|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
32-502 |
0e+00 |
|
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: 915.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 32 VANEPVLAFTQGSPERDALQKALKDLKGRMEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALA 111
Cdd:cd07123 1 PVNEPVLSYAPGSPERAKLQEALAELKSLTVEIPLVIGGKEVRTGNTGKQVMPHDHAHVLATYHYADAALVEKAIEAALE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 112 ARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPS 191
Cdd:cd07123 81 ARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATMLGQGKNVWQAEIDAACELIDFLRFNVKYAEELYAQQPLSSPAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 192 T-NSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFG 270
Cdd:cd07123 161 VwNRLEYRPLEGFVYAVSPFNFTAIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 271 DTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSA 350
Cdd:cd07123 241 DTVLASPHLAGLHFTGSTPTFKSLWKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 351 CSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAK----------------------------------- 395
Cdd:cd07123 321 ASRAYVPESLWPEVKERLLEELKEIKMGDP-DDFSNFMGAVIDEKafdrikgyidhaksdpeaeiiaggkcddsvgyfve 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 ----------------EIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKS 459
Cdd:cd07123 400 ptviettdpkhklmteEIFGPVLTVYVYPDSDFEETLELVDTTSPYALTGAIFAQDRKAIREATDALRNAAGNFYINDKP 479
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 984655788 460 TGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKP 502
Cdd:cd07123 480 TGAVVGQQPFGGARASGTNDKAGSPLNLLRWVSPRTIKETFVP 522
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
33-512 |
0e+00 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 881.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 33 ANEPVLAFTQGSPERDALQKALKDLKGRMEAIPCVVGDEEVWTSDV-QYQVSPFNHGHKVAKFCYADKSLLNKAIEAALA 111
Cdd:TIGR01236 1 ANEPVLPFRPGSPERDLLRKSLKELKSSSLEIPLVIGGEEVYDSNErIPQVNPHNHQAVLAKATNATEEDAMKAVEAALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 112 ARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPS 191
Cdd:TIGR01236 81 AKKDWSNLPFYDRAAIFLKAADLLSGPYRYEILAATMLGQSKTVYQAEIDAVAELIDFFRFNVKYARELYAQQPISAPGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 192 TNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGD 271
Cdd:TIGR01236 161 WNRTEYRPLEGFVYAISPFNFTAIAGNLAGAPALMGNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 272 TVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSAC 351
Cdd:TIGR01236 241 QVLADPDLAGIHFTGSTNTFKHLWKKVAQNLDRYHNFPRIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 352 SRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAK------------------------------------ 395
Cdd:TIGR01236 321 SRLYVPHSKWPEFKSDLLAELQSVKVGDP-DDFRGFMGAVIDEQsfdkivkyiedakkdpealtilyggkyddsqgyfve 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 ----------------EIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKS 459
Cdd:TIGR01236 400 ptvveskdpdhplmseEIFGPVLTVYVYPDDKYKEILDLVDSTSQYGLTGAVFAKDRKAILEADKKLRFAAGNFYINDKC 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 984655788 460 TGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKPLGDWSYAYMQ 512
Cdd:TIGR01236 480 TGAVVGQQPFGGARMSGTNDKAGGPNNLLRWTSPRSIKETFVPLTDWSYPYMY 532
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
47-500 |
0e+00 |
|
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: 722.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 47 RDALQKALKDLKG-RMEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRA 125
Cdd:cd07083 1 RRAMREALRRVKEeFGRAYPLVIGGEWVDTKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 126 QIFLKAADMLSGPRRAEILAKTMVGqGKTVIQaEIDAAAELIDFFRFNAKYAVELEGQQPI--SVPPSTNSTVYRGLeGF 203
Cdd:cd07083 81 RLLLKAADLLRRRRRELIATLTYEV-GKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAVEvvPYPGEDNESFYVGL-GA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 204 VAAISPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGI 282
Cdd:cd07083 158 GVVISPWNFPvAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 283 NFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWP 362
Cdd:cd07083 238 NFTGSLETGKKIYEAAARLAPGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 363 QIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDA------------------------------------------------ 394
Cdd:cd07083 318 PVLERLLKRAERLSVGPPEEN-GTDLGPVIDAeqeakvlsyiehgknegqlvlggkrlegegyfvaptvveevppkaria 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 395 -KEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQdKDVVQEATKVLrnAAGNFYINDKSTGSIVGQQPFGGAR 473
Cdd:cd07083 397 qEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRK-REHLEEARREF--HVGNLYINRKITGALVGVQPFGGFK 473
|
490 500
....*....|....*....|....*..
gi 984655788 474 ASGTNDKPGGPHYILRWTSPQVIKETH 500
Cdd:cd07083 474 LSGTNAKTGGPHYLRRFLEMKAVAERF 500
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
64-500 |
2.59e-114 |
|
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: 346.34 E-value: 2.59e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 64 IPCVVGDEEVWTSDVQYQ--VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRA 141
Cdd:COG1012 6 YPLFIGGEWVAAASGETFdvINPAT-GEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLE--ERR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 142 EILAKTMV-GQGKTVIQAEIDAAaELIDFFRFNAKYAVELEGQQ-PISVPPSTNSTVYRGLeGFVAAISPFNFTAIGGNL 219
Cdd:COG1012 83 EELAALLTlETGKPLAEARGEVD-RAADFLRYYAGEARRLYGETiPSDAPGTRAYVRREPL-GVVGAITPWNFPLALAAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 220 AGAPAL-MGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQV 298
Cdd:COG1012 161 KLAPALaAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 299 AQNLdrfhtfPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVG 378
Cdd:COG1012 241 AENL------KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 379 DPAeDFGTFFSAVIDAK---------------------------------------------------EIFGPVLSVYVY 407
Cdd:COG1012 315 DPL-DPGTDMGPLISEAqlervlayiedavaegaelltggrrpdgeggyfveptvladvtpdmriareEIFGPVLSVIPF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 408 PDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASGTNDKpGGPHYI 487
Cdd:COG1012 394 DD--EEEAIALAND-TEYGLAASVFTRDLARARRVARRLE--AGMVWINDGTTGA-VPQAPFGGVKQSGIGRE-GGREGL 466
|
490
....*....|...
gi 984655788 488 LRWTSPQVIKETH 500
Cdd:COG1012 467 EEYTETKTVTIRL 479
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
103-496 |
4.25e-114 |
|
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: 344.19 E-value: 4.25e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGqGKTVIQAEIDAAaELIDFFRFNAKYAVELEG 182
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLET-GKPIEEALGEVA-RAADTFRYYAGLARRLHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 183 QQ-PISVPPSTNSTVYRGLeGFVAAISPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQ 260
Cdd:cd07078 79 EViPSPDPGELAIVRREPL-GVVGAITPWNFPlLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 261 FVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtfPRLAGECGGKNFHFVHRSADVESVVSGTLRSA 340
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENL------KRVTLELGGKSPLIVFDDADLDAAVKGAVFGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 341 FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAK------------------------- 395
Cdd:cd07078 232 FGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPL-DPDTDMGPLISAAqldrvlayiedakaegakllcggkr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 --------------------------EIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKDVVQEATKVLRna 449
Cdd:cd07078 311 leggkgyfvpptvltdvdpdmpiaqeEIFGPVLPVIPFKDE--EEAIELANDTE-YGLAAGVFTRDLERALRVAERLE-- 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 984655788 450 AGNFYINDKSTGsIVGQQPFGGARASGTNdKPGGPHYILRWTSPQVI 496
Cdd:cd07078 386 AGTVWINDYSVG-AEPSAPFGGVKQSGIG-REGGPYGLEEYTEPKTV 430
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
34-498 |
1.19e-112 |
|
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: 343.05 E-value: 1.19e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 34 NEPVLAFTQGSpERDALQKALKDLKGRMEA-IPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAA 112
Cdd:cd07124 3 NEPFTDFADEE-NRAAFRAALARVREELGReYPLVIGGKEVRTEEKIESRNPADPSEVLGTVQKATKEEAEAAVQAARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 113 RKEWDLKPIADRAQIFLKAADMLSgPRRAEiLAKTMVGQ-GKTVIQAEIDAAaELIDFFRFNAKYAVELEGQQPISVPPS 191
Cdd:cd07124 82 FPTWRRTPPEERARLLLRAAALLR-RRRFE-LAAWMVLEvGKNWAEADADVA-EAIDFLEYYAREMLRLRGFPVEMVPGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 192 TNSTVYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFG 270
Cdd:cd07124 159 DNRYVYRPL-GVGAVISPWNFpLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 271 DTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSA 350
Cdd:cd07124 238 DYLVEHPDVRFIAFTGSREVGLRIYERAAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 351 CSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAK----------------------------------- 395
Cdd:cd07124 318 CSRVIVHESVYDEFLERLVERTKALKVGDP-EDPEVYMGPVIDKGardrirryieigksegrlllggevlelaaegyfvq 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 ----------------EIFGPVLSVYVYPDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKS 459
Cdd:cd07124 397 ptifadvppdhrlaqeEIFGPVLAVIKAKD--FDEALEIAND-TEYGLTGGVFSRSPEHLERARREFE--VGNLYANRKI 471
|
490 500 510
....*....|....*....|....*....|....*....
gi 984655788 460 TGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKE 498
Cdd:cd07124 472 TGALVGRQPFGGFKMSGTGSKAGGPDYLLQFMQPKTVTE 510
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
107-496 |
1.86e-105 |
|
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: 319.56 E-value: 1.86e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 107 EAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGqGKTvIQAEIDAAAELIDFFRFNAKYAVELEGQQPI 186
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLET-GKP-IEEALGEVARAIDTFRYAAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 187 SVPPSTNSTVYRGLEGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPAD 265
Cdd:cd06534 79 SPDPGGEAYVRREPLGVVGVITPWNFpLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 266 GPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtfPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGG 345
Cdd:cd06534 159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENL------KPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 346 QKCSACSRLYVPHSLWPQIKGRLLeehsRIKVGDPAEDFgtffsavIDAKEIFGPVLSVYVYPDDkyKETLQLVDSTTsY 425
Cdd:cd06534 233 QICTAASRLLVHESIYDEFVEKLV----TVLVDVDPDMP-------IAQEEIFGPVLPVIRFKDE--EEAIALANDTE-Y 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 984655788 426 GLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASGTNDKpGGPHYILRWTSPQVI 496
Cdd:cd06534 299 GLTAGVFTRDLNRALRVAERLR--AGTVYINDSSIGV-GPEAPFGGVKNSGIGRE-GGPYGLEEYTRTKTV 365
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
82-496 |
3.49e-100 |
|
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: 309.08 E-value: 3.49e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTVIQAEI 160
Cdd:pfam00171 12 INPAT-GEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLE--ERKDELAELETlENGKPLAEARG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 161 DAAaELIDFFRFNAKYAVELEGQqPISVPPSTNSTVYRGLEGFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSD 236
Cdd:pfam00171 89 EVD-RAIDVLRYYAGLARRLDGE-TLPSDPGRLAYTRREPLGVVGAITPWNFPL---LLPAwkiAPALAaGNTVVLKPSE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 237 TAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtfPRLAGECG 316
Cdd:pfam00171 164 LTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL------KRVTLELG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 317 GKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAK- 395
Cdd:pfam00171 238 GKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDP-LDPDTDMGPLISKAq 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 -------------------------------------------------EIFGPVLSVYVYPDDkyKETLQLVDSTTsYG 426
Cdd:pfam00171 317 lervlkyvedakeegaklltggeagldngyfveptvlanvtpdmriaqeEIFGPVLSVIRFKDE--EEAIEIANDTE-YG 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 427 LTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGqQPFGGARASGTNDKpGGPHYILRWTSPQVI 496
Cdd:pfam00171 394 LAAGVFTSDLERALRVARRLE--AGMVWINDYTTGDADG-LPFGGFKQSGFGRE-GGPYGLEEYTEVKTV 459
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
34-499 |
8.10e-92 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 289.53 E-value: 8.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 34 NEPVLAFTQgsPE-RDALQKALKDLKGRM-EAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALA 111
Cdd:PRK03137 7 HEPFTDFSV--EEnVEAFEEALKKVEKELgQDYPLIIGGERITTEDKIVSINPANKSEVVGRVSKATKELAEKAMQAALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 112 ARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAkTMVGQ-GKTVIQAEIDAAaELIDFFRFNAKYAVEL-EGQQPISVP 189
Cdd:PRK03137 85 AFETWKKWSPEDRARILLRAAAIIR-RRKHEFSA-WLVKEaGKPWAEADADTA-EAIDFLEYYARQMLKLaDGKPVESRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 190 PSTNSTVYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPL 268
Cdd:PRK03137 162 GEHNRYFYIPL-GVGVVISPWNFpFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 269 FGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKC 348
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGLRIYERAAKVQPGQIWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 349 SACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfgTFFSAVIDAK--------------------------------- 395
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN--AYMGPVINQAsfdkimsyieigkeegrlvlggegddskgyfiq 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 ----------------EIFGPVLSVYVYPDdkYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKS 459
Cdd:PRK03137 399 ptifadvdpkarimqeEIFGPVVAFIKAKD--FDHALEIANN-TEYGLTGAVISNNREHLEKARREFH--VGNLYFNRGC 473
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 984655788 460 TGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKET 499
Cdd:PRK03137 474 TGAIVGYHPFGGFNMSGTDSKAGGPDYLLLFLQAKTVSEM 513
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
62-489 |
1.22e-87 |
|
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: 278.70 E-value: 1.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 62 EAIPCVVGDEEVWTsDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRA 141
Cdd:cd07125 32 EAIPIINGEETETG-EGAPVIDPADHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEA-NRG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 142 EILAKTMVGQGKTVIQAeIDAAAELIDFFRFNAKYAVELEGQQPISVPPS-TNSTVYRGLeGFVAAISPFNF---TAIGG 217
Cdd:cd07125 110 ELIALAAAEAGKTLADA-DAEVREAIDFCRYYAAQARELFSDPELPGPTGeLNGLELHGR-GVFVCISPWNFplaIFTGQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 218 NLAgapALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWK 296
Cdd:cd07125 188 IAA---ALAaGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 297 QVAQnldRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWP----QIKGRLLEeh 372
Cdd:cd07125 265 ALAE---RDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAErfieMLKGAMAS-- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 373 srIKVGDPAeDFGTFFSAVIDA-----------------------------------------------KEIFGPVLSVY 405
Cdd:cd07125 340 --LKVGDPW-DLSTDVGPLIDKpagkllrahtelmrgeawliapaplddgngyfvapgiieivgifdltTEVFGPILHVI 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 406 VYPDDKYKETLQLVDStTSYGLTGAVFSQDKDvvqEATKVLRNA-AGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGP 484
Cdd:cd07125 417 RFKAEDLDEAIEDINA-TGYGLTLGIHSRDER---EIEYWRERVeAGNLYINRNITGAIVGRQPFGGWGLSGTGPKAGGP 492
|
....*
gi 984655788 485 HYILR 489
Cdd:cd07125 493 NYLLR 497
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
34-498 |
2.96e-78 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 254.02 E-value: 2.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 34 NEPVLAFTQgSPERDALQKALKDLKGRM-EAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAA 112
Cdd:TIGR01237 3 HEPFTDFAD-EENRQAFFKALATVKEQLgKTYPLVINGERVETENKIVSINPCDKSEVVGTVSKASQEHAEHALQAAAKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 113 RKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAEIDAAaELIDFFRFNAKYAVELEGQQPI-SVPPS 191
Cdd:TIGR01237 82 FEAWKKTDPEERAAILFKAAAIVR-RRRHEFSALLVKEVGKPWNEADAEVA-EAIDFMEYYARQMIELAKGKPVnSREGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 192 TNSTVYRGLeGFVAAISPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFG 270
Cdd:TIGR01237 160 TNQYVYTPT-GVTVVISPWNFPfAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 271 DTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSA 350
Cdd:TIGR01237 239 DYLVDHPKTSLITFTGSREVGTRIFERAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 351 CSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDAK----------------------------------- 395
Cdd:TIGR01237 319 GSRAVVHEKVYDEVVERFVEITESLKVGPP-DSADVYVGPVIDQKsfnkimeyieigkaegrlvsggcgddskgyfigpt 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 --------------EIFGPVLSVYVYPDdkYKETLQLVDSTtSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTG 461
Cdd:TIGR01237 398 ifadvdrkarlaqeEIFGPVVAFIRASD--FDEALEIANNT-EYGLTGGVISNNRDHINRAKAEFE--VGNLYFNRNITG 472
|
490 500 510
....*....|....*....|....*....|....*..
gi 984655788 462 SIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKE 498
Cdd:TIGR01237 473 AIVGYQPFGGFKMSGTDSKAGGPDYLALFMQAKTVTE 509
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
46-496 |
4.92e-67 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 234.06 E-value: 4.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 46 ERDALQKALKDLKGRM-EAIPCVVGDEEvwTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADR 124
Cdd:COG4230 540 VLAALSAALAAAAEKQwQAAPLIAGEAA--SGEARPVRNPADHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEER 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 125 AQIFLKAADMLSGpRRAEILAKTMVGQGKTvIQaeiDAAAEL---IDFFRFnakYAVELEGQQpisvppsTNSTVYRGLe 201
Cdd:COG4230 618 AAILERAADLLEA-HRAELMALLVREAGKT-LP---DAIAEVreaVDFCRY---YAAQARRLF-------AAPTVLRGR- 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 202 GFVAAISPFNFTaiggnLAG-----APALM-GNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQFVPADGPLFGDTVT 274
Cdd:COG4230 682 GVFVCISPWNFP-----LAIftgqvAAALAaGNTVLAKPAEqTPLIAARAV-RLLHEAGVPADVLQLLPGDGETVGAALV 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 275 SSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFprLAgECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRL 354
Cdd:COG4230 756 ADPRIAGVAFTGSTETARLINRTLAARDGPIVPL--IA-ETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSALRVL 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 355 YVPHSLWPQ----IKGRLLEehsrIKVGDPAE---DFGtffsAVIDA--------------------------------- 394
Cdd:COG4230 833 CVQEDIADRvlemLKGAMAE----LRVGDPADlstDVG----PVIDAearanleahiermraegrlvhqlplpeecangt 904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 395 ----------------KEIFGPVLSVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN 456
Cdd:COG4230 905 fvaptlieidsisdleREVFGPVLHVVRY---KADELDKVIDAinATGYGLTLGVHSRIDETIDRVAARAR--VGNVYVN 979
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 984655788 457 DKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVI 496
Cdd:COG4230 980 RNIIGAVVGVQPFGGEGLSGTGPKAGGPHYLLRFATERTV 1019
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
44-496 |
3.58e-66 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 230.86 E-value: 3.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 44 SPERDALQKALKDLKGRMEAIPCVVGDeevwTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIAD 123
Cdd:PRK11904 533 RSELEPLAAAIAAFLEKQWQAGPIING----EGEARPVVSPADRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEE 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 124 RAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAeIDAAAELIDFFRFnakYAVELEGQ--QPISVPPSTNSTVYRGLE 201
Cdd:PRK11904 609 RAAILERAADLLEA-NRAELIALCVREAGKTLQDA-IAEVREAVDFCRY---YAAQARRLfgAPEKLPGPTGESNELRLH 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 202 G---FVAaISPFNFT-AIggnLAG--APALM-GNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQFVPADGPLFGDTV 273
Cdd:PRK11904 684 GrgvFVC-ISPWNFPlAI---FLGqvAAALAaGNTVIAKPAEqTPLIAAEAV-KLLHEAGIPKDVLQLLPGDGATVGAAL 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 274 TSSEHLCGINFTGSVptfkhlwkQVAQNLDRfhtfpRLAG----------ECGGKNFHFVHRSADVESVVSGTLRSAFEY 343
Cdd:PRK11904 759 TADPRIAGVAFTGST--------ETARIINR-----TLAArdgpivpliaETGGQNAMIVDSTALPEQVVDDVVTSAFRS 825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 344 GGQKCSACSRLYVPHSLWPQ----IKGRLLEehsrIKVGDPAE------------------------------------- 382
Cdd:PRK11904 826 AGQRCSALRVLFVQEDIADRviemLKGAMAE----LKVGDPRLlstdvgpvidaeakanldahiermkrearllaqlplp 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 383 ---DFGTFFSAV---IDA-----KEIFGPVLSVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVVQEATKVLRna 449
Cdd:PRK11904 902 agtENGHFVAPTafeIDSisqleREVFGPILHVIRY---KASDLDKVIDAinATGYGLTLGIHSRIEETADRIADRVR-- 976
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 984655788 450 AGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVI 496
Cdd:PRK11904 977 VGNVYVNRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLLRFATEKTV 1023
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
33-493 |
1.89e-61 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 218.20 E-value: 1.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 33 ANEPVLAftqgsperdALQKALKDLKG-RMEAIPCVVGDEevwTSDVQYQV-SPFNHGHKVAKFCYADKSLLNKAIEAAL 110
Cdd:PRK11905 533 SDEATLA---------ALDEALNAFAAkTWHAAPLLAGGD---VDGGTRPVlNPADHDDVVGTVTEASAEDVERALAAAQ 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 111 AARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIqaeiDAAAEL---IDFFRFNAKYAVELEGQQPIs 187
Cdd:PRK11905 601 AAFPEWSATPAAERAAILERAADLMEA-HMPELFALAVREAGKTLA----NAIAEVreaVDFLRYYAAQARRLLNGPGH- 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 188 vppstnstvyRGLeGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQFVPA 264
Cdd:PRK11905 675 ----------KPL-GPVVCISPWNFPlAIfTGQIAAALV-AGNTVLAKPAEqTPLIAARAV-RLLHEAGVPKDALQLLPG 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 265 DGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYG 344
Cdd:PRK11905 742 DGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGP---PVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSA 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 345 GQKCSACSRLYVPHSLWPQI----KGRLLEehsrIKVGDPAE---DFGtffsAVIDAK---------------------- 395
Cdd:PRK11905 819 GQRCSALRVLCLQEDVADRVltmlKGAMDE----LRIGDPWRlstDVG----PVIDAEaqanieahieamraagrlvhql 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 ---------------------------EIFGPVLSVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVVQEATKvl 446
Cdd:PRK11905 891 plpaetekgtfvaptlieidsisdlerEVFGPVLHVVRF---KADELDRVIDDinATGYGLTFGLHSRIDETIAHVTS-- 965
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 984655788 447 RNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSP 493
Cdd:PRK11905 966 RIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTGPKAGGPLYLGRLVRE 1012
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
77-485 |
3.18e-56 |
|
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: 194.78 E-value: 3.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 77 DVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTV 155
Cdd:cd07097 14 DGEENRNPSDTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELE--ARKEELARLLTrEEGKTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 156 IQA--EIDAAaelIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNF-TAIGGNLAgAPALM-GNVVL 231
Cdd:cd07097 92 PEArgEVTRA---GQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFpIAIPAWKI-APALAyGNTVV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 232 WKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprl 311
Cdd:cd07097 168 FKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQL---- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 312 agECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGD------------ 379
Cdd:cd07097 244 --EMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDaldegvdigpvv 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 380 -----------------------------PAEDFGTFFS-AVIDA---------KEIFGPVLSVYVYPDdkYKETLQLVD 420
Cdd:cd07097 322 serqlekdlryieiarsegaklvyggerlKRPDEGYYLApALFAGvtndmriarEEIFGPVAAVIRVRD--YDEALAIAN 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 984655788 421 StTSYGLTGAVFSQDkdvVQEATKVLRNA-AGNFYINDKSTGsiVGQQ-PFGGARASGTNDKPGGPH 485
Cdd:cd07097 400 D-TEFGLSAGIVTTS---LKHATHFKRRVeAGVVMVNLPTAG--VDYHvPFGGRKGSSYGPREQGEA 460
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
25-494 |
1.09e-55 |
|
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: 193.97 E-value: 1.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 25 KHTSSLKVANEPVLAFTQGSPERDALQKalkdlkgrMEAIPcVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNK 104
Cdd:TIGR01238 8 KNSLGIDLDNESELKPLEAQIHAWADKT--------WQAAP-IIGHSYKADGEAQPVTNPADRRDIVGQVFHANLAHVQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAeIDAAAELIDFFRFNAKYAVELEGQQ 184
Cdd:TIGR01238 79 AIDSAQQAFPTWNATPAKERAAKLDRLADLLE-LHMPELMALCVREAGKTIHNA-IAEVREAVDFCRYYAKQVRDVLGEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 185 piSVPPstnstvyrglEGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQF 261
Cdd:TIGR01238 157 --SVES----------RGVFVCISPWNFPlAIfTGQISAALA-AGNTVIAKPAEqTSLIAYRAV-ELMQEAGFPAGTIQL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 262 VPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfHTFPRLAgECGGKNFHFVHRSADVESVVSGTLRSAF 341
Cdd:TIGR01238 223 LPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRED--APVPLIA-ETGGQNAMIVDSTALPEQVVRDVLRSAF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 342 EYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEdFGTFFSAVIDA--------------------------- 394
Cdd:TIGR01238 300 DSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHL-LTTDVGPVIDAeakqnllahiehmsqtqkkiaqltldd 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 395 ------------------------KEIFGPVLSVYVYpddKYKETLQLVD--STTSYGLTGAVFSQDKDVVQEATKVLRn 448
Cdd:TIGR01238 379 sracqhgtfvaptlfelddiaelsEEVFGPVLHVVRY---KARELDQIVDqiNQTGYGLTMGVHSRIETTYRWIEKHAR- 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 984655788 449 aAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQ 494
Cdd:TIGR01238 455 -VGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAGGPHYLYRLTQVQ 499
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
105-477 |
7.24e-53 |
|
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: 185.24 E-value: 7.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA--EIDAAAELidfFRFNAKYAVELE 181
Cdd:cd07145 26 AIEVAEKAKDVMSNLPAYKRYKILMKVAELIE--RRKEELAKLLTIEvGKPIKQSrvEVERTIRL---FKLAAEEAKVLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 182 GQqpisVPPSTNstvYRGLE-----------GFVAAISPFNFTAiggNLAG---APAL-MGNVVLWKPSDTAMLASYAVY 246
Cdd:cd07145 101 GE----TIPVDA---YEYNErriaftvrepiGVVGAITPFNFPA---NLFAhkiAPAIaVGNSVVVKPSSNTPLTAIELA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 247 RILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRS 326
Cdd:cd07145 171 KILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGG------TGKKVALELGGSDPMIVLKD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 327 ADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP------------------AEDF---- 384
Cdd:cd07145 245 ADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPldestdlgplispeaverMENLvnda 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 385 ---------------GTFFSAVI------DAK----EIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvV 439
Cdd:cd07145 325 vekggkilyggkrdeGSFFPPTVlendtpDMIvmkeEVFGPVLPIAKVKDD--EEAVEIANS-TEYGLQASVFTND---I 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 984655788 440 QEATKVLRN-AAGNFYINDKSTGSIvGQQPFGGARASGT 477
Cdd:cd07145 399 NRALKVARElEAGGVVINDSTRFRW-DNLPFGGFKKSGI 436
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
102-492 |
1.26e-52 |
|
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: 184.27 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 102 LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAAElIDFFRFNAKYAVEL 180
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILE--ERRDEIADWLIREsGSTRPKAAFEVGAA-IAILREAAGLPRRP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 181 EGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPS-DTAMLASYAVYRILREAGLPPNI 258
Cdd:cd07104 79 EGEILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDsRTPVTGGLLIAEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 259 IQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSADVESVVSGTLR 338
Cdd:cd07104 159 LNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKK------VALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 339 SAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAK----------------------- 395
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDP-DTVIGPLINERqvdrvhaivedavaagarlltgg 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 ------------------------EIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRNA-A 450
Cdd:cd07104 312 tyeglfyqptvlsdvtpdmpifreEIFGPVAPVIPFDDD--EEAVELAND-TEYGLSAAVFTRD---LERAMAFAERLeT 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 984655788 451 GNFYINDKST--GSIVgqqPFGGARASGTnDKPGGPHYI-----LRWTS 492
Cdd:cd07104 386 GMVHINDQTVndEPHV---PFGGVKASGG-GRFGGPASLeefteWQWIT 430
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
83-477 |
6.67e-52 |
|
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: 182.80 E-value: 6.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 83 SPFnHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA--E 159
Cdd:cd07149 5 SPY-DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLE--ERREEFARTIALEaGKPIKDArkE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 160 IDAAaelIDFFRFNAKYAVELEGQQ-PISVPPSTNSTV---YRGLEGFVAAISPFNFTAiggNLAG---APALM-GNVVL 231
Cdd:cd07149 82 VDRA---IETLRLSAEEAKRLAGETiPFDASPGGEGRIgftIREPIGVVAAITPFNFPL---NLVAhkvGPAIAaGNAVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 232 WKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfhtFPRL 311
Cdd:cd07149 156 LKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--------LKKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 312 AGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 391
Cdd:cd07149 228 TLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDE-DTDVGPM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 392 IDAK-----------------------------------------------EIFGPVLSVYVYpdDKYKETLQLVDStTS 424
Cdd:cd07149 307 ISEAeaerieewveeaveggarlltggkrdgaileptvltdvppdmkvvceEVFAPVVSLNPF--DTLDEAIAMAND-SP 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 984655788 425 YGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASGT 477
Cdd:cd07149 384 YGLQAGVFTNDLQKALKAARELE--VGGVMINDSSTFR-VDHMPYGGVKESGT 433
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
88-456 |
2.49e-50 |
|
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: 179.00 E-value: 2.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVG-QGKTVIQA--EIDAAA 164
Cdd:cd07088 23 GEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIR--ENADELAKLIVEeQGKTLSLArvEVEFTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 165 eliDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIggnLAG---APALM-GNVVLWKPSDTAML 240
Cdd:cd07088 101 ---DYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFF---LIArklAPALVtGNTIVIKPSEETPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 241 ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhTFPRLagECGGKNF 320
Cdd:cd07088 175 NALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENI----TKVSL--ELGGKAP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 321 HFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAK----- 395
Cdd:cd07088 249 AIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDA-ATDMGPLVNEAaldkv 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 ----------------------------------------------EIFGPVLSVYVYpdDKYKETLQLVDStTSYGLTG 429
Cdd:cd07088 328 eemveraveagatlltggkrpegekgyfyeptvltnvrqdmeivqeEIFGPVLPVVKF--SSLDEAIELAND-SEYGLTS 404
|
410 420
....*....|....*....|....*..
gi 984655788 430 AVFSQDKDVVQEATKVLRnaAGNFYIN 456
Cdd:cd07088 405 YIYTENLNTAMRATNELE--FGETYIN 429
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
82-476 |
1.11e-49 |
|
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: 176.85 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA-- 158
Cdd:cd07094 4 HNPYD-GEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLK--KRAEEFAKIIACEgGKPIKDArv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 159 EIDAAaelIDFFRFNAKYAVELEGQQpISVPPSTNSTVYRGLE-----GFVAAISPFNFTAiggNLAG---APAL-MGNV 229
Cdd:cd07094 81 EVDRA---IDTLRLAAEEAERIRGEE-IPLDATQGSDNRLAWTirepvGVVLAITPFNFPL---NLVAhklAPAIaTGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 230 VLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfhtFP 309
Cdd:cd07094 154 VVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG--------GK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 310 RLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE---DFG- 385
Cdd:cd07094 226 RIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDedtDVGp 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 386 ---------------------------------TFFSAVI-----DAK----EIFGPVLSVYVYpdDKYKETLQLVDStT 423
Cdd:cd07094 306 liseeaaerverwveeaveagarllcggerdgaLFKPTVLedvprDTKlsteETFGPVVPIIRY--DDFEEAIRIANS-T 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 984655788 424 SYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDkSTGSIVGQQPFGGARASG 476
Cdd:cd07094 383 DYGLQAGIFTRDLNVAFKAAEKLE--VGGVMVND-SSAFRTDWMPFGGVKESG 432
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
103-492 |
4.14e-49 |
|
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: 175.21 E-value: 4.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEG 182
Cdd:cd07150 24 ERAIAAAYDAFPAWAATTPSERERILLKAAEIME--RRADDLIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRVRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 183 QQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQF 261
Cdd:cd07150 102 ETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALaAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 262 VPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAF 341
Cdd:cd07150 182 VTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG------RHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 342 EYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAK-------------------------- 395
Cdd:cd07150 256 MHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPR-DPDTVIGPLISPRqverikrqvedavakgaklltggkyd 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 ---------------------EIFGPVLSvyVYPDDKYKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRNA-AGNF 453
Cdd:cd07150 335 gnfyqptvltdvtpdmrifreETFGPVTS--VIPAKDAEEALELAND-TEYGLSAAILTND---LQRAFKLAERLeSGMV 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 984655788 454 YINDkSTGSIVGQQPFGGARASGTNdKPGGPHYI-----LRWTS 492
Cdd:cd07150 409 HIND-PTILDEAHVPFGGVKASGFG-REGGEWSMeefteLKWIT 450
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
82-476 |
1.64e-48 |
|
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: 174.42 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK-TMVGQGKTVIQA 158
Cdd:cd07119 18 INPAN-GEVIATVPEGTAEDAKRAIAAARRAfdSGEWPHLPAQERAALLFRIADKIR--EDAEELARlETLNTGKTLRES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 159 EIDAAaELIDFFRFNAKYAVELEGQQpISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 237
Cdd:cd07119 95 EIDID-DVANCFRYYAGLATKETGEV-YDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAaGNTVVIKPSEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 238 AMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRLAGECGG 317
Cdd:cd07119 173 TPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGN------VKKVALELGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 318 KNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVG---DPAEDFG--------- 385
Cdd:cd07119 247 KNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGnglDADTEMGplvsaehre 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 386 ------------------------------------TFFSAV-----IDAKEIFGPVLSVYVYPDDkyKETLQLVDSTTs 424
Cdd:cd07119 327 kvlsyiqlgkeegarlvcggkrptgdelakgyfvepTIFDDVdrtmrIVQEEIFGPVLTVERFDTE--EEAIRLANDTP- 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 984655788 425 YGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDksTGSIVGQQPFGGARASG 476
Cdd:cd07119 404 YGLAGAVWTKDIARANRVARRLR--AGTVWIND--YHPYFAEAPWGGYKQSG 451
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
74-476 |
4.61e-48 |
|
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: 172.49 E-value: 4.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 74 WTSDVQyqvSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGK 153
Cdd:cd07151 10 RTIDVL---NPYT-GETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILE-ERRDEIVEWLIRESGS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 154 TVIQAEIDAAAElIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAiggNLAG---APAL-MGNV 229
Cdd:cd07151 85 TRIKANIEWGAA-MAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPL---HLSMrsvAPALaLGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 230 VLWKP-SDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtf 308
Cdd:cd07151 161 VVLKPaSDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLK----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 309 pRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFF 388
Cdd:cd07151 236 -KVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDP-DTVV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 389 SAVIDAK-----------------------------------------------EIFGPVLSVYVYPDDkyKETLQLVDS 421
Cdd:cd07151 314 GPLINESqvdglldkieqaveegatllvggeaegnvleptvlsdvtndmeiareEIFGPVAPIIKADDE--EEALELAND 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 984655788 422 tTSYGLTGAVFSQDkdvVQEATKV-LRNAAGNFYINDKStgsiVGQQP---FGGARASG 476
Cdd:cd07151 392 -TEYGLSGAVFTSD---LERGVQFaRRIDAGMTHINDQP----VNDEPhvpFGGEKNSG 442
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
88-476 |
5.90e-48 |
|
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: 171.85 E-value: 5.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTVIQA--EIDAAA 164
Cdd:cd07103 7 GEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIR--ERAEDLARLLTlEQGKPLAEArgEVDYAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 165 eliDFFRFNAKYAVELEGQqpiSVPPSTNST---VYRGLEGFVAAISPFNFTAigGNLA--GAPAL-MGNVVLWKPSDTA 238
Cdd:cd07103 85 ---SFLEWFAEEARRIYGR---TIPSPAPGKrilVIKQPVGVVAAITPWNFPA--AMITrkIAPALaAGCTVVLKPAEET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 239 MLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfpRLAGECGGk 318
Cdd:cd07103 157 PLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVK------RVSLELGG- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 319 NFHF-VHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAED-------------- 383
Cdd:cd07103 230 NAPFiVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEgtdmgplinerave 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 384 -------------------------FGTFFSAVI------DAK----EIFGPVLSVYVYPDDkyKETLQLVDStTSYGLT 428
Cdd:cd07103 310 kvealvedavakgakvltggkrlglGGYFYEPTVltdvtdDMLimneETFGPVAPIIPFDTE--DEVIARAND-TPYGLA 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 984655788 429 GAVFSQDKDVVQEATKVLRnaAGNFYINdksTGSIVG-QQPFGGARASG 476
Cdd:cd07103 387 AYVFTRDLARAWRVAEALE--AGMVGIN---TGLISDaEAPFGGVKESG 430
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
91-491 |
2.91e-47 |
|
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: 170.61 E-value: 2.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 91 VAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAaELIDF 169
Cdd:cd07131 28 VGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLK--KRKEELARLVTREmGKPLAEGRGDVQ-EAIDM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 170 FRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRI 248
Cdd:cd07131 105 AQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFpVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVEL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 249 LREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRSAD 328
Cdd:cd07131 185 FAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCAR------PNKRVALEMGGKNPIIVMDDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 329 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE---------------------DFG-- 385
Cdd:cd07131 259 LDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDeetdmgplineaqlekvlnynEIGke 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 386 -------------------------TFFSAV-----IDAKEIFGPVLSvyVYPDDKYKETLQLVDStTSYGLTGAVFSQD 435
Cdd:cd07131 339 egatlllggerltgggyekgyfvepTVFTDVtpdmrIAQEEIFGPVVA--LIEVSSLEEAIEIAND-TEYGLSSAIYTED 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 984655788 436 kdvVQEATKVLRNA-AGNFYINDKSTGSIVgQQPFGGARASGTNDKPGGPHYILRWT 491
Cdd:cd07131 416 ---VNKAFRARRDLeAGITYVNAPTIGAEV-HLPFGGVKKSGNGHREAGTTALDAFT 468
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
105-489 |
3.34e-46 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 173.62 E-value: 3.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSGprRAEILAKTMVGQ-GKTVIQAeIDAAAELIDFFRFnakYAVELEGQ 183
Cdd:PRK11809 687 ALESAVNAAPIWFATPPAERAAILERAADLMEA--QMQTLMGLLVREaGKTFSNA-IAEVREAVDFLRY---YAGQVRDD 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 184 qpisvppSTNSTvYRGLeGFVAAISPFNFT-AI-GGNLAGAPAlMGNVVLWKPSD-TAMLASYAVyRILREAGLPPNIIQ 260
Cdd:PRK11809 761 -------FDNDT-HRPL-GPVVCISPWNFPlAIfTGQVAAALA-AGNSVLAKPAEqTPLIAAQAV-RILLEAGVPAGVVQ 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 261 FVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLD-RFHTFPRLAgECGGKNFHFVHRSADVESVVSGTLRS 339
Cdd:PRK11809 830 LLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLDpQGRPIPLIA-ETGGQNAMIVDSSALTEQVVADVLAS 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 340 AFEYGGQKCSACSRLYVP-----HSLwPQIKGRLLEehsrIKVGDPaEDFGTFFSAVIDA-------------------- 394
Cdd:PRK11809 909 AFDSAGQRCSALRVLCLQddvadRTL-KMLRGAMAE----CRMGNP-DRLSTDIGPVIDAeakanierhiqamrakgrpv 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 395 -------------------------------KEIFGPVLSVYVYpddKYKETLQLVDS--TTSYGLTGAVFSQDKDVVQE 441
Cdd:PRK11809 983 fqaarensedwqsgtfvpptlieldsfdelkREVFGPVLHVVRY---NRNQLDELIEQinASGYGLTLGVHTRIDETIAQ 1059
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 984655788 442 ATKvlRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR 489
Cdd:PRK11809 1060 VTG--SAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYR 1105
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
105-483 |
1.57e-44 |
|
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: 162.44 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTM---VGQGKTVIQAEIDAAAELIDFfrfNAKYAVELE 181
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLK--ANKEELARLIsreTGKPLWEAQTEVAAMAGKIDI---SIKAYHERT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 182 GQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQ 260
Cdd:cd07095 80 GERATPMAQGRAVLRHRPH-GVMAVFGPFNFPGHLPNGHIVPALLaGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 261 FVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprLAGECGGKNFHFVHRSADVESVVSGTLRSA 340
Cdd:cd07095 159 LVQGGRET-GEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKI-----LALEMGGNNPLVVWDVADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 341 FEYGGQKCSACSRLYVPHSLWPQ-IKGRLLEEHSRIKVGDPAEDfGTFFSAVIDA------------------------- 394
Cdd:cd07095 233 FLTAGQRCTCARRLIVPDGAVGDaFLERLVEAAKRLRIGAPDAE-PPFMGPLIIAaaaaryllaqqdllalggepllame 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 395 ------------------------KEIFGPVLSVYVYpdDKYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaA 450
Cdd:cd07095 312 rlvagtaflspgiidvtdaadvpdEEIFGPLLQVYRY--DDFDEAIALANA-TRFGLSAGLLSDDEALFERFLARIR--A 386
|
410 420 430
....*....|....*....|....*....|...
gi 984655788 451 GNFYINDKSTGSiVGQQPFGGARASGtNDKPGG 483
Cdd:cd07095 387 GIVNWNRPTTGA-SSTAPFGGVGLSG-NHRPSA 417
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
104-501 |
1.87e-44 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 163.90 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 104 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILaktmvgqgkTVIQAEI-----DAAAELIDFF---RFNAK 175
Cdd:PRK09407 58 AAFARARAAQRAWAATPVRERAAVLLRFHDLVLE-NREELL---------DLVQLETgkarrHAFEEVLDVAltaRYYAR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 176 YAVELEGQQPIS--VPPSTNSTVYRGLEGFVAAISPFNF---TAIGGNLagaPALM-GNVVLWKP-SDTAMLASYAVyRI 248
Cdd:PRK09407 128 RAPKLLAPRRRAgaLPVLTKTTELRQPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPdSQTPLTALAAV-EL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 249 LREAGLPPNIIQFVPADGPLFGDTVT-SSEHLCginFTGSVPTFKHLWKQVAQNLDRFhtfprlAGECGGKNFHFVHRSA 327
Cdd:PRK09407 204 LYEAGLPRDLWQVVTGPGPVVGTALVdNADYLM---FTGSTATGRVLAEQAGRRLIGF------SLELGGKNPMIVLDDA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 328 DVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVG---DPAEDFGTFFSA---------VIDAK 395
Cdd:PRK09407 275 DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGagyDYSADMGSLISEaqletvsahVDDAV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 --------------------------------------EIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKD 437
Cdd:PRK09407 355 akgatvlaggkarpdlgplfyeptvltgvtpdmelareETFGPVVSVYPVADV--DEAVERANDTP-YGLNASVWTGDTA 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 984655788 438 VVQEATKVLRnaAGNFYINDKST---GSIvgQQPFGGARASGTNDKpGGPHYILRWTSPQVIKETHK 501
Cdd:PRK09407 432 RGRAIAARIR--AGTVNVNEGYAaawGSV--DAPMGGMKDSGLGRR-HGAEGLLKYTESQTIATQRV 493
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
97-476 |
8.81e-44 |
|
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: 160.87 E-value: 8.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 97 ADKSLLNKAIEAALAARKEWDLK-PIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAAELIDFFRFNA 174
Cdd:cd07089 16 AGAADVDAAIAAARRAFDTGDWStDAEERARCLRQLHEALE--ARKEELRALLVAEvGAPVMTARAMQVDGPIGHLRYFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 175 KYAVELEGQQPISVPPS----TNSTVYRGLEGFVAAISPFNFtAIGGNLAG-APAL-MGNVVLWKPSDTAMLASYAVYRI 248
Cdd:cd07089 94 DLADSFPWEFDLPVPALrggpGRRVVRREPVGVVAAITPWNF-PFFLNLAKlAPALaAGNTVVLKPAPDTPLSALLLGEI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 249 LREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHRSAD 328
Cdd:cd07089 173 IAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLL------ELGGKSANIVLDDAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 329 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAK------------- 395
Cdd:cd07089 247 LAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPA-DPGTVMGPLISAAqrdrvegyiargr 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 ---------------------------------------EIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDK 436
Cdd:cd07089 326 degarlvtgggrpagldkgfyveptlfadvdndmriaqeEIFGPVLVVIPYDDD--DEAVRIAND-SDYGLSGGVWSADV 402
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 984655788 437 DVVQEATKVLRnaAGNFYINDKSTGSIVGqqPFGGARASG 476
Cdd:cd07089 403 DRAYRVARRIR--TGSVGINGGGGYGPDA--PFGGYKQSG 438
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
83-498 |
1.27e-43 |
|
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: 160.17 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 83 SPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQA--EI 160
Cdd:cd07101 2 APFT-GEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVL-ERRDELLDLIQLETGKARRHAfeEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 161 DAAAELIDFFRFNAKYAVELEGQQPiSVPPSTNSTVYRGLEGFVAAISPFNF---TAIGGNLagaPALM-GNVVLWKPSD 236
Cdd:cd07101 80 LDVAIVARYYARRAERLLKPRRRRG-AIPVLTRTTVNRRPKGVVGVISPWNYpltLAVSDAI---PALLaGNAVVLKPDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 237 TAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTssEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprlAGECG 316
Cdd:cd07101 156 QTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIV--DNADYVMFTGSTATGRVVAERAGRRLIGC------SLELG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 317 GKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKV------------------- 377
Cdd:cd07101 228 GKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLgaaldygpdmgslisqaql 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 378 --------------------GDPAEDFGTFF-----------SAVIDAKEIFGPVLSVYVYPDDkyKETLQLVDStTSYG 426
Cdd:cd07101 308 drvtahvddavakgatvlagGRARPDLGPYFyeptvltgvteDMELFAEETFGPVVSIYRVADD--DEAIELAND-TDYG 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 984655788 427 LTGAVFSQDKDVVQEATKVLRnaAGNFYIND---KSTGSIvgQQPFGGARASGTNDKpGGPHYILRWTSPQVIKE 498
Cdd:cd07101 385 LNASVWTRDGARGRRIAARLR--AGTVNVNEgyaAAWASI--DAPMGGMKDSGLGRR-HGAEGLLKYTETQTVAV 454
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
87-476 |
1.69e-43 |
|
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: 160.02 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 87 HGHKVAKFCYADKSLLNKAIEAALAA--RKEW-DLKPIAdRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTViqAEIDA 162
Cdd:cd07114 6 TGEPWARVPEASAADVDRAVAAARAAfeGGAWrKLTPTE-RGKLLRRLADLIE--ANAEELAELETRDnGKLI--RETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 163 -AAELIDFFRFNAKYAVELEGQ-QPISVPPSTNSTVYRGLeGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAM 239
Cdd:cd07114 81 qVRYLAEWYRYYAGLADKIEGAvIPVDKGDYLNFTRREPL-GVVAAITPWNSPLLLLAKKLAPALaAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 240 LASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRLAGECGGKN 319
Cdd:cd07114 160 ASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAEN------LAPVTLELGGKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 320 FHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE----------------- 382
Cdd:cd07114 234 PNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDpetqmgplaterqlekv 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 383 --------------------------DFGTFF----------SAVIDAKEIFGPVLSVYVYPDDkyKETLQLVDStTSYG 426
Cdd:cd07114 314 eryvarareegarvltggerpsgadlGAGYFFeptiladvtnDMRIAQEEVFGPVLSVIPFDDE--EEAIALAND-SEYG 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 984655788 427 LTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVgqQPFGGARASG 476
Cdd:cd07114 391 LAAGIWTRDLARAHRVARAIE--AGTVWVNTYRALSPS--SPFGGFKDSG 436
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
103-476 |
2.92e-43 |
|
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: 159.66 E-value: 2.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 103 NKAIEAALAA-RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTM---VGQGKTVIQAEIDAAAELIDFFRFNAKyav 178
Cdd:cd07082 41 LEAAETAYDAgRGWWPTMPLEERIDCLHKFADLLK--ENKEEVANLLmweIGKTLKDALKEVDRTIDYIRDTIEELK--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 179 ELEGQ--QPISVPPSTNS--TVYRGLEGFVAAISPFNFTAiggNLAG---APAL-MGNVVLWKPSDTAMLASYAVYRILR 250
Cdd:cd07082 116 RLDGDslPGDWFPGTKGKiaQVRREPLGVVLAIGPFNYPL---NLTVsklIPALiMGNTVVFKPATQGVLLGIPLAEAFH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 251 EAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQvaqnldrfHTFPRLAGECGGKNFHFVHRSADVE 330
Cdd:cd07082 193 DAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ--------HPMKRLVLELGGKDPAIVLPDADLE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 331 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDF-------------------------- 384
Cdd:cd07082 265 LAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGvditplidpksadfvegliddavakg 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 385 -----------GTFFS-AVIDA---------KEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVVQEAT 443
Cdd:cd07082 345 atvlngggregGNLIYpTLLDPvtpdmrlawEEPFGPVLPIIRVNDI--EEAIELANK-SNYGLQASIFTKDINKARKLA 421
|
410 420 430
....*....|....*....|....*....|...
gi 984655788 444 KVLRnaAGNFYINDKSTGSIvGQQPFGGARASG 476
Cdd:cd07082 422 DALE--VGTVNINSKCQRGP-DHFPFLGRKDSG 451
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
88-476 |
2.93e-43 |
|
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: 159.14 E-value: 2.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAEIDAAAELI 167
Cdd:cd07115 7 GELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILA-NADELARLESLDTGKPIRAARRLDVPRAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 168 DFFRFNAKYAVELEGQQ-PISvPPSTNSTVyRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAV 245
Cdd:cd07115 86 DTFRYYAGWADKIEGEViPVR-GPFLNYTV-REPVGVVGAIVPWNFPLMFAAWKVAPALaAGNTVVLKPAELTPLSALRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 246 YRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfpRLAGECGGKNFHFVHR 325
Cdd:cd07115 164 AELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLK------RVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 326 SADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE---------------------DF 384
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDpktqmgplvsqaqfdrvldyvDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 385 G-----------------------TFFSAV-----IDAKEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDK 436
Cdd:cd07115 318 GreegarlltggkrpgargffvepTIFAAVppemrIAQEEIFGPVVSVMRFRDE--EEALRIANGTE-YGLAAGVWTRDL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 984655788 437 DVVQEATKVLRnaAGNFYINdkSTGSIVGQQPFGGARASG 476
Cdd:cd07115 395 GRAHRVAAALK--AGTVWIN--TYNRFDPGSPFGGYKQSG 430
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
88-476 |
3.16e-43 |
|
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: 159.39 E-value: 3.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTV--IQAEIDAAAE 165
Cdd:cd07090 7 GEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLR-ERNDEIARLETIDNGKPIeeARVDIDSSAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 166 LIDFFrfnAKYAVELEGQQpisVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 242
Cdd:cd07090 86 CLEYY---AGLAPTLSGEH---VPLPGGSFAYTRREplGVCAGIGAWNYPIQIASWKSAPALAcGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 243 YAVYRILREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHF 322
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKH------VTLELGGKSPLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 323 VHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE-------------------- 382
Cdd:cd07090 233 IFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDedtqmgaliseehlekvlgy 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 383 ------------------------DFGTFFS-AVIDA---------KEIFGPVLSVYVYpdDKYKETLQLVDSTTsYGLT 428
Cdd:cd07090 313 iesakqegakvlcggervvpedglENGFYVSpCVLTDctddmtivrEEIFGPVMSILPF--DTEEEVIRRANDTT-YGLA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 984655788 429 GAVFSQDkdvVQEATKVLRN-AAGNFYINDKSTGSIvgQQPFGGARASG 476
Cdd:cd07090 390 AGVFTRD---LQRAHRVIAQlQAGTCWINTYNISPV--EVPFGGYKQSG 433
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
82-477 |
4.02e-43 |
|
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: 158.88 E-value: 4.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQA--- 158
Cdd:cd07093 2 FNPAT-GEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEA-RADELALLESLDTGKPITLArtr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 159 EIDAAAElidFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIggnLAG---APAL-MGNVVLWKP 234
Cdd:cd07093 80 DIPRAAA---NFRFFADYILQLDGESYPQDGGALNYVLRQPV-GVAGLITPWNLPLM---LLTwkiAPALaFGNTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 235 SDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagE 314
Cdd:cd07093 153 SEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSL------E 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 315 CGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPaEDFGTFFSAVIDA 394
Cdd:cd07093 227 LGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDP-LDPDTEVGPLISK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 395 K------------------------------------------------------EIFGPVLSvyVYPDDKYKETLQLVD 420
Cdd:cd07093 306 EhlekvlgyvelaraegatiltgggrpelpdleggyfveptvitgldndsrvaqeEIFGPVVT--VIPFDDEEEAIELAN 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 984655788 421 STTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN-----DKSTgsivgqqPFGGARASGT 477
Cdd:cd07093 384 DTP-YGLAAYVWTRDLGRAHRVARRLE--AGTVWVNcwlvrDLRT-------PFGGVKASGI 435
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
97-496 |
1.02e-42 |
|
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: 157.69 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 97 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLS--GPRRAEILAKTmvgQGKTVIQA--EIDAAAeliDFFRF 172
Cdd:cd07106 16 ASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEanAEELARLLTLE---QGKPLAEAqfEVGGAV---AWLRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 173 NAKYAVELEGQQpiSVPPSTNSTVYRGLeGFVAAISPFNFTAIggnLAG---APALM-GNVVLWKPSDTAMLASYAVYRI 248
Cdd:cd07106 90 TASLDLPDEVIE--DDDTRRVELRRKPL-GVVAAIVPWNFPLL---LAAwkiAPALLaGNTVVLKPSPFTPLCTLKLGEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 249 LREAgLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSAD 328
Cdd:cd07106 164 AQEV-LPPGVLNVVSGGDEL-GPALTSHPDIRKISFTGSTATGKKVMASAAKTLKR------VTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 329 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFF-------------------- 388
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDP-GTTLgpvqnkmqydkvkelvedak 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 389 ------------------------------SAVIDAKEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdv 438
Cdd:cd07106 315 akgakvlaggepldgpgyfipptivddppeGSRIVDEEQFGPVLPVLKYSDE--DEVIARAND-SEYGLGASVWSSD--- 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 984655788 439 VQEATKV-LRNAAGNFYINdkSTGSIVGQQPFGGARASGTndkpG---GPHYILRWTSPQVI 496
Cdd:cd07106 389 LERAEAVaRRLEAGTVWIN--THGALDPDAPFGGHKQSGI----GvefGIEGLKEYTQTQVI 444
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
96-484 |
7.56e-42 |
|
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: 155.14 E-value: 7.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 96 YADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQGKTVI---QAEIDAAAElidFFRF 172
Cdd:cd07152 9 VADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLE--EHADEIADWIVRESGSIRpkaGFEVGAAIG---ELHE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 173 NAKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPS-DTAMLASYAVYRILR 250
Cdd:cd07152 84 AAGLPTQPQGEILPSAPGRLSLARRVPL-GVVGVISPFNFPLILAMRSVAPALaLGNAVVLKPDpRTPVSGGVVIARLFE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 251 EAGLPPNIIQFVPAdGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHRSADVE 330
Cdd:cd07152 163 EAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSL------ELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 331 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDF-------------------------- 384
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQvalgplinarqldrvhaivddsvaag 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 385 ----------GTFFSA-VID---------AKEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVVQEATK 444
Cdd:cd07152 316 arleaggtydGLFYRPtVLSgvkpgmpafDEEIFGPVAPVTVFDSD--EEAVALAND-TEYGLSAGIISRDVGRAMALAD 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 984655788 445 VLRnaAGNFYINDKSTGSIVgQQPFGGARASGTNDKPGGP 484
Cdd:cd07152 393 RLR--TGMLHINDQTVNDEP-HNPFGGMGASGNGSRFGGP 429
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
67-476 |
1.03e-41 |
|
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: 155.41 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 67 VVGDEEVWTSdvqyqVSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK 146
Cdd:cd07086 8 VGSGGETFTS-----RNPAN-GEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALR--KKKEALGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 147 TM---VGQGKTVIQAEIDaaaELIDFfrfnAKYAVELEGQQPISVPPSTNS-----TVYRGLeGFVAAISPFNF-TAIGG 217
Cdd:cd07086 80 LVsleMGKILPEGLGEVQ---EMIDI----CDYAVGLSRMLYGLTIPSERPghrlmEQWNPL-GVVGVITAFNFpVAVPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 218 -NLAgaPALM-GNVVLWKPSDTAMLASYAVYRILREA----GLPPNIIQFVPADGPlFGDTVTSSEHLCGINFTGSVPTF 291
Cdd:cd07086 152 wNAA--IALVcGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 292 KHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEE 371
Cdd:cd07086 229 RRVGETVAR------RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 372 HSRIKVGDPAEDfGTFFSAVID-------------AK---------------------------------------EIFG 399
Cdd:cd07086 303 YKQVRIGDPLDE-GTLVGPLINqaavekylnaieiAKsqggtvltggkridggepgnyveptivtgvtddarivqeETFA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 400 PVLsvYVYPDDKYKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRNA---AGNFYINDKSTGSIVGqQPFGGARASG 476
Cdd:cd07086 382 PIL--YVIKFDSLEEAIAINND-VPQGLSSSIFTED---LREAFRWLGPKgsdCGIVNVNIPTSGAEIG-GAFGGEKETG 454
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
105-477 |
2.79e-41 |
|
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: 154.07 E-value: 2.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 105 AIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQGKTVIQA---EIDAAAELIDFFrfnAKYAVELE 181
Cdd:cd07107 24 AVAAARAAFPEWRATTPLERARMLRELATRLR--EHAEELALIDALDCGNPVSAmlgDVMVAAALLDYF---AGLVTELK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 182 GQqpiSVPPSTNSTVYRGLE--GFVAAISPFN--FTAIGGNLAgAPALMGNVVLWKPSDTAMLASYAVYRILREAgLPPN 257
Cdd:cd07107 99 GE---TIPVGGRNLHYTLREpyGVVARIVAFNhpLMFAAAKIA-APLAAGNTVVVKPPEQAPLSALRLAELAREV-LPPG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 258 IIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRSADVESVVSGTL 337
Cdd:cd07107 174 VFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAE------GIKHVTLELGGKNALIVFPDADPEAAADAAV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 338 RSA-FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAK--------------------- 395
Cdd:cd07107 248 AGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDP-ATTMGPLVSRQqydrvmhyidsakregarlvt 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 ---------------------------------EIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvVQEA 442
Cdd:cd07107 327 gggrpegpaleggfyveptvfadvtpgmriareEIFGPVLSVLRWRDE--AEMVAQANG-VEYGLTAAIWTND---ISQA 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 984655788 443 TKVLRNA-AGNFYINDKST---GSivgqqPFGGARASGT 477
Cdd:cd07107 401 HRTARRVeAGYVWINGSSRhflGA-----PFGGVKNSGI 434
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
82-476 |
2.37e-40 |
|
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: 151.24 E-value: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEI 160
Cdd:cd07147 4 TNPYT-GEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLE--ERFEELAETIVLEaGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 161 DAAaELIDFFRFNAKYAVELEGQ-QPISVPPSTNStvYRGL-----EGFVAAISPFNFTAiggNLAG---APAL-MGNVV 230
Cdd:cd07147 81 EVA-RAIDTFRIAAEEATRIYGEvLPLDISARGEG--RQGLvrrfpIGPVSAITPFNFPL---NLVAhkvAPAIaAGCPF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 231 LWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtfpR 310
Cdd:cd07147 155 VLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDD-ADLLVTDERIKLLSFTGSPAVGWDLKARAGKK--------K 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 311 LAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSA 390
Cdd:cd07147 226 VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDD-ATDVGP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 391 VID-----------------------------------------------AKEIFGPVLSVYVYpdDKYKETLQLVDStT 423
Cdd:cd07147 305 MISeseaervegwvneavdagaklltggkrdgalleptiledvppdmevnCEEVFGPVVTVEPY--DDFDEALAAVND-S 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 984655788 424 SYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASG 476
Cdd:cd07147 382 KFGLQAGVFTRDLEKALRAWDELE--VGGVVINDVPTFR-VDHMPYGGVKDSG 431
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
103-476 |
3.00e-40 |
|
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: 151.12 E-value: 3.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTM---VGQGKTV---IQAE-----IDAAAELIDFFR 171
Cdd:cd07138 39 DRAVAAARRAFPAWSATSVEERAALLERIAEAYE--ARADELAQAItleMGAPITLaraAQVGlgighLRAAADALKDFE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 172 FnakyaVELEGqqpisvppstNSTVYRGLEGFVAAISPFNFTA--IGGNLAgaPALM-GNVVLWKPSDTAMLASYAVYRI 248
Cdd:cd07138 117 F-----EERRG----------NSLVVREPIGVCGLITPWNWPLnqIVLKVA--PALAaGCTVVLKPSEVAPLSAIILAEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 249 LREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTfkhlWKQVAQNLDRfhTFPRLAGECGGKNFHFVHRSAD 328
Cdd:cd07138 180 LDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRA----GKRVAEAAAD--TVKRVALELGGKSANIILDDAD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 329 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE-------------------------- 382
Cdd:cd07138 254 LEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDpattlgplasaaqfdrvqgyiqkgie 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 383 ----------------DFG-----TFFSAV-----IDAKEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDK 436
Cdd:cd07138 334 egarlvaggpgrpeglERGyfvkpTVFADVtpdmtIAREEIFGPVLSIIPYDDE--DEAIAIAND-TPYGLAGYVWSADP 410
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 984655788 437 DVVQEATKVLRnaAGNFYINDkstGSIVGQQPFGGARASG 476
Cdd:cd07138 411 ERARAVARRLR--AGQVHING---AAFNPGAPFGGYKQSG 445
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
82-476 |
5.95e-40 |
|
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: 150.18 E-value: 5.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPfNHGHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA 158
Cdd:cd07118 2 RSP-AHGVVVARYAEGTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIR--ARRERLALIETLEsGKPISQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 159 --EIDAAAELidfFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTA--IGGNLAGAPAlMGNVVLWKP 234
Cdd:cd07118 79 rgEIEGAADL---WRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFliLSQKLPFALA-AGCTVVVKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 235 SD-----TAMLAsyavyRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfp 309
Cdd:cd07118 155 SEftsgtTLMLA-----ELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKK----- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 310 rLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP--------- 380
Cdd:cd07118 225 -VSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPldpetkvga 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 381 ----------------AEDFG--------------------TFFSAV-----IDAKEIFGPVLSVYVYpdDKYKETLQLV 419
Cdd:cd07118 304 iineaqlakitdyvdaGRAEGatlllggerlasaaglfyqpTIFTDVtpdmaIAREEIFGPVLSVLTF--DTVDEAIALA 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 984655788 420 DStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIvgQQPFGGARASG 476
Cdd:cd07118 382 ND-TVYGLSAGVWSKDIDTALTVARRIR--AGTVWVNTFLDGSP--ELPFGGFKQSG 433
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
103-476 |
5.99e-40 |
|
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: 149.65 E-value: 5.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAEIDAAAeLIDFFRFNAKYAVELEG 182
Cdd:cd07105 3 DQAVEAAAAAFPAWSKTPPSERRDILLKAADLLES-RRDEFIEAMMEETGATAAWAGFNVDL-AAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 183 QQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQF 261
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAaGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 262 V---PADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfPRLAgECGGKNFHFVHRSADVESVVSGTLR 338
Cdd:cd07105 161 VthsPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLK-----PVLL-ELGGKAPAIVLEDADLDAAANAALF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 339 SAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHS---------------------------------RIKVGDPAEDF- 384
Cdd:cd07105 235 GAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEklfagpvvlgslvsaaaadrvkelvddalskgaKLVVGGLADESp 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 385 -GTFFSAVI----------DAKEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvvqeATKVLRNA---- 449
Cdd:cd07105 315 sGTSMPPTIldnvtpdmdiYSEESFGPVVSIIRVKDE--EEAVRIAND-SEYGLSAAVFTRD------LARALAVAkrie 385
|
410 420 430
....*....|....*....|....*....|
gi 984655788 450 AGNFYINdkstGSIVG---QQPFGGARASG 476
Cdd:cd07105 386 SGAVHIN----GMTVHdepTLPHGGVKSSG 411
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
88-494 |
4.35e-39 |
|
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: 148.36 E-value: 4.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAA-RKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAEIDAAAEL 166
Cdd:cd07113 25 EQVIASVASATEADVDAAVASAWRAfVSAWAKTTPAERGRILLRLADLIEQ-HGEELAQLETLCSGKSIHLSRAFEVGQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 167 IDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLE-----GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAML 240
Cdd:cd07113 104 ANFLRYFAGWATKINGETLAPSIPSMQGERYTAFTrrepvGVVAGIVPWNFSVMIAVWKIGAALAtGCTIVIKPSEFTPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 241 ASYAVYRILREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNF 320
Cdd:cd07113 184 TLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTL------ELGGKNA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 321 HFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGTF--------FSAVI 392
Cdd:cd07113 257 AAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFgplanqphFDKVC 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 393 DA-----------------------------------------KEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAV 431
Cdd:cd07113 337 SYlddaraegdeivrggealagegyfvqptlvlarsadsrlmrEETFGPVVSFVPYEDE--EELIQLIND-TPFGLTASV 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 984655788 432 FSQDkdvvqeATKVLRNA----AGNFYIN-----DKSTgsivgqqPFGGARASGTNdKPGGPHYILRWTSPQ 494
Cdd:cd07113 414 WTNN------LSKALRYIprieAGTVWVNmhtflDPAV-------PFGGMKQSGIG-REFGSAFIDDYTELK 471
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
88-496 |
8.53e-38 |
|
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: 144.29 E-value: 8.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQA--EIDAAAE 165
Cdd:cd07099 6 GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALAD-HADELAELLHAETGKPRADAglEVLLALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 166 LIDFFrfnAKYAVELEGQQPISVPPSTN---STVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLA 241
Cdd:cd07099 85 AIDWA---ARNAPRVLAPRKVPTGLLMPnkkATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAaGNAVVLKPSEVTPLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 242 SYAVYRILREAGLPPNIIQFVPADGPlfgdtvtSSEHLCG-----INFTGSVPTFKHLWKQVAQNLdrfhtFPRLAgECG 316
Cdd:cd07099 162 GELLAEAWAAAGPPQGVLQVVTGDGA-------TGAALIDagvdkVAFTGSVATGRKVMAAAAERL-----IPVVL-ELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 317 GKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDF------------ 384
Cdd:cd07099 229 GKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDadigpmttarql 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 385 ---------------------------GTFFSAVI------DAK----EIFGPVLSVYVYPDDkyKETLQLVDSTTsYGL 427
Cdd:cd07099 309 divrrhvddavakgakaltggarsnggGPFYEPTVltdvphDMDvmreETFGPVLPVMPVADE--DEAIALANDSR-YGL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 984655788 428 TGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGQQPFGGARASGTNDKpGGPHYILRWTSPQVI 496
Cdd:cd07099 386 SASVFSRDLARAEAIARRLE--AGAVSINDVLLTAGIPALPFGGVKDSGGGRR-HGAEGLREFCRPKAI 451
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
88-476 |
1.08e-37 |
|
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: 143.91 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPiADRAQIFLKAADMLSgpRRAEILAKTM-VGQGKTVIQAEIDAAA 164
Cdd:cd07109 7 GEVFARIARGGAADVDRAVQAARRAfeSGWLRLSP-AERGRLLLRIARLIR--EHADELARLEsLDTGKPLTQARADVEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 165 eLIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTA-IGGNLAgAPAL-MGNVVLWKPSDTAML 240
Cdd:cd07109 84 -AARYFEYYGGAADKLHGE---TIPLGPGYFVYTVREphGVTGHIIPWNYPLqITGRSV-APALaAGNAVVVKPAEDAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 241 ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRLAGECGGKNF 320
Cdd:cd07109 159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAEN------VVPVTLELGGKSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 321 HFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFG--------------- 385
Cdd:cd07109 233 QIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDlgplisakqldrveg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 386 -------------------------------TFFSAV-----IDAKEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTG 429
Cdd:cd07109 313 fvararargarivaggriaegapaggyfvapTLLDDVppdsrLAQEEIFGPVLAVMPFDDE--AEAIALANG-TDYGLVA 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 984655788 430 AVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIVgQQPFGGARASG 476
Cdd:cd07109 390 GVWTRDGDRALRVARRLR--AGQVFVNNYGAGGGI-ELPFGGVKKSG 433
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
82-476 |
1.77e-37 |
|
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: 143.27 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGprRAEILAKTMVGQ-GKTV-IQAE 159
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEA--RSEELARLLALEtGNALrTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 160 IDAAAeLIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSD 236
Cdd:cd07108 79 PEAAV-LADLFRYFGGLAGELKGE---TLPFGPDVLTYTVREplGVVGAILPWNAPLMLAALKIAPALvAGNTVVLKAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 237 TAMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfhtfPRLAG--- 313
Cdd:cd07108 155 DAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA---------DRLIPvsl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 314 ECGGKNFHFVHRSADVESVVSGTLRSA-FEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP---AEDFG---- 385
Cdd:cd07108 225 ELGGKSPMIVFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPldeATDIGaiis 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 386 ------------------------------------------TFFSAV-----IDAKEIFGPVLSVYVYPDdkYKETLQL 418
Cdd:cd07108 305 ekqfakvcgyidlglstsgatvlrggplpgegpladgffvqpTIFSGVdnewrLAREEIFGPVLCAIPWKD--EDEVIAM 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 984655788 419 VDSTTsYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKstgsiVGQQP---FGGARASG 476
Cdd:cd07108 383 ANDSH-YGLAAYVWTRDLGRALRAAHALE--AGWVQVNQG-----GGQQPgqsYGGFKQSG 435
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
88-476 |
2.61e-37 |
|
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: 143.12 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPI--ADRAQIFLKAADMLSgpRRAEILAK--TMVGqGKTV-IQAEIDA 162
Cdd:cd07091 29 EEVICQVAEADEEDVDAAVKAARAAFETGWWRKMdpRERGRLLNKLADLIE--RDRDELAAleSLDN-GKPLeESAKGDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 163 AaELIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAM 239
Cdd:cd07091 106 A-LSIKCLRYYAGWADKIQGK---TIPIDGNFLAYTRREpiGVCGQIIPWNFPLLMLAWKLAPALaAGNTVVLKPAEQTP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 240 LASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDRFhTFprlagECGGK 318
Cdd:cd07091 182 LSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKsNLKKV-TL-----ELGGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 319 NFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVIDAK--- 395
Cdd:cd07091 256 SPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP-DTFQGPQVSKAqfd 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 -----------------------------------------------EIFGPVLSVYvypddKYKETLQLVD--STTSYG 426
Cdd:cd07091 335 kilsyiesgkkegatlltggerhgskgyfiqptvftdvkddmkiakeEIFGPVVTIL-----KFKTEDEVIEraNDTEYG 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 984655788 427 LTGAVFSQDKDVVQEATKVLRnaAGNFYINdksTGSIVGQQ-PFGGARASG 476
Cdd:cd07091 410 LAAGVFTKDINKALRVSRALK--AGTVWVN---TYNVFDAAvPFGGFKQSG 455
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
88-477 |
8.69e-37 |
|
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: 141.31 E-value: 8.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAAEL 166
Cdd:cd07092 7 GEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIE--ENAEELAALESRNtGKPLHLVRDDELPGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 167 IDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAV 245
Cdd:cd07092 85 VDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALaAGNTVVLKPSETTPLTTLLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 246 YRILREaGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHR 325
Cdd:cd07092 165 AELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHL------ELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 326 SADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP------------------------- 380
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPddedtemgplnsaaqrervagfver 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 381 -------------AEDFGTFF----------SAVIDAKEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKD 437
Cdd:cd07092 318 apaharvltggrrAEGPGYFYeptvvagvaqDDEIVQEEIFGPVVTVQPFDDE--DEAIELAND-VEYGLASSVWTRDVG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 984655788 438 VVQEATKVLRnaAGNFYINDKstGSIVGQQPFGGARASGT 477
Cdd:cd07092 395 RAMRLSARLD--FGTVWVNTH--IPLAAEMPHGGFKQSGY 430
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
82-456 |
2.93e-36 |
|
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: 140.07 E-value: 2.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA-- 158
Cdd:cd07102 1 ISPID-GSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLA--ANTDEIAEELTWQmGRPIAQAgg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 159 EIDAAAELIDFFRFNAKYAVelegqQPISVPPSTNST---VYRGLeGFVAAISPFN---FTAIGgnlAGAPALM-GNVVL 231
Cdd:cd07102 78 EIRGMLERARYMISIAEEAL-----ADIRVPEKDGFEryiRREPL-GVVLIIAPWNypyLTAVN---AVIPALLaGNAVI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 232 WKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRL 311
Cdd:cd07102 149 LKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGR------FIKV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 312 AGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAV 391
Cdd:cd07102 222 GLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDP-STTLGPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 392 IDAK-----------------------------------------------------EIFGPVLSVYVYPDDkyKETLQL 418
Cdd:cd07102 301 VSARaadfvraqiadaiakgaralidgalfpedkaggaylaptvltnvdhsmrvmreETFGPVVGIMKVKSD--AEAIAL 378
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 984655788 419 V-DSTtsYGLTGAVFSQDKDVVQE-ATKVlrnAAGNFYIN 456
Cdd:cd07102 379 MnDSE--YGLTASVWTKDIARAEAlGEQL---ETGTVFMN 413
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
97-476 |
3.82e-36 |
|
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: 139.79 E-value: 3.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 97 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGpRRAEILAKTMVGQGKTVIQAEIDAAaELIDFFRFNAKY 176
Cdd:cd07110 16 ATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRE-RREELAELEARDNGKPLDEAAWDVD-DVAGCFEYYADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 177 AVELEGQQPISVP---PSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREA 252
Cdd:cd07110 94 AEQLDAKAERAVPlpsEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAaGCTVVLKPSELTSLTELELAEIAAEA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 253 GLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSADVESV 332
Cdd:cd07110 174 GLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKP------VSLELGGKSPIIVFDDADLEKA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 333 VSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP-------------------------AEDFG-- 385
Cdd:cd07110 248 VEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPleegvrlgplvsqaqyekvlsfiarGKEEGar 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 386 -------------------TFFSAV-----IDAKEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVVQE 441
Cdd:cd07110 328 llcggrrpahlekgyfiapTVFADVptdsrIWREEIFGPVLCVRSFATE--DEAIALAND-SEYGLAAAVISRDAERCDR 404
|
410 420 430
....*....|....*....|....*....|....*
gi 984655788 442 ATKVLRnaAGNFYINdkSTGSIVGQQPFGGARASG 476
Cdd:cd07110 405 VAEALE--AGIVWIN--CSQPCFPQAPWGGYKRSG 435
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
88-476 |
1.03e-35 |
|
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: 139.08 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLK-PIADRAQIFLKAADMLSgpRRAEILA--KTMvGQGKTVIQAEIDAAA 164
Cdd:cd07144 33 GEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVE--KNRDLLAaiEAL-DSGKPYHSNALGDLD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 165 ELIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSDTA 238
Cdd:cd07144 110 EIIAVIRYYAGWADKIQGK---TIPTSPNKLAYTLHEpyGVCGQIIPWNYPL---AMAAwklAPALAaGNTVVIKPAENT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 239 MLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfpRLAGECGGK 318
Cdd:cd07144 184 PLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLK------AVTLECGGK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 319 NFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEE-HSRIKVGDPAED-------------- 383
Cdd:cd07144 258 SPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHvKQNYKVGSPFDDdtvvgpqvsktqyd 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 384 -----------------FGTFFSAVIDAK---------------------EIFGPVLSVYVYPDdkYKETLQLVDSTTsY 425
Cdd:cd07144 338 rvlsyiekgkkegaklvYGGEKAPEGLGKgyfipptiftdvpqdmrivkeEIFGPVVVISKFKT--YEEAIKKANDTT-Y 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 984655788 426 GLTGAVFSQDkdvVQEATKVLRN-AAGNFYINDKSTGSIvgQQPFGGARASG 476
Cdd:cd07144 415 GLAAAVFTKD---IRRAHRVARElEAGMVWINSSNDSDV--GVPFGGFKMSG 461
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
102-482 |
8.51e-35 |
|
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: 135.95 E-value: 8.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 102 LNKAIEAALAARKEwdLKPiADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA--EIDAAaelIDFFRFNAKYAV 178
Cdd:cd07146 23 LREALALAASYRST--LTR-YQRSAILNKAAALLE--ARREEFARLITLEsGLCLKDTryEVGRA---ADVLRFAAAEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 179 ELEGQQpISVPPSTNSTVYRGLE-----GFVAAISPFNFTAiggNLAG---APALM-GNVVLWKPSDTAMLASYAVYRIL 249
Cdd:cd07146 95 RDDGES-FSCDLTANGKARKIFTlreplGVVLAITPFNHPL---NQVAhkiAPAIAaNNRIVLKPSEKTPLSAIYLADLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 250 REAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAqnldrfhtFPRLAGECGGKNFHFVHRSADV 329
Cdd:cd07146 171 YEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--------YKRQLLELGGNDPLIVMDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 330 ESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFFSAVID---------------- 393
Cdd:cd07146 243 ERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDP-ATDMGTVIDeeaaiqienrveeaia 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 394 --AK-----------------------------EIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVVQEA 442
Cdd:cd07146 322 qgARvllgnqrqgalyaptvldhvppdaelvteETFGPVAPVIRVKDL--DEAIAISNS-TAYGLSSGVCTNDLDTIKRL 398
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 984655788 443 TKVLRNAAGNfyINDkSTGSIVGQQPFGGARASGTNDKPG 482
Cdd:cd07146 399 VERLDVGTVN--VNE-VPGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
103-476 |
3.40e-34 |
|
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: 134.27 E-value: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 103 NKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKT-MVGQGKTVIQAEIDAAAELIDFFRFNAKYAVE 179
Cdd:cd07112 27 DRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIE--AHRDELALLeTLDMGKPISDALAVDVPSAANTFRWYAEAIDK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 180 LEGQQPiSVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRILREAGLPPNI 258
Cdd:cd07112 105 VYGEVA-PTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALaAGNSVVLKPAEQSPLTALRLAELALEAGLPAGV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 259 IQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDRFHTfprlagECGGKNFHFV-HRSADVESVVSGT 336
Cdd:cd07112 184 LNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWL------ECGGKSPNIVfADAPDLDAAAEAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 337 LRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDAK--------------------- 395
Cdd:cd07112 258 AAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPL-DPATRMGALVSEAhfdkvlgyiesgkaegarlva 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 -------------------------------EIFGPVLSVYVYPDDkyKETLQLVdSTTSYGLTGAVFSQDKDVVQEATK 444
Cdd:cd07112 337 ggkrvltetggffveptvfdgvtpdmriareEIFGPVLSVITFDSE--EEAVALA-NDSVYGLAASVWTSDLSRAHRVAR 413
|
410 420 430
....*....|....*....|....*....|..
gi 984655788 445 VLRnaAGNFYINDKSTGSIvgQQPFGGARASG 476
Cdd:cd07112 414 RLR--AGTVWVNCFDEGDI--TTPFGGFKQSG 441
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
97-476 |
3.75e-34 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 134.62 E-value: 3.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 97 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTvIQ----AEIDAAAELIDFFr 171
Cdd:PRK13252 41 ATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR--ERNDELAALETlDTGKP-IQetsvVDIVTGADVLEYY- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 172 fnAKYAVELEGQQpisVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAMLASYAVYRI 248
Cdd:PRK13252 117 --AGLAPALEGEQ---IPLRGGSFVYTRREplGVCAGIGAWNYPIQIACWKSAPALaAGNAMIFKPSEVTPLTALKLAEI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 249 LREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSAD 328
Cdd:PRK13252 192 YTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKE------VTMELGGKSPLIVFDDAD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 329 VESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP---AEDFG-------------------- 385
Cdd:PRK13252 265 LDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPmdpATNFGplvsfahrdkvlgyiekgka 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 386 -------------------------TFFSAVIDA-----KEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQD 435
Cdd:PRK13252 345 egarllcggerlteggfangafvapTVFTDCTDDmtivrEEIFGPVMSVLTFDDE--DEVIARANDTE-YGLAAGVFTAD 421
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 984655788 436 kdvVQEATKVL-RNAAGNFYINdkSTGSIVGQQPFGGARASG 476
Cdd:PRK13252 422 ---LSRAHRVIhQLEAGICWIN--TWGESPAEMPVGGYKQSG 458
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
88-476 |
4.05e-34 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 134.27 E-value: 4.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GK---TVIQAEIDAA 163
Cdd:PRK13473 27 GEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIE--ENADEFARLESLNcGKplhLALNDEIPAI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 164 aelIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 242
Cdd:PRK13473 105 ---VDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAaGNTVVLKPSEITPLTA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 243 YAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHF 322
Cdd:PRK13473 182 LKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRTHL------ELGGKAPVI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 323 VHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE---DFGTFFSA--------- 390
Cdd:PRK13473 255 VFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDedtELGPLISAahrdrvagf 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 391 ------------------------------VIDAK--------EIFGPVLSVYVYPDDkyKETLQLVDsTTSYGLTGAVF 432
Cdd:PRK13473 335 verakalghirvvtggeapdgkgyyyeptlLAGARqddeivqrEVFGPVVSVTPFDDE--DQAVRWAN-DSDYGLASSVW 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 984655788 433 SQDKDVVQEATKVLRnaAGNFYINDKstGSIVGQQPFGGARASG 476
Cdd:PRK13473 412 TRDVGRAHRVSARLQ--YGCTWVNTH--FMLVSEMPHGGQKQSG 451
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
103-487 |
1.11e-33 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 133.28 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 103 NKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVG-QGKTVIQA--EIDAAAELIDFFrfnAKYAVE 179
Cdd:PLN02278 65 NDAIASAHDAFPSWSKLTASERSKILRRWYDLII--ANKEDLAQLMTLeQGKPLKEAigEVAYGASFLEYF---AEEAKR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 180 LEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTaiggnLA-----GAPALM-GNVVLWKPSDTAMLASYAVYRILREAG 253
Cdd:PLN02278 140 VYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFP-----LAmitrkVGPALAaGCTVVVKPSELTPLTALAAAELALQAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 254 LPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKNFHFVHRSADVESVV 333
Cdd:PLN02278 215 IPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA------TVKRVSLELGGNAPFIVFDDADLDVAV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 334 SGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGD---------------------------------- 379
Cdd:PLN02278 289 KGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDgfeegvtqgplineaavqkveshvqdavskgakv 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 380 -----PAEDFGTFFS----------AVIDAKEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDkdvVQEATK 444
Cdd:PLN02278 369 llggkRHSLGGTFYEptvlgdvtedMLIFREEVFGPVAPLTRFKTE--EEAIAIANDTE-AGLAAYIFTRD---LQRAWR 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 984655788 445 VlrNAAGNFYINDKSTGSIVGQQ-PFGGARASGTNdKPGGPHYI 487
Cdd:PLN02278 443 V--SEALEYGIVGVNEGLISTEVaPFGGVKQSGLG-REGSKYGI 483
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
82-476 |
1.96e-33 |
|
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: 132.27 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAA-RKEWDLK-PIADRAQIFLKAADMLSgpRRAEILAKT-MVGQGKTVIQA 158
Cdd:cd07143 27 YNPST-GKLITKIAEATEADVDIAVEVAHAAfETDWGLKvSGSKRGRCLSKLADLME--RNLDYLASIeALDNGKTFGTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 159 EIDAAAELIDFFRFNAKYAVELEGQQpISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 237
Cdd:cd07143 104 KRVDVQASADTFRYYGGWADKIHGQV-IETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAaGNTIVLKPSEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 238 AMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhTFPRLAGECGG 317
Cdd:cd07143 183 TPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKS-----NLKKVTLELGG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 318 KNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE--------------- 382
Cdd:cd07143 258 KSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAedtfqgpqvsqiqye 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 383 ------------------------DFGTF-----FSAV-----IDAKEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLT 428
Cdd:cd07143 338 rimsyiesgkaegatvetggkrhgNEGYFieptiFTDVtedmkIVKEEIFGPVVAVIKFKTE--EEAIKRANDST-YGLA 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 984655788 429 GAVFSQDkdvVQEATKVlRNA--AGNFYINDKSTgsIVGQQPFGGARASG 476
Cdd:cd07143 415 AAVFTNN---INNAIRV-ANAlkAGTVWVNCYNL--LHHQVPFGGYKQSG 458
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
105-476 |
6.57e-33 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 131.39 E-value: 6.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 105 AIEAALAA-----RKEWDLKPIADRAQiFLKA-ADMLSgpRRAEILAKT-MVGQGKTVIQAE--IDAAAELIDFFrfnAK 175
Cdd:PLN02467 50 AVEAARKAfkrnkGKDWARTTGAVRAK-YLRAiAAKIT--ERKSELAKLeTLDCGKPLDEAAwdMDDVAGCFEYY---AD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 176 YAVELEGQQ--PISVPPST-NSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILRE 251
Cdd:PLN02467 124 LAEALDAKQkaPVSLPMETfKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAaGCTAVLKPSELASVTCLELADICRE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 252 AGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfPrLAGECGGKNFHFVHRSADVES 331
Cdd:PLN02467 204 VGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVK-----P-VSLELGGKSPIIVFDDVDLDK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 332 VVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP-------------------------AEDFGT 386
Cdd:PLN02467 278 AVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPleegcrlgpvvsegqyekvlkfistAKSEGA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 387 ---------------FF-----------SAVIDAKEIFGPVLSVYVYPDDkyKETLQLVDSTTsYGLTGAVFSQDKDVVQ 440
Cdd:PLN02467 358 tilcggkrpehlkkgFFieptiitdvttSMQIWREEVFGPVLCVKTFSTE--DEAIELANDSH-YGLAGAVISNDLERCE 434
|
410 420 430
....*....|....*....|....*....|....*.
gi 984655788 441 EATKVLRnaAGNFYINdkSTGSIVGQQPFGGARASG 476
Cdd:PLN02467 435 RVSEAFQ--AGIVWIN--CSQPCFCQAPWGGIKRSG 466
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
102-476 |
7.60e-33 |
|
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: 129.89 E-value: 7.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 102 LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQA--EIDAAAELIDFFrfnAKYAV 178
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLR--ERKDELARLITLEmGKPIAEAraEVEKCAWICRYY---AENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 179 ELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFT-------AiggnlagAPALM-GNVVLWKPSDTAMLASYAVYRILR 250
Cdd:cd07100 76 AFLADEPIETDAGKAYVRYEPL-GVVLGIMPWNFPfwqvfrfA-------APNLMaGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 251 EAGLPPNIIQFVPADGPLFgDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprlAGECGGKNFHFVHRSADVE 330
Cdd:cd07100 148 EAGFPEGVFQNLLIDSDQV-EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKS------VLELGGSDPFIVLDDADLD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 331 SVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP---------------AEDF----------- 384
Cdd:cd07100 221 KAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPmdedtdlgplarkdlRDELheqveeavaag 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 385 -------------GTFFSAVI--DAK--------EIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDvvqE 441
Cdd:cd07100 301 atlllggkrpdgpGAFYPPTVltDVTpgmpaydeELFGPVAAVIKVKDE--EEAIALAND-SPFGLGGSVFTTDLE---R 374
|
410 420 430
....*....|....*....|....*....|....*...
gi 984655788 442 ATKVLRN-AAGNFYIND--KSTGSIvgqqPFGGARASG 476
Cdd:cd07100 375 AERVARRlEAGMVFINGmvKSDPRL----PFGGVKRSG 408
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
95-476 |
9.97e-33 |
|
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: 130.16 E-value: 9.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 95 CYAD--KSLLNKAIEAALAARKE--WDLKPiADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTVIQA--EIDAAaelI 167
Cdd:cd07120 12 TYADggVAEAEAAIAAARRAFDEtdWAHDP-RLRARVLLELADAFE--ANAERLARLLAlENGKILGEArfEISGA---I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 168 DFFRFNAKYAVELEGQQpISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKP-SDTAMLASyAV 245
Cdd:cd07120 86 SELRYYAGLARTEAGRM-IEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAaGCTVVVKPaGQTAQINA-AI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 246 YRILREA-GLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprlAGECGGKNFHFVH 324
Cdd:cd07120 164 IRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRL------GLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 325 RSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVG---DPAEDF----------------- 384
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGpglDPASDMgplidranvdrvdrmve 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 385 ----------------------GTFF----------SAVIDAKEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVF 432
Cdd:cd07120 318 raiaagaevvlrggpvteglakGAFLrptllevddpDADIVQEEIFGPVLTLETFDDE--AEAVALAND-TDYGLAASVW 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 984655788 433 SQDkdvVQEATKVLRN-AAGNFYINDKstGSIVGQQPFGGARASG 476
Cdd:cd07120 395 TRD---LARAMRVARAiRAGTVWINDW--NKLFAEAEEGGYRQSG 434
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
82-477 |
2.15e-31 |
|
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: 126.69 E-value: 2.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARK---EWDLKPIADRAQIFLKAADMLSgpRRAEILA--KTMVGqGKTVI 156
Cdd:cd07141 27 INPAT-GEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIE--RDRAYLAslETLDN-GKPFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 157 QAEIDAAAELIDFFRFNAKYAVELEGQqpiSVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWK 233
Cdd:cd07141 103 KSYLVDLPGAIKVLRYYAGWADKIHGK---TIPMDGDFFTYTRHEpvGVCGQIIPWNFPLLMAAWKLAPALaCGNTVVLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 234 PSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTfKHLWKQVA--QNLDrfhtfpRL 311
Cdd:cd07141 180 PAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEV-GKLIQQAAgkSNLK------RV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 312 AGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE---DFG--- 385
Cdd:cd07141 253 TLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDpktEQGpqi 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 386 --------------------------------------TFFSAVID----AK-EIFGPVLSVYvypddKYKETLQLVD-- 420
Cdd:cd07141 333 deeqfkkileliesgkkegaklecggkrhgdkgyfiqpTVFSDVTDdmriAKeEIFGPVQQIF-----KFKTIDEVIEra 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 984655788 421 STTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIvgQQPFGGARASGT 477
Cdd:cd07141 408 NNTTYGLAAAVFTKDIDKAITFSNALR--AGTVWVNCYNVVSP--QAPFGGYKMSGN 460
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
97-481 |
3.75e-31 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 125.84 E-value: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 97 ADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAkTMVGQ--GKTVIQAEIDAAAELidffrfnA 174
Cdd:PRK09457 34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLE--ENKEELA-EVIARetGKPLWEAATEVTAMI-------N 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 175 KYAV------ELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYR 247
Cdd:PRK09457 104 KIAIsiqayhERTGEKRSEMADGAAVLRHRPH-GVVAVFGPYNFPGHLPNGHIVPALLaGNTVVFKPSELTPWVAELTVK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 248 ILREAGLPPNIIQFVPAdGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFhtfprLAGECGGKNFHFVHRSA 327
Cdd:PRK09457 183 LWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPEKI-----LALEMGGNNPLVIDEVA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 328 DVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQ-IKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAK----------- 395
Cdd:PRK09457 257 DIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLTVGRWDAEPQPFMGAVISEQaaqglvaaqaq 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 --------------------------------------EIFGPVLSVYVYPDdkYKETLQLVDStTSYGLTGAVFSQDKD 437
Cdd:PRK09457 337 llalggksllemtqlqagtglltpgiidvtgvaelpdeEYFGPLLQVVRYDD--FDEAIRLANN-TRFGLSAGLLSDDRE 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 984655788 438 VVQEATKVLRnaAGNFYINDKSTGSiVGQQPFGGARASGtNDKP 481
Cdd:PRK09457 414 DYDQFLLEIR--AGIVNWNKPLTGA-SSAAPFGGVGASG-NHRP 453
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
104-476 |
1.82e-30 |
|
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: 123.84 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 104 KAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQ-GKTVIQAEIDAAAELIDFFRFNAKYAVEL 180
Cdd:cd07139 40 AAVAAARRAfdNGPWPRLSPAERAAVLRRLADALE--ARADELARLWTAEnGMPISWSRRAQGPGPAALLRYYAALARDF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 181 EGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNII 259
Cdd:cd07139 118 PFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAaGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 260 QFVPADgplfgdtVTSSEHLCG------INFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHRSADVESVV 333
Cdd:cd07139 198 NVVPAD-------REVGEYLVRhpgvdkVSFTGSTAAGRRIAAVCGERLARVTL------ELGGKSAAIVLDDADLDAAV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 334 SGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE------------------------------- 382
Cdd:cd07139 265 PGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDpatqigplasarqrervegyiakgraegarl 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 383 ----------DFGTFF----------SAVIDAKEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvVQEA 442
Cdd:cd07139 345 vtgggrpaglDRGWFVeptlfadvdnDMRIAQEEIFGPVLSVIPYDDE--DDAVRIAND-SDYGLSGSVWTAD---VERG 418
|
410 420 430
....*....|....*....|....*....|....*
gi 984655788 443 TKVLRNA-AGNFYINDKSTGSivgQQPFGGARASG 476
Cdd:cd07139 419 LAVARRIrTGTVGVNGFRLDF---GAPFGGFKQSG 450
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
88-485 |
2.44e-30 |
|
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: 123.66 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGqGKTVIQ---AEIDAAA 164
Cdd:cd07111 47 GEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDN-GKPIREsrdCDIPLVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 165 ELidfFRFNAKYA----VELEGQQPIsvppstnstvyrgleGFVAAISPFNFTAIGGNLAGAPAL-MGNVVLWKPSDTAM 239
Cdd:cd07111 126 RH---FYHHAGWAqlldTELAGWKPV---------------GVVGQIVPWNFPLLMLAWKICPALaMGNTVVLKPAEYTP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 240 LASYAVYRILREAGLPPNIIQFVPADGPlFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQnldrfhTFPRLAGECGGKN 319
Cdd:cd07111 188 LTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAG------TGKKLSLELGGKS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 320 FHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP---AEDFG----------- 385
Cdd:cd07111 261 PFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPldkAIDMGaivdpaqlkri 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 386 ------------------------------TFFSAVIDA-----KEIFGPVLSvyVYPDDKYKETLQLVDStTSYGLTGA 430
Cdd:cd07111 341 relveegraegadvfqpgadlpskgpfyppTLFTNVPPAsriaqEEIFGPVLV--VLTFRTAKEAVALANN-TPYGLAAS 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 984655788 431 VFSQDKDVVQEATKVLRnaAGNFYINdkSTGSIVGQQPFGGARASGTNdKPGGPH 485
Cdd:cd07111 418 VWSENLSLALEVALSLK--AGVVWIN--GHNLFDAAAGFGGYRESGFG-REGGKE 467
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
88-482 |
4.83e-30 |
|
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: 122.60 E-value: 4.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKE--WDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAEIDAAAE 165
Cdd:cd07142 29 GEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLE-KHADELAALETWDNGKPYEQARYAEVPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 166 LIDFFRFNAKYAVELEGqqpISVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLAS 242
Cdd:cd07142 108 AARLFRYYAGWADKIHG---MTLPADGPHHVYTLHEpiGVVGQIIPWNFPLLMFAWKVGPALAcGNTIVLKPAEQTPLSA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 243 YAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDrfhtfpRLAGECGGKNFH 321
Cdd:cd07142 185 LLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNLK------PVTLELGGKSPF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 322 FVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP------------AEDFG---- 385
Cdd:cd07142 259 IVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPfrkgveqgpqvdKEQFEkils 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 386 ----------------------------TFFSAVID-----AKEIFGPVLSVYVYPDdkYKETLQLVDStTSYGLTGAVF 432
Cdd:cd07142 339 yiehgkeegatlitggdrigskgyyiqpTIFSDVKDdmkiaRDEIFGPVQSILKFKT--VDEVIKRANN-SKYGLAAGVF 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 984655788 433 SQDKDVVQEATKVLRnaAGNFYIN--DKSTGSIvgqqPFGGARASGTNDKPG 482
Cdd:cd07142 416 SKNIDTANTLSRALK--AGTVWVNcyDVFDASI----PFGGYKMSGIGREKG 461
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
84-476 |
8.92e-29 |
|
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: 119.10 E-value: 8.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 84 PFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK--TMvGQGKTVIQ---A 158
Cdd:cd07117 23 PAN-GETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIID--ENKELLAMveTL-DNGKPIREtraV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 159 EIDAAAeliDFFRFNAKyAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 237
Cdd:cd07117 99 DIPLAA---DHFRYFAG-VIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAaGNTVVIKPSST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 238 AMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtFPRLAgECGG 317
Cdd:cd07117 175 TSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKL-----IPATL-ELGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 318 KNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE--------------- 382
Cdd:cd07117 248 KSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDpdtqmgaqvnkdqld 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 383 ----------------------------DFGTFFSAVIDA----------KEIFGPVLSVYVYPDDkyKETLQLVDStTS 424
Cdd:cd07117 328 kilsyvdiakeegakiltgghrltenglDKGFFIEPTLIVnvtndmrvaqEEIFGPVATVIKFKTE--DEVIDMAND-SE 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 984655788 425 YGLTGAVFSQDkdvVQEATKVLRNA-AGNFYINdkSTGSIVGQQPFGGARASG 476
Cdd:cd07117 405 YGLGGGVFTKD---INRALRVARAVeTGRVWVN--TYNQIPAGAPFGGYKKSG 452
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
87-475 |
2.37e-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: 117.62 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 87 HGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMV-GQGKTVIQA--EIDAA 163
Cdd:cd07085 25 TGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLE--ENLDELARLITlEHGKTLADArgDVLRG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 164 AELIDffrFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIggnlagAPALM-------GNVVLWKPSD 236
Cdd:cd07085 103 LEVVE---FACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAM------IPLWMfpmaiacGNTFVLKPSE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 237 TAMLASYAVYRILREAGLPPNIIQFVPADgplfGDTVtssEHLC------GINFTGSVPTFKHLWKQVAQNLDRFHTFpr 310
Cdd:cd07085 174 RVPGAAMRLAELLQEAGLPDGVLNVVHGG----KEAV---NALLdhpdikAVSFVGSTPVGEYIYERAAANGKRVQAL-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 311 lageCGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVG---DPAEDFG-- 385
Cdd:cd07085 245 ----GGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGagdDPGADMGpv 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 386 -------------------------------------------TFFSAV-IDAK----EIFGPVLSVyVYPDDkYKETLQ 417
Cdd:cd07085 321 ispaakeriegliesgveegaklvldgrgvkvpgyengnfvgpTILDNVtPDMKiykeEIFGPVLSI-VRVDT-LDEAIA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984655788 418 LVDStTSYGLTGAVFSQDKDVvqeATKVLRNA-AGNFYINdkstgsI-----VGQQPFGGARAS 475
Cdd:cd07085 399 IINA-NPYGNGAAIFTRSGAA---ARKFQREVdAGMVGIN------VpipvpLAFFSFGGWKGS 452
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
82-478 |
4.38e-28 |
|
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: 116.75 E-value: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNHGHkVAKFCYADKSLLNKAIEAALAA---RKEWdlKPIADRAQIFLKAADMLSGprRAEILAKTMVGQG-KTVIQ 157
Cdd:cd07148 4 VNPFDLKP-IGEVPTVDWAAIDKALDTAHALfldRNNW--LPAHERIAILERLADLMEE--RADELALLIAREGgKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 158 A--EIDAAaelIDFFRFNAKYAVELEGQQ-PISV-PPSTNSTVYRGLE--GFVAAISPFNFTAiggNLA---GAPAL-MG 227
Cdd:cd07148 79 AkvEVTRA---IDGVELAADELGQLGGREiPMGLtPASAGRIAFTTREpiGVVVAISAFNHPL---NLIvhqVAPAIaAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 228 NVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEhLCGINFTGSVPTFKHLWKQVAQNldrfht 307
Cdd:cd07148 153 CPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPR-VAFFSFIGSARVGWMLRSKLAPG------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 308 fPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPA------ 381
Cdd:cd07148 226 -TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTdpdtev 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 382 ------------EDF--------------------GTFFSAVI-----DAK----EIFGPVLSVYVYpdDKYKETLQLVD 420
Cdd:cd07148 305 gplirprevdrvEEWvneavaagarllcggkrlsdTTYAPTVLldpprDAKvstqEIFGPVVCVYSY--DDLDEAIAQAN 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 984655788 421 StTSYGLTGAVFSQDKDVVQEATKVLrnAAGNFYINDKsTGSIVGQQPFGGARASGTN 478
Cdd:cd07148 383 S-LPVAFQAAVFTKDLDVALKAVRRL--DATAVMVNDH-TAFRVDWMPFAGRRQSGYG 436
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
140-476 |
1.57e-27 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 114.45 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 140 RAEILAKTMVG-QGKTVIQAEIDAAAElIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFT--AIG 216
Cdd:PRK10090 11 RASEISALIVEeGGKIQQLAEVEVAFT-ADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPffLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 217 GNLAgaPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLW 295
Cdd:PRK10090 90 RKMA--PALLtGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 296 KQVAQNLdrfhtfPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRI 375
Cdd:PRK10090 168 AAAAKNI------TKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 376 KVGDPAE----DFGTFFSA--------------------------------------VIDAK--------EIFGPVLSVY 405
Cdd:PRK10090 242 QFGNPAErndiAMGPLINAaalerveqkvaraveegarvalggkavegkgyyypptlLLDVRqemsimheETFGPVLPVV 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 984655788 406 VYpdDKYKETLQLVDStTSYGLTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSIvgqQPF-GGARASG 476
Cdd:PRK10090 322 AF--DTLEEAIAMAND-SDYGLTSSIYTQNLNVAMKAIKGLK--FGETYINRENFEAM---QGFhAGWRKSG 385
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
82-476 |
2.34e-27 |
|
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: 114.75 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK--TMvGQGKTV---I 156
Cdd:cd07559 21 YNPVN-GKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIE--ENLELLAVaeTL-DNGKPIretL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 157 QAEIDAAaelIDFFRFNAKYAVELEGQqpIS-VPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKP 234
Cdd:cd07559 97 AADIPLA---IDHFRYFAGVIRAQEGS--LSeIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAaGNTVVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 235 SDTAMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLdrfhtFPrLAGE 314
Cdd:cd07559 172 ASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENL-----IP-VTLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 315 CGGK--NFHFvhrsADVES--------VVSGTLRSAFEYgGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDf 384
Cdd:cd07559 245 LGGKspNIFF----DDAMDadddfddkAEEGQLGFAFNQ-GEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDP- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 385 GTFFSAVIDAK------------------------------------------------------EIFGPVLSVYVYPDD 410
Cdd:cd07559 319 ETMMGAQVSKDqlekilsyvdigkeegaevltggerltlggldkgyfyeptlikggnndmrifqeEIFGPVLAVITFKDE 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 984655788 411 kyKETLQLVDStTSYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINdkSTGSIVGQQPFGGARASG 476
Cdd:cd07559 399 --EEAIAIAND-TEYGLGGGVWTRD---INRALRVARGiQTGRVWVN--CYHQYPAHAPFGGYKKSG 457
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
104-484 |
1.11e-26 |
|
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: 112.78 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 104 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK-TMVGQGKTVIQA---EIDAAAELIDFFRFNAKYAVe 179
Cdd:cd07098 22 EAIAAARAAQREWAKTSFAERRKVLRSLLKYIL--ENQEEICRvACRDTGKTMVDAslgEILVTCEKIRWTLKHGEKAL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 180 legqQPISVPPSTNsTVYRGLE------GFVAAISPFNF---TAIGGNLAgapALM-GNVVLWKPSDTAMLASYAVYRIL 249
Cdd:cd07098 99 ----RPESRPGGLL-MFYKRARveyeplGVVGAIVSWNYpfhNLLGPIIA---ALFaGNAIVVKVSEQVAWSSGFFLSII 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 250 REA----GLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDrfhtfPRLAgECGGKNFHFVHR 325
Cdd:cd07098 171 REClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAESLT-----PVVL-ELGGKDPAIVLD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 326 SADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE---DFGTFFSA---------VID 393
Cdd:cd07098 244 DADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDgdvDVGAMISParfdrleelVAD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 394 A-----------------------------------------KEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVF 432
Cdd:cd07098 324 AvekgarllaggkryphpeypqghyfpptllvdvtpdmkiaqEEVFGPVMVVMKASDD--EEAVEIANS-TEYGLGASVF 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 984655788 433 SQDKDVVQEATKVLRnaAGNFYINDKSTGSIVGQQPFGGARASGTnDKPGGP 484
Cdd:cd07098 401 GKDIKRARRIASQLE--TGMVAINDFGVNYYVQQLPFGGVKGSGF-GRFAGE 449
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
82-383 |
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: 111.53 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPiadraqiflkaadmlsGPRRAEIL---------AKTMVGQ- 151
Cdd:cd07130 17 ISPAN-GEPIARVRQATPEDYESTIKAAQEAFKEWRDVP----------------APKRGEIVrqigdalrkKKEALGKl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 152 -----GKTVIQA--EIDaaaELIDFfrfnAKYAVELEGQQPISVPPSTNSTvYRGLE-----GFVAAISPFNF-TAIGG- 217
Cdd:cd07130 80 vslemGKILPEGlgEVQ---EMIDI----CDFAVGLSRQLYGLTIPSERPG-HRMMEqwnplGVVGVITAFNFpVAVWGw 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 218 NLAGApALMGNVVLWKPSDTAMLASYAVYRI----LREAGLPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVptfkH 293
Cdd:cd07130 152 NAAIA-LVCGNVVVWKPSPTTPLTAIAVTKIvarvLEKNGLPGAIASLVCGGADV-GEALVKDPRVPLVSFTGST----A 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 294 LWKQVAQNLDRfhTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHS 373
Cdd:cd07130 226 VGRQVGQAVAA--RFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYK 303
|
330
....*....|
gi 984655788 374 RIKVGDPAED 383
Cdd:cd07130 304 QVRIGDPLDD 313
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
88-482 |
1.32e-25 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 110.28 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKE--WDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAeidAAAE 165
Cdd:PLN02466 83 GEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLE-KHNDELAALETWDNGKPYEQS---AKAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 166 L---IDFFRFNAKYAVELEGqqpISVPPSTNSTVYRGLE--GFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAM 239
Cdd:PLN02466 159 LpmfARLFRYYAGWADKIHG---LTVPADGPHHVQTLHEpiGVAGQIIPWNFPLLMFAWKVGPALAcGNTIVLKTAEQTP 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 240 LASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFprlagECGGKN 319
Cdd:PLN02466 236 LSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTL-----ELGGKS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 320 FHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQI----KGRLLeehsRIKVGDP--------------- 380
Cdd:PLN02466 311 PFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFvekaKARAL----KRVVGDPfkkgveqgpqidseq 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 381 ---------------------AEDFG--------TFFSAV-----IDAKEIFGPVLSVYvypddKYKETLQLVD--STTS 424
Cdd:PLN02466 387 fekilryiksgvesgatlecgGDRFGskgyyiqpTVFSNVqddmlIAQDEIFGPVQSIL-----KFKDLDEVIRraNNTR 461
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 425 YGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN--DKSTGSIvgqqPFGGARASGTNDKPG 482
Cdd:PLN02466 462 YGLAAGVFTQNLDTANTLSRALR--VGTVWVNcfDVFDAAI----PFGGYKMSGIGREKG 515
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
102-496 |
1.91e-25 |
|
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: 108.86 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 102 LNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSgPRRAEILAKTMVGQGKTVIQAEiDAAAeliDFFRFNAKYAVELE 181
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLA-AKSYDIAAGAVLVTGKGWMFAE-NICG---DQVQLRARAFVIYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 182 GQQP------ISVPPSTNSTVYRGLEGFVAAISPFNF--TAIGGNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAG 253
Cdd:cd07084 76 YRIPhepgnhLGQGLKQQSHGYRWPYGPVLVIGAFNFplWIPLLQLAGALA-MGNPVIVKPHTAVSIVMQIMVRLLHYAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 254 -LPPNIIQFVPADGPLfGDTVTSSEHLCGINFTGSVptfkhlwkQVAQNLDRFHTFPRLAGECGGKNFHFVHRSAD-VES 331
Cdd:cd07084 155 lLPPEDVTLINGDGKT-MQALLLHPNPKMVLFTGSS--------RVAEKLALDAKQARIYLELAGFNWKVLGPDAQaVDY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 332 VVSGTLRSAFEYGGQKCSACSRLYVPHS---------------------------LWPQIKGRL--LEEHSRIKVG---- 378
Cdd:cd07084 226 VAWQCVQDMTACSGQKCTAQSMLFVPENwsktplveklkallarrkledlllgpvQTFTTLAMIahMENLLGSVLLfsgk 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 379 -DPAEDFGTFFSA--------VIDA---------KEIFGPVLSVYVYPDDKYKETLQLVDSTTSYgLTGAVFSQDKDVVQ 440
Cdd:cd07084 306 eLKNHSIPSIYGAcvasalfvPIDEilktyelvtEEIFGPFAIVVEYKKDQLALVLELLERMHGS-LTAAIYSNDPIFLQ 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 984655788 441 EATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVI 496
Cdd:cd07084 385 ELIGNLWVAGRTYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAIKLVWRCHAE 440
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
104-476 |
6.47e-23 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 101.52 E-value: 6.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 104 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTM-VGQGKTVIQA--EIDAAAELIDFFRFNAK--YAV 178
Cdd:PRK11241 52 AAIDAANRALPAWRALTAKERANILRRWFNLMM--EHQDDLARLMtLEQGKPLAEAkgEISYAASFIEWFAEEGKriYGD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 179 ELEGQQPisvppSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPN 257
Cdd:PRK11241 130 TIPGHQA-----DKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAaGCTMVLKPASQTPFSALALAELAIRAGIPAG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 258 IIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGECGGKNFHFVHRSADVESVVSGTL 337
Cdd:PRK11241 205 VFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK------VSLELGGNAPFIVFDDADLDKAVEGAL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 338 RSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAED---------------------------------- 383
Cdd:PRK11241 279 ASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKgvtigplidekavakveehiadalekgarvvcgg 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 384 -----FGTFFSAVI------DAK----EIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDkdvvqeATKVLRN 448
Cdd:PRK11241 359 kahelGGNFFQPTIlvdvpaNAKvakeETFGPLAPLFRFKDE--ADVIAQAND-TEFGLAAYFYARD------LSRVFRV 429
|
410 420 430
....*....|....*....|....*....|
gi 984655788 449 A-AGNFYINDKSTGSIVGQ-QPFGGARASG 476
Cdd:PRK11241 430 GeALEYGIVGINTGIISNEvAPFGGIKASG 459
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
102-496 |
4.50e-21 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 96.12 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 102 LNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMvGQGKTV---IQAEIDAAAELIdffRFNAKY 176
Cdd:PRK09847 59 IDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETL-DTGKPIrhsLRDDIPGAARAI---RWYAEA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 177 AVELEGQqpisVPPSTN---STVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAMLASYAVYRILREA 252
Cdd:PRK09847 135 IDKVYGE----VATTSShelAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAaGNSVILKPSEKSPLSAIRLAGLAKEA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 253 GLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhTFPRLAGECGGKNFHFVHRSA-DVES 331
Cdd:PRK09847 211 GLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDS-----NMKRVWLEAGGKSANIVFADCpDLQQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 332 VVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAeDFGTFFSAVIDA----------------- 394
Cdd:PRK09847 286 AASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPL-DPATTMGTLIDCahadsvhsfiregeskg 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 395 -------------------------------KEIFGPVLSVYVYPDDkyKETLQLVDStTSYGLTGAVFSQDKDVVQEAT 443
Cdd:PRK09847 365 qllldgrnaglaaaigptifvdvdpnaslsrEEIFGPVLVVTRFTSE--EQALQLAND-SQYGLGAAVWTRDLSRAHRMS 441
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 984655788 444 KVLRnaAGNFYINDKSTGSIVgqQPFGGARASGtNDKPGGPHYILRWTSPQVI 496
Cdd:PRK09847 442 RRLK--AGSVFVNNYNDGDMT--VPFGGYKQSG-NGRDKSLHALEKFTELKTI 489
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
88-476 |
9.25e-21 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 95.27 E-value: 9.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAA--RKEWDLKPIADRAQIFLKAADMLSgpRRAEILAK-------TMVGQGKTViqa 158
Cdd:PLN02766 46 GEVIARIAEGDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIE--EHIEELAAldtidagKLFALGKAV--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 159 EIDAAAELidfFRFNAKYAVELEGQQpISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWKPSDT 237
Cdd:PLN02766 121 DIPAAAGL---LRYYAGAADKIHGET-LKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAaGCTMVVKPAEQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 238 AMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ-NLDRfhtfprLAGECG 316
Cdd:PLN02766 197 TPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNLKQ------VSLELG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 317 GKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE-------------- 382
Cdd:PLN02766 271 GKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDprarqgpqvdkqqf 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 383 -------DFG-----------------------TFFSAV-----IDAKEIFGPVLSVYvypddKYK---ETLQLVDStTS 424
Cdd:PLN02766 351 ekilsyiEHGkregatlltggkpcgdkgyyiepTIFTDVtedmkIAQDEIFGPVMSLM-----KFKtveEAIKKANN-TK 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 984655788 425 YGLTGAVFSQDKDVVQEATKVLRnaAGNFYIN-----DKSTgsivgqqPFGGARASG 476
Cdd:PLN02766 425 YGLAAGIVTKDLDVANTVSRSIR--AGTIWVNcyfafDPDC-------PFGGYKMSG 472
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
88-476 |
4.28e-18 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 86.72 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 88 GHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAeiLAKTMVGQ-GKTVIQAEIDAAaEL 166
Cdd:PRK09406 11 GETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQ--VAALMTLEmGKTLASAKAEAL-KC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 167 IDFFRFNAKYAVELEGQQPISVPPSTNS---TVYRGLeGFVAAISPFNFTAIGGNLAGAPALM-GNVVLWK-PSDTAMLA 241
Cdd:PRK09406 88 AKGFRYYAEHAEALLADEPADAAAVGASrayVRYQPL-GVVLAVMPWNFPLWQVVRFAAPALMaGNVGLLKhASNVPQTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 242 SYaVYRILREAGLPPNIIQ--FVPADGPlfgDTVTSSEHLCGINFTGSVPTfkhlWKQVAQnldrfhtfprLAG------ 313
Cdd:PRK09406 167 LY-LADLFRRAGFPDGCFQtlLVGSGAV---EAILRDPRVAAATLTGSEPA----GRAVAA----------IAGdeikkt 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 314 --ECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAE---DFGTFF 388
Cdd:PRK09406 229 vlELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDpdtDVGPLA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 389 SA---------VIDA-------------------------------------KEIFGPVLSVYVYPDdkYKETLQLVDST 422
Cdd:PRK09406 309 TEqgrdevekqVDDAvaagatilcggkrpdgpgwfypptvitditpdmrlytEEVFGPVASLYRVAD--IDEAIEIANAT 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 984655788 423 TsYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINDKSTGSivGQQPFGGARASG 476
Cdd:PRK09406 387 T-FGLGSNAWTRD---EAEQERFIDDlEAGQVFINGMTVSY--PELPFGGVKRSG 435
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
75-437 |
7.34e-18 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 86.35 E-value: 7.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 75 TSDVQYQVSPfnhghkvakfCYADKslLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRR--AEILAKTMVGQG 152
Cdd:PLN00412 40 TRKTQYKVQA----------CTQEE--VNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKApiAECLVKEIAKPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 153 KTVIqAEIDAAAELIDffrfnakYAVElEGQQPISVPPSTNSTVYRGLE------------GFVAAISPFNFTAiggNLA 220
Cdd:PLN00412 108 KDAV-TEVVRSGDLIS-------YTAE-EGVRILGEGKFLVSDSFPGNErnkycltskiplGVVLAIPPFNYPV---NLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 221 G---APALM-GNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSvptfkhlwk 296
Cdd:PLN00412 176 VskiAPALIaGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG--------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 297 qvaqnlDRFHTFPRLAG------ECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLE 370
Cdd:PLN00412 247 ------DTGIAISKKAGmvplqmELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 371 EHSRIKVGDPAEDFG-----TFFSA------VIDAK----------------------------------EIFGPVLSVY 405
Cdd:PLN00412 321 KVAKLTVGPPEDDCDitpvvSESSAnfieglVMDAKekgatfcqewkregnliwpllldnvrpdmriaweEPFGPVLPVI 400
|
410 420 430
....*....|....*....|....*....|..
gi 984655788 406 VYPDDkyKETLQLVDStTSYGLTGAVFSQDKD 437
Cdd:PLN00412 401 RINSV--EEGIHHCNA-SNFGLQGCVFTRDIN 429
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
82-476 |
1.46e-17 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 85.30 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQiflKAADMLSGPR-RAEILAKTMVGQ-GKTVIQA- 158
Cdd:PRK13968 12 VNPAT-GEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQ---KLRDIGKALRaRSEEMAQMITREmGKPINQAr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 159 -EIDAAAELIDFFrfnAKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNFtAIGGNLAGA-PALM-GNVVLWKPS 235
Cdd:PRK13968 88 aEVAKSANLCDWY---AEHGPAMLKAEPTLVENQQAVIEYRPL-GTILAIMPWNF-PLWQVMRGAvPILLaGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 236 DTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEhLCGINFTGSVPTFKHLWKQVAQNLDRfhtfprLAGEC 315
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIGAQAGAALKK------CVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 316 GGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDP--AEDF--------- 384
Cdd:PRK13968 236 GGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPrdEENAlgpmarfdl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 385 ----------------------------GTFFSAVIDA----------KEIFGPVLSVYVYPDDKYkeTLQLVDStTSYG 426
Cdd:PRK13968 316 rdelhhqveatlaegarlllggekiagaGNYYAPTVLAnvtpemtafrEELFGPVAAITVAKDAEH--ALELAND-SEFG 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 984655788 427 LTGAVFSQDKDVVQEATKVLRnaAGNFYINDKSTGSivGQQPFGGARASG 476
Cdd:PRK13968 393 LSATIFTTDETQARQMAARLE--CGGVFINGYCASD--ARVAFGGVKKSG 438
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
74-476 |
4.18e-17 |
|
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: 83.66 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 74 WTSDV--QY--QVSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTmV 149
Cdd:cd07116 9 WVAPVkgEYfdNITPVT-GKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAET-W 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 150 GQGKTV---IQAEIDAAaelIDFFRFNAKYAVELEGqqpiSVPPSTNSTV-YRGLE--GFVAAISPFNFTAIGGNLAGAP 223
Cdd:cd07116 87 DNGKPVretLAADIPLA---IDHFRYFAGCIRAQEG----SISEIDENTVaYHFHEplGVVGQIIPWNFPLLMATWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 224 ALM-GNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNL 302
Cdd:cd07116 160 ALAaGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 303 drfhtFPrLAGECGGK--NFHF----VHRSADVESVVSGTLRSAFEYgGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIK 376
Cdd:cd07116 239 -----IP-VTLELGGKspNIFFadvmDADDAFFDKALEGFVMFALNQ-GEVCTCPSRALIQESIYDRFMERALERVKAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 377 VGDPAE---------------------DFG----------------------------TFF---SAVIDAKEIFGPVLSV 404
Cdd:cd07116 312 QGNPLDtetmigaqasleqlekilsyiDIGkeegaevltggernelggllgggyyvptTFKggnKMRIFQEEIFGPVLAV 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984655788 405 YVYPDdkYKETLQLVDSTTsYGLTGAVFSQDkdvVQEATKVLRN-AAGNFYINdkSTGSIVGQQPFGGARASG 476
Cdd:cd07116 392 TTFKD--EEEALEIANDTL-YGLGAGVWTRD---GNTAYRMGRGiQAGRVWTN--CYHLYPAHAAFGGYKQSG 456
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
104-482 |
2.25e-16 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 81.80 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 104 KAIEAALAARKEWDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVGQGKTVIQAEIDAAAELIDFfrfnAKYAVELEGQ 183
Cdd:PLN02315 60 EGLRACEEAAKIWMQVPAPKRGEIVRQIGDALR--AKLDYLGRLVSLEMGKILAEGIGEVQEIIDM----CDFAVGLSRQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 184 QPISVPPSTNST-----VYRGLeGFVAAISPFNF-TAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRI----LREAG 253
Cdd:PLN02315 134 LNGSIIPSERPNhmmmeVWNPL-GIVGVITAFNFpCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLvaevLEKNN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 254 LPPNIIQFVpADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNldrfhtFPRLAGECGGKNFHFVHRSADVESVV 333
Cdd:PLN02315 213 LPGAIFTSF-CGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR------FGKCLLELSGNNAIIVMDDADIQLAV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 334 SGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDfGTFF------------------------- 388
Cdd:PLN02315 286 RSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEK-GTLLgplhtpeskknfekgieiiksqggk 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 389 ------------------------SAVIDAKEIFGPVLsvYVYPDDKYKETLQLVDSTTSyGLTGAVFSQDKDVVQEATK 444
Cdd:PLN02315 365 iltggsaiesegnfvqptiveispDADVVKEELFGPVL--YVMKFKTLEEAIEINNSVPQ-GLSSSIFTRNPETIFKWIG 441
|
410 420 430
....*....|....*....|....*....|....*...
gi 984655788 445 VLRNAAGNFYINDKSTGSIVGQQpFGGARASGTNDKPG 482
Cdd:PLN02315 442 PLGSDCGIVNVNIPTNGAEIGGA-FGGEKATGGGREAG 478
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
202-477 |
9.36e-12 |
|
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: 66.86 E-value: 9.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 202 GFVAAISPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFVPADGPLFGDTVTSS-E 277
Cdd:cd07135 110 GVVLIIGPWNYpvlLALS-PLVGAIA-AGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALLEQKfD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 278 HlcgINFTGSVPTFKHLWKQVAQNLDrfhtfPrLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVP 357
Cdd:cd07135 187 K---IFYTGSGRVGRIIAEAAAKHLT-----P-VTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 358 HS---------------LWPQ-------------------IKGRLLEEHSRIKVGDPAEDFGTFF--SAVIDAK------ 395
Cdd:cd07135 258 PSvydefveelkkvldeFYPGganaspdytrivnprhfnrLKSLLDTTKGKVVIGGEMDEATRFIppTIVSDVSwddslm 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 396 --EIFGPVLSVYVYPD-DKYKETLQLVDSTtsygLTGAVFSQDKDVVQeatKVL-RNAAGNFYINDKSTGSIVGQQPFGG 471
Cdd:cd07135 338 seELFGPVLPIIKVDDlDEAIKVINSRDTP----LALYIFTDDKSEID---HILtRTRSGGVVINDTLIHVGVDNAPFGG 410
|
....*.
gi 984655788 472 ARASGT 477
Cdd:cd07135 411 VGDSGY 416
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
103-396 |
1.12e-11 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 67.08 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 103 NKAIEAALAARKE----WDLKPIADRAQIFLKAADMLSgpRRAEILAKTMVG-QGKTVIQAEIDAAAELiDFFRFNAKYA 177
Cdd:PLN02419 150 NEEFKAAVSAAKQafplWRNTPITTRQRVMLKFQELIR--KNMDKLAMNITTeQGKTLKDSHGDIFRGL-EVVEHACGMA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 178 VELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIggnlagAPALM-------GNVVLWKPSDTAMLASYAVYRILR 250
Cdd:PLN02419 227 TLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAM------IPLWMfpvavtcGNTFILKPSEKDPGASVILAELAM 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 251 EAGLPPNIIQFVPADGplfgDTVTS---SEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTfprlagECGGKNFHFVHRSA 327
Cdd:PLN02419 301 EAGLPDGVLNIVHGTN----DTVNAicdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQS------NMGAKNHGLVLPDA 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984655788 328 DVESVVSGTLRSAFEYGGQKCSACSRLYV--PHSLWpqiKGRLLEEHSRIKV---GDPAEDFGTFFSAviDAKE 396
Cdd:PLN02419 371 NIDATLNALLAAGFGAAGQRCMALSTVVFvgDAKSW---EDKLVERAKALKVtcgSEPDADLGPVISK--QAKE 439
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
154-476 |
1.42e-11 |
|
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: 66.40 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 154 TVIQAEIDAAAELIDffrfnaKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNF---TAIGgNLAGAPAlMGNVV 230
Cdd:cd07087 61 AVVLGEIDHALKHLK------KWMKPRRVSVPLLLQPAKAYVIPEPL-GVVLIIGPWNYplqLALA-PLIGAIA-AGNTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 231 LWKPSDTAMLASYAVYRILREAgLPPNIIQFVPADGPlfgdtVTS---SEHLCGINFTGSVPTFKHLWKQVAQNLdrfhT 307
Cdd:cd07087 132 VLKPSELAPATSALLAKLIPKY-FDPEAVAVVEGGVE-----VATallAEPFDHIFFTGSPAVGKIVMEAAAKHL----T 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 308 FPRLagECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSlwpqIKGRLLEEHSR-IKV---GDPAE- 382
Cdd:cd07087 202 PVTL--ELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHES----IKDELIEELKKaIKEfygEDPKEs 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 383 -DFGTFFSA--------------------------------VIDAK--------EIFGPVLSVYVYPDdkYKETLQLVDS 421
Cdd:cd07087 276 pDYGRIINErhfdrlasllddgkvviggqvdkeeryiaptiLDDVSpdsplmqeEIFGPILPILTYDD--LDEAIEFINS 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 984655788 422 tTSYGLTGAVFSQDKDVVQeatKVLRN-AAGNFYINDKSTGSIVGQQPFGGARASG 476
Cdd:cd07087 354 -RPKPLALYLFSEDKAVQE---RVLAEtSSGGVCVNDVLLHAAIPNLPFGGVGNSG 405
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
184-476 |
1.67e-10 |
|
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: 63.01 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 184 QPISVPPS-----TNSTVYRGLEGFVAAISPFNF---TAIGgNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAglp 255
Cdd:cd07134 79 KPKRVRTPlllfgTKSKIRYEPKGVCLIISPWNYpfnLAFG-PLVSAIA-AGNTAILKPSELTPHTSAVIAKIIREA--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 256 pniiqFVPADGPLF-GDTVTSSE-------HlcgINFTGSVPTFKHLWKQVAQNLdrfhTFPRLagECGGKNFHFVHRSA 327
Cdd:cd07134 154 -----FDEDEVAVFeGDAEVAQAllelpfdH---IFFTGSPAVGKIVMAAAAKHL----ASVTL--ELGGKSPTIVDETA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 328 DVESVVSGTLRSAFEYGGQKCSACSRLYVPHSlwpqIKGRLLEE-----------------------------HSRIK-- 376
Cdd:cd07134 220 DLKKAAKKIAWGKFLNAGQTCIAPDYVFVHES----VKDAFVEHlkaeiekfygkdaarkaspdlarivndrhFDRLKgl 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 377 ------------VG---DPAEDF--GTFFSAV-----IDAKEIFGPVLSVYVYPD-DkyketlQLVDSTTSYG--LTGAV 431
Cdd:cd07134 296 lddavakgakveFGgqfDAAQRYiaPTVLTNVtpdmkIMQEEIFGPVLPIITYEDlD------EVIEYINAKPkpLALYV 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 984655788 432 FSQDKDVVQeatKVLRN-AAGNFYINDkstgSIV----GQQPFGGARASG 476
Cdd:cd07134 370 FSKDKANVN---KVLARtSSGGVVVND----VVLhflnPNLPFGGVNNSG 412
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
190-476 |
1.33e-09 |
|
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: 60.19 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 190 PSTNSTVYRGLeGFVAAISPFNF---TAIGGnLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFV---P 263
Cdd:cd07133 92 PAKAEVEYQPL-GVVGIIVPWNYplyLALGP-LIAALA-AGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEVAVVtggA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 264 ADGPLFgdtvtSS---EHLCginFTGSVPTFKHLWKQVAQNLdrfhTFPRLagECGGKNFHFVHRSADVESVVSGTLRSA 340
Cdd:cd07133 168 DVAAAF-----SSlpfDHLL---FTGSTAVGRHVMRAAAENL----TPVTL--ELGGKSPAIIAPDADLAKAAERIAFGK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 341 FEYGGQKCSACSRLYVP---------------HSLWPQIKG-----------------RLLEEHSR-----IKVGDPAED 383
Cdd:cd07133 234 LLNAGQTCVAPDYVLVPedkleefvaaakaavAKMYPTLADnpdytsiinerhyarlqGLLEDARAkgarvIELNPAGED 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 384 FGTF----FSAVIDAK--------EIFGPVLSVYVYpdDKYKETLQLVDSTTS----YgltgaVFSQDKdvvQEATKVLR 447
Cdd:cd07133 314 FAATrklpPTLVLNVTddmrvmqeEIFGPILPILTY--DSLDEAIDYINARPRplalY-----YFGEDK---AEQDRVLR 383
|
330 340 350
....*....|....*....|....*....|..
gi 984655788 448 N-AAGNFYINDksTGSIVGQ--QPFGGARASG 476
Cdd:cd07133 384 RtHSGGVTIND--TLLHVAQddLPFGGVGASG 413
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
155-476 |
2.41e-09 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 59.66 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 155 VIQAEIDAAAELIDffrfnaKYAVELEGQQPISVPPSTNSTVYRGLeGFVAAISPFNF---TAIGgNLAGAPAlMGNVVL 231
Cdd:PTZ00381 71 LTVAEIEHLLKHLD------EYLKPEKVDTVGVFGPGKSYIIPEPL-GVVLVIGAWNYplnLTLI-PLAGAIA-AGNTVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 232 WKPSDTAMLASYAVYRILREAgLPPNIIQFVPADgplfgdtVTSSEHLCG-----INFTGSVPTFKHLWKQVAQNLdrfh 306
Cdd:PTZ00381 142 LKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGG-------VEVTTELLKepfdhIFFTGSPRVGKLVMQAAAENL---- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 307 TFPRLagECGGKNFHFVHRSADV----ESVVSGTLRSAfeygGQKCSACSRLYVPHSlwpqIKGRLLEE----------- 371
Cdd:PTZ00381 210 TPCTL--ELGGKSPVIVDKSCNLkvaaRRIAWGKFLNA----GQTCVAPDYVLVHRS----IKDKFIEAlkeaikeffge 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 372 -------HSRIKVGDPAEDFGTFFSAV--------------------------IDAK----EIFGPVLSVYVYPDdkYKE 414
Cdd:PTZ00381 280 dpkksedYSRIVNEFHTKRLAELIKDHggkvvyggevdienkyvaptiivnpdLDSPlmqeEIFGPILPILTYEN--IDE 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984655788 415 TLQLVDStTSYGLTGAVFSQDKDVVQeatKVLRN-AAGNFYINDKSTGSIVGQQPFGGARASG 476
Cdd:PTZ00381 358 VLEFINS-RPKPLALYYFGEDKRHKE---LVLENtSSGAVVINDCVFHLLNPNLPFGGVGNSG 416
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
82-492 |
1.36e-07 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 54.04 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 82 VSPFNhGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIA--DRAQ----IFLKAADMLSGPRRAEILAK-TMVGQGKT 154
Cdd:cd07126 17 LDPLN-GDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKnpERYLlygdVSHRVAHELRKPEVEDFFARlIQRVAPKS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 155 VIQA--EIDAAAELIDFF-----RFNAK-YAV--ELEGQQpisvppstnSTVYRGLEGFVAAISPFNFT----AIggNLA 220
Cdd:cd07126 96 DAQAlgEVVVTRKFLENFagdqvRFLARsFNVpgDHQGQQ---------SSGYRWPYGPVAIITPFNFPleipAL--QLM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 221 GApALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCgINFTGSvptfkhlwKQVAQ 300
Cdd:cd07126 165 GA-LFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRM-TLFTGS--------SKVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 301 NLDRfHTFPRLAGECGGKNFHFVHRS-ADVESVVSGTLRSAFEYGGQKCSACSRLYVpHSLWPQ------IK-------- 365
Cdd:cd07126 235 RLAL-ELHGKVKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFA-HENWVQagildkLKalaeqrkl 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 366 ----------------------------------GRLLEEHSRIKVGDPAEDFGTF-----------FSAVidAKEIFGP 400
Cdd:cd07126 313 edltigpvltwtterildhvdkllaipgakvlfgGKPLTNHSIPSIYGAYEPTAVFvpleeiaieenFELV--TTEVFGP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 401 VLSVYVYPDDKYKETLQLVDSTTSYgLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQ--QPFGGARASGTn 478
Cdd:cd07126 391 FQVVTEYKDEQLPLVLEALERMHAH-LTAAVVSNDIRFLQEVLANTVNGTTYAGIRARTTGAPQNHwfGPAGDPRGAGI- 468
|
490
....*....|....*
gi 984655788 479 dkpGGPHYI-LRWTS 492
Cdd:cd07126 469 ---GTPEAIrLVWSC 480
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
202-476 |
1.83e-07 |
|
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: 53.28 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 202 GFVAAISPFN--FTAIGGNLAGAPAlMGNVVLWKPSDTAMLASYAVYRILREAgLPPNIIQFVPadgplfGDTVTSSEHL 279
Cdd:cd07136 102 GVVLIIAPWNypFQLALAPLIGAIA-AGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVE------GGVEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 280 CG----INFTGSVPTFKHLWKQVAQNLdrfhTFPRLagECGGKNFHFVHRSADVE----SVVSGTLRSAfeygGQKCSAC 351
Cdd:cd07136 174 DQkfdyIFFTGSVRVGKIVMEAAAKHL----TPVTL--ELGGKSPCIVDEDANLKlaakRIVWGKFLNA----GQTCVAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 352 SRLYVPHSlwpqIKGRLLEE------------------HSRI----------------KV-----GDPAE--------DF 384
Cdd:cd07136 244 DYVLVHES----VKEKFIKElkeeikkfygedplespdYGRIinekhfdrlaglldngKIvfggnTDRETlyieptilDN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 385 GTFFSAVIDaKEIFGPVLSVYVYpdDKYKETLQLVDStTSYGLTGAVFSQDKDVvqeATKVLRNAA-GNFYINDKSTGSI 463
Cdd:cd07136 320 VTWDDPVMQ-EEIFGPILPVLTY--DTLDEAIEIIKS-RPKPLALYLFSEDKKV---EKKVLENLSfGGGCINDTIMHLA 392
|
330
....*....|...
gi 984655788 464 VGQQPFGGARASG 476
Cdd:cd07136 393 NPYLPFGGVGNSG 405
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
227-357 |
7.40e-03 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 39.00 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984655788 227 GNVVLWKPSDTAMLASYAVYRILR----EAGLPPNIIQFV--PADGPLFGDTVTSSEhLCGINFTGSVPTFKHLWKQVAQ 300
Cdd:cd07127 221 GNPVIVKPHPAAILPLAITVQVARevlaEAGFDPNLVTLAadTPEEPIAQTLATRPE-VRIIDFTGSNAFGDWLEANARQ 299
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 984655788 301 NLdrfhtfprLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVP 357
Cdd:cd07127 300 AQ--------VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVP 348
|
|
| |
