470
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
32-458 |
1.18e-65 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 225.28 E-value: 1.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 111
Cdd:cd07092 3 DPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 112 LAQQLLHYHAIQASTQEEALAG-----------WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP-- 178
Cdd:cd07092 83 GAVDNFRFFAGAARTLEGPAAGeylpghtsmirREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVV--LKPSETTPlt 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 179 -LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTA 256
Cdd:cd07092 161 tLLLAELAAEVLP-PGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 257 DVDSAVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARGAAA-CDLVQRFVREAq 332
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGqdcTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAqRERVAGFVERA- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 333 SQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALE 411
Cdd:cd07092 319 PAHARVLTGGRRAEGPGyFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 768006441 412 LGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 458
Cdd:cd07092 399 LSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRI 445
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
60-456 |
1.22e-63 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 219.61 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 60 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAiqastqEEA--LAG---- 133
Cdd:cd07103 31 AFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GEVDYAASFLEWFA------EEArrIYGrtip 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 134 -----------WEPMGVIGLILPPTFSFLeMMWR-ICPALAVGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVL 198
Cdd:cd07103 104 spapgkrilviKQPVGVVAAITPWNFPAA-MITRkIAPALAAGCTVV--LKPAEETPlsaLALAELAEEAGLPAGVLNVV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 199 SG-PASLVPILASQPGIRKVAFCGAPEEGRalrrSLAGECAE----LGLALGTESLLLLTDTADVDSAVEGVVDAAWsdR 273
Cdd:cd07103 181 TGsPAEIGEALCASPRVRKISFTGSTAVGK----LLMAQAADtvkrVSLELGGNAPFIVFDDADLDKAVDGAIASKF--R 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 274 GPGGL-----RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSE 347
Cdd:cd07103 255 NAGQTcvcanRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLiNERAVEKVEALVEDAVAKGAKVLTGGKRLGL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 348 RP-FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAH 426
Cdd:cd07103 335 GGyFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTG 414
|
410 420 430
....*....|....*....|....*....|
gi 768006441 427 GLRDPSVPTGGCKESGCSWHGGPDGLYEYL 456
Cdd:cd07103 415 LISDAEAPFGGVKESGLGREGGKEGLEEYL 444
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
32-457 |
6.11e-63 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 217.87 E-value: 6.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAH-PGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDV 110
Cdd:cd07109 3 DPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR-ADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 111 QLAQQLLHYHAIQAST-------QEEALAGW---EPMGVIGLILPPTFSfLEMMWR-ICPALAVGCTVValVPPASPAPL 179
Cdd:cd07109 82 EAAARYFEYYGGAADKlhgetipLGPGYFVYtvrEPHGVTGHIIPWNYP-LQITGRsVAPALAAGNAVV--VKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 180 ---LLAQLAGELGPFPGILNVLSG-PASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDT 255
Cdd:cd07109 159 talRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 256 ADVDSAVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGaVDMGA-RGAAACDLVQRFVREA 331
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGqtcSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPlISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 332 QSQGAQVFQAGDVPSERP----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLG 407
Cdd:cd07109 318 RARGARIVAGGRIAEGAPaggyFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 768006441 408 QALELGYGLQVGTVWINAHGLRDP-SVPTGGCKESGcswHG---GPDGLYEYLR 457
Cdd:cd07109 398 RALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSG---HGrekGLEALYNYTQ 448
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
12-442 |
6.19e-63 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 218.48 E-value: 6.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 12 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 91
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 92 TLESLVTGRAVREVRDGDVQLAQQLLHYHA--IQAST--------QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 161
Cdd:cd07117 82 MVETLDNGKPIRETRAVDIPLAADHFRYFAgvIRAEEgsanmideDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 162 AVGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGEC 237
Cdd:cd07117 162 AAGNTVV--IKPSSTTSlslLELAKIIQDVLP-KGVVNIVTGKGSKSgEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 238 AELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 314
Cdd:cd07117 239 IPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQvccAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 315 AR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALL 388
Cdd:cd07117 319 AQvNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGldkgfFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 768006441 389 VANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 442
Cdd:cd07117 399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSG 452
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
29-442 |
2.82e-62 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 216.31 E-value: 2.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 29 PCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVR 106
Cdd:cd07112 5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 107 DGDVQLAQQLLHYHA--IQ------ASTQEEALA--GWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASP 176
Cdd:cd07112 85 AVDVPSAANTFRWYAeaIDkvygevAPTGPDALAliTREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVV--LKPAEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 177 APL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRsLAGE------CAELGlalGT 246
Cdd:cd07112 163 SPLtalRLAELALEAGLPAGVLNVVPGFGHTAgEALGLHMDVDALAFTGSTEVGRRFLE-YSGQsnlkrvWLECG---GK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 247 ESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACD 322
Cdd:cd07112 239 SPNIVFADAPDLDAAAEAAAAGIFWNQGEvcsAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALvSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 323 LVQRFVREAQSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSA 399
Cdd:cd07112 319 KVLGYIESGKAEGARLVAGGKRVLTETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 768006441 400 SVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 442
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSG 441
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
11-455 |
6.32e-60 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 210.46 E-value: 6.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 11 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG-WSAH-PGVVRAQHLTRLAEVIQKHQR 88
Cdd:cd07143 7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGLKvSGSKRGRCLSKLADLMERNLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 89 LLWTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRIC 158
Cdd:cd07143 87 YLASIEALDNGKTFGTAKRVDVQASADTFRYYGgwadkihgqvIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 159 PALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLA 234
Cdd:cd07143 167 PALAAGNTIV--LKPSELTPLsalYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLVGRKVMEAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 235 -GECAELGLALGTESLLLLTDTADVDSAVegvvdaAWSDRGP---------GGLRLLIQESVWDEAMRRLQERMGRLRSG 304
Cdd:cd07143 245 kSNLKKVTLELGGKSPNIVFDDADLESAV------VWTAYGIffnhgqvccAGSRIYVQEGIYDKFVKRFKEKAKKLKVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 305 RGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGD-VPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRT 382
Cdd:cd07143 319 DPFAEDTFQGPQvSQIQYERIMSYIESGKAEGATVETGGKrHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKT 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006441 383 AKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEY 455
Cdd:cd07143 399 EEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENY 471
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
32-456 |
5.82e-59 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 207.20 E-value: 5.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVR-D-GD 109
Cdd:cd07110 3 NPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwDvDD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 110 V--------QLAQQLLHYHAIQASTQEEALAGW---EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVaLVPP--ASP 176
Cdd:cd07110 83 VagcfeyyaDLAEQLDAKAERAVPLPSEDFKARvrrEPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVV-LKPSelTSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 177 APLLLAQLAGELGPFPGILNVLSGPASLVPI-LASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDT 255
Cdd:cd07110 162 TELELAEIAAEAGLPPGVLNVVTGTGDEAGApLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 256 ADVDSAVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAACDLVQRFVREA 331
Cdd:cd07110 242 ADLEKAVEWAMFGCFWNNGqicSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPlVSQAQYEKVLSFIARG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 332 QSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQ 408
Cdd:cd07110 322 KEEGARLLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAER 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 768006441 409 ALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 456
Cdd:cd07110 402 CDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYL 449
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
14-442 |
6.59e-59 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 207.45 E-value: 6.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHRnSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 93
Cdd:PRK13473 6 LINGELVAGEGE-KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 94 ESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQASTQEEALAGW------EPMGVIGLILPPTFSFLEMMWRICPALA 162
Cdd:PRK13473 85 ESLNCGKPLHLALNDEIPAIVDVFRFFAgaarcLEGKAAGEYLEGHtsmirrDPVGVVASIAPWNYPLMMAAWKLAPALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 163 VGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECA 238
Cdd:PRK13473 165 AGNTVV--LKPSEITPltaLKLAELAADILP-PGVLNVVTGRGATVgDALVGHPKVRMVSLTGSIATGKHVLSAAADSVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 239 ELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA 315
Cdd:PRK13473 242 RTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGqdcTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 316 R-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 392
Cdd:PRK13473 322 LiSAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKgyYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWAND 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 768006441 393 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 442
Cdd:PRK13473 402 SDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSG 451
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
58-455 |
8.05e-59 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 206.80 E-value: 8.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 58 RMAF-KG-WSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAIQAST--------- 126
Cdd:cd07118 29 RKAFdKGpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQAR-GEIEGAADLWRYAASLARTlhgdsynnl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 127 --QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPA---SPAPLLLAQLAGELGPFPGILNVLSGP 201
Cdd:cd07118 108 gdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVV--VKPSeftSGTTLMLAELLIEAGLPAGVVNIVTGY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 202 ASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GG 277
Cdd:cd07118 186 GATVgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGEccnSG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 278 LRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPT 354
Cdd:cd07118 266 SRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIiNEAQLAKITDYVDAGRAEGATLLLGGERLASAAglFYQPT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 355 LVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVP 434
Cdd:cd07118 346 IFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELP 425
|
410 420
....*....|....*....|.
gi 768006441 435 TGGCKESGCSWHGGPDGLYEY 455
Cdd:cd07118 426 FGGFKQSGIGRELGRYGVEEY 446
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
32-442 |
6.44e-58 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 204.13 E-value: 6.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 111
Cdd:cd07108 3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 112 LAQQLLHYHAIQASTQE-EALAG---------WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL-- 179
Cdd:cd07108 83 VLADLFRYFGGLAGELKgETLPFgpdvltytvREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVV--LKAAEDAPLav 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 180 -LLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTAD 257
Cdd:cd07108 161 lLLAEILAQVLP-AGVLNVITGYGEECgAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 258 VDSAVEGVVDAAWSDRG----PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAACDLVQRFVREAQ 332
Cdd:cd07108 240 LDDAVDGAIAGMRFTRQgqscTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAiISEKQFAKVCGYIDLGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 333 S-QGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERL 406
Cdd:cd07108 320 StSGATVLRGGPLPGEGPladgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDL 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 768006441 407 GQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 442
Cdd:cd07108 400 GRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSG 435
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
32-456 |
6.11e-56 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 198.72 E-value: 6.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVvRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGD 109
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEAR-FE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 110 VQLAQQLLHY----------HAIQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL 179
Cdd:cd07120 81 ISGAISELRYyaglarteagRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVV--VKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 180 L---LAQLAGELGPFP-GILNVLSGP-ASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTD 254
Cdd:cd07120 159 InaaIIRILAEIPSLPaGVVNLFTESgSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 255 TADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVRE 330
Cdd:cd07120 239 DADLDAALPKLERALTIFAGQfcmAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLiDRANVDRVDRMVER 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 331 AQSQGAQVFQAGDVPSERP----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERL 406
Cdd:cd07120 319 AIAAGAEVVLRGGPVTEGLakgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 768006441 407 GQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 456
Cdd:cd07120 399 ARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
32-457 |
7.40e-56 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 198.37 E-value: 7.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 111
Cdd:cd07107 3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAML-GDVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 112 LAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASP-APLL 180
Cdd:cd07107 82 VAAALLDYFAglvtelkgetIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPlSALR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 181 LAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVD 259
Cdd:cd07107 162 LAELAREVLP-PGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 260 SAVEGVVDA---AWSDRGPGGL-RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAACDLVQRFVREAQSQ 334
Cdd:cd07107 241 AAADAAVAGmnfTWCGQSCGSTsRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPlVSRQQYDRVMHYIDSAKRE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 335 GAQVFQAGDVPS----ERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQA 409
Cdd:cd07107 321 GARLVTGGGRPEgpalEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 768006441 410 LELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 457
Cdd:cd07107 401 HRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQ 448
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
11-458 |
8.48e-56 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 199.17 E-value: 8.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 11 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAH-PGVVRAQHLTRLAEVIQKHQRL 89
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 90 LWTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICP 159
Cdd:cd07144 88 LAAIEALDSGKPYHSNALGDLDEIIAVIRYYAgwadkiqgktIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 160 ALAVGCTVValVPPASPAPLLL---AQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAG 235
Cdd:cd07144 168 ALAAGNTVV--IKPAENTPLSLlyfANLVKEAGFPPGVVNIIPGYGAVAgSALAEHPDVDKIAFTGSTATGRLVMKAAAQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 236 ECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMG-RLRSGRGLDGAV 311
Cdd:cd07144 246 NLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGqncTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 312 DMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEA 386
Cdd:cd07144 326 VVGPQvSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLgkgyFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768006441 387 LLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 458
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQT 477
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
14-457 |
4.08e-55 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 196.72 E-value: 4.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 93
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 94 ESLVTGRAVREVRdGDVQLAQQLLHYHAIQA-----------STQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALA 162
Cdd:cd07088 81 IVEEQGKTLSLAR-VEVEFTADYIDYMAEWArriegeiipsdRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 163 VGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECA 238
Cdd:cd07088 160 TGNTIV--IKPSEETPLNaleFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQKIMEAAAENIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 239 ELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA 315
Cdd:cd07088 238 KVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQvctCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 316 R-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 392
Cdd:cd07088 318 LvNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAND 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006441 393 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGlrdPSVPTG---GCKESGCSWHGGPDGLYEYLR 457
Cdd:cd07088 398 SEYGLTSYIYTENLNTAMRATNELEFGETYINREN---FEAMQGfhaGWKKSGLGGADGKHGLEEYLQ 462
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
14-457 |
9.61e-55 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 196.18 E-value: 9.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFK--GWSAHPGVVRAQHLTRLAEVIQKHQRLLW 91
Cdd:cd07142 7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 92 TLESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQAST--QEEALAGW---EPMGVIGLILPPTFSFLEMMWRICPAL 161
Cdd:cd07142 87 ALETWDNGKPYEQARYAEVPLAARLFRYYAgwadkIHGMTlpADGPHHVYtlhEPIGVVGQIIPWNFPLLMFAWKVGPAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 162 AVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSG--PASLVPIlASQPGIRKVAFCGAPEEGRALRRSLA-G 235
Cdd:cd07142 167 ACGNTIV--LKPAEQTPLsalLAAKLAAEAGLPDGVLNIVTGfgPTAGAAI-ASHMDVDKVAFTGSTEVGKIIMQLAAkS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 236 ECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVD 312
Cdd:cd07142 244 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQcccAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 313 MGARGA-AACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVA 390
Cdd:cd07142 324 QGPQVDkEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYiQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006441 391 NGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 457
Cdd:cd07142 404 NNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
15-456 |
9.93e-55 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 196.45 E-value: 9.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 15 VNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLE 94
Cdd:PLN02278 29 IGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 95 SLVTGRAVREVRdGDVQLAQQLLHYHAIQA-----------STQEEALAGWEPMGVIGLILPPTFSfLEMMWR-ICPALA 162
Cdd:PLN02278 109 TLEQGKPLKEAI-GEVAYGASFLEYFAEEAkrvygdiipspFPDRRLLVLKQPVGVVGAITPWNFP-LAMITRkVGPALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 163 VGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV--PILASqPGIRKVAFCGAPEEGRALRRSLAGEC 237
Cdd:PLN02278 187 AGCTVV--VKPSELTPLTalaAAELALQAGIPPGVLNVVMGDAPEIgdALLAS-PKVRKITFTGSTAVGKKLMAGAAATV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 238 AELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGPGGL---RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 314
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVcanRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 315 AR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 392
Cdd:PLN02278 344 PLiNEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGtFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAND 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006441 393 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 456
Cdd:PLN02278 424 TEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYL 487
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
32-456 |
2.24e-54 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 194.38 E-value: 2.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWS-AHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDV 110
Cdd:cd07089 3 NPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 111 QLAQQLLHYHAIQAS--TQEEALAGW-------------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPAS 175
Cdd:cd07089 83 DGPIGHLRYFADLADsfPWEFDLPVPalrggpgrrvvrrEPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVV--LKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 176 PAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLL 251
Cdd:cd07089 161 DTPLsalLLGEIIAETDLPAGVVNVVTGSDNAVgEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 252 LTDTADVDSAVEGVVDAAWSDRGPG---GLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRF 327
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGcalTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLiSAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 328 VREAQSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSE 404
Cdd:cd07089 321 IARGRDEGARLVTGGGRPAGLDkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 768006441 405 RLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 456
Cdd:cd07089 401 DVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
14-456 |
7.86e-54 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 193.72 E-value: 7.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFK---GWSAHPGVVRAQHLTRLAEVIQKHQRLL 90
Cdd:cd07141 10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 91 WTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPA 160
Cdd:cd07141 90 ASLETLDNGKPFSKSYLVDLPGAIKVLRYYAgwadkihgktIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 161 LAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSG--PASLVPIlASQPGIRKVAFCGAPEEGRALRRSlAG 235
Cdd:cd07141 170 LACGNTVV--LKPAEQTPLtalYLASLIKEAGFPPGVVNVVPGygPTAGAAI-SSHPDIDKVAFTGSTEVGKLIQQA-AG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 236 EC--AELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGA 310
Cdd:cd07141 246 KSnlKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQcccAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 311 VDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALL 388
Cdd:cd07141 326 TEQGPQiDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFiQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIE 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006441 389 VANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 456
Cdd:cd07141 406 RANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYT 473
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
14-456 |
3.64e-53 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 191.25 E-value: 3.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLW 91
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 92 TLESLVTGRAVREVRDGDVQLAQQLLHYHA-----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPA 160
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAalardfpfeerRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 161 LAVGCTVVALVPPASP-APLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGECAE 239
Cdd:cd07139 162 LAAGCTVVLKPSPETPlDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 240 LGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGPG---GLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR 316
Cdd:cd07139 242 VTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVcvaLTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 317 GAAA-CDLVQRFVREAQSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 392
Cdd:cd07139 322 ASARqRERVEGYIAKGRAEGARLVTGGGRPAGLDrgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIAND 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006441 393 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLrDPSVPTGGCKESGCSWHGGPDGLYEYL 456
Cdd:cd07139 402 SDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRL-DFGAPFGGFKQSGIGREGGPEGLDAYL 464
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
32-455 |
4.40e-53 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 190.98 E-value: 4.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 111
Cdd:cd07090 3 EPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VDID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 112 LAQQLLHYHAIQAST---QEEALAGW-------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPA-PLL 180
Cdd:cd07090 82 SSADCLEYYAGLAPTlsgEHVPLPGGsfaytrrEPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLtALL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 181 LAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDS 260
Cdd:cd07090 162 LAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLEN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 261 AVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGA 336
Cdd:cd07090 242 AVNGAMMANFLSQGqvcSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALiSEEHLEKVLGYIESAKQEGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 337 QVFQAGDVPS-----ERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQAL 410
Cdd:cd07090 322 KVLCGGERVVpedglENGFYvSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAH 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 768006441 411 ELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEY 455
Cdd:cd07090 402 RVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHY 446
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
14-456 |
6.48e-52 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 188.79 E-value: 6.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAF-----KGWSAHPGVVRAQHLTRLAEVIQKHQR 88
Cdd:PLN02467 11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 89 LLWTLESLVTGRAVREVrDGDVQLAQQLLHYHAIQAstqeEALAG------------------WEPMGVIGLILPPTFSF 150
Cdd:PLN02467 91 ELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLA----EALDAkqkapvslpmetfkgyvlKEPLGVVGLITPWNYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 151 LEMMWRICPALAVGCTVVaLVPP--ASPAPLLLAQLAGELGPFPGILNVLS--GPASLVPiLASQPGIRKVAFCGAPEEG 226
Cdd:PLN02467 166 LMATWKVAPALAAGCTAV-LKPSelASVTCLELADICREVGLPPGVLNVVTglGTEAGAP-LASHPGVDKIAFTGSTATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 227 RALRRSLAGECAELGLALGTESLLLLTDTADVDSAVE----------GVVDAAWSdrgpgglRLLIQESVWDEAMRRLQE 296
Cdd:PLN02467 244 RKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEwamfgcfwtnGQICSATS-------RLLVHERIASEFLEKLVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 297 RMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPS--ERPFY-PPTLVSNLPPASPCAQVEVPW 372
Cdd:PLN02467 317 WAKNIKISDPLEEGCRLGPVvSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFiEPTIITDVTTSMQIWREEVFG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 373 PVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGL 452
Cdd:PLN02467 397 PVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGL 476
|
....
gi 768006441 453 YEYL 456
Cdd:PLN02467 477 ENYL 480
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
12-442 |
2.78e-51 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 186.50 E-value: 2.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 12 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 91
Cdd:cd07116 2 DNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 92 TLESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQEEALAG----------WEPMGVIGLILPPTFSFLEMMWRICPAL 161
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEidentvayhfHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 162 AVGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGP-ASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGEC 237
Cdd:cd07116 162 AAGNCVV--LKPAEQTPasiLVLMELIGDLLP-PGVVNVVNGFgLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 238 AELGLALGTESL------LLLTDTADVDSAVEGVVDAAWsDRG-----PGglRLLIQESVWDEAMRRLQERMGRLRSGRG 306
Cdd:cd07116 239 IPVTLELGGKSPniffadVMDADDAFFDKALEGFVMFAL-NQGevctcPS--RALIQESIYDRFMERALERVKAIKQGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 307 LDGAVDMGARGAAA-CDLVQRFVREAQSQGAQVFQAGD-----VPSERPFYPPTLVSNLPPASpCAQVEVPWPVVVASPF 380
Cdd:cd07116 316 LDTETMIGAQASLEqLEKILSYIDIGKEEGAEVLTGGErnelgGLLGGGYYVPTTFKGGNKMR-IFQEEIFGPVLAVTTF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768006441 381 RTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 442
Cdd:cd07116 395 KDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSG 456
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
13-456 |
1.27e-50 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 184.24 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 13 HYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWT 92
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 93 LESLVTGRAVREVRDGDVQLAQQLLHyHAIQA-------STQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGC 165
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLR-AAADAlkdfefeERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 166 TVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELG 241
Cdd:cd07138 160 TVV--LKPSEVAPLsaiILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 242 LALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RG 317
Cdd:cd07138 238 LELGGKSANIILDDADLEKAVPRGVAACFANSGQscnAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPlAS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 318 AAACDLVQRFVREAQSQGAQVFQAGdvpSERP-------FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVA 390
Cdd:cd07138 318 AAQFDRVQGYIQKGIEEGARLVAGG---PGRPeglergyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIA 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768006441 391 NGTPRGGSASVWSERLGQALELGYGLQVGTVWINaHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 456
Cdd:cd07138 395 NDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFL 459
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
13-456 |
3.87e-50 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 183.32 E-value: 3.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 13 HYVNGKWLKPEHRNSVPCQDPITGENLASCLQA-QAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 91
Cdd:cd07131 1 NYIGGEWVDSASGETFDSRNPADLEEVVGTFPLsTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 92 TLESLVTGRAVREVRdGDVQLAQQLLHYHAIQAST-----------QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPA 160
Cdd:cd07131 81 RLVTREMGKPLAEGR-GDVQEAIDMAQYAAGEGRRlfgetvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 161 LAVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSlage 236
Cdd:cd07131 160 LVCGNTVV--FKPAEDTPACalkLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGSTEVGERIGET---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 237 CAELG----LALGTESLLLLTDTADVDSAVEGVVdaaWSDRGPGGLR------LLIQESVWDEAMRRLQERMGRLRSGRG 306
Cdd:cd07131 234 CARPNkrvaLEMGGKNPIIVMDDADLDLALEGAL---WSAFGTTGQRctatsrLIVHESVYDEFLKRFVERAKRLRVGDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 307 LDGAVDMG-ARGAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPF 380
Cdd:cd07131 311 LDEETDMGpLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGyekgyFVEPTVFTDVTPDMRIAQEEIFGPVVALIEV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 381 RTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAhglrdPSV------PTGGCKESGcswHGGPDGLYE 454
Cdd:cd07131 391 SSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNA-----PTIgaevhlPFGGVKKSG---NGHREAGTT 462
|
..
gi 768006441 455 YL 456
Cdd:cd07131 463 AL 464
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
14-457 |
3.51e-49 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 181.17 E-value: 3.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLW 91
Cdd:PLN02766 24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 92 TLESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQAST--QEEALAGW---EPMGVIGLILPPTFSFLEMMWRICPAL 161
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAgaadkIHGETlkMSRQLQGYtlkEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 162 AVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLA-GE 236
Cdd:PLN02766 184 AAGCTMV--VKPAEQTPLsalFYAHLAKLAGVPDGVINVVTGFGPTAgAAIASHMDVDKVSFTGSTEVGRKIMQAAAtSN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 237 CAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDM 313
Cdd:PLN02766 262 LKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEicvASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 314 GAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVAN 391
Cdd:PLN02766 342 GPQvDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYiEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKAN 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768006441 392 GTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 457
Cdd:PLN02766 422 NTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
13-442 |
7.63e-49 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 179.37 E-value: 7.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 13 HYVNGKWLKP----EHRNsvPCQdpiTGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQR 88
Cdd:cd07097 3 NYIDGEWVAGgdgeENRN--PSD---TSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 89 LLWTLESLVTGRAVREVRdGDVQLAQQLLHYHA---------IQASTQE--EALAGWEPMGVIGLILPPTFSFLEMMWRI 157
Cdd:cd07097 78 ELARLLTREEGKTLPEAR-GEVTRAGQIFRYYAgealrlsgeTLPSTRPgvEVETTREPLGVVGLITPWNFPIAIPAWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 158 CPALAVGCTVValVPPASPAPLLLAQLA---GELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSL 233
Cdd:cd07097 157 APALAYGNTVV--FKPAELTPASAWALVeilEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRRIAAAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 234 AGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGA 310
Cdd:cd07097 235 AARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGqrcTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 311 VDMG-ARGAAACDLVQRFVREAQSQGAQVFQAGD-VPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEA 386
Cdd:cd07097 315 VDIGpVVSERQLEKDLRYIEIARSEGAKLVYGGErLKRPDEgyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEA 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 768006441 387 LLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINA--HGLrDPSVPTGGCKESG 442
Cdd:cd07097 395 LAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLptAGV-DYHVPFGGRKGSS 451
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
60-449 |
3.92e-48 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 176.18 E-value: 3.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 60 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLwtLESLV--TGrAVREVRDGDVQLAQQLLHYHA---------IQASTQE 128
Cdd:cd07104 12 AQKAWAATPPQERAAILRKAAEILEERRDEI--ADWLIreSG-STRPKAAFEVGAAIAILREAAglprrpegeILPSDVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 129 --EALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP----LLLAQLAGELGPFPGILNVLSGPA 202
Cdd:cd07104 89 gkESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVV--LKPDSRTPvtggLLIAEIFEEAGLPKGVLNVVPGGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 203 SLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGvvdAAWSDRGPGGL--- 278
Cdd:cd07104 167 SEIgDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSA---AAFGAFLHQGQicm 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 279 ---RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQSQGAQVFQAGDVpsERPFYPPT 354
Cdd:cd07104 244 aagRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGpLINERQVDRVHAIVEDAVAAGARLLTGGTY--EGLFYQPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 355 LVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRD-PSV 433
Cdd:cd07104 322 VLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDePHV 401
|
410
....*....|....*.
gi 768006441 434 PTGGCKESGCSWHGGP 449
Cdd:cd07104 402 PFGGVKASGGGRFGGP 417
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
13-463 |
8.50e-47 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 173.52 E-value: 8.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 13 HYVNGKWLKPEhRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWT 92
Cdd:cd07086 1 GVIGGEWVGSG-GETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 93 LESLVTGRAVREVRdGDVQ-----------LAQQLlhYHAIQASTQEE--ALAGWEPMGVIGLILPPTFSFLEMMWRICP 159
Cdd:cd07086 80 LVSLEMGKILPEGL-GEVQemidicdyavgLSRML--YGLTIPSERPGhrLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 160 ALAVGCTVValVPPASPAPL-------LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRRS 232
Cdd:cd07086 157 ALVCGNTVV--WKPSETTPLtaiavtkILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 233 LAGECAELGLALGTESLLLLTDTADVDSAVEGVVdaaWSDRGPGGLR------LLIQESVWDEAMRRLQERMGRLRSGRG 306
Cdd:cd07086 235 VARRFGRVLLELGGNNAIIVMDDADLDLAVRAVL---FAAVGTAGQRctttrrLIVHESVYDEFLERLVKAYKQVRIGDP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 307 LDGAVDMG-ARGAAACDLVQRFVREAQSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRT 382
Cdd:cd07086 312 LDEGTLVGpLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEpgnYVEPTIVTGVTDDARIVQEETFAPILYVIKFDS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 383 AKEALLVANGTPRGGSASVWSERLGQALE-LG-YGLQVGTVWINA-------HGlrdpsvPTGGCKESGcswhGGpdgly 453
Cdd:cd07086 392 LEEAIAINNDVPQGLSSSIFTEDLREAFRwLGpKGSDCGIVNVNIptsgaeiGG------AFGGEKETG----GG----- 456
|
490
....*....|
gi 768006441 454 eylRPSGTPA 463
Cdd:cd07086 457 ---RESGSDA 463
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
14-457 |
8.60e-47 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 173.84 E-value: 8.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLW 91
Cdd:cd07140 9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 92 TLESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQAST---------QEEALAGWEPMGVIGLILPPTFSFLEMMWRI 157
Cdd:cd07140 89 TIESLDSGAVYTLALKTHVGMSIQTFRYFAgwcdkIQGKTipinqarpnRNLTLTKREPIGVCGIVIPWNYPLMMLAWKM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 158 CPALAVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSL 233
Cdd:cd07140 169 AACLAAGNTVV--LKPAQVTPLTalkFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 234 A-GECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGPGGL---RLLIQESVWDEAMRRLQERMGRLRSGRGLDG 309
Cdd:cd07140 247 AvSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIaagRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 310 AVDMGARGAAA-CDLVQRFVREAQSQGAQVFQAG-DVPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAK-EA 386
Cdd:cd07140 327 STDHGPQNHKAhLDKLVEYCERGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDvDG 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768006441 387 LLV-ANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 457
Cdd:cd07140 407 VLQrANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLK 478
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
14-442 |
8.75e-47 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 173.93 E-value: 8.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLW 91
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 92 TLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 161
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDDIPGAARAIRWYAeaidkvygevATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 162 AVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSlAGEC 237
Cdd:PRK09847 183 AAGNSVI--LKPSEKSPLSairLAGLAKEAGLPDGVLNVVTGFGHEAgQALSRHNDIDAIAFTGSTRTGKQLLKD-AGDS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 238 --AELGLALGTESL-LLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAV 311
Cdd:PRK09847 260 nmKRVWLEAGGKSAnIVFADCPDLQQAASATAAGIFYNQGQvciAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPAT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 312 DMGAR-GAAACDLVQRFVREAQSQGaQVFQAGDVPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVA 390
Cdd:PRK09847 340 TMGTLiDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLA 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 768006441 391 NGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 442
Cdd:PRK09847 419 NDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSG 470
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
14-456 |
3.01e-46 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 172.40 E-value: 3.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 93
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 94 ESLVTGRAVREVRdGDVQLAQQLLHYHAIQA-----------STQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALA 162
Cdd:PRK11241 94 MTLEQGKPLAEAK-GEISYAASFIEWFAEEGkriygdtipghQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 163 VGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECA 238
Cdd:PRK11241 173 AGCTMV--LKPASQTPfsaLALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 239 ELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGPGGL---RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA 315
Cdd:PRK11241 251 KVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVcanRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 316 R-GAAACDLVQRFVREAQSQGAQVFQAGDVPS-ERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGT 393
Cdd:PRK11241 331 LiDEKAVAKVEEHIADALEKGARVVCGGKAHElGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDT 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006441 394 PRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 456
Cdd:PRK11241 411 EFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYL 473
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
28-442 |
2.95e-45 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 168.68 E-value: 2.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 28 VPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRd 107
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 108 GDVQLAQQLLHYHAIQASTQEE---------------ALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVP 172
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGetipvdayeynerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVV--VK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 173 PASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALG-TE 247
Cdd:cd07145 158 PSSNTPLtaiELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGgSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 248 SLLLLTDtADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDL 323
Cdd:cd07145 238 PMIVLKD-ADLERAVSIAVRGRFENAGQvcnAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLiSPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 324 VQRFVREAQSQGAQVFQAGDVPsERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWS 403
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKRD-EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFT 395
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 768006441 404 ERLGQALELGYGLQVGTVWINAHG-LRDPSVPTGGCKESG 442
Cdd:cd07145 396 NDINRALKVARELEAGGVVINDSTrFRWDNLPFGGFKKSG 435
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
32-458 |
4.11e-45 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 168.17 E-value: 4.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 111
Cdd:cd07099 2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 112 LAQQLLHYHAIQAstqEEALA-----------------GWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPA 174
Cdd:cd07099 81 LALEAIDWAARNA---PRVLAprkvptgllmpnkkatvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVV--LKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 175 SPAPL---LLAQLAGELGPFPGILNVLSGPASLVPILASQpGIRKVAFCGAPEEGRALrrslAGECAE----LGLALGTE 247
Cdd:cd07099 156 EVTPLvgeLLAEAWAAAGPPQGVLQVVTGDGATGAALIDA-GVDKVAFTGSVATGRKV----MAAAAErlipVVLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 248 SLLLLTDTADVDSAVEGVVDAAWSDRG--PGGL-RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARGAAA-CDL 323
Cdd:cd07099 231 DPMIVLADADLERAAAAAVWGAMVNAGqtCISVeRVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARqLDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 324 VQRFVREAQSQGAQVFQAGDVPSER-PFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVW 402
Cdd:cd07099 311 VRRHVDDAVAKGAKALTGGARSNGGgPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 768006441 403 SERLGQALELGYGLQVGTVWINAHGLRD--PSVPTGGCKESGCSWHGGPDGLYEYLRP 458
Cdd:cd07099 391 SRDLARAEAIARRLEAGAVSINDVLLTAgiPALPFGGVKDSGGGRRHGAEGLREFCRP 448
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
32-442 |
1.28e-44 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 167.00 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 111
Cdd:cd07149 5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR-KEVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 112 LAQQLLHYHA------------IQASTQEEALAGW---EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASP 176
Cdd:cd07149 84 RAIETLRLSAeeakrlagetipFDASPGGEGRIGFtirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV--LKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 177 APL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSlAGEcAELGLALGTESLLLL 252
Cdd:cd07149 162 TPLsalKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEAIARK-AGL-KKVTLELGSNAAVIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 253 TDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFV 328
Cdd:cd07149 240 DADADLEKAVERCVSGAFANAGQvciSVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMiSEAEAERIEEWV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 329 REAQSQGAQVFQAGDVpsERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQ 408
Cdd:cd07149 320 EEAVEGGARLLTGGKR--DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQK 397
|
410 420 430
....*....|....*....|....*....|....*
gi 768006441 409 ALELGYGLQVGTVWIN-AHGLRDPSVPTGGCKESG 442
Cdd:cd07149 398 ALKAARELEVGGVMINdSSTFRVDHMPYGGVKESG 432
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
13-457 |
4.18e-44 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 167.29 E-value: 4.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 13 HYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLL 90
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 91 WTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPA 160
Cdd:PLN02466 140 AALETWDNGKPYEQSAKAELPMFARLFRYYAgwadkihgltVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 161 LAVGCTVVALVPPASP-APLLLAQLAGELGPFPGILNVLSG-PASLVPILASQPGIRKVAFCGAPEEGR-ALRRSLAGEC 237
Cdd:PLN02466 220 LACGNTIVLKTAEQTPlSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDTGKiVLELAAKSNL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 238 AELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 314
Cdd:PLN02466 300 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQcccAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 315 AR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 392
Cdd:PLN02466 380 PQiDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYiQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANN 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006441 393 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 457
Cdd:PLN02466 460 TRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQ 524
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
32-455 |
8.98e-44 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 164.43 E-value: 8.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVrDGDVQ 111
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA-WFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 112 LAQQLLHY-----HAIQASTQEEALAGW------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP-- 178
Cdd:cd07150 84 FTPELLRAaagecRRVRGETLPSDSPGTvsmsvrRPLGVVAGITPFNYPLILATKKVAFALAAGNTVV--LKPSEETPvi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 179 -LLLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALR----RSLAGECAELGlalGTESLLLL 252
Cdd:cd07150 162 gLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGREIAekagRHLKKITLELG---GKNPLIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 253 TDtADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFV 328
Cdd:cd07150 239 AD-ADLDYAVRAAAFGAFMHQGQicmSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGpLISPRQVERIKRQV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 329 REAQSQGAQVFQAGDVpsERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQ 408
Cdd:cd07150 318 EDAVAKGAKLLTGGKY--DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 768006441 409 ALELGYGLQVGTVWINAHGLRD-PSVPTGGCKESGCSWHGGPDGLYEY 455
Cdd:cd07150 396 AFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEF 443
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
72-457 |
3.16e-42 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 159.83 E-value: 3.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 72 RAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDgDVQLAQQLLHYHAIQA-STQEEALAG--------------WEP 136
Cdd:cd07146 42 RSAILNKAAALLEARREEFARLITLESGLCLKDTRY-EVGRAADVLRFAAAEAlRDDGESFSCdltangkarkiftlREP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 137 MGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSG-PASLVPILASQP 212
Cdd:cd07146 121 LGVVLAITPFNHPLNQVAHKIAPAIAANNRIV--LKPSEKTPLsaiYLADLLYEAGLPPDMLSVVTGePGEIGDELITHP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 213 GIRKVAFCGAPEEGRALRRSLAG--ECAELGlalGTESLLLLTDtADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVW 287
Cdd:cd07146 199 DVDLVTFTGGVAVGKAIAATAGYkrQLLELG---GNDPLIVMDD-ADLERAATLAVAGSYANSGQrctAVKRILVHESVA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 288 DEAMRRLQERMGRLRSGRGLDGAVDMGA---RGAAacDLVQRFVREAQSQGAQVFQAGdvpsER--PFYPPTLVSNLPPA 362
Cdd:cd07146 275 DEFVDLLVEKSAALVVGDPMDPATDMGTvidEEAA--IQIENRVEEAIAQGARVLLGN----QRqgALYAPTVLDHVPPD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 363 SPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN-AHGLRDPSVPTGGCKES 441
Cdd:cd07146 349 AELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNeVPGFRSELSPFGGVKDS 428
|
410
....*....|....*.
gi 768006441 442 GCswhGGPDGLYEYLR 457
Cdd:cd07146 429 GL---GGKEGVREAMK 441
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
60-454 |
4.93e-42 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 158.78 E-value: 4.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 60 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAIQAstqEEALAG------ 133
Cdd:cd07100 11 AFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEAR-AEVEKCAWICRYYAENA---EAFLADepietd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 134 -------WEPMGVIGLILPPTFSFLEMMwRIC-PALAVGCTVvaLVPPASPAP---LLLAQLAGELGPFPGILNVLSGPA 202
Cdd:cd07100 87 agkayvrYEPLGVVLGIMPWNFPFWQVF-RFAaPNLMAGNTV--LLKHASNVPgcaLAIEELFREAGFPEGVFQNLLIDS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 203 SLVPILASQPGIRKVAFCG--------APEEGRALRRSLAgecaELGlalGTESLLLLtDTADVDSAVEGVVDAAWSDRG 274
Cdd:cd07100 164 DQVEAIIADPRVRGVTLTGseragravAAEAGKNLKKSVL----ELG---GSDPFIVL-DDADLDKAVKTAVKGRLQNAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 275 P---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG--ARgAAACDLVQRFVREAQSQGAQVFQAGDVPsERP 349
Cdd:cd07100 236 QsciAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGplAR-KDLRDELHEQVEEAVAAGATLLLGGKRP-DGP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 350 --FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHG 427
Cdd:cd07100 314 gaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMV 393
|
410 420 430
....*....|....*....|....*....|
gi 768006441 428 LRDPSVPTGGCKESGcswHG---GPDGLYE 454
Cdd:cd07100 394 KSDPRLPFGGVKRSG---YGrelGRFGIRE 420
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
32-458 |
6.05e-42 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 159.14 E-value: 6.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRD---- 107
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVevdr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 108 --GDVQLAQQLLHYH--------AIQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPA 177
Cdd:cd07094 85 aiDTLRLAAEEAERIrgeeipldATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVV--LKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 178 PLL---LAQLAGELGPFPGILNVLSG-PASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGEcaELGLALGTESLLLLT 253
Cdd:cd07094 163 PLSaleLAKILVEAGVPEGVLQVVTGeREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGK--RIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 254 DTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVR 329
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQvciSVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLiSEEAAERVERWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 330 EAQSQGAQVFQAGDvpSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQA 409
Cdd:cd07094 321 EAVEAGARLLCGGE--RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 768006441 410 LELGYGLQVGTVWINAHG-LRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 458
Cdd:cd07094 399 FKAAEKLEVGGVMVNDSSaFRTDWMPFGGVKESGVGREGVPYAMEEMTEE 448
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
32-455 |
8.70e-42 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 158.63 E-value: 8.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 111
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 112 LAQQLLHYhaiqASTQEEALA----------------GWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPAS 175
Cdd:cd07101 82 VAIVARYY----ARRAERLLKprrrrgaipvltrttvNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 176 P-APLLLAQLAGELGPFPGILNVLSGPASLV--PILASQPGirkVAFCGAPEEGRALR----RSLAGECAELGlalGTES 248
Cdd:cd07101 158 AlTALWAVELLIEAGLPRDLWQVVTGPGSEVggAIVDNADY---VMFTGSTATGRVVAeragRRLIGCSLELG---GKNP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 249 LLLLTDtADVDSAVEGVVDAAWSDRGPGGL---RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAACDLV 324
Cdd:cd07101 232 MIVLED-ADLDKAAAGAVRACFSNAGQLCVsieRIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSlISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 325 QRFVREAQSQGAQVFQAGdvpSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSA 399
Cdd:cd07101 311 TAHVDDAVAKGATVLAGG---RARPdlgpyFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006441 400 SVWSERLGQALELGYGLQVGTVWIN-----AHGLRDpsVPTGGCKESGCSWHGGPDGLYEY 455
Cdd:cd07101 388 SVWTRDGARGRRIAARLRAGTVNVNegyaaAWASID--APMGGMKDSGLGRRHGAEGLLKY 446
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
17-442 |
3.37e-41 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 157.47 E-value: 3.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 17 GKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHqrllwtlESL 96
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEER-------RDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 97 VTGRAVREvrDGDVQLAQQLlHYHAIQASTQEEA--------------LAGWE------PMGVIGLILPPTFSFLEMMWR 156
Cdd:cd07151 74 IVEWLIRE--SGSTRIKANI-EWGAAMAITREAAtfplrmegrilpsdVPGKEnrvyrePLGVVGVISPWNFPLHLSMRS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 157 ICPALAVGCTVValVPPASPAP----LLLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRR 231
Cdd:cd07151 151 VAPALALGNAVV--LKPASDTPitggLLLAKIFEEAGLPKGVLNVVVGAGSEIgDAFVEHPVPRLISFTGSTPVGRHIGE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 232 SLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGPGGL---RLLIQESVWDEAMRRLQERMGRLRSGRGLD 308
Cdd:cd07151 229 LAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMainRIIVHEDVYDEFVEKFVERVKALPYGDPSD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 309 GAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVpsERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEAL 387
Cdd:cd07151 309 PDTVVGPLiNESQVDGLLDKIEQAVEEGATLLVGGEA--EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEAL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 768006441 388 LVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRD-PSVPTGGCKESG 442
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSG 442
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
13-442 |
1.22e-39 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 153.11 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 13 HYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWT 92
Cdd:PRK13252 9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 93 LESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQE---EALAG-------WEPMGVIGLILPPTFSFLEMMWRICPALA 162
Cdd:PRK13252 89 LETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEgeqIPLRGgsfvytrREPLGVCAGIGAWNYPIQIACWKSAPALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 163 VGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGECAE 239
Cdd:PRK13252 169 AGNAMI--FKPSEVTPLTalkLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 240 LGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR 316
Cdd:PRK13252 247 VTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGqvcTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 317 -GAAACDLVQRFVREAQSQGAQVFQAGDVPSER-----PFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVA 390
Cdd:PRK13252 327 vSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGgfangAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 768006441 391 NGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 442
Cdd:PRK13252 407 NDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSG 458
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
60-457 |
2.48e-39 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 151.19 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 60 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGrAVREVRDGDVQLAQQLLHYHAIQASTQEE---------- 129
Cdd:cd07105 12 AFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG-ATAAWAGFNVDLAAGMLREAASLITQIIGgsipsdkpgt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 130 -ALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAP-LLLAQLAGELGPFPGILNVLS-GP---AS 203
Cdd:cd07105 91 lAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRThWLIGRVFHEAGLPKGVLNVVThSPedaPE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 204 LVPILASQPGIRKVAFCGAPEEGRalrrSLAGECA--------ELGlalGTESLLLLTDtADVDSAVEGVVDAAWSDRGP 275
Cdd:cd07105 171 VVEALIAHPAVRKVNFTGSTRVGR----IIAETAAkhlkpvllELG---GKAPAIVLED-ADLDAAANAALFGAFLNSGQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 276 GGL---RLLIQESVWDEAMRRLQERMGRLRSGrgldGAVDMGARGAAACDLVQRFVREAQSQGAQVFqAGDVPSERP--- 349
Cdd:cd07105 243 ICMsteRIIVHESIADEFVEKLKAAAEKLFAG----PVVLGSLVSAAAADRVKELVDDALSKGAKLV-VGGLADESPsgt 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 350 FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLR 429
Cdd:cd07105 318 SMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVH 397
|
410 420
....*....|....*....|....*....
gi 768006441 430 D-PSVPTGGCKESGCSWHGGPDGLYEYLR 457
Cdd:cd07105 398 DePTLPHGGVKSSGYGRFNGKWGIDEFTE 426
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
60-455 |
3.89e-37 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 145.13 E-value: 3.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 60 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGrAVREVRDGDVQLAQQLLHyHAIQASTQEE---------- 129
Cdd:cd07152 25 AQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESG-SIRPKAGFEVGAAIGELH-EAAGLPTQPQgeilpsapgr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 130 -ALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAP--LLLAQLAGELGPFPGILNVLSGPASLVP 206
Cdd:cd07152 103 lSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSggVVIARLFEEAGLPAGVLHVLPGGADAGE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 207 ILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEgvvDAAWSDRGPGGL------RL 280
Cdd:cd07152 183 ALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAAS---NGAWGAFLHQGQicmaagRH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 281 LIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDvpSERPFYPPTLVSNL 359
Cdd:cd07152 260 LVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLiNARQLDRVHAIVDDSVAAGARLEAGGT--YDGLFYRPTVLSGV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 360 PPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRD-PSVPTGGC 438
Cdd:cd07152 338 KPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDePHNPFGGM 417
|
410
....*....|....*...
gi 768006441 439 KESGC-SWHGGPDGLYEY 455
Cdd:cd07152 418 GASGNgSRFGGPANWEEF 435
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
22-455 |
9.28e-37 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 145.41 E-value: 9.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 22 PEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRA 101
Cdd:PRK09407 28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 102 VREVRDGDVQLAQQLLHYhaiqASTQEEALA----------------GWEPMGVIGLILPPTFSFLEMMWRICPALAVGC 165
Cdd:PRK09407 108 RRHAFEEVLDVALTARYY----ARRAPKLLAprrragalpvltktteLRQPKGVVGVISPWNYPLTLAVSDAIPALLAGN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 166 TVVAlvPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLV--PILAsqpGIRKVAFCGAPEEGRAL-----RRsLAG 235
Cdd:PRK09407 184 AVVL--KPDSQTPltaLAAVELLYEAGLPRDLWQVVTGPGPVVgtALVD---NADYLMFTGSTATGRVLaeqagRR-LIG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 236 ECAELGlalGTESLLLLTDtADVDSAVEGVVDAAWSDRGPGGL---RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVD 312
Cdd:PRK09407 258 FSLELG---GKNPMIVLDD-ADLDKAAAGAVRACFSNAGQLCIsieRIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSAD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 313 MGA-RGAAACDLVQRFVREAQSQGAQVFqAGDVPseRP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEA 386
Cdd:PRK09407 334 MGSlISEAQLETVSAHVDDAVAKGATVL-AGGKA--RPdlgplFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEA 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006441 387 LLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN-----AHGLRDpsVPTGGCKESGCSWHGGPDGLYEY 455
Cdd:PRK09407 411 VERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVD--APMGGMKDSGLGRRHGAEGLLKY 482
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
58-458 |
2.07e-35 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 141.21 E-value: 2.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 58 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVrDGDVQLAQQLLHYHAIQAstqeEALAG---- 133
Cdd:cd07124 79 RAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREM----LRLRGfpve 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 134 ----------WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSG 200
Cdd:cd07124 154 mvpgednryvYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVV--LKPAEDTPViaaKLVEILEEAGLPPGVVNFLPG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 201 PASLV-PILASQPGIRKVAFCGAPEEG--------------RALRRSLagecAELGlalGTESlLLLTDTADVDSAVEGV 265
Cdd:cd07124 232 PGEEVgDYLVEHPDVRFIAFTGSREVGlriyeraakvqpgqKWLKRVI----AEMG---GKNA-IIVDEDADLDEAAEGI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 266 VDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGaQVFQA 341
Cdd:cd07124 304 VRSAFGFQGqkcSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPViDKGARDRIRRYIEIGKSEG-RLLLG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 342 GDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWS---ERLGQALElgyG 415
Cdd:cd07124 383 GEVLELAAegyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSrspEHLERARR---E 459
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 768006441 416 LQVGTVWINahglRD-----PSV-PTGGCKESGC-SWHGGPDGLYEYLRP 458
Cdd:cd07124 460 FEVGNLYAN----RKitgalVGRqPFGGFKMSGTgSKAGGPDYLLQFMQP 505
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
136-456 |
7.86e-35 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 137.56 E-value: 7.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 136 PMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLV-PILASQ 211
Cdd:PRK10090 71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIV--IKPSEFTPnnaIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 212 PGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---GGLRLLIQESVWD 288
Cdd:PRK10090 149 PKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQvcnCAERVYVQKGIYD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 289 EAMRRLQERMGRLRSGRGLDG-AVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPC 365
Cdd:PRK10090 229 QFVNRLGEAMQAVQFGNPAERnDIAMGPLiNAAALERVEQKVARAVEEGARVALGGKAVEGKGyYYPPTLLLDVRQEMSI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 366 AQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSW 445
Cdd:PRK10090 309 MHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGG 388
|
330
....*....|.
gi 768006441 446 HGGPDGLYEYL 456
Cdd:PRK10090 389 ADGKHGLHEYL 399
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
136-443 |
1.94e-32 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 131.21 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 136 PMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLVPILASQP 212
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFV--LKPASRTPlsaLILGEVLAETGLPKGAFSVLPCSRDDADLLVTDE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 213 GIRKVAFCGAPEEGRALRrSLAGEcAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGPGGL---RLLIQESVWDE 289
Cdd:cd07147 201 RIKLLSFTGSPAVGWDLK-ARAGK-KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCIsvqRVLVHRSVYDE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 290 AMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVpsERPFYPPTLVSNLPPASPCAQV 368
Cdd:cd07147 279 FKSRLVARVKALKTGDPKDDATDVGPMiSESEAERVEGWVNEAVDAGAKLLTGGKR--DGALLEPTILEDVPPDMEVNCE 356
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768006441 369 EVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN-AHGLRDPSVPTGGCKESGC 443
Cdd:cd07147 357 EVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdVPTFRVDHMPYGGVKDSGI 432
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
14-458 |
6.63e-32 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 130.39 E-value: 6.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKP-EHRNSVPCQDPitGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWT 92
Cdd:cd07083 22 VIGGEWVDTkERMVSVSPFAP--SEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 93 LESLVTGRAVREVRDgDVQLAQQLLHYHAIQA---STQEEALAG---------WEPMGVIGLILPPTFSFLEMMWRICPA 160
Cdd:cd07083 100 TLTYEVGKNWVEAID-DVAEAIDFIRYYARAAlrlRYPAVEVVPypgednesfYVGLGAGVVISPWNFPVAIFTGMIVAP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 161 LAVGCTVVAlvPPASPAPLLLA---QLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLA-- 234
Cdd:cd07083 179 VAVGNTVIA--KPAEDAVVVGYkvfEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKKIYEAAArl 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 235 ----GECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGL 307
Cdd:cd07083 257 apgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGqkcSAASRLILTQGAYEPVLERLLKRAERLSVGPPE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 308 DGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFYPPTLVSNLPPASPCAQVEVPWPV--VVASPFRTAK 384
Cdd:cd07083 337 ENGTDLGPViDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVlsVIRYKDDDFA 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006441 385 EALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAH--GLRDPSVPTGGCKESGCSWH-GGPDGLYEYLRP 458
Cdd:cd07083 417 EALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKitGALVGVQPFGGFKLSGTNAKtGGPHYLRRFLEM 493
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
496-738 |
9.65e-32 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 129.86 E-value: 9.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 496 APPYGLFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK 574
Cdd:COG1012 3 TPEYPLFIGGEWVAAASGETFDVINpATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPP-------------AERAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 575 --STLASRLER------------QGAELKAAEAEVELSARRLR-AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVC 639
Cdd:COG1012 70 ilLRAADLLEErreelaalltleTGKPLAEARGEVDRAADFLRyYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAIT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 640 PDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS 718
Cdd:COG1012 150 PWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGS 229
|
250 260
....*....|....*....|.
gi 768006441 719 AQ-GSQFVEWAsAGNLKPVWA 738
Cdd:COG1012 230 TAvGRRIAAAA-AENLKRVTL 249
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
14-442 |
1.09e-31 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 129.61 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHrNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSA-HPGVVRAQHLTRLAEVIQKHQRLLWT 92
Cdd:cd07082 5 LINGEWKESSG-KTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 93 LESLVTGR----AVREV-RDGD--VQLAQQLLHYHA------IQASTQE-EALAGWEPMGVIgLILPP-------TFSfl 151
Cdd:cd07082 84 LLMWEIGKtlkdALKEVdRTIDyiRDTIEELKRLDGdslpgdWFPGTKGkIAQVRREPLGVV-LAIGPfnyplnlTVS-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 152 emmwRICPALAVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV--PILASqPGIRKVAFCGAPEEG 226
Cdd:cd07082 161 ----KLIPALIMGNTVV--FKPATQGVLLgipLAEAFHDAGFPKGVVNVVTGRGREIgdPLVTH-GRIDVISFTGSTEVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 227 RALRRSLAGECAELGLAlGTESLLLLTDtADVDSAVEGVVDAAWS---DRGPGGLRLLIQESVWDEAMRRLQERMGRLRS 303
Cdd:cd07082 234 NRLKKQHPMKRLVLELG-GKDPAIVLPD-ADLELAAKEIVKGALSysgQRCTAIKRVLVHESVADELVELLKEEVAKLKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 304 GRGLDGAVDMGA---RGAAacDLVQRFVREAQSQGAQVFQAGDVPSERPFYPpTLVSNLPPASPCAQVEVPWPVVVASPF 380
Cdd:cd07082 312 GMPWDNGVDITPlidPKSA--DFVEGLIDDAVAKGATVLNGGGREGGNLIYP-TLLDPVTPDMRLAWEEPFGPVLPIIRV 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006441 381 RTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSV-PTGGCKESG 442
Cdd:cd07082 389 NDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSG 451
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
134-452 |
1.17e-31 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 129.34 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 134 WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPpaspaplllAQLAGELGPFPGI----LNVLSGPASLVPI-- 207
Cdd:cd07098 118 YEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVS---------EQVAWSSGFFLSIirecLAACGHDPDLVQLvt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 208 --------LASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGP---G 276
Cdd:cd07098 189 clpetaeaLTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQnciG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 277 GLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFqAGDVPSERP------ 349
Cdd:cd07098 269 IERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMiSPARFDRLEELVADAVEKGARLL-AGGKRYPHPeypqgh 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 350 FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLR 429
Cdd:cd07098 348 YFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVN 427
|
330 340
....*....|....*....|....*
gi 768006441 430 --DPSVPTGGCKESGCSWHGGPDGL 452
Cdd:cd07098 428 yyVQQLPFGGVKGSGFGRFAGEEGL 452
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
11-424 |
2.80e-28 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 119.16 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 11 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLL 90
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 91 WTLESLVTGRAVREVRdGDVQLAQQLLHY-----HAIQASTQEEALAG------WEPMGVIGLILPptFSFLEM--MWRI 157
Cdd:cd07085 81 ARLITLEHGKTLADAR-GDVLRGLEVVEFacsipHLLKGEYLENVARGidtysyRQPLGVVAGITP--FNFPAMipLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 158 CPALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRAL-RRSl 233
Cdd:cd07085 158 PMAIACGNTFV--LKPSERVPGaamRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIyERA- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 234 agecAELG---LALG--TESLLLLTDtADVDSAVEGVVDAAWsdrGPGGLR------LLIQESVWDEAMRRLQERMGRLR 302
Cdd:cd07085 235 ----AANGkrvQALGgaKNHAVVMPD-ADLEQTANALVGAAF---GAAGQRcmalsvAVAVGDEADEWIPKLVERAKKLK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 303 SGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAG-DVPSerPFYP------PTLVSNLPPASPCAQVEVPWPV 374
Cdd:cd07085 307 VGAGDDPGADMGPViSPAAKERIEGLIESGVEEGAKLVLDGrGVKV--PGYEngnfvgPTILDNVTPDMKIYKEEIFGPV 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 768006441 375 VVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN 424
Cdd:cd07085 385 LSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN 434
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
33-458 |
3.83e-28 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 118.50 E-value: 3.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 33 PITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVR----EVRDG 108
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAqaggEIRGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 109 D------VQLAQQLLHYHAIQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVvaLVPPASPAPLL-- 180
Cdd:cd07102 83 LerarymISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAV--ILKHSPQTPLCge 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 181 -LAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVD 259
Cdd:cd07102 161 rFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 260 SAVEGVVDAAWSDRGP---GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG--ARGAAAcDLVQRFVREAQSQ 334
Cdd:cd07102 241 AAAESLVDGAFFNSGQsccSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGpvVSARAA-DFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 335 GA------QVFQAGDVPSerPFYPPTLVSNLPPASPCAQVEVPWPVV----VASPfrtaKEALLVANGTPRGGSASVWSE 404
Cdd:cd07102 320 GAralidgALFPEDKAGG--AYLAPTVLTNVDHSMRVMREETFGPVVgimkVKSD----AEAIALMNDSEYGLTASVWTK 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 768006441 405 RLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 458
Cdd:cd07102 394 DIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRP 447
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
72-442 |
5.42e-27 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 115.22 E-value: 5.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 72 RAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQLAQQLLHY--HA----------IQASTQEEALAGWEPMGV 139
Cdd:PRK09406 47 RARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYaeHAealladepadAAAVGASRAYVRYQPLGV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 140 IGLILPPTFSFLEMMWRICPALAVGCtvVALVPPASPAP---LLLAQLAGELGpFP-GILNVLSGPASLVPILASQPGIR 215
Cdd:PRK09406 127 VLAVMPWNFPLWQVVRFAAPALMAGN--VGLLKHASNVPqtaLYLADLFRRAG-FPdGCFQTLLVGSGAVEAILRDPRVA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 216 KVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGPGGL---RLLIQESVWDEAMR 292
Cdd:PRK09406 204 AATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIaakRFIVHADVYDAFAE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 293 RLQERMGRLRSGRGLDGAVDMGARGA-AACDLVQRFVREAQSQGAQVFQAGDVPsERP--FYPPTLVSNLPPASPCAQVE 369
Cdd:PRK09406 284 KFVARMAALRVGDPTDPDTDVGPLATeQGRDEVEKQVDDAVAAGATILCGGKRP-DGPgwFYPPTVITDITPDMRLYTEE 362
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006441 370 VPWPVvvASPFRTAK--EALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 442
Cdd:PRK09406 363 VFGPV--ASLYRVADidEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSG 435
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
14-409 |
2.92e-26 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 113.07 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 14 YVNGKWLKPEHrnSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 93
Cdd:cd07130 2 VYDGEWGGGGG--VVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 94 ESLVTGRAVREVRdGDVQ-----------LAQQLlhYHAIQAStqEEA----LAGWEPMGVIGLIlpPTFSFLEMMWRIC 158
Cdd:cd07130 80 VSLEMGKILPEGL-GEVQemidicdfavgLSRQL--YGLTIPS--ERPghrmMEQWNPLGVVGVI--TAFNFPVAVWGWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 159 PALAVGCTVVALVPPASPAPL-------LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRR 231
Cdd:cd07130 153 AAIALVCGNVVVWKPSPTTPLtaiavtkIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 232 SLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAwsdRGPGGL------RLLIQESVWDEAMRRLQERMGRLRSGR 305
Cdd:cd07130 233 AVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAA---VGTAGQrctttrRLIVHESIYDEVLERLKKAYKQVRIGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 306 GLDGAVDMGA-RGAAACDLVQRFVREAQSQGAQVFQAGDVpSERP--FYPPTLVSNLPPAsPCAQVEVPWPVVVASPFRT 382
Cdd:cd07130 310 PLDDGTLVGPlHTKAAVDNYLAAIEEAKSQGGTVLFGGKV-IDGPgnYVEPTIVEGLSDA-PIVKEETFAPILYVLKFDT 387
|
410 420
....*....|....*....|....*..
gi 768006441 383 AKEALLVANGTPRGGSASVWSERLGQA 409
Cdd:cd07130 388 LEEAIAWNNEVPQGLSSSIFTTDLRNA 414
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
60-456 |
3.10e-26 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 113.49 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 60 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVrDGDVQLAQQLLHYHAIQA-----STQEEALAG- 133
Cdd:PRK03137 85 AFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMlkladGKPVESRPGe 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 134 -----WEPMGViGLILPP-TFSFLEMMWRICPALAVGCTVVAlvPPASPAPLLLAQLAG---ELGPFPGILNVLSG-PAS 203
Cdd:PRK03137 164 hnryfYIPLGV-GVVISPwNFPFAIMAGMTLAAIVAGNTVLL--KPASDTPVIAAKFVEvleEAGLPAGVVNFVPGsGSE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 204 LVPILASQPGIRKVAFCGAPEEG-----RA---------LRRSLAgecaELGlalGTESLLLlTDTADVDSAVEGVVDAA 269
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGlriyeRAakvqpgqiwLKRVIA----EMG---GKDAIVV-DEDADLDLAAESIVASA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 270 WSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAvDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVP 345
Cdd:PRK03137 313 FGFSGqkcSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPViNQASFDKIMSYIEIGKEEGRLVLGGEGDD 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 346 SERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWS---ERLGQALELgygLQVGTVW 422
Cdd:PRK03137 392 SKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISnnrEHLEKARRE---FHVGNLY 468
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 768006441 423 IN---------AHglrdpsvPTGGCKESGC-SWHGGPDGLYEYL 456
Cdd:PRK03137 469 FNrgctgaivgYH-------PFGGFNMSGTdSKAGGPDYLLLFL 505
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
498-736 |
6.80e-25 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 108.84 E-value: 6.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 498 PYGLFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSpgaraallwalAAALERRK-- 574
Cdd:cd07091 3 PTGLFINNEFvDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRK-----------MDPRERGRll 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 575 STLASRLERQGAELKAAEA-------------EVELSARRLR---AWGARVQaqGHTLQVAGlRGPVLRLREPLGVLAVV 638
Cdd:cd07091 72 NKLADLIERDRDELAALESldngkpleesakgDVALSIKCLRyyaGWADKIQ--GKTIPIDG-NFLAYTRREPIGVCGQI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 639 CPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFG 717
Cdd:cd07091 149 IPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTG 228
|
250 260
....*....|....*....|
gi 768006441 718 S-AQGSQFVEWASAGNLKPV 736
Cdd:cd07091 229 StAVGRTIMEAAAKSNLKKV 248
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
499-736 |
2.87e-24 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 107.04 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 499 YGLFVGGRFQAP-GARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--S 575
Cdd:cd07559 1 YDNFINGEWVAPsKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSV-------------AERANilN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 576 TLASRLERQGAELKAAE-------------AEVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDE 642
Cdd:cd07559 68 KIADRIEENLELLAVAEtldngkpiretlaADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 643 WPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGS 722
Cdd:cd07559 148 FPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVG 227
|
250
....*....|....
gi 768006441 723 QFVEWASAGNLKPV 736
Cdd:cd07559 228 RLIMQYAAENLIPV 241
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
521-736 |
3.42e-24 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 106.64 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 521 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKS--TLASRLERQGAELKAAEA----- 593
Cdd:cd07092 5 ATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPA-------------ERSKAllKLADAIEENAEELAALESrntgk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 594 --------EVELSARRLR--AWGARVQ--------AQGHTLQVaglrgpvlrLREPLGVLAVVCPDEWPLLAFVSLLAPA 655
Cdd:cd07092 72 plhlvrddELPGAVDNFRffAGAARTLegpaageyLPGHTSMI---------RREPIGVVAQIAPWNYPLMMAAWKIAPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 656 LAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKP 735
Cdd:cd07092 143 LAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKR 222
|
.
gi 768006441 736 V 736
Cdd:cd07092 223 V 223
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
527-736 |
9.20e-24 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 105.31 E-value: 9.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 527 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAsRLER--QGAELKAAEAEVELSARRLRA 604
Cdd:pfam00171 21 ATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELA-ELETleNGKPLAEARGEVDRAIDVLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 605 W-GARVQAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMAT 683
Cdd:pfam00171 100 YaGLARRLDGETLPSDPGRLAYTR-REPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768006441 684 V-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVEwASAGNLKPV 736
Cdd:pfam00171 179 AgLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAvGRHIAE-AAAQNLKRV 232
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
32-455 |
1.35e-23 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 104.94 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 32 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 111
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 112 LAQQLLHYHAIQAST----------QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCT-VVALVPPASPAPLL 180
Cdd:PRK13968 92 KSANLCDWYAEHGPAmlkaeptlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGyLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 181 LAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDS 260
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 261 AVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG--ARGAAACDLVQRfVREAQSQG 335
Cdd:PRK13968 252 AVKAAVAGRYQNTGqvcAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGpmARFDLRDELHHQ-VEATLAEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 336 AQVFQAGD-VPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGY 414
Cdd:PRK13968 331 ARLLLGGEkIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 768006441 415 GLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEY 455
Cdd:PRK13968 411 RLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
502-736 |
3.74e-23 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 103.54 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 502 FVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAF--PGWAGQSPGARAALLWALAAALERRKSTLA 578
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINpANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 579 sRLE--RQGAELKAAEAEVELSARRLRAW--------GARVQAQGHTLQVAglrgpvlrLREPLGVLAVVCPDEWPLLAF 648
Cdd:cd07119 81 -RLEtlNTGKTLRESEIDIDDVANCFRYYaglatketGEVYDVPPHVISRT--------VREPVGVCGLITPWNYPLLQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 649 VSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEW 727
Cdd:cd07119 152 AWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMR 231
|
....*....
gi 768006441 728 ASAGNLKPV 736
Cdd:cd07119 232 AAAGNVKKV 240
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
501-736 |
5.20e-23 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 103.34 E-value: 5.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 501 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFP--GWAGQSPgaraallwalaaaLERRK--S 575
Cdd:cd07142 6 LFINGQFVDAASGKTFPTIDpRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTG-------------YERSRilL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 576 TLASRLERQGAELKAAE-------------AEVELSARRLRAW-GARVQAQGHTLQVAGLRGpVLRLREPLGVLAVVCPD 641
Cdd:cd07142 73 RFADLLEKHADELAALEtwdngkpyeqaryAEVPLAARLFRYYaGWADKIHGMTLPADGPHH-VYTLHEPIGVVGQIIPW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 642 EWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ 720
Cdd:cd07142 152 NFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTE 231
|
250
....*....|....*..
gi 768006441 721 -GSQFVEWASAGNLKPV 736
Cdd:cd07142 232 vGKIIMQLAAKSNLKPV 248
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
540-736 |
6.66e-23 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 102.29 E-value: 6.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 540 AVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVELSARRLR---AWGARVQAQGHT 615
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLeTGKPIEEALGEVARAADTFRyyaGLARRLHGEVIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 616 LQVAGLRGpvLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVT 694
Cdd:cd07078 83 SPDPGELA--IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNVVT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 768006441 695 GDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRV 202
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
502-720 |
7.60e-23 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 102.71 E-value: 7.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 502 FVGGRFQAPGARssRPIRDSS--GNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAS 579
Cdd:cd07097 4 YIDGEWVAGGDG--EENRNPSdtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 580 RLER-QGAELKAAEAEVELSARRLRAWGARVQAQ-GHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALA 657
Cdd:cd07097 82 LLTReEGKTLPEARGEVTRAGQIFRYYAGEALRLsGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006441 658 YGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ 720
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTA 225
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
521-736 |
8.54e-23 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 102.13 E-value: 8.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 521 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAsRLERQ--GAELKAAE-AEVEL 597
Cdd:cd07115 5 ATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELA-RLESLdtGKPIRAARrLDVPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 598 SARRLRAWGARVQAQGHtlQVAGLRGPVLR--LREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAL 675
Cdd:cd07115 84 AADTFRYYAGWADKIEG--EVIPVRGPFLNytVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768006441 676 EVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07115 162 RIAELMAEAgFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRV 223
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
498-734 |
1.51e-22 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 101.91 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 498 PYGLFVGGRFQAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKS-- 575
Cdd:PRK13473 2 QTKLLINGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPK-------------ERAEAll 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 576 TLASRLERQGAELKAAEA-------------EVELSARRLR--AWGARVQ--------AQGHTLQVaglrgpvlRlREPL 632
Cdd:PRK13473 69 KLADAIEENADEFARLESlncgkplhlalndEIPAIVDVFRffAGAARCLegkaageyLEGHTSMI--------R-RDPV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 633 GVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQA 712
Cdd:PRK13473 140 GVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRM 219
|
250 260
....*....|....*....|...
gi 768006441 713 MWYFGS-AQGSQFVEwASAGNLK 734
Cdd:PRK13473 220 VSLTGSiATGKHVLS-AAADSVK 241
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
522-736 |
2.30e-22 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 100.87 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 522 SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSAR 600
Cdd:cd07150 8 DGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEgGSTYGKAWFETTFTPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 601 RLRAWGARVQA-QGHTLQ--VAGLRGPVlrLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV 677
Cdd:cd07150 88 LLRAAAGECRRvRGETLPsdSPGTVSMS--VRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 678 CQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07150 166 AEIMEEAgLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKI 225
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
529-736 |
8.74e-22 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 99.14 E-value: 8.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 529 VAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVELSARRLRAwga 607
Cdd:cd07106 13 APVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLeQGKPLAEAQFEVGGAVAWLRY--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 608 rvqaqghtlqVAGLRGPVLRLRE-----------PLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALE 676
Cdd:cd07106 90 ----------TASLDLPDEVIEDddtrrvelrrkPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 677 VCQDMATVFPAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07106 160 LGELAQEVLPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRV 218
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
527-763 |
1.06e-21 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 98.97 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 527 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELK-AAEAEVELSARRLRA 604
Cdd:cd07108 11 GEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALEtGNALRtQARPEAAVLADLFRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 605 WGarvqaqghtlQVAG-LRGPVLRL---------REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLA 674
Cdd:cd07108 91 FG----------GLAGeLKGETLPFgpdvltytvREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 675 LEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPVWASRG-------CPRAwD 747
Cdd:cd07108 161 LLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGgkspmivFPDA-D 239
|
250
....*....|....*.
gi 768006441 748 QEAEGAGPELGLRVAR 763
Cdd:cd07108 240 LDDAVDGAIAGMRFTR 255
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
529-737 |
1.55e-21 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 98.44 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 529 VAEGGAKDIRGAVEAAHQAFPG--WAGQSPgaraallwalaaalERRKSTL---ASRLERQGAEL-------------KA 590
Cdd:cd07112 18 VAACDAADVDRAVAAARRAFESgvWSRLSP--------------AERKAVLlrlADLIEAHRDELalletldmgkpisDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 591 AEAEVELSARRLRaWGARVQAQghtlqVAGLRGPV------LRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVM 664
Cdd:cd07112 84 LAVDVPSAANTFR-WYAEAIDK-----VYGEVAPTgpdalaLITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006441 665 VPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEWASAGNLKPVW 737
Cdd:cd07112 158 KPAEQSPLTALRLAELALEAgLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGStEVGRRFLEYSGQSNLKRVW 232
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
521-736 |
1.61e-21 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 98.46 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 521 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ--GAELKAAEAEVELS 598
Cdd:cd07109 5 STGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLdtGKPLTQARADVEAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 599 ARRLRAWGARVQA-QGHTLQVaglrGP---VLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLA 674
Cdd:cd07109 85 ARYFEYYGGAADKlHGETIPL----GPgyfVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006441 675 LEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07109 161 LRLAELAEEAgLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPV 223
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
498-736 |
1.69e-21 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 98.75 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 498 PYGLFVGGRFqAPGARSSRP--IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPG-WAGQSPGARA-ALLWALAAALERR 573
Cdd:cd07143 6 PTGLFINGEF-VDSVHGGTVkvYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGLKVSGSKRgRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 574 KSTLAS--RLERQGAELKAAEAEVELSARRLRAWGARV-QAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVS 650
Cdd:cd07143 85 LDYLASieALDNGKTFGTAKRVDVQASADTFRYYGGWAdKIHGQVIETDIKKLTYTR-HEPIGVCGQIIPWNFPLLMCAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 651 LLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEWA 728
Cdd:cd07143 164 KIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGStLVGRKVMEAA 243
|
....*...
gi 768006441 729 SAGNLKPV 736
Cdd:cd07143 244 AKSNLKKV 251
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
521-736 |
5.18e-21 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 96.68 E-value: 5.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 521 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--STLASRLERQGAELKAAEA----- 593
Cdd:cd07107 5 ATGQVLARVPAASAADVDRAVAAARAAFPEWRATTP-------------LERARmlRELATRLREHAEELALIDAldcgn 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 594 -------EVELSARRLRAWGARV-QAQGHTLQVAGlRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMV 665
Cdd:cd07107 72 pvsamlgDVMVAAALLDYFAGLVtELKGETIPVGG-RNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006441 666 PSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07107 151 PPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHV 221
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
502-736 |
1.03e-20 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 96.18 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 502 FVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASR 580
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNpATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 581 L-ERQGAELKAAEAEVELSARRLR--AWGARvQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALA 657
Cdd:cd07088 81 IvEEQGKTLSLARVEVEFTADYIDymAEWAR-RIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 658 YGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
521-720 |
1.63e-19 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 92.03 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 521 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSA 599
Cdd:cd07145 7 ANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEvGKPIKQSRVEVERTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 600 R--RLRAWGARVqAQGHTLQVAGL----RGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLL 673
Cdd:cd07145 87 RlfKLAAEEAKV-LRGETIPVDAYeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768006441 674 ALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ 720
Cdd:cd07145 166 AIELAKILEEAgLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTA 213
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
499-753 |
1.66e-19 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 92.52 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 499 YGLFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTL 577
Cdd:cd07117 1 YGLFINGEWvKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 578 ASrLER--QGAELKAAEA-EVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAP 654
Cdd:cd07117 81 AM-VETldNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 655 ALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLK 734
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLI 239
|
250 260
....*....|....*....|....*..
gi 768006441 735 PVWASRGCPRA--------WDQEAEGA 753
Cdd:cd07117 240 PATLELGGKSAniifddanWDKALEGA 266
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
499-736 |
2.35e-19 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 91.74 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 499 YGLFVGGRFQAP-GARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--S 575
Cdd:cd07116 1 YDNFIGGEWVAPvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSV-------------AERANilN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 576 TLASRLERQGAELKAAE-------------AEVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDE 642
Cdd:cd07116 68 KIADRMEANLEMLAVAEtwdngkpvretlaADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 643 WPLLAFVSLLAPALAYGNTVVMVPSAACP---LLALEVCQDMatvFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS- 718
Cdd:cd07116 148 FPLLMATWKLAPALAAGNCVVLKPAEQTPasiLVLMELIGDL---LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGEt 224
|
250
....*....|....*...
gi 768006441 719 AQGSQFVEWASAgNLKPV 736
Cdd:cd07116 225 TTGRLIMQYASE-NIIPV 241
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
542-736 |
2.60e-19 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 90.37 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 542 EAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVELSARRLR---AWGARVQAQGHTLQ 617
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLeTGKPIEEALGEVARAIDTFRyaaGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 618 VAGLRGpvLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGD 696
Cdd:cd06534 81 DPGGEA--YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 768006441 697 RDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPV 198
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
499-734 |
2.67e-19 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 91.69 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 499 YGLFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAgQSPGARAALLWALAAALERRKSTL 577
Cdd:cd07111 22 FGHFINGKWVKPENRKSFPTINpATGEVLASVLQAEEEDVDAAVAAARTAFESWS-ALPGHVRARHLYRIARHIQKHQRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 578 ASRLER--QGAELKAA-EAEVELSARRLRAWGarVQAQghtLQVAGLRGPvlrlrEPLGVLAVVCPDEWPLLAFVSLLAP 654
Cdd:cd07111 101 FAVLESldNGKPIRESrDCDIPLVARHFYHHA--GWAQ---LLDTELAGW-----KPVGVVGQIVPWNFPLLMLAWKICP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 655 ALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDrDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAG 731
Cdd:cd07111 171 ALAMGNTVVLKPAEYTPLTALlfaEICAEAG--LPPGVLNIVTGN-GSFGSALANHPGVDKVAFTGSTEVGRALRRATAG 247
|
...
gi 768006441 732 NLK 734
Cdd:cd07111 248 TGK 250
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
500-736 |
4.82e-19 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 90.96 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 500 GLFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPG-WAGQSPGARaallwalaaalERRKSTL 577
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNpATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAER-----------GRILLRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 578 ASRLERQGAELKAAEA-------------EVELSARRLR---AWGARVQaqGHTLQV-----AGLRGPVLRLREPLGVLA 636
Cdd:cd07113 70 ADLIEQHGEELAQLETlcsgksihlsrafEVGQSANFLRyfaGWATKIN--GETLAPsipsmQGERYTAFTRREPVGVVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 637 VVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQdMATV--FPAGLANVVTGDRDhLTRCLALHQDVQAMW 714
Cdd:cd07113 148 GIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAE-LAKEagIPDGVLNVVNGKGA-VGAQLISHPDVAKVS 225
|
250 260
....*....|....*....|..
gi 768006441 715 YFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07113 226 FTGSVATGKKIGRQAASDLTRV 247
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
501-741 |
5.44e-19 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 91.11 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 501 LFVGGRFQAPGARSSRPIRDSSGNLH-GYVAEGGAKDIRGAVEAAHQAFPG--WAGQSPGaraallwalaaaleRRKSTL 577
Cdd:PRK09847 22 LFINGEYTAAAENETFETVDPVTQAPlAKIARGKSVDIDRAVSAARGVFERgdWSLSSPA--------------KRKAVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 578 ---ASRLERQGAELKAAEA-------------EVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPD 641
Cdd:PRK09847 88 nklADLMEAHAEELALLETldtgkpirhslrdDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 642 EWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ 720
Cdd:PRK09847 168 NFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTR 247
|
250 260
....*....|....*....|..
gi 768006441 721 -GSQFVEWASAGNLKPVWASRG 741
Cdd:PRK09847 248 tGKQLLKDAGDSNMKRVWLEAG 269
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
498-736 |
5.81e-19 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 90.63 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 498 PYGLFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPG--WAGQSPGARAALLWALAAALERRK 574
Cdd:cd07140 5 PHQLFINGEFvDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 575 STLAS--RLERQGAELKAAEAEVELSARRLR---AWGARVQaqGHTLQVAGLRgP----VLRLREPLGVLAVVCPDEWPL 645
Cdd:cd07140 85 EELATieSLDSGAVYTLALKTHVGMSIQTFRyfaGWCDKIQ--GKTIPINQAR-PnrnlTLTKREPIGVCGIVIPWNYPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 646 LAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQ 723
Cdd:cd07140 162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAgFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPiGKH 241
|
250
....*....|...
gi 768006441 724 FVEWASAGNLKPV 736
Cdd:cd07140 242 IMKSCAVSNLKKV 254
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
501-736 |
7.66e-19 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 90.64 E-value: 7.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 501 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAF---PgWAGQSPgaraallwalaaaLERRKST 576
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDpRTGEVIAHVAEGDAEDVNRAVAAARKAFdegP-WPKMTA-------------YERSRIL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 577 L--ASRLERQGAEL-------------KAAEAEVELSARRLR---AW-----GARVQAQG-HTLQVaglrgpvlrLREPL 632
Cdd:PLN02466 126 LrfADLLEKHNDELaaletwdngkpyeQSAKAELPMFARLFRyyaGWadkihGLTVPADGpHHVQT---------LHEPI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 633 GVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQ 711
Cdd:PLN02466 197 GVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASHMDVD 276
|
250 260
....*....|....*....|....*.
gi 768006441 712 AMWYFGSAQGSQFV-EWASAGNLKPV 736
Cdd:PLN02466 277 KLAFTGSTDTGKIVlELAAKSNLKPV 302
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
521-734 |
1.01e-18 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 89.71 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 521 SSGNLHGYVAEGGAKDIRGAVEAAHQAF--PGWAgQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVEL 597
Cdd:cd07120 5 ATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWA-HDPRLRARVLLELADAFEANAERLARLLALeNGKILGEARFEISG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 598 SARRLRAWG--ARVQAqGHTLQVAGLRGPVLrLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAL 675
Cdd:cd07120 84 AISELRYYAglARTEA-GRMIEPEPGSFSLV-LREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006441 676 EV--CQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLK 734
Cdd:cd07120 162 AIirILAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLK 222
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
501-736 |
1.55e-18 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 89.49 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 501 LFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAF-----PGWAGQSPGaraallwalaaaleRRK 574
Cdd:PLN02766 23 LFINGEFvDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFdhgpwPRMSGFERG--------------RIM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 575 STLASRLERQGAELKAAEA-------------EVELSARRLRAW-GARVQAQGHTLQVAG-LRGpvLRLREPLGVLAVVC 639
Cdd:PLN02766 89 MKFADLIEEHIEELAALDTidagklfalgkavDIPAAAGLLRYYaGAADKIHGETLKMSRqLQG--YTLKEPIGVVGHII 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 640 PDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQ--DMATVfPAGLANVVTGDRDHLTRCLALHQDVQAMWYFG 717
Cdd:PLN02766 167 PWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHlaKLAGV-PDGVINVVTGFGPTAGAAIASHMDVDKVSFTG 245
|
250 260
....*....|....*....|
gi 768006441 718 SAQ-GSQFVEWASAGNLKPV 736
Cdd:PLN02766 246 STEvGRKIMQAAATSNLKQV 265
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
498-736 |
1.73e-18 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 89.39 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 498 PYGLFVGGRFQAPGARSSRP-IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGAraallwalaaalERRK-- 574
Cdd:cd07144 7 PTGLFINNEFVKSSDGETIKtVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGE------------ERGEll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 575 STLASRLERQGAELKAAEA----------------EVELSARRLRAWGARVQAQGHTLQVAGLRgpvLRLREPLGVLAVV 638
Cdd:cd07144 75 DKLADLVEKNRDLLAAIEAldsgkpyhsnalgdldEIIAVIRYYAGWADKIQGKTIPTSPNKLA---YTLHEPYGVCGQI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 639 CPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFG 717
Cdd:cd07144 152 IPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTG 231
|
250
....*....|....*....
gi 768006441 718 SAQGSQFVEWASAGNLKPV 736
Cdd:cd07144 232 STATGRLVMKAAAQNLKAV 250
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
15-424 |
2.19e-18 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 89.42 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 15 VNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLE 94
Cdd:PLN02419 118 IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 95 SLVTGRAVREvRDGDVQLAQQLLHYHAIQASTQE-----------EALAGWEPMGVIGLILPPTFSFLEMMWRICPALAV 163
Cdd:PLN02419 198 TTEQGKTLKD-SHGDIFRGLEVVEHACGMATLQMgeylpnvsngvDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTC 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 164 GCTVVALVPPASP-APLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGECAELGL 242
Cdd:PLN02419 277 GNTFILKPSEKDPgASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQS 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 243 ALGTESLLLLTDTADVDSAVEGVVDAAWsdrGPGGLRLLIQESV--------WDEamrRLQERMGRLRSGRGLDGAVDMG 314
Cdd:PLN02419 357 NMGAKNHGLVLPDANIDATLNALLAAGF---GAAGQRCMALSTVvfvgdaksWED---KLVERAKALKVTCGSEPDADLG 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 315 -ARGAAACDLVQRFVREAQSQGAQVFQAGD---VPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALL 388
Cdd:PLN02419 431 pVISKQAKERICRLIQSGVDDGAKLLLDGRdivVPGYEKgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAIS 510
|
410 420 430
....*....|....*....|....*....|....*.
gi 768006441 389 VANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN 424
Cdd:PLN02419 511 IINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
493-736 |
5.31e-18 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 87.87 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 493 PSPAPPYGLFVGGRFQAPGARSSRP-IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPG-----WAGQSPGARAALLWAL 566
Cdd:PLN02467 2 AIPVPRRQLFIGGEWREPVLGKRIPvVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 567 AAALERRKSTLAsRLERQ--GAELKAAEAEV-------ELSARRLRAWGARvQAQGHTLQVAGLRGPVlrLREPLGVLAV 637
Cdd:PLN02467 82 AAKITERKSELA-KLETLdcGKPLDEAAWDMddvagcfEYYADLAEALDAK-QKAPVSLPMETFKGYV--LKEPLGVVGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 638 VCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALE---VCQDMAtvFPAGLANVVTGDRDHLTRCLALHQDVQAMW 714
Cdd:PLN02467 158 ITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLEladICREVG--LPPGVLNVVTGLGTEAGAPLASHPGVDKIA 235
|
250 260
....*....|....*....|..
gi 768006441 715 YFGSAQGSQFVEWASAGNLKPV 736
Cdd:PLN02467 236 FTGSTATGRKIMTAAAQMVKPV 257
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
501-718 |
6.92e-18 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 87.17 E-value: 6.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 501 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--STL 577
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINpATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSV-------------EERAAllERI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 578 ASRLERQGAELKAAEAEvELSARRlrAWGARVQAQG------HTLQVAGL------RGPVLRLREPLGVLAVVCPDEWPL 645
Cdd:cd07138 68 AEAYEARADELAQAITL-EMGAPI--TLARAAQVGLgighlrAAADALKDfefeerRGNSLVVREPIGVCGLITPWNWPL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768006441 646 LAFVSLLAPALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS 718
Cdd:cd07138 145 NQIVLKVAPALAAGCTVVLKPSEVAPLSAIilaEILDEAG--LPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGS 218
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
529-736 |
7.64e-18 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 87.22 E-value: 7.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 529 VAEGGAKDIRGAVEAAHQAF--PGWAGQSPgaraallwalaaaLERRK--STLASRLERQGAELKAAE--------AEVE 596
Cdd:cd07114 13 VPEASAADVDRAVAAARAAFegGAWRKLTP-------------TERGKllRRLADLIEANAEELAELEtrdngkliRETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 597 LSARRLRAW-----GARVQAQGHTLQVAglRGPVLR--LREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAA 669
Cdd:cd07114 80 AQVRYLAEWyryyaGLADKIEGAVIPVD--KGDYLNftRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEH 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006441 670 CPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07114 158 TPASTLELAKLAEEAgFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPV 225
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
501-738 |
7.68e-18 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 87.19 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 501 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAS 579
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNpATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 580 RLER-QGAELKAAEAEVelsARRLR----AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAP 654
Cdd:cd07085 83 LITLeHGKTLADARGDV---LRGLEvvefACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 655 ALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDRDHLTRCLAlHQDVQAMWYFGSAQGSQFVEWASAG 731
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMrlaELLQEAG--LPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYIYERAAA 236
|
....*..
gi 768006441 732 NLKPVWA 738
Cdd:cd07085 237 NGKRVQA 243
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
521-736 |
1.20e-17 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 86.47 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 521 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--STLASRLERQGAELKAAE------ 592
Cdd:cd07093 5 ATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSP-------------AERARilHKVADLIEARADELALLEsldtgk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 593 -------AEVELSARRLRAWGARVQAQGHTL--QVAGLRGPVlrLREPLGVLAVVCPdeW--PLLAFVSLLAPALAYGNT 661
Cdd:cd07093 72 pitlartRDIPRAAANFRFFADYILQLDGESypQDGGALNYV--LRQPVGVAGLITP--WnlPLMLLTWKIAPALAFGNT 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768006441 662 VVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEwASAGNLKPV 736
Cdd:cd07093 148 VVLKPSEWTPLTAWLLAELANEAgLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGEtATGRTIMR-AAAPNLKPV 223
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
501-736 |
1.46e-17 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 86.09 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 501 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPG--WAGQSPGARAALLWALAAALERRKSTL 577
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSpATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 578 ASRLERQ-GAELKAAE-AEVELSARRLRAWGArvQAQGHTL---QVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLL 652
Cdd:cd07139 81 ARLWTAEnGMPISWSRrAQGPGPAALLRYYAA--LARDFPFeerRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 653 APALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDRD---HLTRclalHQDVQAMWYFGSAQGSQFVE 726
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYllaEAAEEAG--LPPGVVNVVPADREvgeYLVR----HPGVDKVSFTGSTAAGRRIA 232
|
250
....*....|
gi 768006441 727 WASAGNLKPV 736
Cdd:cd07139 233 AVCGERLARV 242
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
521-736 |
2.50e-17 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 85.48 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 521 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAsRLERQGAELKAAEAEVELS-- 598
Cdd:cd07110 5 ATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELA-ELEARDNGKPLDEAAWDVDdv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 599 ----------ARRLRAWGARvqaqghTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSA 668
Cdd:cd07110 84 agcfeyyadlAEQLDAKAER------AVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006441 669 ACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07110 158 LTSLTELELAEIAAEAgLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPV 226
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
1-459 |
2.83e-17 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 85.66 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 1 MAWLDTQDRCLGHYVNGKWlkPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLA 80
Cdd:PLN02315 11 LSEIGLSSRNLGCYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 81 EVIQKHQRLLWTLESLVTGR----AVREVR------DGDVQLAQQLLHYHAIQASTQEEALAGWEPMGVIGLILPPTFSF 150
Cdd:PLN02315 89 DALRAKLDYLGRLVSLEMGKilaeGIGEVQeiidmcDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 151 LEMMWRICPALAVGCTVVALVPPASP-----APLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEE 225
Cdd:PLN02315 169 AVLGWNACIALVCGNCVVWKGAPTTPlitiaMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 226 GRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAA---WSDRGPGGLRLLIQESVWDEAMRRLQERMGRLR 302
Cdd:PLN02315 249 GLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAvgtAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 303 SGRGLDGAVDMGA-RGAAACDLVQRFVREAQSQGAQVFQAGD-VPSERPFYPPTLVSnLPPASPCAQVEVPWPVVVASPF 380
Cdd:PLN02315 329 IGDPLEKGTLLGPlHTPESKKNFEKGIEIIKSQGGKILTGGSaIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKF 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 381 RTAKEALLVANGTPRGGSASVWSERLGQALElgyglqvgtvWINAH----GLRDPSVPT---------GGCKESGCSWHG 447
Cdd:PLN02315 408 KTLEEAIEINNSVPQGLSSSIFTRNPETIFK----------WIGPLgsdcGIVNVNIPTngaeiggafGGEKATGGGREA 477
|
490
....*....|..
gi 768006441 448 GPDGLYEYLRPS 459
Cdd:PLN02315 478 GSDSWKQYMRRS 489
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
527-736 |
4.85e-17 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 84.41 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 527 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLER-------------RKSTLAS--RLErQGAELKAA 591
Cdd:cd07103 11 GEVPDAGAADADAAIDAAAAAFKTWRKTTA-------------RERaailrrwadlireRAEDLARllTLE-QGKPLAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 592 EAEVELSARRLRaW----GARVQAQGHTLQVAGLRgpVLRLREPLGVLAVVCPdeW--PLLAFVSLLAPALAYGNTVVMV 665
Cdd:cd07103 77 RGEVDYAASFLE-WfaeeARRIYGRTIPSPAPGKR--ILVIKQPVGVVAAITP--WnfPAAMITRKIAPALAAGCTVVLK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006441 666 PSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEwASAGNLKPV 736
Cdd:cd07103 152 PAEETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGStAVGKLLMA-QAADTVKRV 223
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
13-442 |
3.67e-16 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 82.11 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 13 HYVNGKWLKPEHRNSVPCQDPITGE---NLASCLQAQAEDVAAAVeaaRMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRL 89
Cdd:PLN00412 18 YYADGEWRTSSSGKSVAITNPSTRKtqyKVQACTQEEVNKAMESA---KAAQKAWAKTPLWKRAELLHKAAAILKEHKAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 90 LwtLESLV------TGRAVREV-RDGDV----------QLAQ-QLLHYHAIQASTQEE-ALAGWEPMGVIGLILPPTFSF 150
Cdd:PLN00412 95 I--AECLVkeiakpAKDAVTEVvRSGDLisytaeegvrILGEgKFLVSDSFPGNERNKyCLTSKIPLGVVLAIPPFNYPV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 151 LEMMWRICPALAVGCTVVaLVPP--ASPAPLLLAQ---LAGelgpFP-GILNVLSGPASLV-PILASQPGIRKVAFCGAp 223
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVV-LKPPtqGAVAALHMVHcfhLAG----FPkGLISCVTGKGSEIgDFLTMHPGVNCISFTGG- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 224 EEGRALRRSlAGECA---ELGlalGTESLLLLTDtADVDSAVEGVVDAAWS---DRGPGGLRLLIQESVWDEAMRRLQER 297
Cdd:PLN00412 247 DTGIAISKK-AGMVPlqmELG---GKDACIVLED-ADLDLAAANIIKGGFSysgQRCTAVKVVLVMESVADALVEKVNAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 298 MGRLRSGRGLDGAVDMGARGAAACDLVQRFVREAQSQGAQVFQagDVPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVA 377
Cdd:PLN00412 322 VAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQ--EWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768006441 378 SPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPS-VPTGGCKESG 442
Cdd:PLN00412 400 IRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSG 465
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
536-736 |
4.45e-16 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 81.42 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 536 DIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLR-AWGARVQAQG 613
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIREsGSTRPKAAFEVGAAIAILReAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 614 HTLQvAGLRGPVLRL-REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACP-----LLAlEVCQDMAtvFPA 687
Cdd:cd07104 81 EILP-SDVPGKESMVrRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA-EIFEEAG--LPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768006441 688 GLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKV 205
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
526-736 |
6.96e-16 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 80.84 E-value: 6.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 526 HGYV----AEGGAKDIRGAVEAAHQAFP-GWAGQSPGARAALLWALAAALERRKSTLASRLE--RQGAELKAAEAEVELS 598
Cdd:cd07118 6 HGVVvaryAEGTVEDVDAAVAAARKAFDkGPWPRMSGAERAAVLLKVADLIRARRERLALIEtlESGKPISQARGEIEGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 599 ARRLR-AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV 677
Cdd:cd07118 86 ADLWRyAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLML 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006441 678 CQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVEwASAGNLKPV 736
Cdd:cd07118 166 AELLIEAgLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRvGKAIAA-AAARNLKKV 225
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
502-736 |
7.37e-16 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 80.85 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 502 FVGGRF--QAPGAR--SSRPIRDSsgNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTL 577
Cdd:cd07131 2 YIGGEWvdSASGETfdSRNPADLE--EVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 578 ASRLERQ-GAELKAAEAEVElsarrlRAWGARVQAQGHTLQVAGLRGP-------VLRLREPLGVLAVVCPDEWPLLAFV 649
Cdd:cd07131 80 ARLVTREmGKPLAEGRGDVQ------EAIDMAQYAAGEGRRLFGETVPselpnkdAMTRRQPIGVVALITPWNFPVAIPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 650 SLLAPALAYGNTVVMVPSAACPLLALEVCQD-MATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWA 728
Cdd:cd07131 154 WKIFPALVCGNTVVFKPAEDTPACALKLVELfAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGET 233
|
....*...
gi 768006441 729 SAGNLKPV 736
Cdd:cd07131 234 CARPNKRV 241
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
76-454 |
1.79e-15 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 79.77 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 76 LTRLAEVIQKHQRLLWTL----------ESLV-TGRAVREVRDGDVQLAQQLLHYHAI---QASTQEEALAGWEPMGVIG 141
Cdd:cd07148 50 LERLADLMEERADELALLiareggkplvDAKVeVTRAIDGVELAADELGQLGGREIPMgltPASAGRIAFTTREPIGVVV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 142 LILPPTFSFLEMMWRICPALAVGCTVvaLVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVA 218
Cdd:cd07148 130 AISAFNHPLNLIVHQVAPAIAAGCPV--IVKPALATPLsclAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 219 FCGAPEEGRALRRSLA--GECAelgLALGTESLLLLTDTADVDSAVEGVVDAAWSDRGPGGL---RLLIQESVWDEAMRR 293
Cdd:cd07148 208 FIGSARVGWMLRSKLApgTRCA---LEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVsvqRVFVPAEIADDFAQR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 294 LQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFqAGDVPSERPFYPPTLVSNLPPASPCAQVEVPW 372
Cdd:cd07148 285 LAAAAEKLVVGDPTDPDTEVGPLiRPREVDRVEEWVNEAVAAGARLL-CGGKRLSDTTYAPTVLLDPPRDAKVSTQEIFG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 373 PVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAH-GLRDPSVPTGGCKESGCSWHGGPDG 451
Cdd:cd07148 364 PVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHtAFRVDWMPFAGRRQSGYGTGGIPYT 443
|
...
gi 768006441 452 LYE 454
Cdd:cd07148 444 MHD 446
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
29-442 |
2.85e-15 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 79.55 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 29 PCQDPITGE-NLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVrD 107
Cdd:cd07125 49 PVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADA-D 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 108 GDVQLAQQLLHYHAIQA-----------STQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVAlvPPASP 176
Cdd:cd07125 128 AEVREAIDFCRYYAAQArelfsdpelpgPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIA--KPAEQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 177 APL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGECAELgLALGTES---- 248
Cdd:cd07125 206 TPLiaaRAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTETAKLINRALAERDGPI-LPLIAETggkn 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 249 LLLLTDTADVDSAVEGVVDAAWSDRGP--GGLRLLI-QESVWDEAMRRLQERMGRLRSGRGLDGAVDMG--ARGAAAcDL 323
Cdd:cd07125 285 AMIVDSTALPEQAVKDVVQSAFGSAGQrcSALRLLYlQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGplIDKPAG-KL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 324 VQRFVREAQSQGAQVFQAgDVPSERP-FYPPTLVSNlpPASPCAQVEVPWPV--VVASPFRTAKEALLVANGTPRGGSAS 400
Cdd:cd07125 364 LRAHTELMRGEAWLIAPA-PLDDGNGyFVAPGIIEI--VGIFDLTTEVFGPIlhVIRFKAEDLDEAIEDINATGYGLTLG 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 768006441 401 VWSERLGQALELGYGLQVGTVWINahglRD------PSVPTGGCKESG 442
Cdd:cd07125 441 IHSRDEREIEYWRERVEAGNLYIN----RNitgaivGRQPFGGWGLSG 484
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
499-710 |
4.13e-15 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 78.80 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 499 YGLFVGGR-FQAPGARSSRPIRDSSGNLhGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTL 577
Cdd:cd07124 33 YPLVIGGKeVRTEEKIESRNPADPSEVL-GTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 578 ASRLERQ-GAELKAAEAEV-------ELSARRLRAWGARVqaqghtlqVAGLRGPVLRLR-EPLGVLAVVCPDEWPLLAF 648
Cdd:cd07124 112 AAWMVLEvGKNWAEADADVaeaidflEYYAREMLRLRGFP--------VEMVPGEDNRYVyRPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006441 649 VSLLAPALAYGNTVVMVPSAACPLLA---LEVCQDMAtvFPAGLANVVTGDRDHLTRCLALHQDV 710
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIAaklVEILEEAG--LPPGVVNFLPGPGEEVGDYLVEHPDV 246
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
58-413 |
9.33e-15 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 77.31 E-value: 9.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 58 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ-----LAQQLLHYHAiQASTQEEALA 132
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQ-TEVAamagkIDISIKAYHE-RTGERATPMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 133 GWE------PMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPAS 203
Cdd:cd07095 88 QGRavlrhrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVV--FKPSELTPAvaeLMVELWEEAGLPPGVLNLVQGGRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 204 LVPILASQPGIRKVAFCGAPEEGRALRRSLAGECAE-LGLALGTESLLLLTDTADVDSAVEGVVDAAW---SDRGPGGLR 279
Cdd:cd07095 166 TGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFltaGQRCTCARR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 280 LLIQESVW-DEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSER-PFYPPTLV 356
Cdd:cd07095 246 LIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLiIAAAAARYLLAQQDLLALGGEPLLAMERLVAGtAFLSPGII 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006441 357 sNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWS------ERLGQALELG 413
Cdd:cd07095 326 -DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSddealfERFLARIRAG 387
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
521-696 |
6.75e-14 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 74.92 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 521 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKSTL---ASRLERQGAE---------- 587
Cdd:cd07082 24 IDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPL-------------EERIDCLhkfADLLKENKEEvanllmweig 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 588 --LKAAEAEVELSARRLRawgarvqaqgHTLQVAG-LRGPVLRL--------------REPLGVLAVVCPDEWPLLAFVS 650
Cdd:cd07082 91 ktLKDALKEVDRTIDYIR----------DTIEELKrLDGDSLPGdwfpgtkgkiaqvrREPLGVVLAIGPFNYPLNLTVS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768006441 651 LLAPALAYGNTVVMVPSAACPLLA---LEVCQDMAtvFPAGLANVVTGD 696
Cdd:cd07082 161 KLIPALIMGNTVVFKPATQGVLLGiplAEAFHDAG--FPKGVVNVVTGR 207
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
529-736 |
1.37e-13 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 73.92 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 529 VAEGGAKDIRGAVEAAHQAF-PGwagqSPgaraallWALAAALERRK--STLASRLERQGAELKAAEA------------ 593
Cdd:cd07141 38 VQEGDKADVDKAVKAARAAFkLG----SP-------WRTMDASERGRllNKLADLIERDRAYLASLETldngkpfsksyl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 594 -EVELSARRLR---AWGARVQaqGHTLQVaglRGPVLRL--REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPS 667
Cdd:cd07141 107 vDLPGAIKVLRyyaGWADKIH--GKTIPM---DGDFFTYtrHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006441 668 AACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVEWASAGNLKPV 736
Cdd:cd07141 182 EQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEvGKLIQQAAGKSNLKRV 252
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
522-720 |
1.75e-13 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 73.40 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 522 SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQGAE-LKAAEAEVELSAR 600
Cdd:cd07149 8 DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKpIKDARKEVDRAIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 601 --RLRAWGARvQAQGHTLQVAGLRGPVLR----LREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLA 674
Cdd:cd07149 88 tlRLSAEEAK-RLAGETIPFDASPGGEGRigftIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768006441 675 LEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVqAMWYF-GSAQ 720
Cdd:cd07149 167 LKLAELLLEAgLPKGALNVVTGSGETVGDALVTDPRV-RMISFtGSPA 213
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
527-736 |
2.58e-13 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 73.05 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 527 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGAraallwalaaalERRK--STLASRLERQGAELKA---AEA-------- 593
Cdd:cd07089 11 GTAPDAGAADVDAAIAAARRAFDTGDWSTDAE------------ERARclRQLHEALEARKEELRAllvAEVgapvmtar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 594 --EVELSARRLRAWG------ARVQAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMV 665
Cdd:cd07089 79 amQVDGPIGHLRYFAdladsfPWEFDLPVPALRGGPGRRVVR-REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006441 666 PSAACPLLALEVCQDMA-TVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEwASAGNLKPV 736
Cdd:cd07089 158 PAPDTPLSALLLGEIIAeTDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGStAVGRRIMA-QAAATLKRV 229
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
518-736 |
2.75e-13 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 72.72 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 518 IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAsRLERQ--GAELKAAEAEV 595
Cdd:cd07090 2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIA-RLETIdnGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 596 ELSARRLRAWGARVQA-QGHTLQVAGLRGPVLRlREPLGVlaVVCPDEW--PLLAFVSLLAPALAYGNTVVMVPSAACPL 672
Cdd:cd07090 81 DSSADCLEYYAGLAPTlSGEHVPLPGGSFAYTR-REPLGV--CAGIGAWnyPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768006441 673 LALEvcqdMATVF-----PAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07090 158 TALL----LAEILteaglPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHV 221
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
522-719 |
1.19e-12 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 70.92 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 522 SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSAR 600
Cdd:cd07094 8 DGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEgGKPIKDARVEVDRAID 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 601 RLRAWGARVQA-QGHTLQVAGLRGPVLRL----REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAL 675
Cdd:cd07094 88 TLRLAAEEAERiRGEEIPLDATQGSDNRLawtiREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 768006441 676 EVCQdmaTVFPAGLA----NVVTGDRDHLTRCLALHQDVQAMWYFGSA 719
Cdd:cd07094 168 ELAK---ILVEAGVPegvlQVVTGEREVLGDAFAADERVAMLSFTGSA 212
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
536-736 |
5.57e-12 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 68.37 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 536 DIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRK--STLASRLERQGAELKAAEAE------------VELSARR 601
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPS-------------ERRDilLKAADLLESRRDEFIEAMMEetgataawagfnVDLAAGM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 602 LRAWGARV-QAQGHTLQVAGLRGPVLRLREPLGVLAVVCPdeW--PL-LAFVSLLAPaLAYGNTVVMVPSAACPLLALEV 677
Cdd:cd07105 68 LREAASLItQIIGGSIPSDKPGTLAMVVKEPVGVVLGIAP--WnaPViLGTRAIAYP-LAAGNTVVLKASELSPRTHWLI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006441 678 CQDM-ATVFPAGLANVVTGDRDH---LTRCLALHQDVQAMWYFGSAQ-GSQFVEWAsAGNLKPV 736
Cdd:cd07105 145 GRVFhEAGLPKGVLNVVTHSPEDapeVVEALIAHPAVRKVNFTGSTRvGRIIAETA-AKHLKPV 207
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
12-305 |
2.71e-11 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 66.52 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 12 GHYVNGKWL--KPEHRNSVpcqDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRL 89
Cdd:PRK09457 2 TLWINGDWIagQGEAFESR---NPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 90 LWTLESLVTGRAVREVRD------GDVQLAQQllHYHAIQASTQEEALAG-----WEPMGVIGLILPPTFSFLEMMWRIC 158
Cdd:PRK09457 79 LAEVIARETGKPLWEAATevtamiNKIAISIQ--AYHERTGEKRSEMADGaavlrHRPHGVVAVFGPYNFPGHLPNGHIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 159 PALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEEGRALRRSLAG 235
Cdd:PRK09457 157 PALLAGNTVV--FKPSELTPWvaeLTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006441 236 ECAE-LGLALGTESLLLLTDTADVDSAVEGVVDAAW---SDRGPGGLRLLIQESVW-DEAMRRLQERMGRLRSGR 305
Cdd:PRK09457 235 QPEKiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFisaGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGR 309
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
529-696 |
5.10e-11 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 65.87 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 529 VAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAS--RLErQGAELKAAEAEVELSARRLRaWG 606
Cdd:PLN02278 56 VPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQlmTLE-QGKPLKEAIGEVAYGASFLE-YF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 607 AR--VQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPL--LALEVCQDMA 682
Cdd:PLN02278 134 AEeaKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLtaLAAAELALQA 213
|
170
....*....|....
gi 768006441 683 TVfPAGLANVVTGD 696
Cdd:PLN02278 214 GI-PPGVLNVVMGD 226
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
537-736 |
7.35e-11 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 64.96 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 537 IRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLR---AWGARVQAQ 612
Cdd:cd07102 20 VRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQmGRPIAQAGGEIRGMLERARymiSIAEEALAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 613 GHTLQVAGLRGPVLRlrEPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQ--DMATVfPAGLA 690
Cdd:cd07102 100 IRVPEKDGFERYIRR--EPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAafAEAGL-PEGVF 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 768006441 691 NVVTGDRDHLTRCLALHqDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07102 177 QVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAIQRAAAGRFIKV 221
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
523-698 |
1.90e-10 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 63.78 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 523 GNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVELSARR 601
Cdd:cd07099 6 GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAeTGKPRADAGLEVLLALEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 602 LRAW---GARVQAQGHTLQVAGLRGPVLRL-REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV 677
Cdd:cd07099 86 IDWAarnAPRVLAPRKVPTGLLMPNKKATVeYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELL 165
|
170 180
....*....|....*....|..
gi 768006441 678 CQDMATV-FPAGLANVVTGDRD 698
Cdd:cd07099 166 AEAWAAAgPPQGVLQVVTGDGA 187
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
523-736 |
2.12e-10 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 63.47 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 523 GNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARR 601
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVREsGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 602 LR-AWGARVQAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPllaleVCQD 680
Cdd:cd07152 81 LHeAAGLPTQPQGEILPSAPGRLSLAR-RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTP-----VSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006441 681 M--ATVF-----PAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07152 155 VviARLFeeaglPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKV 216
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
64-356 |
1.15e-09 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 62.30 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 64 WSAHPGVVRAQHLTRLAEVIQKH-QRLLWTL--ESLVT-GRAVREVRDgdvqlAQQLLHYHAIQAStQEEALAGWEPMGV 139
Cdd:PRK11809 698 WFATPPAERAAILERAADLMEAQmQTLMGLLvrEAGKTfSNAIAEVRE-----AVDFLRYYAGQVR-DDFDNDTHRPLGP 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 140 IGLILPPTFSFLEMMWRICPALAVGCTVVAlvPPASPAPLLLAQ---LAGELGPFPGILNVLSGPASLV-PILASQPGIR 215
Cdd:PRK11809 772 VVCISPWNFPLAIFTGQVAAALAAGNSVLA--KPAEQTPLIAAQavrILLEAGVPAGVVQLLPGRGETVgAALVADARVR 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 216 KVAFCGAPEEGRALRRSLAGE----------CAELGlalGTESLLlltdtadVDSA------VEGVVDAAWSDRGP--GG 277
Cdd:PRK11809 850 GVMFTGSTEVARLLQRNLAGRldpqgrpiplIAETG---GQNAMI-------VDSSalteqvVADVLASAFDSAGQrcSA 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 278 LRLL-IQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQSQGAQVFQAGDVPSERP----FY 351
Cdd:PRK11809 920 LRVLcLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGpVIDAEAKANIERHIQAMRAKGRPVFQAARENSEDWqsgtFV 999
|
....*
gi 768006441 352 PPTLV 356
Cdd:PRK11809 1000 PPTLI 1004
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
536-720 |
1.87e-09 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 60.75 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 536 DIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ--------GAELKAAEAEVELS--ARRLRAW 605
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISREtgkplweaQTEVAAMAGKIDISikAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 606 GARVQAQGHTLqvaglrgpVLRLRePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV- 684
Cdd:cd07095 81 ERATPMAQGRA--------VLRHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAg 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 768006441 685 FPAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQ 720
Cdd:cd07095 152 LPPGVLNLVQGGRE-TGEALAAHEGIDGLLFTGSAA 186
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
535-696 |
2.03e-09 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 60.40 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 535 KDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ--GAELKAAeAEVELSARRLRawgarvQAQ 612
Cdd:cd07151 32 EDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIREsgSTRIKAN-IEWGAAMAITR------EAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 613 GHTLQVAGLRGPVL------RL-REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACP----LLalevcqdM 681
Cdd:cd07151 105 TFPLRMEGRILPSDvpgkenRVyREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPitggLL-------L 177
|
170 180
....*....|....*....|
gi 768006441 682 ATVF-----PAGLANVVTGD 696
Cdd:cd07151 178 AKIFeeaglPKGVLNVVVGA 197
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
135-447 |
2.57e-09 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 60.32 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 135 EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL---LLAQLAGELGPfPGILNVLSGPASLVPILASQ 211
Cdd:cd07134 99 EPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAI--LKPSELTPHtsaVIAKIIREAFD-EDEVAVFEGDAEVAQALLEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 212 PgIRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAWSDRG-----PGglRLLIQESV 286
Cdd:cd07134 176 P-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGqtciaPD--YVFVHESV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 287 WDEAMRRLQERMGRLRSGRGLDGAVDMGAR--GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFYPPTLVSNLPPASP 364
Cdd:cd07134 253 KDAFVEHLKAEIEKFYGKDAARKASPDLARivNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQRYIAPTVLTNVTPDMK 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 365 CAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN---AHGLrDPSVPTGGCKES 441
Cdd:cd07134 333 IMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNdvvLHFL-NPNLPFGGVNNS 411
|
....*..
gi 768006441 442 GC-SWHG 447
Cdd:cd07134 412 GIgSYHG 418
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
502-698 |
2.64e-09 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 60.29 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 502 FVGGRFQAPGARssRPIRDSSGN--LHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaalERRKSTL-- 577
Cdd:cd07125 36 IINGEETETGEG--APVIDPADHerTIGEVSLADAEDVDAALAIAAAAFAGWSATPV--------------EERAEILek 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 578 -ASRLERQGAELKA----------AEAEVELS---------ARRLRAWGARVQAQGHTLQVAGLRgpvlrlREPLGVLAV 637
Cdd:cd07125 100 aADLLEANRGELIAlaaaeagktlADADAEVReaidfcryyAAQARELFSDPELPGPTGELNGLE------LHGRGVFVC 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768006441 638 VCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDM--ATVfPAGLANVVTGDRD 698
Cdd:cd07125 174 ISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLheAGV-PRDVLQLVPGDGE 235
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
502-726 |
5.47e-09 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 59.15 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 502 FVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASR 580
Cdd:PRK11241 14 LINGEWlDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 581 LE-RQGAELKAAEAEVELSARRLRaWGARVQAQ--GHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALA 657
Cdd:PRK11241 94 MTlEQGKPLAEAKGEISYAASFIE-WFAEEGKRiyGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768006441 658 YGNTVVMVPSAACPL--LALEVCQDMATVfPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVE 726
Cdd:PRK11241 173 AGCTMVLKPASQTPFsaLALAELAIRAGI-PAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEiGRQLME 243
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
527-735 |
1.01e-08 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 58.38 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 527 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAW 605
Cdd:TIGR01238 66 GQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREaGKTIHNAIAEVREAVDFCRYY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 606 GARVQaqgHTLQVAGLRgpvlrlrePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV- 684
Cdd:TIGR01238 146 AKQVR---DVLGEFSVE--------SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAg 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 768006441 685 FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKP 735
Cdd:TIGR01238 215 FPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDA 265
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
534-720 |
1.51e-08 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 58.05 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 534 AKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ--------GAELKAAEAEVELSarrLRAW 605
Cdd:PRK09457 36 AAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIAREtgkplweaATEVTAMINKIAIS---IQAY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 606 GARVqaqGHTLQVAGLRGPVLRLRePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV--CQDMAT 683
Cdd:PRK09457 113 HERT---GEKRSEMADGAAVLRHR-PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTvkLWQQAG 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 768006441 684 VfPAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQ 720
Cdd:PRK09457 189 L-PAGVLNLVQGGRE-TGKALAAHPDIDGLLFTGSAN 223
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
483-741 |
1.77e-08 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 57.83 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 483 STLPAGPEIGPSPAPPYGL--FVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGAR 559
Cdd:PLN02419 96 SWLSTSPEQSTQPQMPPRVpnLIGGSFvESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 560 AALLWALAAALERRKSTLASRLE-RQGAELKAAEAEVELSARRLR-AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAV 637
Cdd:PLN02419 176 QRVMLKFQELIRKNMDKLAMNITtEQGKTLKDSHGDIFRGLEVVEhACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 638 VCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQ-DMATVFPAGLANVVTGDRDHLTrCLALHQDVQAMWYF 716
Cdd:PLN02419 256 ICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAElAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFV 334
|
250 260
....*....|....*....|....*
gi 768006441 717 GSAQGSQFVEWASAGNLKPVWASRG 741
Cdd:PLN02419 335 GSNTAGMHIYARAAAKGKRIQSNMG 359
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
582-730 |
2.29e-08 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 57.05 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 582 ERQGAELKAAEAEVELSARRLR---AWGARVQaqGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAY 658
Cdd:PRK10090 21 EEGGKIQQLAEVEVAFTADYIDymaEWARRYE--GEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIARKMAPALLT 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768006441 659 GNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEWASA 730
Cdd:PRK10090 99 GNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSvSAGEKIMAAAAK 172
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
571-719 |
4.71e-08 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 56.21 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 571 ERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAWGA---RVQAQGHTLQVAGLRGP--VLRLREPLGVLAVVCPDEWP 644
Cdd:cd07146 54 EARREEFARLITLEsGLCLKDTRYEVGRAADVLRFAAAealRDDGESFSCDLTANGKArkIFTLREPLGVVLAITPFNHP 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768006441 645 LLAFVSLLAPALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSA 719
Cdd:cd07146 134 LNQVAHKIAPAIAANNRIVLKPSEKTPLSAIylaDLLYEAG--LPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGV 209
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
527-696 |
5.57e-08 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 56.10 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 527 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEV-------ELS 598
Cdd:PRK03137 65 GRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEaGKPWAEADADTaeaidflEYY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 599 ARRLRAWgarvqAQGHTlqVAGLRGPVLRLR-EPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV 677
Cdd:PRK03137 145 ARQMLKL-----ADGKP--VESRPGEHNRYFyIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKF 217
|
170 180
....*....|....*....|
gi 768006441 678 CQDMATV-FPAGLANVVTGD 696
Cdd:PRK03137 218 VEVLEEAgLPAGVVNFVPGS 237
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
537-736 |
1.07e-07 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 55.16 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 537 IRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--STLASRLERQGAEL------------KAAEAEVELSARRL 602
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSF-------------AERAAllRKLADLLRERKDELarlitlemgkpiAEARAEVEKCAWIC 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 603 R--AWGARVQAQGHTLQVAGLRGPVlrLREPLGVLAVVCPdeW--PLLAFVSLLAPALAYGNTVVMVPSAACPLLAL--- 675
Cdd:cd07100 68 RyyAENAEAFLADEPIETDAGKAYV--RYEPLGVVLGIMP--WnfPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALaie 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768006441 676 EVCQDMAtvFPAGLANVVTGDRDHLTRCLAlHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07100 144 ELFREAG--FPEGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGKNLKKS 201
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
527-676 |
1.62e-07 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 55.26 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 527 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaalERRKSTL---ASRLERQGAELKA------------A 591
Cdd:PRK11905 582 GTVTEASAEDVERALAAAQAAFPEWSATPA--------------AERAAILeraADLMEAHMPELFAlavreagktlanA 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 592 EAEVELSARRLRAWGARVQaqgHTLQVAGlrgpvlrlREPLGVlaVVCPDEW--PLLAFVSLLAPALAYGNTVVMVPSAA 669
Cdd:PRK11905 648 IAEVREAVDFLRYYAAQAR---RLLNGPG--------HKPLGP--VVCISPWnfPLAIFTGQIAAALVAGNTVLAKPAEQ 714
|
....*..
gi 768006441 670 CPLLALE 676
Cdd:PRK11905 715 TPLIAAR 721
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
60-314 |
1.85e-07 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 54.82 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 60 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGR----AVREVRDgdvqlAQQLLHYHAIQAS---TQEEALA 132
Cdd:PRK11904 597 AFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKtlqdAIAEVRE-----AVDFCRYYAAQARrlfGAPEKLP 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 133 G---------WEPMGVIGLILPPTFS---FLEmmwRICPALAVGCTVVAlvPPASPAPL---LLAQLAGELGPFPGILNV 197
Cdd:PRK11904 672 GptgesnelrLHGRGVFVCISPWNFPlaiFLG---QVAAALAAGNTVIA--KPAEQTPLiaaEAVKLLHEAGIPKDVLQL 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 198 LSGP-ASLVPILASQPGIRKVAFCGAPEEGRALRRSLAGE-------CAELGlalGTESLLlltdtadVDSA--VEGVV- 266
Cdd:PRK11904 747 LPGDgATVGAALTADPRIAGVAFTGSTETARIINRTLAARdgpivplIAETG---GQNAMI-------VDSTalPEQVVd 816
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 768006441 267 DAAWSDRGPGG-----LRLL-IQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 314
Cdd:PRK11904 817 DVVTSAFRSAGqrcsaLRVLfVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVG 870
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
579-736 |
2.27e-07 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 54.07 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 579 SRLERQGAELKAAEAEVELSARRLRAWGARVQAQgHTLQVAGLRGPVLRlrEPLGVLAVVCPDEWPLLAFVSLLAPALAY 658
Cdd:cd07087 51 PPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRVS-VPLLLQPAKAYVIP--EPLGVVLIIGPWNYPLQLALAPLIGAIAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 659 GNTVVMVPSAACP----LLALEVcqdmATVFPAGLANVVTGDRDHLTRCLALHQDVqaMWYFGSAQGSQFVEWASAGNLK 734
Cdd:cd07087 128 GNTVVLKPSELAPatsaLLAKLI----PKYFDPEAVAVVEGGVEVATALLAEPFDH--IFFTGSPAVGKIVMEAAAKHLT 201
|
..
gi 768006441 735 PV 736
Cdd:cd07087 202 PV 203
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
497-736 |
3.96e-07 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 53.35 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 497 PPYGLFVGGRFQAPGARSSRP-IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLER--- 572
Cdd:PRK13252 5 PLQSLYIDGAYVEATSGETFEvINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTA-------------MERsri 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 573 -RKStlASRLERQGAELKAAE-------------AEVELSARRLRAWGARVQA-QGHTLQvagLRGP--VLRLREPLGVL 635
Cdd:PRK13252 72 lRRA--VDILRERNDELAALEtldtgkpiqetsvVDIVTGADVLEYYAGLAPAlEGEQIP---LRGGsfVYTRREPLGVC 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 636 AVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVcqdmATVF-----PAGLANVVTGDRDhLTRCLALHQDV 710
Cdd:PRK13252 147 AGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKL----AEIYteaglPDGVFNVVQGDGR-VGAWLTEHPDI 221
|
250 260
....*....|....*....|....*.
gi 768006441 711 QAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:PRK13252 222 AKVSFTGGVPTGKKVMAAAAASLKEV 247
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
522-698 |
5.92e-07 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 52.63 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 522 SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEV----- 595
Cdd:cd07147 8 TGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEaGKPIKDARGEVaraid 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 596 --ELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLrePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLL 673
Cdd:cd07147 88 tfRIAAEEATRIYGEVLPLDISARGEGRQGLVRRF--PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLS 165
|
170 180
....*....|....*....|....*.
gi 768006441 674 ALEVCQDMA-TVFPAGLANVVTGDRD 698
Cdd:cd07147 166 ALILGEVLAeTGLPKGAFSVLPCSRD 191
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
571-706 |
7.17e-07 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 52.23 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 571 ERRKSTLASRLER----------QGAELKAA--------EAEVELS------------ARRLRAWgARVQAQGHTLQVAG 620
Cdd:cd07134 13 ALRASTAAERIAKlkrlkkailaRREEIIAAlaadfrkpAAEVDLTeilpvlseinhaIKHLKKW-MKPKRVRTPLLLFG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 621 LRGPVLRlrEPLGVLAVVCPDEWPL-LAFvSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDH 699
Cdd:cd07134 92 TKSKIRY--EPKGVCLIISPWNYPFnLAF-GPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAEV 168
|
....*..
gi 768006441 700 LTRCLAL 706
Cdd:cd07134 169 AQALLEL 175
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
579-736 |
1.23e-06 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 51.95 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 579 SRLERQGAELKAAEAEVELSARRLRAWGARVQAQGHTLQvagLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAY 658
Cdd:PTZ00381 60 HPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKVDTVGVF---GPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 659 GNTVVMVPSAacplLALEVCQDMATVFPAGLAN----VVTGDRDHLTRCLALHQDVqaMWYFGSAQGSQFVEWASAGNLK 734
Cdd:PTZ00381 137 GNTVVLKPSE----LSPHTSKLMAKLLTKYLDPsyvrVIEGGVEVTTELLKEPFDH--IFFTGSPRVGKLVMQAAAENLT 210
|
..
gi 768006441 735 PV 736
Cdd:PTZ00381 211 PC 212
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
502-720 |
1.35e-06 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 51.41 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 502 FVGGRFQAPGAR---SSRPIRDSSgnlHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLA 578
Cdd:cd07086 2 VIGGEWVGSGGEtftSRNPANGEP---IARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 579 SRLERQ-GAELKAAEAEVE-----------LSaRRLrawgarvqaQGHTlqVAGLRgPVLRLRE---PLGVLAVVCPDEW 643
Cdd:cd07086 79 RLVSLEmGKILPEGLGEVQemidicdyavgLS-RML---------YGLT--IPSER-PGHRLMEqwnPLGVVGVITAFNF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 644 PLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-----FPAGLANVVTGDRDhLTRCLALHQDVQAMWYFGS 718
Cdd:cd07086 146 PVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVlekngLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGS 224
|
..
gi 768006441 719 AQ 720
Cdd:cd07086 225 TE 226
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
53-357 |
3.93e-06 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 50.63 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 53 AVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGR----AVREVRDgdvqlAQQLLHYHAIQAsTQE 128
Cdd:PRK11905 595 ALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKtlanAIAEVRE-----AVDFLRYYAAQA-RRL 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 129 EALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVAlvPPASPAPlLLAQLAGEL----GPFPGILNVLSGPASL 204
Cdd:PRK11905 669 LNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLA--KPAEQTP-LIAARAVRLlheaGVPKDALQLLPGDGRT 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 205 V-PILASQPGIRKVAFCGAPEEGRALRRSLAGEC-------AELGlalGTESLLlltdtadVDS------AVEGVVDAAW 270
Cdd:PRK11905 746 VgAALVADPRIAGVMFTGSTEVARLIQRTLAKRSgppvpliAETG---GQNAMI-------VDSsalpeqVVADVIASAF 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 271 SDRGP--GGLRLL-IQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQSQGAQVFQAgDVPS 346
Cdd:PRK11905 816 DSAGQrcSALRVLcLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGpVIDAEAQANIEAHIEAMRAAGRLVHQL-PLPA 894
|
330
....*....|....
gi 768006441 347 ERP---FYPPTLVS 357
Cdd:PRK11905 895 ETEkgtFVAPTLIE 908
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
631-721 |
4.75e-06 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 49.75 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 631 PLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVP---SAACPLLALEvCQDMATvFPAGLANVVTGDRDHLTRCLALH 707
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPptqGAVAALHMVH-CFHLAG-FPKGLISCVTGKGSEIGDFLTMH 235
|
90
....*....|....
gi 768006441 708 QDVQAMWYFGSAQG 721
Cdd:PLN00412 236 PGVNCISFTGGDTG 249
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
53-356 |
9.21e-06 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 49.55 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 53 AVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGR----AVREVRDgdvqlAQQLLHYHAIQASTQE 128
Cdd:COG4230 598 ALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKtlpdAIAEVRE-----AVDFCRYYAAQARRLF 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 129 EALAGWEPMGVIGLILPptfsflemmW---------RICPALAVGCTVVAlvPPASPAPlLLAQLAGEL----GPFPGIL 195
Cdd:COG4230 673 AAPTVLRGRGVFVCISP---------WnfplaiftgQVAAALAAGNTVLA--KPAEQTP-LIAARAVRLlheaGVPADVL 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 196 NVLSGPASLV-PILASQPGIRKVAFCGAPEEGRALRRSLAGEcaelglalGTESLLLLTDTAD-----VDS------AVE 263
Cdd:COG4230 741 QLLPGDGETVgAALVADPRIAGVAFTGSTETARLINRTLAAR--------DGPIVPLIAETGGqnamiVDSsalpeqVVD 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 264 GVVDAAWSDRGP--GGLRLL-IQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVF 339
Cdd:COG4230 813 DVLASAFDSAGQrcSALRVLcVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPViDAEARANLEAHIERMRAEGRLVH 892
|
330 340
....*....|....*....|
gi 768006441 340 QAgDVPSERP---FYPPTLV 356
Cdd:COG4230 893 QL-PLPEECAngtFVAPTLI 911
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
512-679 |
1.45e-05 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 48.66 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 512 ARSSRPIRDSSGNLH------------GYVAEGGAKDIRGAVEAAHQAFPGWAgQSPGaraallwalaaalERRKSTL-- 577
Cdd:PRK11904 550 QWQAGPIINGEGEARpvvspadrrrvvGEVAFADAEQVEQALAAARAAFPAWS-RTPV-------------EERAAILer 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 578 -ASRLERQGAELKA------------AEAEVELSARRLRAWGArvQAQGHTLQVAGLRGPV-----LRLrEPLGVLAVVC 639
Cdd:PRK11904 616 aADLLEANRAELIAlcvreagktlqdAIAEVREAVDFCRYYAA--QARRLFGAPEKLPGPTgesneLRL-HGRGVFVCIS 692
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 768006441 640 PDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQ 679
Cdd:PRK11904 693 PWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVK 732
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
627-723 |
2.14e-05 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 47.62 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 627 RLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDM--ATVFPAGLANVVTGDRdHLTRCL 704
Cdd:cd07084 96 GYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLhyAGLLPPEDVTLINGDG-KTMQAL 174
|
90
....*....|....*....
gi 768006441 705 ALHQDVQAMWYFGSAQGSQ 723
Cdd:cd07084 175 LLHPNPKMVLFTGSSRVAE 193
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
509-696 |
5.67e-05 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 46.41 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 509 APGARSSRPIRDS-SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKSTLASR---LERQ 584
Cdd:PRK09407 27 DGAAGPTREVTAPfTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVR-------------ERAAVLLRFHdlvLENR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 585 GAELKAAEAEvelsarrlrAWGARVQAQGHTLQVAGL-----------------RG--PVL----RLREPLGVLAVVCPD 641
Cdd:PRK09407 94 EELLDLVQLE---------TGKARRHAFEEVLDVALTaryyarrapkllaprrrAGalPVLtkttELRQPKGVVGVISPW 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 768006441 642 EWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALeVCQDMATV--FPAGLANVVTGD 696
Cdd:PRK09407 165 NYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTAL-AAVELLYEagLPRDLWQVVTGP 220
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
135-447 |
7.65e-05 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 45.86 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 135 EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVV---ALVPPASPAplLLAQLAGELGPfPGILNVLSGPASLVPILASQ 211
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVlkpSELAPATSA--LLAKLIPEYLD-TKAIKVIEGGVPETTALLEQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 212 PGiRKVAFCGAPEEGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGVVDAAW-SDRGPGGLR---LLIQESVW 287
Cdd:cd07137 177 KW-DKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIApdyVLVEESFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 288 DEAMRRLQErmgRLRSGRGLDGAVDMGARGAAACDLVQRFVR--EAQSQGAQVFQAGDVPSERPFYPPTLVSNLPPASPC 365
Cdd:cd07137 256 PTLIDALKN---TLEKFFGENPKESKDLSRIVNSHHFQRLSRllDDPSVADKIVHGGERDEKNLYIEPTILLDPPLDSSI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 366 AQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSErlGQALELGYGLQV--GTVWINAHGLR--DPSVPTGGCKES 441
Cdd:cd07137 333 MTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTK--NKELKRRIVAETssGGVTFNDTVVQyaIDTLPFGGVGES 410
|
....*..
gi 768006441 442 GC-SWHG 447
Cdd:cd07137 411 GFgAYHG 417
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
629-736 |
1.76e-04 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 44.80 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 629 REPLGVLAVVCPDEWPL-LAFVSLLApALAYGNTVVMVPSAACPLLAlEVCQDM-ATVFPAGLANVVTGDRD---HLtrc 703
Cdd:cd07136 98 YEPYGVVLIIAPWNYPFqLALAPLIG-AIAAGNTAVLKPSELTPNTS-KVIAKIiEETFDEEYVAVVEGGVEenqEL--- 172
|
90 100 110
....*....|....*....|....*....|...
gi 768006441 704 laLHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07136 173 --LDQKFDYIFFTGSVRVGKIVMEAAAKHLTPV 203
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
579-698 |
2.17e-04 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 44.40 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 579 SRLERQGAELKAAEAEVELSARRLRAWgARVQAQGHTLQVAGLRGPVLRlrEPLGVLAVVCPDEWPL-LAFVSLLApALA 657
Cdd:cd07133 52 SRHETLLAEILPSIAGIKHARKHLKKW-MKPSRRHVGLLFLPAKAEVEY--QPLGVVGIIVPWNYPLyLALGPLIA-ALA 127
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 768006441 658 YGNTVVMVPSAACPLLAlEVCQDM-ATVFPAGLANVVTGDRD 698
Cdd:cd07133 128 AGNRVMIKPSEFTPRTS-ALLAELlAEYFDEDEVAVVTGGAD 168
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
527-735 |
3.45e-04 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 44.11 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 527 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAW 605
Cdd:cd07083 47 GTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEvGKNWVEAIDDVAEAIDFIRYY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 606 GarVQAQGHTLQVAGLRGPVLRLRE----PLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDM 681
Cdd:cd07083 127 A--RAALRLRYPAVEVVPYPGEDNEsfyvGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIF 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768006441 682 ATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVeWASAGNLKP 735
Cdd:cd07083 205 HEAgFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKI-YEAAARLAP 258
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
527-674 |
3.53e-04 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 44.16 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 527 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaalERRKSTL---ASRLERQGAELKA------------A 591
Cdd:COG4230 585 GTVVEATAADVEAALAAAQAAFPAWSATPV--------------EERAAILeraADLLEAHRAELMAllvreagktlpdA 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 592 EAEVelsarR-----LRAWGARVQAQGHTLQVaglrgpvlrlREPLGVlaVVCPDEW--PLLAFVSLLAPALAYGNTVVM 664
Cdd:COG4230 651 IAEV-----ReavdfCRYYAAQARRLFAAPTV----------LRGRGV--FVCISPWnfPLAIFTGQVAAALAAGNTVLA 713
|
170
....*....|
gi 768006441 665 VPSAACPLLA 674
Cdd:COG4230 714 KPAEQTPLIA 723
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
629-736 |
3.73e-04 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 43.75 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 629 REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQ 708
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQVVQGGVPETTALLEQKF 185
|
90 100
....*....|....*....|....*...
gi 768006441 709 DvqAMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07135 186 D--KIFYTGSGRVGRIIAEAAAKHLTPV 211
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
158-404 |
4.09e-04 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 43.73 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 158 CPALaVGCTVvaLVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV--PILASqPGIRKVAFCGAPEEGRALRRS 232
Cdd:cd07123 192 APAL-MGNVV--LWKPSDTAVLsnyLVYKILEEAGLPPGVINFVPGDGPVVgdTVLAS-PHLAGLHFTGSTPTFKSLWKQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 233 -------------LAGECaelglalGTESLLLLTDTADVDSAVEGVVDAAWSDRG---PGGLRLLIQESVWDEAMRRLQE 296
Cdd:cd07123 268 igenldryrtyprIVGET-------GGKNFHLVHPSADVDSLVTATVRGAFEYQGqkcSAASRAYVPESLWPEVKERLLE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 297 RMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQ-GAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWP 373
Cdd:cd07123 341 ELKEIKMGDPDDFSNFMGAViDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFvEPTVIETTDPKHKLMTEEIFGP 420
|
250 260 270
....*....|....*....|....*....|....
gi 768006441 374 VVVASPFRTAK--EAL-LVANGTPRGGSASVWSE 404
Cdd:cd07123 421 VLTVYVYPDSDfeETLeLVDTTSPYALTGAIFAQ 454
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
58-234 |
4.62e-04 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 43.38 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 58 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQLAQqLLHYHAIQASTQEEALAGWE-- 135
Cdd:cd07084 9 DISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQ-LRARAFVIYSYRIPHEPGNHlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 136 ------------PMGVIGLILPPTFSFLEMMWRICPALAVGCTVvaLVPPASPAPLLLAQ---LAGELGPFP-GILNVLS 199
Cdd:cd07084 88 qglkqqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPV--IVKPHTAVSIVMQImvrLLHYAGLLPpEDVTLIN 165
|
170 180 190
....*....|....*....|....*....|....*
gi 768006441 200 GPASLVPILASQPGIRKVAFCGAPEEGRALRRSLA 234
Cdd:cd07084 166 GDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAK 200
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
527-674 |
7.49e-04 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 43.04 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 527 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAW 605
Cdd:PRK11809 674 GYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREaGKTFSNAIAEVREAVDFLRYY 753
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768006441 606 GARVQAQ----GHtlqvaglrgpvlrlrEPLGVlaVVCPDEW--PLLAFVSLLAPALAYGNTVVMVPSAACPLLA 674
Cdd:PRK11809 754 AGQVRDDfdndTH---------------RPLGP--VVCISPWnfPLAIFTGQVAAALAAGNSVLAKPAEQTPLIA 811
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
630-743 |
8.56e-04 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 42.40 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 630 EPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAlevcQDMATVFPAGLAN----VVTGDRDHLTrcLA 705
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATS----ALLAKLIPEYLDTkaikVIEGGVPETT--AL 173
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 768006441 706 LHQDVQAMWYFGSAQGSQFVEWASAGNLKPVWASRG--CP 743
Cdd:cd07137 174 LEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGgkCP 213
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
628-696 |
8.74e-04 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 42.68 E-value: 8.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 628 LREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDM-ATVFPAGLANVVTGD 696
Cdd:cd07101 115 NRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLiEAGLPRDLWQVVTGP 184
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
629-736 |
9.16e-04 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 42.59 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 629 REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAlevcQDMATVFPAGLAN----VVTGDRDHLTRCL 704
Cdd:cd07132 98 KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATA----KLLAELIPKYLDKecypVVLGGVEETTELL 173
|
90 100 110
....*....|....*....|....*....|..
gi 768006441 705 ALHQDVqaMWYFGSAQGSQFVEWASAGNLKPV 736
Cdd:cd07132 174 KQRFDY--IFYTGSTSVGKIVMQAAAKHLTPV 203
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
595-689 |
3.80e-03 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 40.48 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 595 VELSARRLRAWGARVQAQGHTLQVAGLRGpvLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLA 674
Cdd:cd07148 90 VELAADELGQLGGREIPMGLTPASAGRIA--FTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSC 167
|
90
....*....|....*
gi 768006441 675 LEVcqdMATVFPAGL 689
Cdd:cd07148 168 LAF---VDLLHEAGL 179
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
537-721 |
3.87e-03 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 40.60 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 537 IRGAVEAAHQAFPGWAGQSPgaraallwalaaalERRKS---TLASRLERQGAELKA-AEAEVELSARRL-----RAWG- 606
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSP--------------ARRAAfleAIADEIEALGDELVArAHAETGLPEARLqgelgRTTGq 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 607 ----ARVQAQGHTLQV---------AGLRGPVLRLRE-PLGVLAVVCPDEWPlLAFvSLL----APALAYGNTVVMVPSA 668
Cdd:cd07129 67 lrlfADLVREGSWLDAridpadpdrQPLPRPDLRRMLvPLGPVAVFGASNFP-LAF-SVAggdtASALAAGCPVVVKAHP 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 768006441 669 ACP----LLALEVCQDM-ATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQG 721
Cdd:cd07129 145 AHPgtseLVARAIRAALrATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRG 202
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
159-403 |
7.28e-03 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 39.69 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 159 PALAVGCTVValVPPASPAPLL---LAQLAGELGPFP-GILNVLSGPASlvPILASQPGIRKVAFCGAPEEGRALRRSLA 234
Cdd:PRK11903 171 PALLAGVPVI--VKPATATAWLtqrMVKDVVAAGILPaGALSVVCGSSA--GLLDHLQPFDVVSFTGSAETAAVLRSHPA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 235 GECAELGLALGTESL---LLLTD----TADVDSAVEGVVDAAWSDRGPGGL---RLLIQESVWDEAMRRLQERMGRLRSG 304
Cdd:PRK11903 247 VVQRSVRVNVEADSLnsaLLGPDaapgSEAFDLFVKEVVREMTVKSGQKCTairRIFVPEALYDAVAEALAARLAKTTVG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768006441 305 RGLDGAVDMG-----ARGAAACDLVQRFVREAQS--QGAQVFQAGDVPSERPFYPPTL-VSNLPPASPCAQ-VEVPWPVV 375
Cdd:PRK11903 327 NPRNDGVRMGplvsrAQLAAVRAGLAALRAQAEVlfDGGGFALVDADPAVAACVGPTLlGASDPDAATAVHdVEVFGPVA 406
|
250 260 270
....*....|....*....|....*....|.
gi 768006441 376 VASPFRTAKEAL-LVANGtprGGS--ASVWS 403
Cdd:PRK11903 407 TLLPYRDAAHALaLARRG---QGSlvASVYS 434
|
|
| |
