|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
5-447 |
0e+00 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 855.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 5 SSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDFTIKGLSDWAED 84
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 85 EPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYP 164
Cdd:cd07132 81 EPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 165 VIKGGVPETTELLKEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTC 244
Cdd:cd07132 161 VVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 245 VAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSKKVAHGGTWDQPSRYIAPTILVDV 324
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 325 DPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITVPTLPFGG 404
Cdd:cd07132 321 KPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568971234 405 VGNSGMGAYHGKKSFETFSHRRSCLVRSLRNEEANKARYPPSP 447
Cdd:cd07132 401 VGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
5-430 |
0e+00 |
|
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: 746.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 5 SSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDFTIKGLSDWAED 84
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 85 EPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYP 164
Cdd:cd07087 81 RRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 165 VIKGGVPETTELLKEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTC 244
Cdd:cd07087 161 VVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 245 VAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSKKVAHGGTWDQPSRYIAPTILVDV 324
Cdd:cd07087 241 IAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 325 DPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITVPTLPFGG 404
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGG 400
|
410 420
....*....|....*....|....*.
gi 568971234 405 VGNSGMGAYHGKKSFETFSHRRSCLV 430
Cdd:cd07087 401 VGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
5-451 |
0e+00 |
|
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: 648.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 5 SSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDFTIKGLSDWAED 84
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 85 EPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYP 164
Cdd:cd07136 81 KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 165 VIKGGVPETTELLKEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTC 244
Cdd:cd07136 161 VVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 245 VAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSKKVAHGGTWDQPSRYIAPTILVDV 324
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 325 DPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITVPTLPFGG 404
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 568971234 405 VGNSGMGAYHGKKSFETFSHRRSCLVRSLRNEeaNKARYPPSPAKQM 451
Cdd:cd07136 401 VGNSGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPPYKGKKK 445
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
2-450 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 641.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 2 SNISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDFTIKGLSDW 81
Cdd:PTZ00381 7 EIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 82 AEDEPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKD 161
Cdd:PTZ00381 87 LKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 162 LYPVIKGGVPETTELLKEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSG 241
Cdd:PTZ00381 167 YVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 242 QTCVAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSK--KVAHGGTWDQPSRYIAPT 319
Cdd:PTZ00381 247 QTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHggKVVYGGEVDIENKYVAPT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 320 ILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITVPT 399
Cdd:PTZ00381 327 IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPN 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 568971234 400 LPFGGVGNSGMGAYHGKKSFETFSHRRSCLVRSLRNEEANKARYPP-SPAKQ 450
Cdd:PTZ00381 407 LPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPyTSFKS 458
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
1-427 |
0e+00 |
|
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: 606.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 1 MSNISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDFTIKGLSD 80
Cdd:cd07135 4 LDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 81 WAEDEPVAKTRQTQ-EDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMD 159
Cdd:cd07135 84 WAKDEKVKDGPLAFmFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 160 KDLYPVIKGGVPETTELLKEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMN 239
Cdd:cd07135 164 PDAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 240 SGQTCVAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSK--KVAHGGTWDQPSRYIA 317
Cdd:cd07135 244 AGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTkgKVVIGGEMDEATRFIP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 318 PTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITV 397
Cdd:cd07135 324 PTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGV 403
|
410 420 430
....*....|....*....|....*....|
gi 568971234 398 PTLPFGGVGNSGMGAYHGKKSFETFSHRRS 427
Cdd:cd07135 404 DNAPFGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
4-430 |
0e+00 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 538.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 4 ISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDFTIKGLSDWAE 83
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 84 DEPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLY 163
Cdd:cd07137 81 PEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 164 PVIKGGVPETTELLKEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKF-MNSGQ 242
Cdd:cd07137 161 KVIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 243 TCVAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSKKVA----HGGTWDQPSRYIAP 318
Cdd:cd07137 241 ACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVAdkivHGGERDEKNLYIEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 319 TILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITVP 398
Cdd:cd07137 321 TILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAID 400
|
410 420 430
....*....|....*....|....*....|..
gi 568971234 399 TLPFGGVGNSGMGAYHGKKSFETFSHRRSCLV 430
Cdd:cd07137 401 TLPFGGVGESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
26-430 |
0e+00 |
|
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: 524.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 26 RVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDFTIKGLSDWAEDEPVAKTRQTQEDDLYIHSEPL 105
Cdd:cd07134 22 RIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPLLLFGTKSKIRYEPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 106 GVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYPVIKGGVPETTELLKEKFDHIM 185
Cdd:cd07134 102 GVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAEVAQALLELPFDHIF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 186 YTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLK 265
Cdd:cd07134 182 FTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 266 KSLKDFYGEDA--KQSHDYGRIINDRHFQRVINLIDSK-----KVAHGGTWDQPSRYIAPTILVDVDPQSPVMQEEIFGP 338
Cdd:cd07134 262 AEIEKFYGKDAarKASPDLARIVNDRHFDRLKGLLDDAvakgaKVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 339 VMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITVPTLPFGGVGNSGMGAYHGKKS 418
Cdd:cd07134 342 VLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGSYHGVYG 421
|
410
....*....|..
gi 568971234 419 FETFSHRRSCLV 430
Cdd:cd07134 422 FKAFSHERAVLR 433
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
5-427 |
3.04e-168 |
|
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: 480.06 E-value: 3.04e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 5 SSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALA---SNLRKNEWTSYyeEVAHVLDEIDFTIKGLSDW 81
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISadfGHRSRHETLLA--EILPSIAGIKHARKHLKKW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 82 AEDEPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKD 161
Cdd:cd07133 79 MKPSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 162 LYPVIKGGVPETTELLKEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSG 241
Cdd:cd07133 159 EVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 242 QTCVAPDYILCDPSIQNEIVEKLKKSLKDFYGeDAKQSHDYGRIINDRHFQRVINLIDSKK--------VAHGGTWDQPS 313
Cdd:cd07133 239 QTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEDARakgarvieLNPAGEDFAAT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 314 RYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIV 393
Cdd:cd07133 318 RKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLL 397
|
410 420 430
....*....|....*....|....*....|....
gi 568971234 394 HITVPTLPFGGVGNSGMGAYHGKKSFETFSHRRS 427
Cdd:cd07133 398 HVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-445 |
3.33e-156 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 451.49 E-value: 3.33e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 1 MSNISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDFTIKGLSD 80
Cdd:PLN02203 5 GETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 81 WAEDEPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDK 160
Cdd:PLN02203 85 WMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 161 DLYPVIKGGVPETTELLKEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVD---KDCDLDVACRRIAWGKF 237
Cdd:PLN02203 165 KAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 238 MN-SGQTCVAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSKKVA----HGGTWDQP 312
Cdd:PLN02203 245 GScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAasivHGGSIDEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 313 SRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVI 392
Cdd:PLN02203 325 KLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 568971234 393 VHITVPTLPFGGVGNSGMGAYHGKKSFETFSHRRSCLVRSLRNEEanKARYPP 445
Cdd:PLN02203 405 IQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEF--EFRYPP 455
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
8-430 |
1.41e-151 |
|
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: 437.41 E-value: 1.41e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWtSYYEEVAHVLDEIDFTIKGLSDWAEDEPV 87
Cdd:cd07078 4 VAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLHGEVIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 88 AKTRQTQeddLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQY-MDKDLYPVI 166
Cdd:cd07078 83 SPDPGEL---AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 167 KGGVPETTELL--KEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTC 244
Cdd:cd07078 160 TGDGDEVGAALasHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 245 VAPDYILCDPSIQNEIVEKLKKSLKDFYGED-AKQSHDYGRIINDRHFQRVINLIDS-----KKVAHGGTWDQ--PSRYI 316
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEDakaegAKLLCGGKRLEggKGYFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 317 APTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHiT 396
Cdd:cd07078 320 PPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVG-A 398
|
410 420 430
....*....|....*....|....*....|....
gi 568971234 397 VPTLPFGGVGNSGMGAYHGKKSFETFSHRRSCLV 430
Cdd:cd07078 399 EPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
2-445 |
5.55e-136 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 399.81 E-value: 5.55e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 2 SNISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDFTIKGLSDW 81
Cdd:PLN02174 10 ADASILVTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 82 AEDEPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKD 161
Cdd:PLN02174 90 MAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 162 LYPVIKGGVPETTELLKEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKF-MNS 240
Cdd:PLN02174 170 AVRVVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 241 GQTCVAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSK----KVAHGGTWDQPSRYI 316
Cdd:PLN02174 250 GQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKevsdKIVYGGEKDRENLKI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 317 APTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHIT 396
Cdd:PLN02174 330 APTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLA 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 568971234 397 VPTLPFGGVGNSGMGAYHGKKSFETFSHRRSCLVRSLRNEEAnkARYPP 445
Cdd:PLN02174 410 LHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSA--VRYPP 456
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
10-430 |
4.95e-124 |
|
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: 365.01 E-value: 4.95e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 10 RARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEeVAHVLDEIDFTIKGLSDWAEDEPVAK 89
Cdd:cd06534 2 AARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGE-VARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 90 TRQTQeddLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQY-MDKDLYPVIKG 168
Cdd:cd06534 81 DPGGE---AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 169 GVPET-TELLK-EKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVA 246
Cdd:cd06534 158 GGDEVgAALLShPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 247 PDYILCDPSIQNEIVEKLKkslkdfygedakqshdygriindrhfqrvinlidskkvahggtwdqpsryiapTILVDVDP 326
Cdd:cd06534 238 ASRLLVHESIYDEFVEKLV-----------------------------------------------------TVLVDVDP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 327 QSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHiTVPTLPFGGVG 406
Cdd:cd06534 265 DMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIG-VGPEAPFGGVK 343
|
410 420
....*....|....*....|....
gi 568971234 407 NSGMGAYHGKKSFETFSHRRSCLV 430
Cdd:cd06534 344 NSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
8-427 |
3.79e-109 |
|
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: 330.94 E-value: 3.79e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNewtsyyeeVAHVLDEIDFTIKGLsDWAEDEPV 87
Cdd:COG1012 49 VAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKP--------LAEARGEVDRAADFL-RYYAGEAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 88 AKTRQTQEDDL-----YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSE----VSDHMADLLSTL-IPqy 157
Cdd:COG1012 120 RLYGETIPSDApgtraYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEqtplSALLLAELLEEAgLP-- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 158 mdKDLYPVIKGGVPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWG 235
Cdd:COG1012 198 --AGVLNVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 236 KFMNSGQTCVAPDYILCDPSIQNEIVEKLK---KSLKdfYGEDAKQSHDYGRIINDRHFQRVINLIDS-----KKVAHGG 307
Cdd:COG1012 276 AFGNAGQRCTAASRLLVHESIYDEFVERLVaaaKALK--VGDPLDPGTDMGPLISEAQLERVLAYIEDavaegAELLTGG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 308 TWDQPSR--YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGG 385
Cdd:COG1012 354 RRPDGEGgyFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGM 433
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 568971234 386 VTANDVIVHiTVPTLPFGGVGNSGMGAYHGKKSFETFSHRRS 427
Cdd:COG1012 434 VWINDGTTG-AVPQAPFGGVKQSGIGREGGREGLEEYTETKT 474
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
4-430 |
1.16e-100 |
|
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: 308.38 E-value: 1.16e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 4 ISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKnEWTSYYEEVAHVLDEIDFTIKGLSDWAE 83
Cdd:cd07099 20 VAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGK-PRADAGLEVLLALEAIDWAARNAPRVLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 84 DEPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSE----VSDHMADLLSTLIPqymD 159
Cdd:cd07099 99 PRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEvtplVGELLAEAWAAAGP---P 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 160 KDLYPVIKGGVPETTELLKEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMN 239
Cdd:cd07099 176 QGVLQVVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 240 SGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLID------SKKVAHGGTWDQP 312
Cdd:cd07099 256 AGQTCISVERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRRHVDdavakgAKALTGGARSNGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 313 SRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVI 392
Cdd:cd07099 336 GPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVL 415
|
410 420 430
....*....|....*....|....*....|....*...
gi 568971234 393 VHITVPTLPFGGVGNSGMGAYHGKKSFETFSHRRSCLV 430
Cdd:cd07099 416 LTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
7-427 |
1.69e-99 |
|
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: 305.61 E-value: 1.69e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 7 IVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEeVAHVLDEIDFTIkglsDWAED-- 84
Cdd:pfam00171 34 AIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGE-VDRAIDVLRYYA----GLARRld 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 85 ---EPVAKTRQTqeddlYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLI-----Pq 156
Cdd:pfam00171 109 getLPSDPGRLA-----YTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFeeaglP- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 157 ymdKDLYPVIKGGVPETTELL--KEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAW 234
Cdd:pfam00171 183 ---AGVLNVVTGSGAEVGEALveHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 235 GKFMNSGQTCVAPDYILCDPSIQNEIVEKLK---KSLKdfYGEDAKQSHDYGRIINDRHFQRVINLIDSK-----KVAHG 306
Cdd:pfam00171 260 GAFGNAGQVCTATSRLLVHESIYDEFVEKLVeaaKKLK--VGDPLDPDTDMGPLISKAQLERVLKYVEDAkeegaKLLTG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 307 GTWDQPS-RYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGG 385
Cdd:pfam00171 338 GEAGLDNgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGM 417
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 568971234 386 VTANDVIVhITVPTLPFGGVGNSGMGAYHGKKSFETFSHRRS 427
Cdd:pfam00171 418 VWINDYTT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
103-426 |
5.92e-77 |
|
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: 246.29 E-value: 5.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSdhmADLLSTLIPQYMD-----KDLYPVIKGGVPETTELL 177
Cdd:cd07104 97 VPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRT---PVTGGLLIAEIFEeaglpKGVLNVVPGGGSEIGDAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 178 KE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 255
Cdd:cd07104 174 VEhpRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHES 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 256 IQNEIVEKLK---KSLKdfYGEDAKQSHDYGRIINDRHFQRVINLIDSK-----KVAHGGTWDQpsRYIAPTILVDVDPQ 327
Cdd:cd07104 254 VYDEFVEKLVakaKALP--VGDPRDPDTVIGPLINERQVDRVHAIVEDAvaagaRLLTGGTYEG--LFYQPTVLSDVTPD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 328 SPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNN-DKVIKkmIAETSSGGVtandviVHI---TV---PTL 400
Cdd:cd07104 330 MPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDlERAMA--FAERLETGM------VHIndqTVndePHV 401
|
330 340
....*....|....*....|....*.
gi 568971234 401 PFGGVGNSGMGAYHGKKSFETFSHRR 426
Cdd:cd07104 402 PFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
4-427 |
4.03e-74 |
|
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: 239.84 E-value: 4.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 4 ISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNewTSYY-EEVAHVLDEIDFTIKGLSDWA 82
Cdd:cd07102 20 VRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP--IAQAgGEIRGMLERARYMISIAEEAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 83 EDEPVAKTRQTQEddlYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSE----VSDHMADLLS-TLIPqy 157
Cdd:cd07102 98 ADIRVPEKDGFER---YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPqtplCGERFAAAFAeAGLP-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 158 mdKDLYPVIKGGVPETTELLKEK-FDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGK 236
Cdd:cd07102 173 --EGVFQVLHLSHETSAALIADPrIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 237 FMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRV------------INLIDSKkv 303
Cdd:cd07102 251 FFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVraqiadaiakgaRALIDGA-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 304 aHGGTWDQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSS 383
Cdd:cd07102 329 -LFPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLET 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 568971234 384 GGVTAN--DVIvhitVPTLPFGGVGNSGMGAYHGKKSFETFSHRRS 427
Cdd:cd07102 408 GTVFMNrcDYL----DPALAWTGVKDSGRGVTLSRLGYDQLTRPKS 449
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
2-432 |
1.07e-73 |
|
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: 239.12 E-value: 1.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 2 SNISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDFTIKGLSDW 81
Cdd:cd07098 18 EDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 82 AEDEPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYM--- 158
Cdd:cd07098 98 LRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLaac 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 159 --DKDLYPVIKGgVPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAW 234
Cdd:cd07098 178 ghDPDLVQLVTC-LPETAEALTShpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 235 GKFMNSGQTCVAPDYILCDPSIQNEIVEKLKK---SLKDFYGEDAkqSHDYGRIINDRHFQRVINLIDS----------- 300
Cdd:cd07098 257 GTFQSSGQNCIGIERVIVHEKIYDKLLEILTDrvqALRQGPPLDG--DVDVGAMISPARFDRLEELVADavekgarllag 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 301 -KKVAHGGtwdQPS-RYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMI 378
Cdd:cd07098 335 gKRYPHPE---YPQgHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIA 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 568971234 379 AETSSGGVTANDVIVHITVPTLPFGGVGNSGMGAYHGKKSFetfshRRSCLVRS 432
Cdd:cd07098 412 SQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAGEEGL-----RGLCNPKS 460
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
103-426 |
2.36e-70 |
|
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: 229.91 E-value: 2.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQY-MDKDLYPVIKGGVPETTELL--KE 179
Cdd:cd07150 118 RPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELvdDP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 180 KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNE 259
Cdd:cd07150 198 RVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 260 IVEKL---KKSLKdfYGEDAKQSHDYGRIINDRHFQRVINLID---SK--KVAHGGTWDQPsrYIAPTILVDVDPQSPVM 331
Cdd:cd07150 278 FVKKFvarASKLK--VGDPRDPDTVIGPLISPRQVERIKRQVEdavAKgaKLLTGGKYDGN--FYQPTVLTDVTPDMRIF 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 332 QEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNN-DKVIKkmIAETSSGGVtandviVHITVPTL------PFGG 404
Cdd:cd07150 354 REETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDlQRAFK--LAERLESGM------VHINDPTIldeahvPFGG 425
|
330 340
....*....|....*....|..
gi 568971234 405 VGNSGMGAYHGKKSFETFSHRR 426
Cdd:cd07150 426 VKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
103-411 |
1.94e-69 |
|
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: 227.32 E-value: 1.94e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSE----VSDHMADLLSTL-IPqymdKDLYPVIKGGVPETTELL 177
Cdd:cd07103 116 QPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEetplSALALAELAEEAgLP----AGVLNVVTGSPAEIGEAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 178 KEKFD--HIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 255
Cdd:cd07103 192 CASPRvrKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 256 IQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLID------SKKVAHGGTWDQPSRYIAPTILVDVDPQS 328
Cdd:cd07103 272 IYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALVEdavakgAKVLTGGKRLGLGGYFYEPTVLTDVTDDM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 329 PVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIvhITVPTLPFGGVGNS 408
Cdd:cd07103 352 LIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGL--ISDAEAPFGGVKES 429
|
...
gi 568971234 409 GMG 411
Cdd:cd07103 430 GLG 432
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
8-389 |
3.26e-68 |
|
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: 224.84 E-value: 3.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEwTSYYEEVAHVLDEIDFTIkglsDWA---ED 84
Cdd:cd07088 41 VDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTL-SLARVEVEFTADYIDYMA----EWArriEG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 85 EPVAKTRQTQedDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTL-----IPqymd 159
Cdd:cd07088 116 EIIPSDRPNE--NIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELvdeagLP---- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 160 KDLYPVIKGGVPETTELL--KEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKF 237
Cdd:cd07088 190 AGVLNIVTGRGSVVGDALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 238 MNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLID-----SKKVAHGGTwdQ 311
Cdd:cd07088 270 INCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVkVGDPFDAATDMGPLVNEAALDKVEEMVEraveaGATLLTGGK--R 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 312 PSR----YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVT 387
Cdd:cd07088 348 PEGekgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETY 427
|
..
gi 568971234 388 AN 389
Cdd:cd07088 428 IN 429
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
103-423 |
9.01e-67 |
|
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: 219.76 E-value: 9.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLipqymdkdlypVIKGGVP----------- 171
Cdd:cd07105 97 EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRV-----------FHEAGLPkgvlnvvthsp 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 172 ----ETTELLkekFDH-----IMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQ 242
Cdd:cd07105 166 edapEVVEAL---IAHpavrkVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 243 TCVAPDYILCDPSIQNEIVEKLKKSLKDFYGEDakqsHDYGRIINDRHFQRVINLID---SK--KVAHGGTWDQPSR--Y 315
Cdd:cd07105 243 ICMSTERIIVHESIADEFVEKLKAAAEKLFAGP----VVLGSLVSAAAADRVKELVDdalSKgaKLVVGGLADESPSgtS 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 316 IAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHi 395
Cdd:cd07105 319 MPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVH- 397
|
330 340
....*....|....*....|....*...
gi 568971234 396 TVPTLPFGGVGNSGMGAYHGKKSFETFS 423
Cdd:cd07105 398 DEPTLPHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
8-423 |
1.22e-64 |
|
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: 215.12 E-value: 1.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGIS--------KAL-----------ASNLRknewtsYYEEVAHVL 68
Cdd:cd07093 25 VAAAKEAFPGWSRMSPAERARILHKVADLIEARADELAllesldtgKPItlartrdipraAANFR------FFADYILQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 69 DEIDFTikglsdwaedepvaktrqtQEDDL--YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHM 146
Cdd:cd07093 99 DGESYP-------------------QDGGAlnYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 147 ADLLSTLIPQY-MDKDLYPVIKGGVPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDC 223
Cdd:cd07093 160 AWLLAELANEAgLPPGVVNVVHGFGPEAGAALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 224 DLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLK---KSLKdfYGEDAKQSHDYGRIINDRHFQRVINLIDS 300
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVeraKALK--VGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 301 KK------VAHGGTWDQPSR----YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNN 370
Cdd:cd07093 318 ARaegatiLTGGGRPELPDLeggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 568971234 371 DKVIKKMIAETSSGGVTANDVIV-HItvpTLPFGGVGNSGMGAYHGKKSFETFS 423
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVNCWLVrDL---RTPFGGVKASGIGREGGDYSLEFYT 448
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
8-416 |
2.16e-64 |
|
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: 213.93 E-value: 2.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTRPLQFRVEQLEAlqrminenlkgISKALASNLrknewtsyyEEVAHVL------------DEIDFTI 75
Cdd:cd07106 25 VAAAKAAFPGWSATPLEERRAALLA-----------IADAIEANA---------EELARLLtleqgkplaeaqFEVGGAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 76 kglsDWAE-----DEPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSE----VSDHM 146
Cdd:cd07106 85 ----AWLRytaslDLPDEVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPftplCTLKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 147 ADLLSTLIPqymdKDLYPVIKGGvPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCD 224
Cdd:cd07106 161 GELAQEVLP----PGVLNVVSGG-DELGPALTShpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 225 LDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDFY-GEDAKQSHDYGRIINDRHFQRVINLIDS--- 300
Cdd:cd07106 236 IDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEDaka 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 301 --KKVAHGGTW-DQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKM 377
Cdd:cd07106 316 kgAKVLAGGEPlDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAV 395
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 568971234 378 IAETSSGGVTANDvivHITV-PTLPFGGVGNSGMGAYHGK 416
Cdd:cd07106 396 ARRLEAGTVWINT---HGALdPDAPFGGHKQSGIGVEFGI 432
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
8-422 |
3.09e-64 |
|
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: 214.58 E-value: 3.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTR-PLQFRVEQLEALQRMINEN---LKGIS-----KALASNLRKNewtsyyeevahvLDEIDFTIKGL 78
Cdd:cd07144 51 VKAARKAFESWWSKvTGEERGELLDKLADLVEKNrdlLAAIEaldsgKPYHSNALGD------------LDEIIAVIRYY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 79 SDWAeDEPVAKTRQTQEDDL-YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQY 157
Cdd:cd07144 119 AGWA-DKIQGKTIPTSPNKLaYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 158 -MDKDLYPVIKGGVPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAW 234
Cdd:cd07144 198 gFPPGVVNIIPGYGAVAGSALAEhpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 235 GKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDFY--GEDAKQSHDYGRIINDRHFQRVINLID-----SKKVAHGG 307
Cdd:cd07144 278 GIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEkgkkeGAKLVYGG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 308 TWDQPSR----YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSS 383
Cdd:cd07144 358 EKAPEGLgkgyFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEA 437
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 568971234 384 GGV---TANDVIVHItvptlPFGGVGNSGMGAYHGKKSFETF 422
Cdd:cd07144 438 GMVwinSSNDSDVGV-----PFGGFKMSGIGRELGEYGLETY 474
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
11-427 |
3.92e-64 |
|
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: 213.64 E-value: 3.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 11 ARDAFNSGK-TRPLQFRVEQLEALQRMINENLKGIskaLASNLRKNEWTSYYEEVAHVldeiDFTIKGLSDWAE-----D 84
Cdd:cd07089 28 ARRAFDTGDwSTDAEERARCLRQLHEALEARKEEL---RALLVAEVGAPVMTARAMQV----DGPIGHLRYFADladsfP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 85 EPVAKTRQTQEDDLY---IHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQymdKD 161
Cdd:cd07089 101 WEFDLPVPALRGGPGrrvVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAE---TD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 162 LYP----VIKGGVPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWG 235
Cdd:cd07089 178 LPAgvvnVVTGSDNAVGEALTTdpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 236 KFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDS-----KKVAHGGtw 309
Cdd:cd07089 258 CMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGDPADPGTVMGPLISAAQRDRVEGYIARgrdegARLVTGG-- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 310 DQPSR-----YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSG 384
Cdd:cd07089 336 GRPAGldkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTG 415
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568971234 385 GVTANDviVHITVPTLPFGGVGNSGMGAYHGKKSFETFSHRRS 427
Cdd:cd07089 416 SVGING--GGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
11-422 |
1.63e-63 |
|
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: 212.36 E-value: 1.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 11 ARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALAsnlrknewtsyyEEV---------AHV---LDEIDFTIKGL 78
Cdd:cd07138 45 ARRAFPAWSATSVEERAALLERIAEAYEARADELAQAIT------------LEMgapitlaraAQVglgIGHLRAAADAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 79 SDWAEDEPVAKTRqtqeddlyIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDhmadlLSTLI-PQY 157
Cdd:cd07138 113 KDFEFEERRGNSL--------VVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAP-----LSAIIlAEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 158 MDKDLYP-----VIKGGVPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACR 230
Cdd:cd07138 180 LDEAGLPagvfnLVNGDGPVVGEALSAhpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 231 RIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDS-----KKVA 304
Cdd:cd07138 260 RGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIQKgieegARLV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 305 HGGTwDQPSR-----YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIA 379
Cdd:cd07138 340 AGGP-GRPEGlergyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVAR 418
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568971234 380 ETSSGGVTANDVIVHitvPTLPFGGVGNSGMGAYHGKKSFETF 422
Cdd:cd07138 419 RLRAGQVHINGAAFN---PGAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
99-420 |
3.59e-63 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 210.94 E-value: 3.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 99 YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSE---VSDHM-ADLLSTL-IPqymdKDLYPVIKGGVPET 173
Cdd:cd07109 112 YTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEdapLTALRlAELAEEAgLP----AGALNVVTGLGAEA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 174 TELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYIL 251
Cdd:cd07109 188 GAALVAhpGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 252 CDPSIQNEIVEKLK---KSLKDFYGEDakqSHDYGRIINDRHFQRVINLIDSKK-----VAHGGTW--DQPSR--YIAPT 319
Cdd:cd07109 268 VHRSIYDEVLERLVerfRALRVGPGLE---DPDLGPLISAKQLDRVEGFVARARargarIVAGGRIaeGAPAGgyFVAPT 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 320 ILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITVpT 399
Cdd:cd07109 345 LLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGI-E 423
|
330 340
....*....|....*....|..
gi 568971234 400 LPFGGVGNSGmgayHGK-KSFE 420
Cdd:cd07109 424 LPFGGVKKSG----HGReKGLE 441
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
104-426 |
4.43e-63 |
|
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: 210.61 E-value: 4.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 104 PLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKP---SEVSDHMadLLSTLIPQY-MDKDLYPVIKGGvPETTELLKE 179
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPdprTPVSGGV--VIARLFEEAgLPAGVLHVLPGG-ADAGEALVE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 180 --KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQ 257
Cdd:cd07152 187 dpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 258 NEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDSK-----KVAHGGTWDQpsRYIAPTILVDVDPQSPVM 331
Cdd:cd07152 267 DAYTAKLAAKAKHLpVGDPATGQVALGPLINARQLDRVHAIVDDSvaagaRLEAGGTYDG--LFYRPTVLSGVKPGMPAF 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 332 QEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVhITVPTLPFGGVGNSGMG 411
Cdd:cd07152 345 DEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTV-NDEPHNPFGGMGASGNG 423
|
330
....*....|....*.
gi 568971234 412 AYHG-KKSFETFSHRR 426
Cdd:cd07152 424 SRFGgPANWEEFTQWQ 439
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
103-427 |
2.33e-62 |
|
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: 208.94 E-value: 2.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDhmadlLSTL----------IPqymdKDLYPVIKGGVPE 172
Cdd:cd07114 118 EPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP-----ASTLelaklaeeagFP----PGVVNVVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 173 TTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYI 250
Cdd:cd07114 189 TGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 251 LCDPSIQNEIVEKLK---KSLKdfYGEDAKQSHDYGRIINDRHFQRVINLIDSKK-----VAHGGtwDQPSR-------Y 315
Cdd:cd07114 269 LVQRSIYDEFVERLVaraRAIR--VGDPLDPETQMGPLATERQLEKVERYVARAReegarVLTGG--ERPSGadlgagyF 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 316 IAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDviVHI 395
Cdd:cd07114 345 FEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YRA 422
|
330 340 350
....*....|....*....|....*....|..
gi 568971234 396 TVPTLPFGGVGNSGMGAYHGKKSFETFSHRRS 427
Cdd:cd07114 423 LSPSSPFGGFKDSGIGRENGIEAIREYTQTKS 454
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
8-430 |
9.57e-62 |
|
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: 207.60 E-value: 9.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDF------TIKGLSDW 81
Cdd:cd07108 25 VAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVLADLFRYfgglagELKGETLP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 82 AEDEPVAKTRQtqeddlyihsEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSD----HMADLLSTLIPqy 157
Cdd:cd07108 105 FGPDVLTYTVR----------EPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPlavlLLAEILAQVLP-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 158 mdKDLYPVIKGGVPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRR-IAW 234
Cdd:cd07108 173 --AGVLNVITGYGEECGAALVDhpDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGaIAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 235 GKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLID------SKKVAHGG 307
Cdd:cd07108 251 MRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDlglstsGATVLRGG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 308 T-----WDQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETS 382
Cdd:cd07108 331 PlpgegPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALE 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 568971234 383 SGGVTANDviVHITVPTLPFGGVGNSGMG-AYHGKKSFETFSHRRSCLV 430
Cdd:cd07108 411 AGWVQVNQ--GGGQQPGQSYGGFKQSGLGrEASLEGMLEHFTQKKTVNI 457
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
99-411 |
1.64e-61 |
|
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: 207.45 E-value: 1.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 99 YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPqymdKDLYP-----VIKGGVPET 173
Cdd:cd07091 136 YTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIK----EAGFPpgvvnIVPGFGPTA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 174 TELLKE--KFDHIMYTGSTAVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYI 250
Cdd:cd07091 212 GAAISShmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 251 LCDPSIQNEIVEKLKKSLKDFY-GEDAKQSHDYGRIINDRHFQRVINLIDSKKVA-----HGGT-WDQPSRYIAPTILVD 323
Cdd:cd07091 292 FVQESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEgatllTGGErHGSKGYFIQPTVFTD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 324 VDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDviVHITVPTLPFG 403
Cdd:cd07091 372 VKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNT--YNVFDAAVPFG 449
|
....*...
gi 568971234 404 GVGNSGMG 411
Cdd:cd07091 450 GFKQSGFG 457
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
103-430 |
1.97e-61 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 206.42 E-value: 1.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTL-----IPqymdKDLYPVIKGGVPETTELL 177
Cdd:cd07118 118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELlieagLP----AGVVNIVTGYGATVGQAM 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 178 KE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 255
Cdd:cd07118 194 TEhpDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHES 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 256 IQNEIVEKLK-KSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSKK-----VAHGGTWDQ--PSRYIAPTILVDVDPQ 327
Cdd:cd07118 274 IADAFVAAVVaRSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRaegatLLLGGERLAsaAGLFYQPTIFTDVTPD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 328 SPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNN-DKVIkKMIAETSSGGVTANDVIVhiTVPTLPFGGVG 406
Cdd:cd07118 354 MAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDiDTAL-TVARRIRAGTVWVNTFLD--GSPELPFGGFK 430
|
330 340
....*....|....*....|....
gi 568971234 407 NSGMGAYHGKKSFETFSHRRSCLV 430
Cdd:cd07118 431 QSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
99-431 |
2.44e-61 |
|
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: 206.39 E-value: 2.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 99 YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQY-MDKDLYPVIKGGvPETTELL 177
Cdd:cd07090 111 YTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQLL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 178 KEKFD--HIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 255
Cdd:cd07090 190 CEHPDvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 256 IQNEIVEKL-KKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSKK-----VAHGGTWDQPSR------YIAPTILVD 323
Cdd:cd07090 270 IKDEFTERLvERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKqegakVLCGGERVVPEDglengfYVSPCVLTD 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 324 VDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDviVHITVPTLPFG 403
Cdd:cd07090 350 CTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVEVPFG 427
|
330 340
....*....|....*....|....*...
gi 568971234 404 GVGNSGMGAYHGKKSFETFSHRRSCLVR 431
Cdd:cd07090 428 GYKQSGFGRENGTAALEHYTQLKTVYVE 455
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
11-411 |
2.36e-60 |
|
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: 203.71 E-value: 2.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 11 ARDAFNSGK-TRPLQfRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDF------TIKGLS--DW 81
Cdd:cd07092 28 AHAAFPSWRrTTPAE-RSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFRFfagaarTLEGPAagEY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 82 AEDepvaktrQTQeddlYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDhmadlLSTLIPQYMDKD 161
Cdd:cd07092 107 LPG-------HTS----MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP-----LTTLLLAELAAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 162 LYP-----VIKGGVPETTELL--KEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAW 234
Cdd:cd07092 171 VLPpgvvnVVCGGGASAGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIAT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 235 GKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLID-----SKKVAHGGT 308
Cdd:cd07092 251 AGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVErapahARVLTGGRR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 309 WDQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTA 388
Cdd:cd07092 331 AEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWV 410
|
410 420
....*....|....*....|....
gi 568971234 389 NDvivHITVPT-LPFGGVGNSGMG 411
Cdd:cd07092 411 NT---HIPLAAeMPHGGFKQSGYG 431
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
11-422 |
5.05e-60 |
|
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: 203.19 E-value: 5.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 11 ARDAFNSG--KTRPLQFRVEQLEALQRMINENLKGISKALAsnlRKNEWTSYYEEVAHVLDEIDfTIKGLSDWAEDEPVA 88
Cdd:cd07139 45 ARRAFDNGpwPRLSPAERAAVLRRLADALEARADELARLWT---AENGMPISWSRRAQGPGPAA-LLRYYAALARDFPFE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 89 KTRQTQE-DDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQymdKDLYP--- 164
Cdd:cd07139 121 ERRPGSGgGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEE---AGLPPgvv 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 165 -VIKGGVpETTELLKEK--FDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSG 241
Cdd:cd07139 198 nVVPADR-EVGEYLVRHpgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 242 QTCVAPDYILCDPSIQNEIVEKLK---KSLKdfYGEDAKQSHDYGRIINDRHFQRVINLIDSKK------VAHGGTWDQP 312
Cdd:cd07139 277 QVCVALTRILVPRSRYDEVVEALAaavAALK--VGDPLDPATQIGPLASARQRERVEGYIAKGRaegarlVTGGGRPAGL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 313 SR--YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNND----KVIKKMiaetSSGGV 386
Cdd:cd07139 355 DRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVerglAVARRI----RTGTV 430
|
410 420 430
....*....|....*....|....*....|....*..
gi 568971234 387 TANdvivHITV-PTLPFGGVGNSGMGAYHGKKSFETF 422
Cdd:cd07139 431 GVN----GFRLdFGAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
103-422 |
2.14e-58 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 199.53 E-value: 2.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTL-----IPQymdkDLYPVIKGGVPETTELL 177
Cdd:PLN02278 159 QPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELalqagIPP----GVLNVVMGDAPEIGDAL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 178 --KEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 255
Cdd:PLN02278 235 laSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 256 IQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLID---SK--KVAHGGTWDQPSR-YIAPTILVDVDPQS 328
Cdd:PLN02278 315 IYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVESHVQdavSKgaKVLLGGKRHSLGGtFYEPTVLGDVTEDM 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 329 PVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITVPtlPFGGVGNS 408
Cdd:PLN02278 395 LIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQS 472
|
330
....*....|....
gi 568971234 409 GMGAYHGKKSFETF 422
Cdd:PLN02278 473 GLGREGSKYGIDEY 486
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
99-427 |
3.03e-58 |
|
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: 198.05 E-value: 3.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 99 YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDhmadlLSTL-IPQYMDKDLYP-----VIKGGVPE 172
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTP-----LSALrIAELMAEAGFPagvlnVVTGFGEV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 173 TTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYI 250
Cdd:cd07115 187 AGAALVEhpDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 251 LCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLID------SKKVAHGGTWDQPSRYIAPTILVD 323
Cdd:cd07115 267 LVHESIYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDRVLDYVDvgreegARLLTGGKRPGARGFFVEPTIFAA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 324 VDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANdvIVHITVPTLPFG 403
Cdd:cd07115 347 VPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFG 424
|
330 340
....*....|....*....|....
gi 568971234 404 GVGNSGMGAYHGKKSFETFSHRRS 427
Cdd:cd07115 425 GYKQSGFGREMGREALDEYTEVKS 448
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
8-411 |
5.28e-58 |
|
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: 197.43 E-value: 5.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNeWTSYYEEVAHVLDEIDF------TIKGLSDW 81
Cdd:cd07149 27 IAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKP-IKDARKEVDRAIETLRLsaeeakRLAGETIP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 82 AEDEPVAKTRQTqeddlYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQ-YMDK 160
Cdd:cd07149 106 FDASPGGEGRIG-----FTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEaGLPK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 161 DLYPVIKGGVPET-TELLKEK-FDHIMYTGSTAVGKIVMAAAAkhLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFM 238
Cdd:cd07149 181 GALNVVTGSGETVgDALVTDPrVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 239 NSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDSK-----KVAHGGTWDqp 312
Cdd:cd07149 259 NAGQVCISVQRIFVHEDIYDEFLERFVAATKKLvVGDPLDEDTDVGPMISEAEAERIEEWVEEAveggaRLLTGGKRD-- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 313 SRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDvi 392
Cdd:cd07149 337 GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMIND-- 414
|
410 420
....*....|....*....|....
gi 568971234 393 vhitVPT-----LPFGGVGNSGMG 411
Cdd:cd07149 415 ----SSTfrvdhMPYGGVKESGTG 434
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
8-411 |
5.81e-58 |
|
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: 197.44 E-value: 5.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGktrplqfRVEQLEALQRminenlKGISKALASNLRKNEwtsyyEEVAhVLDEIDfTIKGLSD-WAEDEP 86
Cdd:cd07112 30 VAAARRAFESG-------VWSRLSPAER------KAVLLRLADLIEAHR-----DELA-LLETLD-MGKPISDaLAVDVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 87 VA----------------KTRQTQEDDL-YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDhmadl 149
Cdd:cd07112 90 SAantfrwyaeaidkvygEVAPTGPDALaLITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSP----- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 150 LSTL----------IPqymdKDLYPVIKGGVPETTELL--KEKFDHIMYTGSTAVGKIVMAAAAK-HLTPVTLELGGKSP 216
Cdd:cd07112 165 LTALrlaelaleagLP----AGVLNVVPGFGHTAGEALglHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 217 CYVDKDC-DLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDFYGEDA-KQSHDYGRIINDRHFQRV 294
Cdd:cd07112 241 NIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPlDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 295 INLIDSKK-----VAHGGTWDQPSR---YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYV 366
Cdd:cd07112 321 LGYIESGKaegarLVAGGKRVLTETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 568971234 367 FSNNDKVIKKMIAETSSGGVTANDV-IVHITVptlPFGGVGNSGMG 411
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFdEGDITT---PFGGFKQSGNG 443
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
2-427 |
1.31e-57 |
|
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: 197.18 E-value: 1.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 2 SNISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNewtsYYEEVAHVLDEIDftikgLSDW 81
Cdd:cd07131 37 SDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKP----LAEGRGDVQEAID-----MAQY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 82 AEDEpvakTRQTQ---------EDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLST 152
Cdd:cd07131 108 AAGE----GRRLFgetvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 153 LipqYMDKDLYP----VIKGGVPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLD 226
Cdd:cd07131 184 L---FAEAGLPPgvvnVVHGRGEEVGEALVEhpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 227 VACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLK---KSLKDFYGEDAKQshDYGRIINDRHFQRVINLID---- 299
Cdd:cd07131 261 LALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVeraKRLRVGDGLDEET--DMGPLINEAQLEKVLNYNEigke 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 300 -SKKVAHGG---TWDQPSR--YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKV 373
Cdd:cd07131 339 eGATLLLGGerlTGGGYEKgyFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNK 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971234 374 IKKMIAETSSGgvtandvIVHITVPT------LPFGGVGNSGMGayH---GKKSFETFSHRRS 427
Cdd:cd07131 419 AFRARRDLEAG-------ITYVNAPTigaevhLPFGGVKKSGNG--HreaGTTALDAFTEWKA 472
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
99-423 |
1.65e-57 |
|
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: 196.37 E-value: 1.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 99 YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQY--MDKDLYPVIKGGVPETTEL 176
Cdd:cd07151 125 RVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLAKIFEEagLPKGVLNVVVGAGSEIGDA 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 177 LKEkfdH-----IMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYIL 251
Cdd:cd07151 205 FVE---HpvprlISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRII 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 252 CDPSIQNEIVEKLK---KSLKdfYGEDAKQSHDYGRIINDRHFQRVINLIDSKK-----VAHGGTWDqpSRYIAPTILVD 323
Cdd:cd07151 282 VHEDVYDEFVEKFVervKALP--YGDPSDPDTVVGPLINESQVDGLLDKIEQAVeegatLLVGGEAE--GNVLEPTVLSD 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 324 VDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHiTVPTLPFG 403
Cdd:cd07151 358 VTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVN-DEPHVPFG 436
|
330 340
....*....|....*....|
gi 568971234 404 GVGNSGMGAYHGKKSFETFS 423
Cdd:cd07151 437 GEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
4-419 |
3.01e-57 |
|
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: 194.60 E-value: 3.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 4 ISSIVNRARDAFNSGKTRPLQFRVEQL-----------EALQRMINENL-KGISKALAsnlrknewtsyyeEVAHVLDEI 71
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLrkladllrerkDELARLITLEMgKPIAEARA-------------EVEKCAWIC 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 72 DFTIKGLSDWAEDEPVaktrQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLS 151
Cdd:cd07100 68 RYYAENAEAFLADEPI----ETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 152 TLI-----PqymdKDLYPVIKGGVPETTELLKEkfDHIM---YTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDC 223
Cdd:cd07100 144 ELFreagfP----EGVFQNLLIDSDQVEAIIAD--PRVRgvtLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 224 DLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDsKK 302
Cdd:cd07100 218 DLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALkVGDPMDEDTDLGPLARKDLRDELHEQVE-EA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 303 VAHGGTW-------DQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIK 375
Cdd:cd07100 297 VAAGATLllggkrpDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAE 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 568971234 376 KMIAETSSGGVTANDVIVhiTVPTLPFGGVGNSGMG---AYHGKKSF 419
Cdd:cd07100 377 RVARRLEAGMVFINGMVK--SDPRLPFGGVKRSGYGrelGRFGIREF 421
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
63-415 |
4.16e-57 |
|
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: 194.88 E-value: 4.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 63 EVAHVLDEIDFTI-KGLSDWAE--DEPVAKTRQTQEddLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKP 139
Cdd:cd07146 78 EVGRAADVLRFAAaEALRDDGEsfSCDLTANGKARK--IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 140 SEVSDHMADLLSTLIPQY-MDKDLYPVIKGGVPETTELL--KEKFDHIMYTGSTAVGKIVMAAAA-KHLTpvtLELGGKS 215
Cdd:cd07146 156 SEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDELitHPDVDLVTFTGGVAVGKAIAATAGyKRQL---LELGGND 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 216 PCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKL-KKSLKDFYGEDAKQSHDYGRIIND---RHF 291
Cdd:cd07146 233 PLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLvEKSAALVVGDPMDPATDMGTVIDEeaaIQI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 292 QRVIN--LIDSKKVAHGGTWDqpSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSN 369
Cdd:cd07146 313 ENRVEeaIAQGARVLLGNQRQ--GALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTN 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 568971234 370 NDKVIKKMIAETSSGGVTANDViVHITVPTLPFGGVGNSGMGAYHG 415
Cdd:cd07146 391 DLDTIKRLVERLDVGTVNVNEV-PGFRSELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
8-411 |
1.66e-55 |
|
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: 191.03 E-value: 1.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNewtsyYEEVAHVLDEIDFTIKGLSDWAED-EP 86
Cdd:cd07110 25 VRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKP-----LDEAAWDVDDVAGCFEYYADLAEQlDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 87 VAKTRQTQED---DLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSD----HMADLLSTL-IPqym 158
Cdd:cd07110 100 KAERAVPLPSedfKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSltelELAEIAAEAgLP--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 159 dKDLYPVIKGGVPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGK 236
Cdd:cd07110 177 -PGVLNVVTGTGDEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGC 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 237 FMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLK-----DFYGEDAkqshDYGRIINDRHFQRVINLIDSKK------VAH 305
Cdd:cd07110 256 FWNNGQICSATSRLLVHESIADAFLERLATAAEairvgDPLEEGV----RLGPLVSQAQYEKVLSFIARGKeegarlLCG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 306 GGTWDQPSR--YIAPTILVDVDPQSPVMQEEIFGPVMpivCVRSL---DEAIKFINQREKPLALYVFSNNDKVIKKMIAE 380
Cdd:cd07110 332 GRRPAHLEKgyFIAPTVFADVPTDSRIWREEIFGPVL---CVRSFateDEAIALANDSEYGLAAAVISRDAERCDRVAEA 408
|
410 420 430
....*....|....*....|....*....|.
gi 568971234 381 TSSGGVTANdvIVHITVPTLPFGGVGNSGMG 411
Cdd:cd07110 409 LEAGIVWIN--CSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
98-412 |
2.05e-55 |
|
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: 190.92 E-value: 2.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 98 LYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIpqymdkdlypvIKGGVPETT--- 174
Cdd:cd07097 129 VETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEIL-----------EEAGLPAGVfnl 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 175 ----------ELLK-EKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQT 243
Cdd:cd07097 198 vmgsgsevgqALVEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 244 CVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLID-----SKKVAHGG---TWDQPSR 314
Cdd:cd07097 278 CTASSRLIVTEGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIEiarseGAKLVYGGerlKRPDEGY 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 315 YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGgvtandvIVH 394
Cdd:cd07097 358 YLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAG-------VVM 430
|
330 340
....*....|....*....|....
gi 568971234 395 ITVPT------LPFGGVGNSGMGA 412
Cdd:cd07097 431 VNLPTagvdyhVPFGGRKGSSYGP 454
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
104-416 |
1.25e-54 |
|
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: 188.67 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 104 PLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDH----MADLLstlIPQYMDKDLYPVIKGGVPETTELLKE 179
Cdd:cd07101 118 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALtalwAVELL---IEAGLPRDLWQVVTGPGSEVGGAIVD 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 180 KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNE 259
Cdd:cd07101 195 NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 260 IVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLID---SK--KVAHGGTwdqpSR------YIAPTILVDVDPQ 327
Cdd:cd07101 275 FVRRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVDdavAKgaTVLAGGR----ARpdlgpyFYEPTVLTGVTED 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 328 SPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDvivhITVPTL-----PF 402
Cdd:cd07101 351 MELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE----GYAAAWasidaPM 426
|
330
....*....|....
gi 568971234 403 GGVGNSGMGAYHGK 416
Cdd:cd07101 427 GGMKDSGLGRRHGA 440
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
63-384 |
4.92e-54 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 185.71 E-value: 4.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 63 EVAHVLDEIDFTikglSDWA---EDEPVAKTRQTQedDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKP 139
Cdd:PRK10090 33 EVAFTADYIDYM----AEWArryEGEIIQSDRPGE--NILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 140 SEVSDHMADLLSTLIPQY-MDKDLYPVIKGGVPETTELL--KEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSP 216
Cdd:PRK10090 107 SEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELagNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 217 CYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSH-DYGRIINDRHFQRV 294
Cdd:PRK10090 187 AIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVqFGNPAERNDiAMGPLINAAALERV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 295 INLIDS-----KKVAHGG-TWDQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFS 368
Cdd:PRK10090 267 EQKVARaveegARVALGGkAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYT 346
|
330
....*....|....*.
gi 568971234 369 NNDKVIKKMIAETSSG 384
Cdd:PRK10090 347 QNLNVAMKAIKGLKFG 362
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
11-411 |
5.30e-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: 184.09 E-value: 5.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 11 ARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKnewtsyyeEVAHVLDEIDFTIKGLSDWAEDEPVAKT 90
Cdd:cd07145 30 AEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGK--------PIKQSRVEVERTIRLFKLAAEEAKVLRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 91 RQTQEDD--------LYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEvsdhmadlLSTLIPQYMDKDL 162
Cdd:cd07145 102 ETIPVDAyeynerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS--------NTPLTAIELAKIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 163 YpviKGGVPETT-------------ELLK-EKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVA 228
Cdd:cd07145 174 E---EAGLPPGVinvvtgygsevgdEIVTnPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 229 CRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLI-DSK----K 302
Cdd:cd07145 251 VSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVnDAVekggK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 303 VAHGGTWDQPSrYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETS 382
Cdd:cd07145 331 ILYGGKRDEGS-FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELE 409
|
410 420
....*....|....*....|....*....
gi 568971234 383 SGGVTANDViVHITVPTLPFGGVGNSGMG 411
Cdd:cd07145 410 AGGVVINDS-TRFRWDNLPFGGFKKSGIG 437
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
8-431 |
7.63e-53 |
|
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: 184.65 E-value: 7.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSgkTRPLQF----RVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDeidfTIKGLSDWAe 83
Cdd:cd07143 50 VEVAHAAFET--DWGLKVsgskRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRVDVQASAD----TFRYYGGWA- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 84 DEPVAKTRQTQEDDL-YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQY-MDKD 161
Cdd:cd07143 123 DKIHGQVIETDIKKLtYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 162 LYPVIKGGVPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFM 238
Cdd:cd07143 203 VINVVSGYGRTCGNAISShmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 239 NSGQTCVAPDYILCDPSIQNEIVEKLK---KSLK--DFYGEDAKQshdyGRIINDRHFQRVINLIDSKKvAHGGTWDQPS 313
Cdd:cd07143 283 NHGQVCCAGSRIYVQEGIYDKFVKRFKekaKKLKvgDPFAEDTFQ----GPQVSQIQYERIMSYIESGK-AEGATVETGG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 314 R-------YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGV 386
Cdd:cd07143 358 KrhgnegyFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTV 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 568971234 387 TANDV-IVHitvPTLPFGGVGNSGMGAYHGKKSFETFSHRRSCLVR 431
Cdd:cd07143 438 WVNCYnLLH---HQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
8-424 |
1.02e-52 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 184.55 E-value: 1.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTR-----PLQFRVEQLEALQRMINENLKGISKALASN----LRKNEWT--------SYYEEVAHVLDE 70
Cdd:PLN02467 51 VEAARKAFKRNKGKdwartTGAVRAKYLRAIAAKITERKSELAKLETLDcgkpLDEAAWDmddvagcfEYYADLAEALDA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 71 idftikglsdwAEDEPVakTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSD----HM 146
Cdd:PLN02467 131 -----------KQKAPV--SLPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASvtclEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 147 ADLLST--LIPQYMDkdlypVIKGGVPETTELLKEK--FDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKD 222
Cdd:PLN02467 198 ADICREvgLPPGVLN-----VVTGLGTEAGAPLASHpgVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 223 CDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDSK 301
Cdd:PLN02467 273 VDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIkISDPLEEGCRLGPVVSEGQYEKVLKFISTA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 302 K-----VAHGGTWDQPSR---YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKV 373
Cdd:PLN02467 353 KsegatILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLER 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 568971234 374 IKKMIAETSSGGVTANdvivhITVPT---LPFGGVGNSGMGAYHGKKSFETFSH 424
Cdd:PLN02467 433 CERVSEAFQAGIVWIN-----CSQPCfcqAPWGGIKRSGFGRELGEWGLENYLS 481
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
96-423 |
3.59e-52 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 182.32 E-value: 3.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 96 DDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMA-DLLSTLIPQYMDKDLYPVIKGGVPETT 174
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTAlKVAEIMEEAGLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 175 ELLKEK--FDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILC 252
Cdd:TIGR01804 205 PLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 253 DPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDSKK-----VAHGGtwDQPSR-------YIAPT 319
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIEKGKaegatLATGG--GRPENvglqngfFVEPT 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 320 ILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDviVHITVPT 399
Cdd:TIGR01804 363 VFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAE 440
|
330 340
....*....|....*....|....
gi 568971234 400 LPFGGVGNSGMGAYHGKKSFETFS 423
Cdd:TIGR01804 441 APFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
11-411 |
4.29e-52 |
|
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: 181.86 E-value: 4.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 11 ARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKnewtSYYEEVAHVLDEIDfTIKGLSDWAE---DEPV 87
Cdd:cd07094 30 ARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGK----PIKDARVEVDRAID-TLRLAAEEAErirGEEI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 88 ---AKTRQTQEDDLYIHsEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMA-DLLSTLIPQYMDKDLY 163
Cdd:cd07094 105 pldATQGSDNRLAWTIR-EPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSAlELAKILVEAGVPEGVL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 164 PVIKGGVPETTELL--KEKFDHIMYTGSTAVGKIVMAAAAKhlTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSG 241
Cdd:cd07094 184 QVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 242 QTCVAPDYILCDPSIQNEIVEKLK---KSLKdfYGEDAKQSHDYGRIINDRHFQRVINLIDsKKVAHGGTW----DQPSR 314
Cdd:cd07094 262 QVCISVQRIYVHEELYDEFIEAFVaavKKLK--VGDPLDEDTDVGPLISEEAAERVERWVE-EAVEAGARLlcggERDGA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 315 YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDViVH 394
Cdd:cd07094 339 LFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDS-SA 417
|
410
....*....|....*..
gi 568971234 395 ITVPTLPFGGVGNSGMG 411
Cdd:cd07094 418 FRTDWMPFGGVKESGVG 434
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
99-423 |
1.18e-51 |
|
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: 181.39 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 99 YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMdkdlYP-----VIKGGVPET 173
Cdd:cd07141 140 YTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAG----FPpgvvnVVPGYGPTA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 174 TELLKE--KFDHIMYTGSTAVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYI 250
Cdd:cd07141 216 GAAISShpDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 251 LCDPSIQNEIVEKL-----KKSLKDFYGEDAKQshdyGRIINDRHFQRVINLIDSKK------VAHGGTWDQPSRYIAPT 319
Cdd:cd07141 296 FVQESIYDEFVKRSverakKRVVGNPFDPKTEQ----GPQIDEEQFKKILELIESGKkegaklECGGKRHGDKGYFIQPT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 320 ILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNN-DKVIkkmiaeTSSGGVTANDVIV---HI 395
Cdd:cd07141 372 VFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDiDKAI------TFSNALRAGTVWVncyNV 445
|
330 340
....*....|....*....|....*...
gi 568971234 396 TVPTLPFGGVGNSGMGAYHGKKSFETFS 423
Cdd:cd07141 446 VSPQAPFGGYKMSGNGRELGEYGLQEYT 473
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
11-412 |
3.38e-51 |
|
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: 180.88 E-value: 3.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 11 ARDAFNSGKTRPLQFRVEQL----EALQRMINEnlkgISKALASNLRKNewtsYYEEVAHVLDEIDFtikgLSDWAED-- 84
Cdd:cd07124 78 ARAAFPTWRRTPPEERARLLlraaALLRRRRFE----LAAWMVLEVGKN----WAEADADVAEAIDF----LEYYAREml 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 85 --EPVAKTRQTQEDDLYiHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIpqymdkdl 162
Cdd:cd07124 146 rlRGFPVEMVPGEDNRY-VYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEIL-------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 163 ypvIKGGVP------------ETTELLKE--KFDHIMYTGSTAVGKIVMAAAAK------HLTPVTLELGGKSPCYVDKD 222
Cdd:cd07124 217 ---EEAGLPpgvvnflpgpgeEVGDYLVEhpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 223 CDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLK---KSLKdfYGEDAKQSHDYGRIINDRHFQRVINLID 299
Cdd:cd07124 294 ADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVertKALK--VGDPEDPEVYMGPVIDKGARDRIRRYIE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 300 SKK----VAHGGTWDQPSR---YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDK 372
Cdd:cd07124 372 IGKsegrLLLGGEVLELAAegyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPE 451
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 568971234 373 VIKKMIAETSSGGVTANDVIVHITVPTLPFGGVGNSGMGA 412
Cdd:cd07124 452 HLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGS 491
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
103-427 |
5.77e-51 |
|
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: 179.23 E-value: 5.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQY-MDKDLYPVIKGGVPETTELLKEKF 181
Cdd:cd07142 140 EPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAAIASHM 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 182 --DHIMYTGSTAVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQN 258
Cdd:cd07142 220 dvDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 259 EIVEKLK-KSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSKK------VAHGGTWDQPSRYIAPTILVDVDPQSPVM 331
Cdd:cd07142 300 EFVEKAKaRALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKeegatlITGGDRIGSKGYYIQPTIFSDVKDDMKIA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 332 QEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANdvIVHITVPTLPFGGVGNSGMG 411
Cdd:cd07142 380 RDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVN--CYDVFDASIPFGGYKMSGIG 457
|
330
....*....|....*.
gi 568971234 412 AYHGKKSFETFSHRRS 427
Cdd:cd07142 458 REKGIYALNNYLQVKA 473
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
104-415 |
1.25e-50 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 179.30 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 104 PLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQY-MDKDLYPVIKGGVPETTELLKEKFD 182
Cdd:PRK09407 154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALVDNAD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 183 HIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVE 262
Cdd:PRK09407 234 YLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 263 KL---KKSLK-----DFygedakqSHDYGRIINDRHFQRVINLIDSkKVAHGGTW--------DQPSRYIAPTILVDVDP 326
Cdd:PRK09407 314 AFvaaVRAMRlgagyDY-------SADMGSLISEAQLETVSAHVDD-AVAKGATVlaggkarpDLGPLFYEPTVLTGVTP 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 327 QSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDvivhITVPTL-----P 401
Cdd:PRK09407 386 DMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNE----GYAAAWgsvdaP 461
|
330
....*....|....
gi 568971234 402 FGGVGNSGMGAYHG 415
Cdd:PRK09407 462 MGGMKDSGLGRRHG 475
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
11-423 |
1.52e-50 |
|
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: 178.27 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 11 ARDAFNSGKTR--PLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYE--EVAHVLDeidfTIKGLSDWAEDEP 86
Cdd:cd07119 44 ARRAFDSGEWPhlPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDidDVANCFR----YYAGLATKETGEV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 87 VAKTRQTQEddlYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQY-MDKDLYPV 165
Cdd:cd07119 120 YDVPPHVIS---RTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 166 IKGGVPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQT 243
Cdd:cd07119 197 VTGSGATVGAELAEspDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 244 CVAPDYILCDPSIQNEIVEKLKKSLKDF---YGEDAkqSHDYGRIINDRHFQRVINLID-----SKKVAHGGtwDQPSR- 314
Cdd:cd07119 277 CSAGSRLLVEESIHDKFVAALAERAKKIklgNGLDA--DTEMGPLVSAEHREKVLSYIQlgkeeGARLVCGG--KRPTGd 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 315 ------YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTA 388
Cdd:cd07119 353 elakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWI 432
|
410 420 430
....*....|....*....|....*....|....*
gi 568971234 389 NDviVHITVPTLPFGGVGNSGMGAYHGKKSFETFS 423
Cdd:cd07119 433 ND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
99-411 |
1.81e-50 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 177.79 E-value: 1.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 99 YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDhmadlLSTLIPQYMDKDLYP-----VIKGGVPET 173
Cdd:PRK13473 133 MIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITP-----LTALKLAELAADILPpgvlnVVTGRGATV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 174 TELL--KEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYIL 251
Cdd:PRK13473 208 GDALvgHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIY 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 252 CDPSIQNEIVEKLK---KSLKdfYGEDAKQSHDYGRIINDRHFQRVINLIDSKK-------VAHGGTWDQPSRYIAPTIL 321
Cdd:PRK13473 288 AQRGIYDDLVAKLAaavATLK--VGDPDDEDTELGPLISAAHRDRVAGFVERAKalghirvVTGGEAPDGKGYYYEPTLL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 322 VDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDvivHIT-VPTL 400
Cdd:PRK13473 366 AGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT---HFMlVSEM 442
|
330
....*....|.
gi 568971234 401 PFGGVGNSGMG 411
Cdd:PRK13473 443 PHGGQKQSGYG 453
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
103-431 |
1.90e-49 |
|
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: 175.32 E-value: 1.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSdhmadllstliPQYMDKDLYPVIKGGVPE--------TT 174
Cdd:cd07113 141 EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFT-----------PLTLLRVAELAKEAGIPDgvlnvvngKG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 175 ELLKEKFDH-----IMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDY 249
Cdd:cd07113 210 AVGAQLISHpdvakVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPER 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 250 ILCDPSIQNEIVEKLKKSLKDFY-GEDAKQSHDYGRIINDRHFQRVINLIDSKK------VAHGGTWDQPSRYIAPTILV 322
Cdd:cd07113 290 FYVHRSKFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLDDARaegdeiVRGGEALAGEGYFVQPTLVL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 323 DVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANdviVHITV-PTLP 401
Cdd:cd07113 370 ARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLdPAVP 446
|
330 340 350
....*....|....*....|....*....|
gi 568971234 402 FGGVGNSGMGAYHGKKSFETFSHRRSCLVR 431
Cdd:cd07113 447 FGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
2-430 |
2.40e-49 |
|
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: 175.06 E-value: 2.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 2 SNISSIVNRARDAFNSGKTRPLQFRVEQLealqRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDftikgLSDW 81
Cdd:cd07086 35 EDVEAAVAAAREAFKEWRKVPAPRRGEIV----RQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMID-----ICDY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 82 AedepVAKTRQtqeddLY---IHSE-----------PLGVVLVIGAWNYPF-----NLTIqpmvgAIAAGNAVVLKPSEV 142
Cdd:cd07086 106 A----VGLSRM-----LYgltIPSErpghrlmeqwnPLGVVGVITAFNFPVavpgwNAAI-----ALVCGNTVVWKPSET 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 143 SDHMADLLSTLIPQYMDKDLYP-----VIKGGVpETTELLK--EKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKS 215
Cdd:cd07086 172 TPLTAIAVTKILAEVLEKNGLPpgvvnLVTGGG-DGGELLVhdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 216 PCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRV 294
Cdd:cd07086 251 AIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 295 INLIDSKK-----VAHGG---TWDQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYV 366
Cdd:cd07086 331 LNAIEIAKsqggtVLTGGkriDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSI 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568971234 367 FSNN-DKVIKKMIAETSSGGvtandvIVHITVPT------LPFGGVGNSGMGAYHGKKSFETFSHRRSCLV 430
Cdd:cd07086 411 FTEDlREAFRWLGPKGSDCG------IVNVNIPTsgaeigGAFGGEKETGGGRESGSDAWKQYMRRSTCTI 475
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
60-409 |
3.96e-49 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 175.12 E-value: 3.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 60 YYEEVAHVLDEIDFT---IKGLSDWAEDEPVakTRQTQEDDLYiHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVV 136
Cdd:PRK03137 127 WAEADADTAEAIDFLeyyARQMLKLADGKPV--ESRPGEHNRY-FYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 137 LKPSEVSDHMADLLSTLIPQY-MDKDLYPVIKGGVPETTELLkekFDH-----IMYTGSTAVGKIVMAAAAK------HL 204
Cdd:PRK03137 204 LKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYL---VDHpktrfITFTGSREVGLRIYERAAKvqpgqiWL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 205 TPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKQSHDYGR 284
Cdd:PRK03137 281 KRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGP 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 285 IINDRHFQRVINLIDSKK-----VAHGGTWDQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQRE 359
Cdd:PRK03137 361 VINQASFDKIMSYIEIGKeegrlVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTE 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 568971234 360 KPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITVPTLPFGGVGNSG 409
Cdd:PRK03137 441 YGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSG 490
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
103-431 |
1.97e-48 |
|
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: 172.17 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYPVIKGGVPETTELLKEKFD 182
Cdd:cd07107 115 EPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALVRHPD 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 183 --HIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGkfMN---SGQTCVAPDYILCDPSIQ 257
Cdd:cd07107 195 vkRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAG--MNftwCGQSCGSTSRLFVHESIY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 258 NEIVEKLKKSLKDFY-GEDAKQSHDYGRIINDRHFQRVINLIDSKK------VAHGGTWDQPS----RYIAPTILVDVDP 326
Cdd:cd07107 273 DEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIDSAKregarlVTGGGRPEGPAleggFYVEPTVFADVTP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 327 QSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITvpTLPFGGVG 406
Cdd:cd07107 353 GMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFL--GAPFGGVK 430
|
330 340
....*....|....*....|....*
gi 568971234 407 NSGMGAYHGKKSFETFSHRRSCLVR 431
Cdd:cd07107 431 NSGIGREECLEELLSYTQEKNVNVR 455
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
92-411 |
4.78e-47 |
|
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: 168.68 E-value: 4.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 92 QTQEDDLYIH-SEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYPVIKGGV 170
Cdd:cd07559 123 EIDEDTLSYHfHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 171 PETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYV-----DKDCDLDVACRRIAWGKFMNSGQT 243
Cdd:cd07559 203 SEAGKPLAShpRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFAFNQGEV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 244 CVAPDYILCDPSIQNEIVEKLKKSLkdfygEDAKQSHDY------GRIINDRHFQRVINLIDSKK-----VAHGGTWDQP 312
Cdd:cd07559 283 CTCPSRALVQESIYDEFIERAVERF-----EAIKVGNPLdpetmmGAQVSKDQLEKILSYVDIGKeegaeVLTGGERLTL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 313 SR-----YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVT 387
Cdd:cd07559 358 GGldkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVW 437
|
330 340
....*....|....*....|....
gi 568971234 388 ANdvIVHITVPTLPFGGVGNSGMG 411
Cdd:cd07559 438 VN--CYHQYPAHAPFGGYKKSGIG 459
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
100-411 |
5.96e-47 |
|
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: 168.40 E-value: 5.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 100 IHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYPVIKGGVPETTELLKE 179
Cdd:cd07117 132 VLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 180 K--FDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQ 257
Cdd:cd07117 212 HpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 258 NEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDSKK-----VAHGG---TWDQPSR--YIAPTILVDVDP 326
Cdd:cd07117 292 DEFVAKLKEKFENVkVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKeegakILTGGhrlTENGLDKgfFIEPTLIVNVTN 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 327 QSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANdvIVHITVPTLPFGGVG 406
Cdd:cd07117 372 DMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN--TYNQIPAGAPFGGYK 449
|
....*
gi 568971234 407 NSGMG 411
Cdd:cd07117 450 KSGIG 454
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
4-427 |
1.02e-46 |
|
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: 167.75 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 4 ISSIVNRARDAFNS-GKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKnewtSYYE---EVAHVLDEIDFTIKGL- 78
Cdd:cd07082 40 ILEAAETAYDAGRGwWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGK----TLKDalkEVDRTIDYIRDTIEELk 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 79 --------SDWAEDepvaktrqTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSE---VSDHMa 147
Cdd:cd07082 116 rldgdslpGDWFPG--------TKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATqgvLLGIP- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 148 dLLSTLIPQYMDKDLYPVIKGGVPETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKhlTPVTLELGGKSPCYVDKDCDL 225
Cdd:cd07082 187 -LAEAFHDAGFPKGVVNVVTGRGREIGDPLVThgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 226 DVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKK---SLKDFYGEDAkqSHDYGRIINDRHFQRVINLID--- 299
Cdd:cd07082 264 ELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEevaKLKVGMPWDN--GVDITPLIDPKSADFVEGLIDdav 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 300 SK--KVAHGGTWDQPSrYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKM 377
Cdd:cd07082 342 AKgaTVLNGGGREGGN-LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKL 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 568971234 378 IAETSSGGVTANDVIVHiTVPTLPFGGVGNSGMGAYHGKKSFETFSHRRS 427
Cdd:cd07082 421 ADALEVGTVNINSKCQR-GPDHFPFLGRKDSGIGTQGIGDALRSMTRRKG 469
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
100-423 |
1.82e-46 |
|
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: 166.75 E-value: 1.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 100 IHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKP--------SEVSDHMADLLStlIPqymdKDLYPVIKGGVP 171
Cdd:cd07120 113 VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPagqtaqinAAIIRILAEIPS--LP----AGVVNLFTESGS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 172 ETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDY 249
Cdd:cd07120 187 EGAAHLVAspDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSR 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 250 ILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLID------SKKVAHGGTWDQ---PSRYIAPT 319
Cdd:cd07120 267 VLVQRSIADEVRDRLAARLAAVkVGPGLDPASDMGPLIDRANVDRVDRMVEraiaagAEVVLRGGPVTEglaKGAFLRPT 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 320 ILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDvivHITV-P 398
Cdd:cd07120 347 LLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND---WNKLfA 423
|
330 340
....*....|....*....|....*
gi 568971234 399 TLPFGGVGNSGMGAYHGKKSFETFS 423
Cdd:cd07120 424 EAEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
77-435 |
7.32e-45 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 163.45 E-value: 7.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 77 GLSDWAEDEPVAKTRQTQEddlYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDhmadlLSTLIPQ 156
Cdd:PLN02766 134 GAADKIHGETLKMSRQLQG---YTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTP-----LSALFYA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 157 YMDKD------LYPVIKGGVPETTELLKEKFD--HIMYTGSTAVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDV 227
Cdd:PLN02766 206 HLAKLagvpdgVINVVTGFGPTAGAAIASHMDvdKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDM 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 228 ACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDSKK---- 302
Cdd:PLN02766 286 AVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWvVGDPFDPRARQGPQVDKQQFEKILSYIEHGKrega 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 303 --VAHGGTWDQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVikkmiAE 380
Cdd:PLN02766 366 tlLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDV-----AN 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 568971234 381 TSSGGVTANDVIVHITV---PTLPFGGVGNSGMGAYHGKKSFETFSHRRScLVRSLRN 435
Cdd:PLN02766 441 TVSRSIRAGTIWVNCYFafdPDCPFGGYKMSGFGRDQGMDALDKYLQVKS-VVTPLYN 497
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
103-435 |
4.92e-44 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 161.90 E-value: 4.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLipqYMDKDLYP----VIKGGVPETTELLK 178
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKL---LHEAGLPPgvlnVVSGFGPTAGAALA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 179 EKF--DHIMYTGSTAVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 255
Cdd:PLN02466 271 SHMdvDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHER 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 256 IQNEIVEKLK-KSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDS------KKVAHGGTWDQPSRYIAPTILVDVDPQS 328
Cdd:PLN02466 351 VYDEFVEKAKaRALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSgvesgaTLECGGDRFGSKGYYIQPTVFSNVQDDM 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 329 PVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTAN--DVIvhitVPTLPFGGVG 406
Cdd:PLN02466 431 LIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVF----DAAIPFGGYK 506
|
330 340
....*....|....*....|....*....
gi 568971234 407 NSGMGAYHGKKSFETFSHRRScLVRSLRN 435
Cdd:PLN02466 507 MSGIGREKGIYSLNNYLQVKA-VVTPLKN 534
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
104-411 |
1.50e-43 |
|
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: 158.95 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 104 PLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLS-TLIPQYMDKDLYPVIKGGVPETTELLK-EKF 181
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGeVLAETGLPKGAFSVLPCSRDDADLLVTdERI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 182 DHIMYTGSTAVG-KIVMAAAAKHltpVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEI 260
Cdd:cd07147 203 KLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 261 VEKLKKSLKDFYGEDAK-QSHDYGRIINDRHFQRVINLIDSK-----KVAHGGTWDQPSryIAPTILVDVDPQSPVMQEE 334
Cdd:cd07147 280 KSRLVARVKALKTGDPKdDATDVGPMISESEAERVEGWVNEAvdagaKLLTGGKRDGAL--LEPTILEDVPPDMEVNCEE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 335 IFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDvivhitVPT-----LPFGGVGNSG 409
Cdd:cd07147 358 VFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIND------VPTfrvdhMPYGGVKDSG 431
|
..
gi 568971234 410 MG 411
Cdd:cd07147 432 IG 433
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
8-426 |
1.66e-43 |
|
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: 159.22 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNewtsYYE---EVAHVLDEIDFTI------KGl 78
Cdd:cd07085 44 VAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKT----LADargDVLRGLEVVEFACsiphllKG- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 79 sdwaedepvaktrQTQED-----DLYIHSEPLGVVLVIGAWNYPF--NLTIQPMvgAIAAGNAVVLKPSE----VSDHMA 147
Cdd:cd07085 119 -------------EYLENvargiDTYSYRQPLGVVAGITPFNFPAmiPLWMFPM--AIACGNTFVLKPSErvpgAAMRLA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 148 DLLstlipqymDKDLYP-----VIKGGVPETTELLkekfDH-----IMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPC 217
Cdd:cd07085 184 ELL--------QEAGLPdgvlnVVHGGKEAVNALL----DHpdikaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 218 YVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLK---KSLKDFYGEDAKQshDYGRIINDRHFQRV 294
Cdd:cd07085 252 VVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVeraKKLKVGAGDDPGA--DMGPVISPAAKERI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 295 INLIDSKkVAHGGTW------DQPSRY-----IAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLA 363
Cdd:cd07085 330 EGLIESG-VEEGAKLvldgrgVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568971234 364 LYVFSNNDKVIKKMIAETSSGGVTANdviVHITVPT--LPFGGVGNSGMGAYH--GKKSFETFSHRR 426
Cdd:cd07085 409 AAIFTRSGAAARKFQREVDAGMVGIN---VPIPVPLafFSFGGWKGSFFGDLHfyGKDGVRFYTQTK 472
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
99-430 |
5.02e-43 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 158.12 E-value: 5.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 99 YIHSEPLGVVLVIGAWNYPfnltIQ-------PmvgAIAAGNAVVLKPSEVSDHMA-DLLSTLIPQYMDKDLYPVIKG-G 169
Cdd:PRK13252 137 YTRREPLGVCAGIGAWNYP----IQiacwksaP---ALAAGNAMIFKPSEVTPLTAlKLAEIYTEAGLPDGVFNVVQGdG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 170 vpETTELLKE--KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAP 247
Cdd:PRK13252 210 --RVGAWLTEhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNG 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 248 DYILCDPSIQNEIVEKLKKSLKDFY-GEDAKQSHDYGRIINDRHFQRVINLIDSKK-----VAHGGTWDQPSR-----YI 316
Cdd:PRK13252 288 TRVFVQKSIKAAFEARLLERVERIRiGDPMDPATNFGPLVSFAHRDKVLGYIEKGKaegarLLCGGERLTEGGfangaFV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 317 APTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGgvtandvIVHI- 395
Cdd:PRK13252 368 APTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAG-------ICWIn 440
|
330 340 350
....*....|....*....|....*....|....*....
gi 568971234 396 ----TVPTLPFGGVGNSGMGAYHGKKSFETFSHRRSCLV 430
Cdd:PRK13252 441 twgeSPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
64-423 |
3.59e-42 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 155.82 E-value: 3.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 64 VAHVL-DEIDFTIKGLSDWAE--DEPVAKTRQTQEDDL-YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKP 139
Cdd:PRK09847 113 IRHSLrDDIPGAARAIRWYAEaiDKVYGEVATTSSHELaMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 140 SEVSDHMADLLSTLIPQYMDKD-LYPVIKGGVPETTELLK--EKFDHIMYTGSTAVGKIVMAAAAK-HLTPVTLELGGKS 215
Cdd:PRK09847 193 SEKSPLSAIRLAGLAKEAGLPDgVLNVVTGFGHEAGQALSrhNDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 216 PCYVDKDC-DLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDFY-GEDAKQSHDYGRIINDRHFQR 293
Cdd:PRK09847 273 ANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADS 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 294 VINLI-----------DSKKVAHGGtwdqpsrYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPL 362
Cdd:PRK09847 353 VHSFIregeskgqlllDGRNAGLAA-------AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGL 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568971234 363 ALYVFSNNDKVIKKMIAETSSGGVTAN-----DVivhitvpTLPFGGVGNSGMGAYHGKKSFETFS 423
Cdd:PRK09847 426 GAAVWTRDLSRAHRMSRRLKAGSVFVNnyndgDM-------TVPFGGYKQSGNGRDKSLHALEKFT 484
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
92-416 |
6.09e-41 |
|
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: 152.16 E-value: 6.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 92 QTQEDDLYIHsEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQymdKDLYP----VIK 167
Cdd:cd07111 136 QLLDTELAGW-KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAE---AGLPPgvlnIVT 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 168 GGvPETTELLKEK--FDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCV 245
Cdd:cd07111 212 GN-GSFGSALANHpgVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCC 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 246 APDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDSKKvAHGGT-----WDQPSR--YIA 317
Cdd:cd07111 291 AGSRLLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADvfqpgADLPSKgpFYP 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 318 PTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTAN-----Dvi 392
Cdd:cd07111 370 PTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINghnlfD-- 447
|
330 340
....*....|....*....|....
gi 568971234 393 vhitvPTLPFGGVGNSGMGAYHGK 416
Cdd:cd07111 448 -----AAAGFGGYRESGFGREGGK 466
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
8-409 |
1.53e-38 |
|
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: 144.72 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYyEEVAHVLDEIDFTIKGLSD--WAEDE 85
Cdd:cd07095 6 VAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQ-TEVAAMAGKIDISIKAYHErtGERAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 86 PVAKTRqtqeddLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSE----VSDHMADLLStliPQYMDKD 161
Cdd:cd07095 85 PMAQGR------AVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSEltpaVAELMVELWE---EAGLPPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 162 LYPVIKGGVPETTELLK-EKFDHIMYTGSTAVGKIVMAAAAKHltP---VTLELGGKSPCYVDKDCDLDVACRRIAWGKF 237
Cdd:cd07095 156 VLNLVQGGRETGEALAAhEGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 238 MNSGQTCV-APDYILCDPSIQNEIVEKLKKSLK-----DFYGEDAKqshdYGRIINDRHFQRVINLIDsKKVAHGGT--- 308
Cdd:cd07095 234 LTAGQRCTcARRLIVPDGAVGDAFLERLVEAAKrlrigAPDAEPPF----MGPLIIAAAAARYLLAQQ-DLLALGGEpll 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 309 ----WDQPSRYIAPTILvDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSG 384
Cdd:cd07095 309 amerLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAG 387
|
410 420 430
....*....|....*....|....*....|.
gi 568971234 385 GVTANdvivhitVPT------LPFGGVGNSG 409
Cdd:cd07095 388 IVNWN-------RPTtgasstAPFGGVGLSG 411
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
99-411 |
9.52e-38 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 143.40 E-value: 9.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 99 YIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLipqymdkdlypVIKGGVPE------ 172
Cdd:cd07140 142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAEL-----------TVKAGFPKgvinil 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 173 --TTELLKEKF-DH-----IMYTGSTAVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQT 243
Cdd:cd07140 211 pgSGSLVGQRLsDHpdvrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGEN 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 244 CVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDsKKVAHGGTW-------DQPSRY 315
Cdd:cd07140 291 CIAAGRLFVEESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLVEYCE-RGVKEGATLvyggkqvDRPGFF 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 316 IAPTILVDVDPQSPVMQEEIFGPVMPIVCVRS--LDEAIKFINQREKPLALYVFSnndKVIKKmiAETSSGGVTANDVIV 393
Cdd:cd07140 370 FEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFT---KDINK--ALYVSDKLEAGTVFV 444
|
330 340
....*....|....*....|.
gi 568971234 394 HITVPT---LPFGGVGNSGMG 411
Cdd:cd07140 445 NTYNKTdvaAPFGGFKQSGFG 465
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
2-415 |
2.49e-36 |
|
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: 140.02 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 2 SNISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNeWTSYYEEVAHVLDEIDFTIKGLSDW 81
Cdd:cd07083 55 AEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKN-WVEAIDDVAEAIDFIRYYARAALRL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 82 AEDEPVAKTRQTQEDDLYIhsEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEvsdhMADLLSTLIPQYM-DK 160
Cdd:cd07083 134 RYPAVEVVPYPGEDNESFY--VGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAE----DAVVVGYKVFEIFhEA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 161 DLYPVIKGGVPETTELL------KEKFDHIMYTGSTAVGKIVMAAAAKHLT------PVTLELGGKSPCYVDKDCDLDVA 228
Cdd:cd07083 208 GFPPGVVQFLPGVGEEVgaylteHERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 229 CRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDSKK----- 302
Cdd:cd07083 288 VEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKnegql 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 303 VAHGGTWDQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLD--EAIKFINQREKPLALYVFSNNDKVIKKMIAE 380
Cdd:cd07083 368 VLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARRE 447
|
410 420 430
....*....|....*....|....*....|....*
gi 568971234 381 TSSGGVTANDVIVHITVPTLPFGGVGNSGMGAYHG 415
Cdd:cd07083 448 FHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
98-422 |
6.41e-35 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 135.80 E-value: 6.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 98 LYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTL-----IPqymdKDLYPVIKGGVPE 172
Cdd:PRK11241 140 LIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELairagIP----AGVFNVVTGSAGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 173 -----TTELLKEKfdhIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAP 247
Cdd:PRK11241 216 vggelTSNPLVRK---LSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 248 DYILCDPSIQNEIVEKLKKSLKDFY-GEDAKQSHDYGRIINDRHFQRVINLID------SKKVAHGGTWDQPSRYIAPTI 320
Cdd:PRK11241 293 NRLYVQDGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEEHIAdalekgARVVCGGKAHELGGNFFQPTI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 321 LVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITVPtl 400
Cdd:PRK11241 373 LVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVA-- 450
|
330 340
....*....|....*....|..
gi 568971234 401 PFGGVGNSGMGAYHGKKSFETF 422
Cdd:PRK11241 451 PFGGIKASGLGREGSKYGIEDY 472
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
4-411 |
9.01e-32 |
|
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: 126.38 E-value: 9.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 4 ISSIVNRARDAF-NSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKnEWTSYYEEVAHVLDEIDFTIKGLSDWA 82
Cdd:cd07148 23 IDKALDTAHALFlDRNNWLPAHERIAILERLADLMEERADELALLIAREGGK-PLVDAKVEVTRAIDGVELAADELGQLG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 83 EDE-PVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSevsdhMADLLSTLipQYMDKd 161
Cdd:cd07148 102 GREiPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA-----LATPLSCL--AFVDL- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 162 lypVIKGGVPE-----------TTELL--KEKFDHIMYTGSTAVGKIVMAAAAKHlTPVTLELGGKSPCYVDKDCDLDVA 228
Cdd:cd07148 174 ---LHEAGLPEgwcqavpcenaVAEKLvtDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 229 CRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKL-KKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSK-----K 302
Cdd:cd07148 250 IPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLaAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAvaagaR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 303 VAHGGTWDQPSRYiAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETS 382
Cdd:cd07148 330 LLCGGKRLSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLD 408
|
410 420 430
....*....|....*....|....*....|.
gi 568971234 383 SGGVTANDvivHIT--VPTLPFGGVGNSGMG 411
Cdd:cd07148 409 ATAVMVND---HTAfrVDWMPFAGRRQSGYG 436
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
77-411 |
2.25e-31 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 125.36 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 77 GLSDW-AEDEPV---AKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLST 152
Cdd:PRK13968 95 NLCDWyAEHGPAmlkAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 153 LipqYMDKDLYPVIKGGVPETTELLKEKFDH-----IMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDV 227
Cdd:PRK13968 175 V---FKDAGIPQGVYGWLNADNDGVSQMINDsriaaVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 228 ACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKL---KKSLKdfYGEDAKQSHDYGRI----INDRHFQRVIN---- 296
Cdd:PRK13968 252 AVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFvaaAAALK--MGDPRDEENALGPMarfdLRDELHHQVEAtlae 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 297 ----LIDSKKVAHGGTwdqpsrYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDK 372
Cdd:PRK13968 330 garlLLGGEKIAGAGN------YYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDET 403
|
330 340 350
....*....|....*....|....*....|....*....
gi 568971234 373 VIKKMIAETSSGGVTANDVIVhiTVPTLPFGGVGNSGMG 411
Cdd:PRK13968 404 QARQMAARLECGGVFINGYCA--SDARVAFGGVKKSGFG 440
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
10-419 |
4.02e-31 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 124.46 E-value: 4.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 10 RARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNewtsyyeeVAHVLDEIDFTIKGLSDWAE------ 83
Cdd:PRK09406 31 RAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT--------LASAKAEALKCAKGFRYYAEhaeall 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 84 -DEPvAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKpsevsdHMADllstlIPQ---YMD 159
Cdd:PRK09406 103 aDEP-ADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLK------HASN-----VPQtalYLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 160 kDLYPviKGGVPE---TTELL-KEKFDHIM---------YTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLD 226
Cdd:PRK09406 171 -DLFR--RAGFPDgcfQTLLVgSGAVEAILrdprvaaatLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 227 VACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDSkKVAH 305
Cdd:PRK09406 248 RAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALrVGDPTDPDTDVGPLATEQGRDEVEKQVDD-AVAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 306 GGTW-------DQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMI 378
Cdd:PRK09406 327 GATIlcggkrpDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFI 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 568971234 379 AETSSGGVTANDVIVhiTVPTLPFGGVGNSGMG---AYHGKKSF 419
Cdd:PRK09406 407 DDLEAGQVFINGMTV--SYPELPFGGVKRSGYGrelSAHGIREF 448
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
7-412 |
9.81e-31 |
|
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: 124.23 E-value: 9.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 7 IVNRARDAFNSGKTRPLQFRVEQLEALQRMINEN---LKGIS-----KALAsnlrknewtsyyEEVAHVLDEIDF----- 73
Cdd:cd07125 74 ALAIAAAAFAGWSATPVEERAEILEKAADLLEANrgeLIALAaaeagKTLA------------DADAEVREAIDFcryya 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 74 --TIKGLSDWAEDEPVAKTRQtqeddlyIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLS 151
Cdd:cd07125 142 aqARELFSDPELPGPTGELNG-------LELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 152 TL-----IPQYMdkdLYPVIKGGVPETTELLK-EKFDHIMYTGSTAVGKI---VMAAAAKHLTPVTLELGGKSPCYVDKD 222
Cdd:cd07125 215 ELlheagVPRDV---LQLVPGDGEEIGEALVAhPRIDGVIFTGSTETAKLinrALAERDGPILPLIAETGGKNAMIVDST 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 223 CDLDVACRRIAWGKFMNSGQTCVAPDyILCdpsIQNEIVEKLKKSLKDFY-----GEDAKQSHDYGRIINDRHFQRVINL 297
Cdd:cd07125 292 ALPEQAVKDVVQSAFGSAGQRCSALR-LLY---LQEEIAERFIEMLKGAMaslkvGDPWDLSTDVGPLIDKPAGKLLRAH 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 298 ID-----SKKVAHGGTWDQPSRYIAPTILVDVDpqSPVMQEEIFGPVMPIVCVRS--LDEAIKFINQREKPLALYVFSNN 370
Cdd:cd07125 368 TElmrgeAWLIAPAPLDDGNGYFVAPGIIEIVG--IFDLTTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSRD 445
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 568971234 371 DKVIKKMIAETSSGGVTANDVIVHITVPTLPFGGVGNSGMGA 412
Cdd:cd07125 446 EREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGP 487
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
8-414 |
1.30e-30 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 123.45 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNeWTSYYEEVAHVLDEIDFTIkGLSDWAEDEPV 87
Cdd:TIGR01722 44 VASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKT-HSDALGDVARGLEVVEHAC-GVNSLLKGETS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 88 akTRQTQEDDLYIHSEPLGVVLVIGAWNYP--FNLTIQPMvgAIAAGNAVVLKPSEVSDHMADLLSTLIPQY-MDKDLYP 164
Cdd:TIGR01722 122 --TQVATRVDVYSIRQPLGVCAGITPFNFPamIPLWMFPI--AIACGNTFVLKPSEKVPSAAVKLAELFSEAgAPDGVLN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 165 VIKGGVPETTELLKE-KFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQT 243
Cdd:TIGR01722 198 VVHGDKEAVDRLLEHpDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 244 CVAPDYILCDPSIQN---EIVEKLKKsLKDFYGEDAkqSHDYGRIINDRHFQRVINLIDSkKVAHGGTWDQPSR------ 314
Cdd:TIGR01722 278 CMAISAAVLVGAADEwvpEIRERAEK-IRIGPGDDP--GAEMGPLITPQAKDRVASLIAG-GAAEGAEVLLDGRgykvdg 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 315 -----YIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTAN 389
Cdd:TIGR01722 354 yeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN 433
|
410 420
....*....|....*....|....*
gi 568971234 390 dVIVHITVPTLPFGGVGNSGMGAYH 414
Cdd:TIGR01722 434 -VPIPVPLPYFSFTGWKDSFFGDHH 457
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
3-417 |
2.14e-29 |
|
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: 119.62 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 3 NISSIVNRARDAFNSGKTRPLQFRVEqleaLQRMINENLKGISKALASNLRKNEWTSYYE---EVAHVLDEIDFTIkGLS 79
Cdd:cd07130 35 DYESTIKAAQEAFKEWRDVPAPKRGE----IVRQIGDALRKKKEALGKLVSLEMGKILPEglgEVQEMIDICDFAV-GLS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 80 dwaedepvaktRQtqeddLY---IHSE-----------PLGVVLVIGAWNYP-----FNLTIqpmvgAIAAGNAVVLKPS 140
Cdd:cd07130 110 -----------RQ-----LYgltIPSErpghrmmeqwnPLGVVGVITAFNFPvavwgWNAAI-----ALVCGNVVVWKPS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 141 EVSDHMADLLSTLIPQYMDK-----DLYPVIKGGVPETTELLKEK-FDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGK 214
Cdd:cd07130 169 PTTPLTAIAVTKIVARVLEKnglpgAIASLVCGGADVGEALVKDPrVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 215 SPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQR 293
Cdd:cd07130 249 NAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVrIGDPLDDGTLVGPLHTKAAVDN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 294 VINLIDSKKVAHGG------TWDQPSRYIAPTIlVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVF 367
Cdd:cd07130 329 YLAAIEEAKSQGGTvlfggkVIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIF 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 568971234 368 SNNDKVIKKMIaetssgGVTANDV-IVHITVPTlpfggvgnSGM---GAYHGKK 417
Cdd:cd07130 408 TTDLRNAFRWL------GPKGSDCgIVNVNIGT--------SGAeigGAFGGEK 447
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
92-430 |
3.62e-29 |
|
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: 119.09 E-value: 3.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 92 QTQEDDLYIH-SEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYPVIKGGV 170
Cdd:cd07116 123 EIDENTVAYHfHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 171 PETTELL--KEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSP-----CYVDKDCD-LDVACRRIAWGKFmNSGQ 242
Cdd:cd07116 203 LEAGKPLasSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniffaDVMDADDAfFDKALEGFVMFAL-NQGE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 243 TCVAPDYILCDPSIQNEIVEKLKKSLKDFygedaKQSH--DYGRIINDR----HFQRVINLIDSKK-----VAHGGTWDQ 311
Cdd:cd07116 282 VCTCPSRALIQESIYDRFMERALERVKAI-----KQGNplDTETMIGAQasleQLEKILSYIDIGKeegaeVLTGGERNE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 312 PSR-----YIAPTiLVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGV 386
Cdd:cd07116 357 LGGllgggYYVPT-TFKGGNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRV 435
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568971234 387 TANdvIVHITVPTLPFGGVGNSGMGAYHGKKSFETFSHRRSCLV 430
Cdd:cd07116 436 WTN--CYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
104-412 |
8.34e-29 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 118.32 E-value: 8.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 104 PLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKP---SEVSD-HMAD-LLSTLIPqymdKDLYPVIKGGVPETTELLK 178
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPptqGAVAAlHMVHcFHLAGFP----KGLISCVTGKGSEIGDFLT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 179 EK--FDHIMYTGstavGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 255
Cdd:PLN00412 234 MHpgVNCISFTG----GDTGIAISKKaGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMES 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 256 IQNEIVEKLKKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSKKvAHGGTWDQPSR----YIAPTILVDVDPQSPVM 331
Cdd:PLN00412 310 VADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAK-EKGATFCQEWKregnLIWPLLLDNVRPDMRIA 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 332 QEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNN-DKVIkkMIAETSSGGVtandviVHITVPT------LPFGG 404
Cdd:PLN00412 389 WEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDiNKAI--LISDAMETGT------VQINSAPargpdhFPFQG 460
|
....*...
gi 568971234 405 VGNSGMGA 412
Cdd:PLN00412 461 LKDSGIGS 468
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
63-430 |
1.06e-24 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 106.46 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 63 EVAHVLDEIDFTIkGLSdwaedepvaktrqTQEDDLYIHSE-----------PLGVVLVIGAWNYP-----FNLTIqpmv 126
Cdd:PLN02315 116 EVQEIIDMCDFAV-GLS-------------RQLNGSIIPSErpnhmmmevwnPLGIVGVITAFNFPcavlgWNACI---- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 127 gAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYP-----VIKGGVPETTELLKE-KFDHIMYTGSTAVGKIVMAAA 200
Cdd:PLN02315 178 -ALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPgaiftSFCGGAEIGEAIAKDtRIPLVSFTGSSKVGLMVQQTV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 201 AKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKqsh 280
Cdd:PLN02315 257 NARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPL--- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 281 DYGRIINDRH-------FQRVINLIDSK--KVAHGGTWDQPS-RYIAPTIlVDVDPQSPVMQEEIFGPVMPIVCVRSLDE 350
Cdd:PLN02315 334 EKGTLLGPLHtpeskknFEKGIEIIKSQggKILTGGSAIESEgNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 351 AIKFINQREKPLALYVFSNNDKVIKKMIaetssgGVTANDV-IVHITVPTL------PFGGVGNSGMGAYHGKKSFETFS 423
Cdd:PLN02315 413 AIEINNSVPQGLSSSIFTRNPETIFKWI------GPLGSDCgIVNVNIPTNgaeiggAFGGEKATGGGREAGSDSWKQYM 486
|
....*..
gi 568971234 424 HRRSCLV 430
Cdd:PLN02315 487 RRSTCTI 493
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
103-415 |
3.60e-24 |
|
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: 104.99 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIpqymdkdlypvIKGGVPETT-ELL---- 177
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELM-----------QEAGFPAGTiQLLpgrg 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 178 ---------KEKFDHIMYTGSTAVGKIVMAAAAKHL---TPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCV 245
Cdd:TIGR01238 228 advgaaltsDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCS 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 246 APDYILCDPSIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLID-----SKKVAHGGTWD----QPSRY 315
Cdd:TIGR01238 308 ALRVLCVQEDVADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDAEAKQNLLAHIEhmsqtQKKIAQLTLDDsracQHGTF 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 316 IAPTiLVDVDPQSPvMQEEIFGPVMPIVCVRS--LDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIV 393
Cdd:TIGR01238 388 VAPT-LFELDDIAE-LSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQV 465
|
330 340
....*....|....*....|..
gi 568971234 394 HITVPTLPFGGVGNSGMGAYHG 415
Cdd:TIGR01238 466 GAVVGVQPFGGQGLSGTGPKAG 487
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
4-409 |
7.28e-24 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 103.88 E-value: 7.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 4 ISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYyEEVAHVLDEIDFTIKGLSD--W 81
Cdd:PRK09457 39 VDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAA-TEVTAMINKIAISIQAYHErtG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 82 AEDEPVAKTRQTqeddlyIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTL-----IPq 156
Cdd:PRK09457 118 EKRSEMADGAAV------LRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLwqqagLP- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 157 ymdKDLYPVIKGGvPETTELL--KEKFDHIMYTGSTAVGKIVMAAAAKHltP---VTLELGGKSPCYVDKDCDLDVACRR 231
Cdd:PRK09457 191 ---AGVLNLVQGG-RETGKALaaHPDIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 232 IAWGKFMNSGQTCVAPDYILCDPSIQ-NEIVEKLKKSLKdfygedakqshdygRIINDRHFQR-------VIN------L 297
Cdd:PRK09457 265 IIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAK--------------RLTVGRWDAEpqpfmgaVISeqaaqgL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 298 IDSKK--VAHGGT-------WDQPSRYIAPTILvDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFS 368
Cdd:PRK09457 331 VAAQAqlLALGGKsllemtqLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLS 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 568971234 369 NNDKVIKKMIAETSSGgvtandvIVHITVPT------LPFGGVGNSG 409
Cdd:PRK09457 410 DDREDYDQFLLEIRAG-------IVNWNKPLtgassaAPFGGVGASG 449
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
8-427 |
4.22e-23 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 102.13 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 8 VNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYyEEVAHVLDEIDFTIkGLSDWAEDEPV 87
Cdd:PLN02419 157 VSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSH-GDIFRGLEVVEHAC-GMATLQMGEYL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 88 AKTrqTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYPVIK 167
Cdd:PLN02419 235 PNV--SNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 168 GGVPETTELL--KEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCV 245
Cdd:PLN02419 313 HGTNDTVNAIcdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCM 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 246 APDYILC---DPSIQNEIVEKlKKSLKDFYGEDAKQshDYGRIINDRHFQRVINLIDS------KKVAHGGTWDQPS--- 313
Cdd:PLN02419 393 ALSTVVFvgdAKSWEDKLVER-AKALKVTCGSEPDA--DLGPVISKQAKERICRLIQSgvddgaKLLLDGRDIVVPGyek 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 314 -RYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANdvi 392
Cdd:PLN02419 470 gNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN--- 546
|
410 420 430
....*....|....*....|....*....|....*....
gi 568971234 393 VHITVPTLPFGGVGNSGMGA----YHGKKSFETFSHRRS 427
Cdd:PLN02419 547 VPIPVPLPFFSFTGNKASFAgdlnFYGKAGVDFFTQIKL 585
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
84-431 |
3.77e-21 |
|
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: 95.38 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 84 DEPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQ--YMDKD 161
Cdd:cd07084 80 HEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 162 LYPVIKGGVPETTELLKE-KFDHIMYTGSTAVGKIVMAAAakHLTPVTLELGGKSPCYVDKDCD-LDVACRRIAWGKFMN 239
Cdd:cd07084 160 DVTLINGDGKTMQALLLHpNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTAC 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 240 SGQTCVAPDYILC--DPSIQnEIVEKLKKSLKDFYGEDA----KQSHDYGRIINDR--HFQRVInLIDSKKVAHGGTWDQ 311
Cdd:cd07084 238 SGQKCTAQSMLFVpeNWSKT-PLVEKLKALLARRKLEDLllgpVQTFTTLAMIAHMenLLGSVL-LFSGKELKNHSIPSI 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 312 PSRYIAPTILVDVDP---QSPVMQEEIFGPVMPIVCVRSLDEA--IKFINQREKPLALYVFSNNDKVIKKMIAETSSGGV 386
Cdd:cd07084 316 YGACVASALFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGR 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 568971234 387 TANDVIVHITVPTLPFGGVGNSGMGAYHGKKSFET--FSHRRSCLVR 431
Cdd:cd07084 396 TYAILRGRTGVAPNQNHGGGPAADPRGAGIGGPEAikLVWRCHAEQA 442
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
104-409 |
1.62e-17 |
|
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: 84.95 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 104 PL-GVVLVIGawnyPFNLTiqpmvgAIAA---------GNAVVLKPSEvsdhMADLLSTLIPQYMDKDLYP--VIK---G 168
Cdd:cd07123 169 PLeGFVYAVS----PFNFT------AIGGnlagapalmGNVVLWKPSD----TAVLSNYLVYKILEEAGLPpgVINfvpG 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 169 GVPETTE--LLKEKFDHIMYTGSTAVGKIVMAAAAKHLT-----P-VTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNS 240
Cdd:cd07123 235 DGPVVGDtvLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQ 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 241 GQTCVAPD--YIlcdP-SIQNEIVEKLKKSLKDF-YGEDAKQSHDYGRIINDRHFQRVINLIDSKK------VAHGGTWD 310
Cdd:cd07123 315 GQKCSAASraYV---PeSLWPEVKERLLEELKEIkMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKsdpeaeIIAGGKCD 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 311 QPSRY-IAPTILVDVDPQSPVMQEEIFGPVmpiVCV-----RSLDEAIKFINQREkPLALY--VFSNNDKVIKKmiAET- 381
Cdd:cd07123 392 DSVGYfVEPTVIETTDPKHKLMTEEIFGPV---LTVyvypdSDFEETLELVDTTS-PYALTgaIFAQDRKAIRE--ATDa 465
|
330 340 350
....*....|....*....|....*....|.
gi 568971234 382 ---SSGGVTANDVIVHITVPTLPFGGVGNSG 409
Cdd:cd07123 466 lrnAAGNFYINDKPTGAVVGQQPFGGARASG 496
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
104-411 |
1.04e-16 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 83.10 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 104 PLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSE----VSDHMADLLstlipqymdkdlypvIKGGVPE-TTELL- 177
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEqtplIAAQAVRIL---------------LEAGVPAgVVQLLp 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 178 ------------KEKFDHIMYTGSTAVGKIVMAAAAKHL------TPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMN 239
Cdd:PRK11809 833 grgetvgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDS 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 240 SGQTCVAPDyILCdpsIQNEIVEKLKKSLKDFYGEDA-----KQSHDYGRIIN-------DRHFQRVINliDSKKV---- 303
Cdd:PRK11809 913 AGQRCSALR-VLC---LQDDVADRTLKMLRGAMAECRmgnpdRLSTDIGPVIDaeakaniERHIQAMRA--KGRPVfqaa 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 304 -AHGGTWDQPSrYIAPTI--LVDVDPqspvMQEEIFGPVMPIVCVRS--LDEAIKFINQREKPLALYVFSNNDKVIKKMI 378
Cdd:PRK11809 987 rENSEDWQSGT-FVPPTLieLDSFDE----LKREVFGPVLHVVRYNRnqLDELIEQINASGYGLTLGVHTRIDETIAQVT 1061
|
330 340 350
....*....|....*....|....*....|...
gi 568971234 379 AETSSGGVTANDVIVHITVPTLPFGGVGNSGMG 411
Cdd:PRK11809 1062 GSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
102-411 |
1.94e-15 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 79.14 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 102 SEPLGVVLVIGAWNYPfnLTIqpMVG----AIAAGNAVVLKPSEVSdhmadllsTLIPQYMDKDLYpviKGGVPETT-EL 176
Cdd:PRK11905 674 HKPLGPVVCISPWNFP--LAI--FTGqiaaALVAGNTVLAKPAEQT--------PLIAARAVRLLH---EAGVPKDAlQL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 177 L-------------KEKFDHIMYTGSTAVGKIVMAAAAKHLT-PVTL--ELGGKSPCYVDKDCDLDVACRRIAWGKFMNS 240
Cdd:PRK11905 739 LpgdgrtvgaalvaDPRIAGVMFTGSTEVARLIQRTLAKRSGpPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSA 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 241 GQTCVAPDyILCdpsIQNEIVEKLKKSLKDFYGE-----DAKQSHDYGRIIND-------RHFQ------RVINLIDSKK 302
Cdd:PRK11905 819 GQRCSALR-VLC---LQEDVADRVLTMLKGAMDElrigdPWRLSTDVGPVIDAeaqanieAHIEamraagRLVHQLPLPA 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 303 VAHGGTwdqpsrYIAPTILvDVDPQSpVMQEEIFGPVMPIVCVRS--LDEAIKFINQREKPLALYVFSNNDKVIKKMIAE 380
Cdd:PRK11905 895 ETEKGT------FVAPTLI-EIDSIS-DLEREVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSR 966
|
330 340 350
....*....|....*....|....*....|.
gi 568971234 381 TSSGGVTANDVIVHITVPTLPFGGVGNSGMG 411
Cdd:PRK11905 967 IRAGNIYVNRNIIGAVVGVQPFGGEGLSGTG 997
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
62-386 |
2.39e-11 |
|
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: 65.58 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 62 EEVAHVLDEIDFtIKGLSDWaeDEPVAKTRQTQEDDLYiHSEPLGVVLVIG-----AWN-YPfnltiqPMVGAIAAGNAV 135
Cdd:cd07127 155 EAVAYAWREMSR-IPPTAEW--EKPQGKHDPLAMEKTF-TVVPRGVALVIGcstfpTWNgYP------GLFASLATGNPV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 136 VLKPsevsdHMADLL----------STLIPQYMDKDLypVIKGGVPETTELLKEKFDH-----IMYTGSTAVGKIVMAAA 200
Cdd:cd07127 225 IVKP-----HPAAILplaitvqvarEVLAEAGFDPNL--VTLAADTPEEPIAQTLATRpevriIDFTGSNAFGDWLEANA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 201 AKHLtpVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCdPS--IQN--------EIVEKLKKSLKD 270
Cdd:cd07127 298 RQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYV-PRdgIQTddgrksfdEVAADLAAAIDG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 271 FYGEDAKQSHDYGRIINDRHFQRVIN-------LIDSKKVAHGGTWDQPSRyiAPTIL-VDVDPQSPVMQEEiFGPVMPI 342
Cdd:cd07127 375 LLADPARAAALLGAIQSPDTLARIAEarqlgevLLASEAVAHPEFPDARVR--TPLLLkLDASDEAAYAEER-FGPIAFV 451
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 568971234 343 VCVRSLDEAIKFINQ--REK-PLALYVFSNNDKVIKKMIAETSSGGV 386
Cdd:cd07127 452 VATDSTDHSIELAREsvREHgAMTVGVYSTDPEVVERVQEAALDAGV 498
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
104-359 |
1.16e-10 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 63.33 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 104 PLGVVLVIGAWNYPFNLTIqpmVG-----AIAAGNAVVLKPSevSDHMA--DLLSTLIPQY-----MDKDLYPVIKGGVP 171
Cdd:cd07129 105 PLGPVAVFGASNFPLAFSV---AGgdtasALAAGCPVVVKAH--PAHPGtsELVARAIRAAlratgLPAGVFSLLQGGGR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 172 ET-TELLKekfdH-----IMYTGSTAVGKIVMAAAAKHLT--PVTLELGGKSPCYVdkdcdLD--VACRRIAWGK-F--- 237
Cdd:cd07129 180 EVgVALVK----HpaikaVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFI-----LPgaLAERGEAIAQgFvgs 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 238 --MNSGQTCVAPDYILcdpSIQNEIVEKLKKSLKDFYGEDAKQSHDYGRIIndRHFQRVINLI----DSKKVAHGGTWDQ 311
Cdd:cd07129 251 ltLGAGQFCTNPGLVL---VPAGPAGDAFIAALAEALAAAPAQTMLTPGIA--EAYRQGVEALaaapGVRVLAGGAAAEG 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568971234 312 PSRYiAPTILVdVDPQS----PVMQEEIFGPVMPIVCVRSLDEAIKFINQRE 359
Cdd:cd07129 326 GNQA-APTLFK-VDAAAfladPALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
103-411 |
7.41e-09 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 58.29 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLipqymdkdLYpviKGGVPETT-ELL---- 177
Cdd:PRK11904 683 HGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKL--------LH---EAGIPKDVlQLLpgdg 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 178 ---------KEKFDHIMYTGSTAVGKIV-MAAAAKHLTPVTL--ELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCV 245
Cdd:PRK11904 752 atvgaaltaDPRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCS 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 246 APDyILCdpsIQNEIVEKLKKSLKDFY-----GEDAKQSHDYGRIIN-------DRHFQRVINliDSKKVAHG--GTWDQ 311
Cdd:PRK11904 832 ALR-VLF---VQEDIADRVIEMLKGAMaelkvGDPRLLSTDVGPVIDaeakanlDAHIERMKR--EARLLAQLplPAGTE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 312 PSRYIAPTI--LVDVDpqspVMQEEIFGPVMPIVCVRS--LDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVT 387
Cdd:PRK11904 906 NGHFVAPTAfeIDSIS----QLEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVY 981
|
330 340
....*....|....*....|....
gi 568971234 388 ANDVIVHITVPTLPFGGVGNSGMG 411
Cdd:PRK11904 982 VNRNQIGAVVGVQPFGGQGLSGTG 1005
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
128-376 |
4.31e-08 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 55.19 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 128 AIAAGNAVVLKPS----EVSDHMADLL-STLIPQYMDKDLYPVI-KGGVPETTELLKEK-FDHIMYTGSTAVGKivmaAA 200
Cdd:cd07122 119 ALKTRNAIIFSPHprakKCSIEAAKIMrEAAVAAGAPEGLIQWIeEPSIELTQELMKHPdVDLILATGGPGMVK----AA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 201 AKHLTPVtleLG---GKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKslkdfYGedak 277
Cdd:cd07122 195 YSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVDDEIYDEVRAELKR-----RG---- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 278 qshdyGRIINDRHFQRVINLI-DSKKVAHGGTWDQPSRYIA-------P---TILV----DVDPQSPVMQEEIFgPVMPI 342
Cdd:cd07122 263 -----AYFLNEEEKEKLEKALfDDGGTLNPDIVGKSAQKIAelagievPedtKVLVaeetGVGPEEPLSREKLS-PVLAF 336
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568971234 343 VCVRSLDEAIkfinqrEKPLALYVF----------SNNDKVIKK 376
Cdd:cd07122 337 YRAEDFEEAL------EKARELLEYggaghtavihSNDEEVIEE 374
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
106-383 |
4.72e-08 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 55.35 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 106 GVVLVIGAWNYPfnltIQPMVGAIA----AGNAVVLKPSEVSDHMADLLSTLIpqyMDKDLYP-----VIKGGVPETTEL 176
Cdd:cd07128 146 GVAVHINAFNFP----VWGMLEKFApallAGVPVIVKPATATAYLTEAVVKDI---VESGLLPegalqLICGSVGDLLDH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 177 LKEkFDHIMYTGSTAVGKI--VMAAAAKHLTPVTLE--------LGgksPCYVDKDCDLDVACRRIAWGKFMNSGQTCVA 246
Cdd:cd07128 219 LGE-QDVVAFTGSAATAAKlrAHPNIVARSIRFNAEadslnaaiLG---PDATPGTPEFDLFVKEVAREMTVKAGQKCTA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 247 PDYILCDPSIQNEIVEKLKKSL-KDFYGEDAKQSHDYGRIINDRHFQRV---INLIDSKKVAHGGTWDQPSR-------- 314
Cdd:cd07128 295 IRRAFVPEARVDAVIEALKARLaKVVVGDPRLEGVRMGPLVSREQREDVraaVATLLAEAEVVFGGPDRFEVvgadaekg 374
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568971234 315 -YIAPTILV--DVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSS 383
Cdd:cd07128 375 aFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAP 446
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
103-411 |
5.69e-08 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 55.33 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 103 EPLGVVLVIGAWNYPfnLTI---QpMVGAIAAGNAVVLKPSEvsdhmadllST-LIPQYMDKDLYpviKGGVP------- 171
Cdd:COG4230 679 RGRGVFVCISPWNFP--LAIftgQ-VAAALAAGNTVLAKPAE---------QTpLIAARAVRLLH---EAGVPadvlqll 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 172 ----ETT--ELLK-EKFDHIMYTGSTAVGKIV-MAAAAKHLTPVTL--ELGGKSPCYVD------KDCDlDVacrrIAwG 235
Cdd:COG4230 744 pgdgETVgaALVAdPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIVDssalpeQVVD-DV----LA-S 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 236 KFMNSGQTCVAPDyILCdpsIQNEIVEKLKKSLK---DFY--GEDAKQSHDYGRIIND---RHFQRVINLIDSK------ 301
Cdd:COG4230 818 AFDSAGQRCSALR-VLC---VQEDIADRVLEMLKgamAELrvGDPADLSTDVGPVIDAearANLEAHIERMRAEgrlvhq 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 302 ----KVAHGGTwdqpsrYIAPTI--LVDVDpqspVMQEEIFGPVMPIVCVRS--LDEAIKFINQREKPLALYVFSNNDKV 373
Cdd:COG4230 894 lplpEECANGT------FVAPTLieIDSIS----DLEREVFGPVLHVVRYKAdeLDKVIDAINATGYGLTLGVHSRIDET 963
|
330 340 350
....*....|....*....|....*....|....*...
gi 568971234 374 IKKMIAETSSGGVTANDVIVHITVPTLPFGGVGNSGMG 411
Cdd:COG4230 964 IDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTG 1001
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
7-265 |
1.43e-07 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, 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. This group includes families ALDH18, ALDH19, and ALDH20 and represents 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: 143396 [Multi-domain] Cd Length: 397 Bit Score: 53.38 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 7 IVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLK---GISK-ALASNLRKNEWTsyYEEVAHVLDEidftikglsdWA 82
Cdd:cd07077 21 IINAIANALYDTRQRLASEAVSERGAYIRSLIANWIammGCSEsKLYKNIDTERGI--TASVGHIQDV----------LL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 83 EDEpvaktrqtqeDDLYIHSEPLGVVLVIGAWNYPFnLTIQPMVGAIAAGNAVVLKPS---EVSDHMADLLS-TLIPQYM 158
Cdd:cd07077 89 PDN----------GETYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHpsaPFTNRALALLFqAADAAHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 159 DKDLYPVI-KGGVPETTELLK-EKFDHIMYTGSTAVGKivmaAAAKH--LTPVTLELGGKSPCYVDKDCDLDVACRRIAW 234
Cdd:cd07077 158 PKILVLYVpHPSDELAEELLShPKIDLIVATGGRDAVD----AAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHD 233
|
250 260 270
....*....|....*....|....*....|.
gi 568971234 235 GKFMNsGQTCVAPDYILCDPSIQNEIVEKLK 265
Cdd:cd07077 234 SKFFD-QNACASEQNLYVVDDVLDPLYEEFK 263
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
94-409 |
1.79e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 53.04 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 94 QEDDLY---IHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQymdkdlyPVIKGGV 170
Cdd:cd07081 82 TGDENGgtlIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQ-------AAVAAGA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 171 PE---------TTELLKEKFDH-----IMYTGstavGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGK 236
Cdd:cd07081 155 PEnligwidnpSIELAQRLMKFpgiglLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 237 FMNSGQTCVAPDYILCDPSIQNEIVEKLK-KSLKDFYGEDAKQSHDYgrIINDRHFQRVINLIDSKKVAHGGTWDQPSRY 315
Cdd:cd07081 231 TFDNGVICASEQSVIVVDSVYDEVMRLFEgQGAYKLTAEELQQVQPV--ILKNGDVNRDIVGQDAYKIAAAAGLKVPQET 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 316 IAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIkfinqrEKPLALY----------VFSNNDKVIKKMiaetSSGG 385
Cdd:cd07081 309 RILIGEVTSLAEHEPFAHEKLSPVLAMYRAANFADAD------AKALALKleggcghtsaMYSDNIKAIENM----NQFA 378
|
330 340
....*....|....*....|....
gi 568971234 386 VTANDVIVHITVPTlPFGGVGNSG 409
Cdd:cd07081 379 NAMKTSRFVKNGPC-SQGGLGDLY 401
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
44-384 |
2.90e-06 |
|
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: 49.42 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 44 ISKALASNLRKNEWTSYY----EEVA-----HVLDEIDFTIKGLSDWAEDEP--------VAKTRQTQEDDLYihSEPLG 106
Cdd:cd07126 67 VSHRVAHELRKPEVEDFFarliQRVApksdaQALGEVVVTRKFLENFAGDQVrflarsfnVPGDHQGQQSSGY--RWPYG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 107 VVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLK-PSEVSDHMADLLSTLIPQYM---DKDLypvIKGGVPETTELLKE-KF 181
Cdd:cd07126 145 PVAIITPFNFPLEIPALQLMGALFMGNKPLLKvDSKVSVVMEQFLRLLHLCGMpatDVDL---IHSDGPTMNKILLEaNP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 182 DHIMYTGSTAV---------GKIVMAAAA---KHLTPVTLELGgkspcYVDKDCDLDV-ACrriawgkfmnSGQTCVAPD 248
Cdd:cd07126 222 RMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQDAyAC----------SGQKCSAQS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 249 YILCDPS-IQNEIVEKLKKslkdFYGEDAKQSHDYGRII---NDRHFQRVINL--IDSKKVAHGG----TWDQPSRY--I 316
Cdd:cd07126 287 ILFAHENwVQAGILDKLKA----LAEQRKLEDLTIGPVLtwtTERILDHVDKLlaIPGAKVLFGGkpltNHSIPSIYgaY 362
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568971234 317 APTIlVDVDPQSPVMQE-------EIFGPvMPIVCV---RSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSG 384
Cdd:cd07126 363 EPTA-VFVPLEEIAIEEnfelvttEVFGP-FQVVTEykdEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNG 438
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
3-268 |
1.03e-05 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 47.44 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 3 NISSIVNRARDAF-NSGKTRPLQFRVEQLEALQR-MINenlkgISKALASNLRKNEwtsYYEEVAHVLDEIDFTikglsd 80
Cdd:pfam05893 8 EILDLLERAAKLWaDPNYSKRHIETLAQITGYSEaMLN-----YLKSLMAFCRRRN---LQNVLESELGQPFIL------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 81 waeDEPVaktrqtQEDDLYIHSEPLGVVLVIGAWNYPFnLTIQPMVGAIAAGNAVVLKPSEvSDHM--ADLLSTLIPQYM 158
Cdd:pfam05893 74 ---DEWL------PTKPSYEKAFPPGLVFHVLSGNVPL-LPVMSILMGLLVKNVNLLKVSS-SDPFtaAALLASFADLDP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 159 DKDLYPVI-----KGGVPETTELLKEKFDHIMYTGSTAVGKIVM--AAAAKHLtpvtLELGGK-SPCYVDKDCDLDVACR 230
Cdd:pfam05893 143 THPLADSLsvvywDGGSTQLEDLIVANADVVIAWGGEDAINAIRecLKPGKQW----IDFGAKiSFAVVDREAALDKAAE 218
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568971234 231 RIAWGKFMNSGQTCVAPDYILCDPSIQN---EIVEKLKKSL 268
Cdd:pfam05893 219 RAADDICVFDQQACLSPQTVFVESDDKItpdEFAERLAAAL 259
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
104-353 |
5.50e-05 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 45.31 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 104 PLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKP----SEVSDHMADLLSTLI-----PQymdkDLYPVIKGGVPETT 174
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgaKKVSAYAVELINKAIaeaggPD----NLVVTVEEPTIETT 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 175 ELLkekFDH-----IMYTGSTAVGKIVMAAAAKhltpvtlELG---GKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVA 246
Cdd:cd07121 173 NEL---MAHpdinlLVVTGGPAVVKAALSSGKK-------AIGagaGNPPVVVDETADIEKAARDIVQGASFDNNLPCIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 247 PDYILCDPSIQNEIVEKLKKS----LKDFYGEDAKQS---HDYGRIINDRHFQRvinliDSKKVAH--GGTWDQPSRyia 317
Cdd:cd07121 243 EKEVIAVDSVADYLIAAMQRNgayvLNDEQAEQLLEVvllTNKGATPNKKWVGK-----DASKILKaaGIEVPADIR--- 314
|
250 260 270
....*....|....*....|....*....|....*.
gi 568971234 318 pTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIK 353
Cdd:cd07121 315 -LIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
126-353 |
2.25e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 43.35 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 126 VGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYP-----VIKGGVPETTELLkekFDH-----IMYTGSTAV--- 192
Cdd:PRK15398 151 ISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAAGGPenlvvTVAEPTIETAQRL---MKHpgialLVVTGGPAVvka 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 193 ----GKIVMAAAAkhltpvtlelgGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKsl 268
Cdd:PRK15398 228 amksGKKAIGAGA-----------GNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEK-- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971234 269 kdfygEDAKQshdygriINDRHFQRVINLIDSKKVAHGGTW-DQPSRYIA-----------PTILVDVDPQSPVMQEEIF 336
Cdd:PRK15398 295 -----NGAVL-------LTAEQAEKLQKVVLKNGGTVNKKWvGKDAAKILeaaginvpkdtRLLIVETDANHPFVVTELM 362
|
250
....*....|....*..
gi 568971234 337 GPVMPIVCVRSLDEAIK 353
Cdd:PRK15398 363 MPVLPVVRVKDVDEAIA 379
|
|
| |
