|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
5-446 |
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: 824.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 5 QLAVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEILGLEGEINLAVSKLAEWAAP 84
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 85 RPVNKNLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMSLYLDSEMYQ 163
Cdd:cd07132 81 EPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLaELIPKYLDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 164 VVTGGVPETQELLKQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTC 243
Cdd:cd07132 161 VVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 244 IAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDYGRIINRRHFKRIMALLEGSTVAIGGDCDESECYIAPTVLRDV 323
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 324 KPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLSDLPFGG 403
Cdd:cd07132 321 KPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 47086741 404 VGYSGTGRYHGKYSFDQVSHLRSCLIKKLNMEAVNQMRYPPHT 446
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 ... |
7-429 |
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: 686.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEILGLEGEINLAVSKLAEWAAPRP 86
Cdd:cd07087 3 LVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 87 VNKNLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMSLYLDSEMYQVV 165
Cdd:cd07087 83 VSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLaKLIPKYFDPEAVAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 166 TGGVPETQELLKQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIA 245
Cdd:cd07087 163 EGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 246 PDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDYGRIINRRHFKRIMALLEGSTVAIGGDCDESECYIAPTVLRDVKP 325
Cdd:cd07087 243 PDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 326 ASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLSDLPFGGVG 405
Cdd:cd07087 323 DSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVG 402
|
410 420
....*....|....*....|....
gi 47086741 406 YSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:cd07087 403 NSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
5-457 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 613.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 5 QLAVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEILGLEGEINLAVSKLAEWAAP 84
Cdd:PTZ00381 10 PPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 85 RPVNKNLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMSLYLDSEMYQ 163
Cdd:PTZ00381 90 EKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMaKLLTKYLDPSYVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 164 VVTGGVPETQELLKQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTC 243
Cdd:PTZ00381 170 VIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTC 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 244 IAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDYGRIINRRHFKRIMALLE--GSTVAIGGDCDESECYIAPTVLR 321
Cdd:PTZ00381 250 VAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDIENKYVAPTIIV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 322 DVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLSDLPF 401
Cdd:PTZ00381 330 NPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPF 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 47086741 402 GGVGYSGTGRYHGKYSFDQVSHLRSCLIKKLNMEAVNQMRYPPHTTEKLRWARVLL 457
Cdd:PTZ00381 410 GGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSWVLSFLL 465
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
8-454 |
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: 606.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 8 VQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEILGLEGEINLAVSKLAEWAAPRPV 87
Cdd:cd07136 4 VEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPKRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 88 NKNLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMSLYLDSEMYQVVT 166
Cdd:cd07136 84 KTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIaKIIEETFDEEYVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 167 GGVPETQELLKQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAP 246
Cdd:cd07136 164 GGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 247 DYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDYGRIINRRHFKRIMALLEGSTVAIGGDCDESECYIAPTVLRDVKPA 326
Cdd:cd07136 244 DYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNVTWD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 327 SKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLSDLPFGGVGY 406
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGVGN 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 47086741 407 SGTGRYHGKYSFDQVSHLRSCLIKKLNMEAVnqMRYPPHTTEKLRWAR 454
Cdd:cd07136 404 SGMGSYHGKYSFDTFSHKKSILKKSTWFDLP--LRYPPYKGKKKKLKK 449
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
7-426 |
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: 573.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEILGLEGEINLAVSKLAEWAAPRP 86
Cdd:cd07135 10 IHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAKDEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 87 VNKNLLTIS-DDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMSLYLDSEMYQV 164
Cdd:cd07135 90 VKDGPLAFMfGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLaELVPKYLDPDAFQV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 165 VTGGVPETQELLKQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCI 244
Cdd:cd07135 170 VQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 245 APDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDYGRIINRRHFKRIMALLEGS--TVAIGGDCDESECYIAPTVLRD 322
Cdd:cd07135 250 APDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTkgKVVIGGEMDEATRFIPPTIVSD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 323 VKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLSDLPFG 402
Cdd:cd07135 330 VSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFG 409
|
410 420
....*....|....*....|....
gi 47086741 403 GVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:cd07135 410 GVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
3-429 |
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: 516.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 3 REQLAVQQARKAFLtgRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEILGLEGEINLAVSKLAEWA 82
Cdd:cd07134 1 RRVFAAQQAHALAL--RASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 83 APRPVNKNLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMSLYLDSEM 161
Cdd:cd07134 79 KPKRVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIaKIIREAFDEDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 162 YQVVTGGVPETQELLKQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQ 241
Cdd:cd07134 159 VAVFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 242 TCIAPDYILCESSIQDRVIDEIQKCIKEFY--TIDPKTFEDYGRIINRRHFKRIMALLE-----GSTVAIGGDCDESECY 314
Cdd:cd07134 239 TCIAPDYVFVHESVKDAFVEHLKAEIEKFYgkDAARKASPDLARIVNDRHFDRLKGLLDdavakGAKVEFGGQFDAAQRY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 315 IAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHF 394
Cdd:cd07134 319 IAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHF 398
|
410 420 430
....*....|....*....|....*....|....*
gi 47086741 395 TLSDLPFGGVGYSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:cd07134 399 LNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
8-428 |
4.25e-174 |
|
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: 496.16 E-value: 4.25e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 8 VQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEILGLEGEINLAVSKLAEWAAPRPV 87
Cdd:cd07137 5 VRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPEKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 88 NKNLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMSLYLDSEMYQVVT 166
Cdd:cd07137 85 KTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLaKLIPEYLDTKAIKVIE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 167 GGVPETQELLKQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNC-GQTCIA 245
Cdd:cd07137 165 GGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQACIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 246 PDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDYGRIINRRHFKRIMALLEGSTVAI----GGDCDESECYIAPTVLR 321
Cdd:cd07137 245 PDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADkivhGGERDEKNLYIEPTILL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 322 DVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLSDLPF 401
Cdd:cd07137 325 DPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPF 404
|
410 420
....*....|....*....|....*..
gi 47086741 402 GGVGYSGTGRYHGKYSFDQVSHLRSCL 428
Cdd:cd07137 405 GGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
3-426 |
5.49e-163 |
|
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: 468.12 E-value: 5.49e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 3 REQLAVQQArkAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDL-YKSANSTQLFEILGLEGEINLAVSKLAEW 81
Cdd:cd07133 1 QALLERQKA--AFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 82 AAPRPVNKNLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMSLYLDSE 160
Cdd:cd07133 79 MKPSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLaELLAEYFDED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 161 MYQVVTGGVPETQELLKQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCG 240
Cdd:cd07133 159 EVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 241 QTCIAPDYILCESSIQDRVIDEIQKCIKEFYtIDPKTFEDYGRIINRRHFKRIMALLE-----GSTV---AIGGDCDESE 312
Cdd:cd07133 239 QTCVAPDYVLVPEDKLEEFVAAAKAAVAKMY-PTLADNPDYTSIINERHYARLQGLLEdarakGARVielNPAGEDFAAT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 313 CYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMV 392
Cdd:cd07133 318 RKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLL 397
|
410 420 430
....*....|....*....|....*....|....
gi 47086741 393 HFTLSDLPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:cd07133 398 HVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
8-456 |
2.79e-149 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 434.92 E-value: 2.79e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 8 VQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEILGLEGEINLAVSKLAEWAAPRPV 87
Cdd:PLN02203 12 VAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMAPKKA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 88 NKNLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMSLYLDSEMYQVVT 166
Cdd:PLN02203 92 KLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLaANIPKYLDSKAVKVIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 167 GGVPETQELLKQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYID---KNCDIRIACRRITWGKYLNC-GQT 242
Cdd:PLN02203 172 GGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSCaGQA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 243 CIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDYGRIINRRHFKRIMALLEGSTVAI----GGDCDESECYIAPT 318
Cdd:PLN02203 252 CIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAAsivhGGSIDEKKLFIEPT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 319 VLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLSD 398
Cdd:PLN02203 332 ILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYACDS 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 47086741 399 LPFGGVGYSGTGRYHGKYSFDQVSHLRSCLIKKLNMEAvnQMRYPPHTTEKLRWARVL 456
Cdd:PLN02203 412 LPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEF--EFRYPPWNDFKLGFLRLV 467
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
7-429 |
2.31e-130 |
|
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: 385.02 E-value: 2.31e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTqLFEILGLEGEINLAVSKLAEWAAPRP 86
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEA-LGEVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 87 VNKNLLTISddvFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA-SVMELMSLY-LDSEMYQV 164
Cdd:cd07078 82 PSPDPGELA---IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTAlLLAELLAEAgLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 165 VTGGVPET-QELLKQ-RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQT 242
Cdd:cd07078 159 VTGDGDEVgAALASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 243 CIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALLE-----GSTVAIGGDCDESE--CY 314
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDtDMGPLISAAQLDRVLAYIEdakaeGAKLLCGGKRLEGGkgYF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 315 IAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHF 394
Cdd:cd07078 319 VPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGA 398
|
410 420 430
....*....|....*....|....*....|....*
gi 47086741 395 TLSdLPFGGVGYSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:cd07078 399 EPS-APFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
8-461 |
4.04e-125 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 373.23 E-value: 4.04e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 8 VQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEILGLEGEINLAVSKLAEWAAPRPV 87
Cdd:PLN02174 16 VTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 88 NKNLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMSLYLDSEMYQVVT 166
Cdd:PLN02174 96 KTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLaKLLEQYLDSSAVRVVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 167 GGVPETQELLKQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKY-LNCGQTCIA 245
Cdd:PLN02174 176 GAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACIS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 246 PDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDYGRIINRRHFKRIMALLEGSTVA----IGGDCDESECYIAPTVLR 321
Cdd:PLN02174 256 PDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSdkivYGGEKDRENLKIAPTILL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 322 DVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLSDLPF 401
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPF 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 402 GGVGYSGTGRYHGKYSFDQVSHLRSCLIKKLNMEAVnqMRYPPHTTEKLRWARVLLLKQI 461
Cdd:PLN02174 416 GGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSA--VRYPPYSRGKLRLLKALVDSNI 473
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
7-426 |
2.09e-103 |
|
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: 317.45 E-value: 2.09e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQlfeilgleGEINLAVSKLaEWAA--P 84
Cdd:COG1012 48 AVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEAR--------GEVDRAADFL-RYYAgeA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 85 RPVNKNLLTISD---DVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvMELMSLYLDSEM 161
Cdd:COG1012 119 RRLYGETIPSDApgtRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSA--LLLAELLEEAGL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 162 ----YQVVTGGVPET-QELLKQ-RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGK 235
Cdd:COG1012 197 pagvLNVVTGDGSEVgAALVAHpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 236 YLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALL-----EGSTVAIGGDCD 309
Cdd:COG1012 277 FGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGtDMGPLISEAQLERVLAYIedavaEGAELLTGGRRP 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 310 ESE--CYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLA 387
Cdd:COG1012 357 DGEggYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWI 436
|
410 420 430
....*....|....*....|....*....|....*....
gi 47086741 388 NDCMVHfTLSDLPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:COG1012 437 NDGTTG-AVPQAPFGGVKQSGIGREGGREGLEEYTETKT 474
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
11-429 |
6.88e-102 |
|
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: 309.54 E-value: 6.88e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 11 ARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTqLFEILGLEGEINLA---VSKLAEWAAPRPV 87
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFRYAaglADKLGGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 88 NKNLLTIsddvflQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA-SVMELMSLY-LDSEMYQVV 165
Cdd:cd06534 82 PGGEAYV------RREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTAlALAELLQEAgLPPGVVNVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 166 TGGVPET-QELLKQ-RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTC 243
Cdd:cd06534 156 PGGGDEVgAALLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQIC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 244 IAPDYILCESSIQDRVIDEIQkcikefytidpktfedygriinrrhfkrimallegstvaiggdcdesecyiapTVLRDV 323
Cdd:cd06534 236 TAASRLLVHESIYDEFVEKLV-----------------------------------------------------TVLVDV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 324 KPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLSdLPFGG 403
Cdd:cd06534 263 DPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-APFGG 341
|
410 420
....*....|....*....|....*.
gi 47086741 404 VGYSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:cd06534 342 VKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
7-426 |
1.38e-92 |
|
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: 288.66 E-value: 1.38e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTqlfeilglEGEINLAVSKLAEWA-APR 85
Cdd:pfam00171 34 AIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEA--------RGEVDRAIDVLRYYAgLAR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 86 PVNKNLLTISDDV--FLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvMELMSLY----LDS 159
Cdd:pfam00171 106 RLDGETLPSDPGRlaYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTA--LLLAELFeeagLPA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 160 EMYQVVTGGVPETQELLKQ--RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYL 237
Cdd:pfam00171 184 GVLNVVTGSGAEVGEALVEhpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 238 NCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALL-----EGSTVAIGGDCDES 311
Cdd:pfam00171 264 NAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDtDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 312 E-CYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDC 390
Cdd:pfam00171 344 NgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDY 423
|
410 420 430
....*....|....*....|....*....|....*.
gi 47086741 391 MVhFTLSDLPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:pfam00171 424 TT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
7-414 |
9.70e-89 |
|
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: 278.72 E-value: 9.70e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLfeilglegEINLAVSKLAEWA---- 82
Cdd:cd07099 23 AVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL--------EVLLALEAIDWAArnap 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 83 ---APRPVNKNLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAS--VMELMSLYL 157
Cdd:cd07099 95 rvlAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGEllAEAWAAAGP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 158 DSEMYQVVTGGVPETQELLKQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYL 237
Cdd:cd07099 175 PQGVLQVVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 238 NCGQTCIAPDYILCESSIQDRVIDE-IQKCIKEFYTIDPKTFEDYGRIIN-------RRHFKRimALLEGSTVAIGG-DC 308
Cdd:cd07099 255 NAGQTCISVERVYVHESVYDEFVARlVAKARALRPGADDIGDADIGPMTTarqldivRRHVDD--AVAKGAKALTGGaRS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 309 DESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLAN 388
Cdd:cd07099 333 NGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSIN 412
|
410 420
....*....|....*....|....*.
gi 47086741 389 DCMVHFTLSDLPFGGVGYSGTGRYHG 414
Cdd:cd07099 413 DVLLTAGIPALPFGGVKDSGGGRRHG 438
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
5-430 |
7.05e-74 |
|
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: 240.66 E-value: 7.05e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 5 QLAVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEILGLEGEINLAVSKLAEWAAP 84
Cdd:cd07098 21 DEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 85 --RPVNKNLLTISDDVflQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVME------LMSLY 156
Cdd:cd07098 101 esRPGGLLMFYKRARV--EYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLsiirecLAACG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 157 LDSEMYQVVTGgVPETQELLKQ--RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWG 234
Cdd:cd07098 179 HDPDLVQLVTC-LPETAEALTShpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 235 KYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFyTIDPKTFEDY--GRIINRRHFKRIMALL-----EGSTVAIGG- 306
Cdd:cd07098 258 TFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQAL-RQGPPLDGDVdvGAMISPARFDRLEELVadaveKGARLLAGGk 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 307 ----DCDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSS 382
Cdd:cd07098 337 ryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLET 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 47086741 383 GALLANDCMVHFTLSDLPFGGVGYSGTGRYHGkysfdqVSHLRS-CLIK 430
Cdd:cd07098 417 GMVAINDFGVNYYVQQLPFGGVKGSGFGRFAG------EEGLRGlCNPK 459
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
1-419 |
2.05e-68 |
|
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: 225.77 E-value: 2.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 1 MSREQL--AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITnalrkdlyksanstqlfEILGLE---------G 69
Cdd:cd07103 16 AGAADAdaAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLA-----------------RLLTLEqgkplaearG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 70 EINLAVSkLAEWAA------------PRPVNKNLLTIsddvflqPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVV 137
Cdd:cd07103 79 EVDYAAS-FLEWFAeearriygrtipSPAPGKRILVI-------KQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 138 KPSEVSSHTAsvMELMSLYLD----SEMYQVVTGGVPE-TQELLKqrfDHI-----FyTGNSTVGKLVMEAASHHLTPVT 207
Cdd:cd07103 151 KPAEETPLSA--LALAELAEEaglpAGVLNVVTGSPAEiGEALCA---SPRvrkisF-TGSTAVGKLLMAQAADTVKRVS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 208 LELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYT---IDPKTfeDYGRI 284
Cdd:cd07103 225 LELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVgngLDEGT--DMGPL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 285 INRRHFKRIMALLE-----GSTVAIGGD-CDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDRE 358
Cdd:cd07103 303 INERAVEKVEALVEdavakGAKVLTGGKrLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTP 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47086741 359 KPLALYVFSSSKKVIKQMISETSSGALLANdcmvHFTLSD--LPFGGVGYSGTGRYHGKYSFD 419
Cdd:cd07103 383 YGLAAYVFTRDLARAWRVAEALEAGMVGIN----TGLISDaeAPFGGVKESGLGREGGKEGLE 441
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
7-419 |
2.02e-66 |
|
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: 220.51 E-value: 2.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEILglEGEINLAVskLAEWAaprp 86
Cdd:cd07093 24 AVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIP--RAAANFRF--FADYI---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 87 vnknlLTISDDVFLQP---------EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMsly 156
Cdd:cd07093 96 -----LQLDGESYPQDggalnyvlrQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLaELA--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 157 LDSEM----YQVVTGGVPETQELLKQ--RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRR 230
Cdd:cd07093 168 NEAGLppgvVNVVHGFGPEAGAALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 231 ITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIM-----ALLEGSTVAI 304
Cdd:cd07093 248 AVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDtEVGPLISKEHLEKVLgyvelARAEGATILT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 305 GGDCDESE-----CYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISE 379
Cdd:cd07093 328 GGGRPELPdleggYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARR 407
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 47086741 380 TSSGALLANDCMVHftlsDL--PFGGVGYSGTGRYHGKYSFD 419
Cdd:cd07093 408 LEAGTVWVNCWLVR----DLrtPFGGVKASGIGREGGDYSLE 445
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
5-420 |
9.92e-66 |
|
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: 219.06 E-value: 9.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 5 QLAVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKsanstqlfeILGL-EGEINLAVSKL---AE 80
Cdd:cd07088 38 DRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGK---------TLSLaRVEVEFTADYIdymAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 81 WAapRPVNKNLLTiSD----DVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvMELMSLY 156
Cdd:cd07088 109 WA--RRIEGEIIP-SDrpneNIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNA--LEFAELV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 157 LDSEM----YQVVTGGVPETQELL--KQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRR 230
Cdd:cd07088 184 DEAGLpagvLNIVTGRGSVVGDALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 231 ITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALLE-----GSTVAI 304
Cdd:cd07088 264 IVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAtDMGPLVNEAALDKVEEMVEraveaGATLLT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 305 GGDCDESEC--YIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSS 382
Cdd:cd07088 344 GGKRPEGEKgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEF 423
|
410 420 430
....*....|....*....|....*....|....*...
gi 47086741 383 GALLANdcMVHFTLSDLPFGGVGYSGTGRYHGKYSFDQ 420
Cdd:cd07088 424 GETYIN--RENFEAMQGFHAGWKKSGLGGADGKHGLEE 459
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
5-429 |
1.54e-65 |
|
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: 218.36 E-value: 1.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 5 QLAVQQARKAFLTG---RSKSLDyRIKQLKNLSRFIKERAADItnALRKDLYKSANSTQLfeilglEGEINLAVSkLAEW 81
Cdd:cd07118 22 DAAVAAARKAFDKGpwpRMSGAE-RAAVLLKVADLIRARRERL--ALIETLESGKPISQA------RGEIEGAAD-LWRY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 82 AAPRPVNKNLLT---ISDDVF--LQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvMELMSLY 156
Cdd:cd07118 92 AASLARTLHGDSynnLGDDMLglVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT--LMLAELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 157 LDSEM----YQVVTG-GVPETQELLK-QRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRR 230
Cdd:cd07118 170 IEAGLpagvVNIVTGyGATVGQAMTEhPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 231 ITWGKYLNCGQTCIAPDYILCESSIQD----RVIDEIQKcIKEFYTIDPKTfeDYGRIINRRHFKRIMALL-----EGST 301
Cdd:cd07118 250 VVFGVYFNAGECCNSGSRLLVHESIADafvaAVVARSRK-VRVGDPLDPET--KVGAIINEAQLAKITDYVdagraEGAT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 302 VAIGGDCDESEC--YIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISE 379
Cdd:cd07118 327 LLLGGERLASAAglFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARR 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 47086741 380 TSSGALLANDCMVHFtlSDLPFGGVGYSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:cd07118 407 IRAGTVWVNTFLDGS--PELPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
1-426 |
5.67e-64 |
|
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: 214.03 E-value: 5.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 1 MSREQL--AVQQARKAFLTGRSKSLDYRIKQL-KNLSRFIKER---AADITNALRKDLYKSANstqlfEILGLEGEINLA 74
Cdd:cd07102 15 ASLEAVraALERARAAQKGWRAVPLEERKAIVtRAVELLAANTdeiAEELTWQMGRPIAQAGG-----EIRGMLERARYM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 75 VSKLAEWAAPRPV-NKNLLTisddVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEvssHTASVMELM 153
Cdd:cd07102 90 ISIAEEALADIRVpEKDGFE----RYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSP---QTPLCGERF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 154 SLYLD-----SEMYQVVTGGVPETQELLKQ-RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIA 227
Cdd:cd07102 163 AAAFAeaglpEGVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 228 CRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDY-GRIINRRHFKRIM-----ALLEGST 301
Cdd:cd07102 243 AESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTlGPVVSARAADFVRaqiadAIAKGAR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 302 VAIGG----DCDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMI 377
Cdd:cd07102 323 ALIDGalfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 47086741 378 SETSSGALLANDCmvHFTLSDLPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:cd07102 403 EQLETGTVFMNRC--DYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKS 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
7-425 |
3.80e-61 |
|
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: 206.23 E-value: 3.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDlyksANSTQLFEilglEGEINLAVSKLAEWAA-PR 85
Cdd:cd07104 5 AYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRE----SGSTRPKA----AFEVGAAIAILREAAGlPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 86 PVNKNLLTiSDdvflQP--------EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHT-----ASVMEL 152
Cdd:cd07104 77 RPEGEILP-SD----VPgkesmvrrVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgglliAEIFEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 153 MSLylDSEMYQVVTGGVPETQELL--KQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRR 230
Cdd:cd07104 152 AGL--PKGVLNVVPGGGSEIGDALveHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 231 ITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTfED--YGRIINRRHFKRIMALLE-----GSTVA 303
Cdd:cd07104 230 AAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRD-PDtvIGPLINERQVDRVHAIVEdavaaGARLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 304 IGGDCDESecYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSkkvikqmiseTSSG 383
Cdd:cd07104 309 TGGTYEGL--FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRD----------LERA 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 47086741 384 ALLANDC---MVHF---TLSD---LPFGGVGYSGTGRYHGKYSFDQVSHLR 425
Cdd:cd07104 377 MAFAERLetgMVHIndqTVNDephVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
7-418 |
1.71e-60 |
|
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: 205.43 E-value: 1.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDL---YKSANSTQLFeiLGLeGEINLAVSKLAEWAA 83
Cdd:cd07138 41 AVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMgapITLARAAQVG--LGI-GHLRAAADALKDFEF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 84 PRPVNKNLLTIsddvflqpEPLGVVLIIGAWNYP---IAVTLQPlvgAIAAGNAVVVKPSEVSSHTAsvmelmslYLDSE 160
Cdd:cd07138 118 EERRGNSLVVR--------EPIGVCGLITPWNWPlnqIVLKVAP---ALAAGCTVVLKPSEVAPLSA--------IILAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 161 M----------YQVVTGGVPETQELLK--QRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIAC 228
Cdd:cd07138 179 IldeaglpagvFNLVNGDGPVVGEALSahPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 229 RRITWGKYLNCGQTCIAPDYILCESSIQDRVIdEIQKCIKEFYTI----DPKTFedYGRIINRRHFKRIMALL-----EG 299
Cdd:cd07138 259 PRGVAACFANSGQSCNAPTRMLVPRSRYAEAE-EIAAAAAEAYVVgdprDPATT--LGPLASAAQFDRVQGYIqkgieEG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 300 STVAIGG----DCDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQ 375
Cdd:cd07138 336 ARLVAGGpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARA 415
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 47086741 376 MISETSSGALLANDCMVHFtlsDLPFGGVGYSGTGRYHGKYSF 418
Cdd:cd07138 416 VARRLRAGQVHINGAAFNP---GAPFGGYKQSGNGREWGRYGL 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
6-414 |
4.20e-59 |
|
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: 201.31 E-value: 4.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTG--RSKSLDyRIKQLKNLSRFIKERAADITNALRKDLYKS--------ANSTQLFEILG-----LEGE 70
Cdd:cd07109 23 RAVQAARRAFESGwlRLSPAE-RGRLLLRIARLIREHADELARLESLDTGKPltqaradvEAAARYFEYYGgaadkLHGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 71 -InlavsklaewaaprPVNKNLLtisddVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsv 149
Cdd:cd07109 102 tI--------------PLGPGYF-----VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 150 MELMSLYLDSEM----YQVVTGGVPETQELLKQ--RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCD 223
Cdd:cd07109 161 LRLAELAEEAGLpagaLNVVTGLGAEAGAALVAhpGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 224 IRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFyTIDPKTFE-DYGRIINRRHFKRIMALLE---- 298
Cdd:cd07109 241 LEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRAL-RVGPGLEDpDLGPLISAKQLDRVEGFVArara 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 299 -GSTVAIGG----DCDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVI 373
Cdd:cd07109 320 rGARIVAGGriaeGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 47086741 374 KQMISETSSGALLANDcmvHFTLS--DLPFGGVGYSGTGRYHG 414
Cdd:cd07109 400 LRVARRLRAGQVFVNN---YGAGGgiELPFGGVKKSGHGREKG 439
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
7-429 |
1.01e-58 |
|
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: 200.47 E-value: 1.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLD--YRIKQLKNLSRFIKERAADITNALRKDLYKsanstqlfeilgLEGEINLAVSKLAEW--- 81
Cdd:cd07114 24 AVAAARAAFEGGAWRKLTptERGKLLRRLADLIEANAEELAELETRDNGK------------LIRETRAQVRYLAEWyry 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 82 ---------AAPRPVNK-NLLtisddVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSShtASVME 151
Cdd:cd07114 92 yagladkieGAVIPVDKgDYL-----NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP--ASTLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 152 LMSLYLDSEM----YQVVTGGVPETQELLKQ--RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIR 225
Cdd:cd07114 165 LAKLAEEAGFppgvVNVVTGFGPETGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 226 IACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKefyTI------DPKTfeDYGRIINRRHFKRIMALL-- 297
Cdd:cd07114 245 AAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARAR---AIrvgdplDPET--QMGPLATERQLEKVERYVar 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 298 ---EGSTVAIGG-DCDESEC----YIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSS 369
Cdd:cd07114 320 areEGARVLTGGeRPSGADLgagyFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47086741 370 KKVIKQMISETSSGALLANDcmvHFTLS-DLPFGGVGYSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNT---YRALSpSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
7-426 |
1.09e-58 |
|
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: 200.55 E-value: 1.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTG-RSKSLDYRIKQLKNLSRFIKERAADitnaLRKDLYKSANSTQLFEILGLEGEINLAVSKLAE----- 80
Cdd:cd07089 24 AIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEE----LRALLVAEVGAPVMTARAMQVDGPIGHLRYFADladsf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 81 -WAAPRPVNKNLLTISDDVfLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVMelmslyldS 159
Cdd:cd07089 100 pWEFDLPVPALRGGPGRRV-VRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLL--------G 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 160 EMYQ----------VVTGGVPETQELLKQ--RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIA 227
Cdd:cd07089 171 EIIAetdlpagvvnVVTGSDNAVGEALTTdpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 228 CRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDeiqkCIKEFYT-------IDPKTFedYGRIINRRHFKRIMALL--- 297
Cdd:cd07089 251 APAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVE----ALAAAFEalpvgdpADPGTV--MGPLISAAQRDRVEGYIarg 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 298 --EGSTVAIGG---DCDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSK-- 370
Cdd:cd07089 325 rdEGARLVTGGgrpAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVdr 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 47086741 371 --KVIKQMisetSSGALLANDcmVHFTLSDLPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:cd07089 405 ayRVARRI----RTGSVGING--GGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
1-422 |
4.45e-58 |
|
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: 198.73 E-value: 4.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 1 MSREQ--LAVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLfeilglegEINLAVS-- 76
Cdd:cd07145 18 LSREEvrEAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV--------EVERTIRlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 77 KLAEWAAPR-----------PVNKNLLtisddVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSH 145
Cdd:cd07145 90 KLAAEEAKVlrgetipvdayEYNERRI-----AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 146 TAsvMELMSLYLDSEM----YQVVTGGVPET-QELLKQ-RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYID 219
Cdd:cd07145 165 TA--IELAKILEEAGLppgvINVVTGYGSEVgDEIVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 220 KNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDP---KTfeDYGRIINRRHFKRIM-- 294
Cdd:cd07145 243 KDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPldeST--DLGPLISPEAVERMEnl 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 295 ---ALLEGSTVAIGGDCDESeCYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKK 371
Cdd:cd07145 321 vndAVEKGGKILYGGKRDEG-SFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDIN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 47086741 372 VIKQMISETSSGALLANDCmVHFTLSDLPFGGVGYSGTGRYHGKYSFDQVS 422
Cdd:cd07145 400 RALKVARELEAGGVVINDS-TRFRWDNLPFGGFKKSGIGREGVRYTMLEMT 449
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
2-426 |
5.29e-58 |
|
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: 198.14 E-value: 5.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 2 SREQL--AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQlfeilgleGEINLAVSKLA 79
Cdd:cd07106 17 SEAQLdqAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ--------FEVGGAVAWLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 80 EWAAPR-PVnknlLTISDD----VFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELM 153
Cdd:cd07106 89 YTASLDlPD----EVIEDDdtrrVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLgELA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 154 SLYLDSEMYQVVTGGvPETQELLKQ--RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRI 231
Cdd:cd07106 165 QEVLPPGVLNVVSGG-DELGPALTShpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 232 TWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYT---IDPKTFedYGRIINRRHFKRIMALLE-----GSTVA 303
Cdd:cd07106 244 FWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVgdgLDPGTT--LGPVQNKMQYDKVKELVEdakakGAKVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 304 IGGDCDESECY-IAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSS 382
Cdd:cd07106 322 AGGEPLDGPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 47086741 383 GALLANDcmvHFTLS-DLPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:cd07106 402 GTVWINT---HGALDpDAPFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
6-429 |
3.54e-57 |
|
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: 196.28 E-value: 3.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTGRSKSLD--YRIKQLKNLSRFIkERAAD-------------ITNALRKDLYKSANSTQLFeilgleGE 70
Cdd:cd07112 28 RAVAAARRAFESGVWSRLSpaERKAVLLRLADLI-EAHRDelalletldmgkpISDALAVDVPSAANTFRWY------AE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 71 inlAVSKLAEWAAPRPvNKNLLTISDdvflqpEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvM 150
Cdd:cd07112 101 ---AIDKVYGEVAPTG-PDALALITR------EPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTA--L 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 151 ELMSLYLDSEM----YQVVTGGVPETQELL--KQRFDHIFYTGNSTVGKLVME-AASHHLTPVTLELGGKSPCYIDKNC- 222
Cdd:cd07112 169 RLAELALEAGLpagvLNVVPGFGHTAGEALglHMDVDALAFTGSTEVGRRFLEySGQSNLKRVWLECGGKSPNIVFADAp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 223 DIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYT---IDPKTfeDYGRIINRRHFKRIM----- 294
Cdd:cd07112 249 DLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPgdpLDPAT--RMGALVSEAHFDKVLgyies 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 295 ALLEGSTVAIGGDCDESE---CYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSS-K 370
Cdd:cd07112 327 GKAEGARLVAGGKRVLTEtggFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDlS 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086741 371 KVIKqmisetSSGALLANdcMVH---FTLSDL--PFGGVGYSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:cd07112 407 RAHR------VARRLRAG--TVWvncFDEGDIttPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
7-426 |
5.53e-57 |
|
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: 195.74 E-value: 5.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAAD------------ITNALRKDLYKSANStqlFEILG-----LEG 69
Cdd:cd07115 24 AVAAARAAFEAWSAMDPAERGRILWRLAELILANADElarlesldtgkpIRAARRLDVPRAADT---FRYYAgwadkIEG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 70 EInlavsklaewaapRPVNKNLLTisddvFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA-S 148
Cdd:cd07115 101 EV-------------IPVRGPFLN-----YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAlR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 149 VMELMS-LYLDSEMYQVVTGGVPETQELLKQR--FDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIR 225
Cdd:cd07115 163 IAELMAeAGFPAGVLNVVTGFGEVAGAALVEHpdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 226 IACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYT---IDPKTfeDYGRIINRRHFKRIMALL----- 297
Cdd:cd07115 243 AAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPgdpLDPKT--QMGPLVSQAQFDRVLDYVdvgre 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 298 EGSTVAIGGDCD-ESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQM 376
Cdd:cd07115 321 EGARLLTGGKRPgARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 47086741 377 ISETSSGALLANdcMVHFTLSDLPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:cd07115 401 AAALKAGTVWIN--TYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKS 448
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
6-419 |
6.05e-57 |
|
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: 196.28 E-value: 6.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTGRSKSLD--YRIKQLKNLSRFIkERAADITNALrkdlyKSANSTQLFEIlGLEGEINLAVSKL---AE 80
Cdd:cd07091 45 AAVKAARAAFETGWWRKMDprERGRLLNKLADLI-ERDRDELAAL-----ESLDNGKPLEE-SAKGDVALSIKCLryyAG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 81 WA-----APRPVNKNLLTisddvFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvmelmsL 155
Cdd:cd07091 118 WAdkiqgKTIPIDGNFLA-----YTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSA-------L 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 156 YLdSEMYQ----------VVTGGVPETQELLKQ--RFDHIFYTGNSTVGKLVMEAAS-HHLTPVTLELGGKSPCYIDKNC 222
Cdd:cd07091 186 YL-AELIKeagfppgvvnIVPGFGPTAGAAISShmDVDKIAFTGSTAVGRTIMEAAAkSNLKKVTLELGGKSPNIVFDDA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 223 DIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDP---KTFEdyGRIINRRHFKRIMALL-- 297
Cdd:cd07091 265 DLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPfdpDTFQ--GPQVSKAQFDKILSYIes 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 298 ---EGSTVAIGGDCDESECY-IAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVI 373
Cdd:cd07091 343 gkkEGATLLTGGERHGSKGYfIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKA 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 47086741 374 KQMISETSSGALLAND-CMVHftlSDLPFGGVGYSGTGRYHGKYSFD 419
Cdd:cd07091 423 LRVSRALKAGTVWVNTyNVFD---AAVPFGGFKQSGFGRELGEEGLE 466
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
7-423 |
6.50e-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: 196.03 E-value: 6.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSanstqLFEILGlegEINLAVSkLAEWAAP-- 84
Cdd:cd07131 42 AVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKP-----LAEGRG---DVQEAID-MAQYAAGeg 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 85 -RP---------VNKNLLTISddvflqpEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAS--VMEL 152
Cdd:cd07131 113 rRLfgetvpselPNKDAMTRR-------QPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALklVELF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 153 MSLYLDSEMYQVVTGGVPETQELLKQ--RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRR 230
Cdd:cd07131 186 AEAGLPPGVVNVVHGRGEEVGEALVEhpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 231 ITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYT---IDPKTfeDYGRIINRRHFKRI-----MALLEGSTV 302
Cdd:cd07131 266 ALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVgdgLDEET--DMGPLINEAQLEKVlnyneIGKEEGATL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 303 AIGG-----DCDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMI 377
Cdd:cd07131 344 LLGGerltgGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRAR 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 47086741 378 SETSSGALLAN----DCMVHftlsdLPFGGVGYSGTG-RYHGKYSFDQVSH 423
Cdd:cd07131 424 RDLEAGITYVNaptiGAEVH-----LPFGGVKKSGNGhREAGTTALDAFTE 469
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
7-425 |
1.36e-55 |
|
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: 191.77 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDlyksANSTQLFEIlgleGEINLAVSKL---AEWAA 83
Cdd:cd07150 26 AIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDE----GGSTYGKAW----FETTFTPELLraaAGECR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 84 pRPVNKNLLTISDDVFLQP--EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHT----ASVMELMSLyl 157
Cdd:cd07150 98 -RVRGETLPSDSPGTVSMSvrRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIglkiAEIMEEAGL-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 158 DSEMYQVVTGGVPETQELLKQ--RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGK 235
Cdd:cd07150 175 PKGVFNVVTGGGAEVGDELVDdpRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 236 YLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPK---TFedYGRIINRRHFKRIM-----ALLEGSTVAIGGD 307
Cdd:cd07150 255 FMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRdpdTV--IGPLISPRQVERIKrqvedAVAKGAKLLTGGK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 308 CDESECYiaPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREkplalYVFSSSkkVIKQMISETSSGALLA 387
Cdd:cd07150 333 YDGNFYQ--PTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTE-----YGLSAA--ILTNDLQRAFKLAERL 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 47086741 388 NDCMVHF---TLSD---LPFGGVGYSGTGRYHGKYSFDQVSHLR 425
Cdd:cd07150 404 ESGMVHIndpTILDeahVPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
6-429 |
8.09e-55 |
|
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: 190.63 E-value: 8.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTGRSKSLDYRIKQL--------KNLSRF-----------IKE-RAADITNALRKDLYKSAnstqlfEIL 65
Cdd:cd07559 42 LAVDAAHEAFKTWGKTSVAERANILnkiadrieENLELLavaetldngkpIREtLAADIPLAIDHFRYFAG------VIR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 66 GLEGEINLavsklaewaaprpVNKNLLTIsddVFlqPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSh 145
Cdd:cd07559 116 AQEGSLSE-------------IDEDTLSY---HF--HEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTP- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 146 tASVMELMSLY---LDSEMYQVVTGGVPETQELLK--QRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYI-- 218
Cdd:cd07559 177 -LSILVLMELIgdlLPKGVVNVVTGFGSEAGKPLAshPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfd 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 219 ---DKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQ---KCIKEFYTIDPKTFedYGRIINRRHFKR 292
Cdd:cd07559 256 damDADDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVerfEAIKVGNPLDPETM--MGAQVSKDQLEK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 293 IMALL-----EGSTVAIGGD-----CDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLA 362
Cdd:cd07559 334 ILSYVdigkeEGAEVLTGGErltlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLG 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47086741 363 LYVFSSSKKVIKQMISETSSGALLANdCMvHFTLSDLPFGGVGYSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:cd07559 414 GGVWTRDINRALRVARGIQTGRVWVN-CY-HQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILV 478
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
7-411 |
4.67e-54 |
|
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: 187.80 E-value: 4.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKS--------ANSTQLFEILGLE-----GE-IN 72
Cdd:cd07149 26 AIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPikdarkevDRAIETLRLSAEEakrlaGEtIP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 73 LAvsklaewAAPRPVNKNLLTISddvflqpEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-E 151
Cdd:cd07149 106 FD-------ASPGGEGRIGFTIR-------EPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLaE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 152 LM-SLYLDSEMYQVVTGGVPET-QELLK-QRFDHIFYTGNSTVGKLVMEAAShhLTPVTLELGGKSPCYIDKNCDIRIAC 228
Cdd:cd07149 172 LLlEAGLPKGALNVVTGSGETVgDALVTdPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 229 RRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIM-----ALLEGSTV 302
Cdd:cd07149 250 ERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDtDVGPMISEAEAERIEewveeAVEGGARL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 303 AIGGDCDESecYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSS 382
Cdd:cd07149 330 LTGGKRDGA--ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEV 407
|
410 420
....*....|....*....|....*....
gi 47086741 383 GALLANDcMVHFTLSDLPFGGVGYSGTGR 411
Cdd:cd07149 408 GGVMIND-SSTFRVDHMPYGGVKESGTGR 435
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
7-425 |
1.52e-53 |
|
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: 186.38 E-value: 1.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNAlrkdlyKSANSTQLFEiLGLEGEINLAVSKLAEWA-APR 85
Cdd:cd07092 24 AVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAAL------ESRNTGKPLH-LVRDDELPGAVDNFRFFAgAAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 86 PVNKNLLT------ISddvFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMSLYLD 158
Cdd:cd07092 97 TLEGPAAGeylpghTS---MIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLaELAAEVLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 159 SEMYQVVTGGVPETQELL--KQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKY 236
Cdd:cd07092 174 PGVVNVVCGGGASAGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 237 LNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALLE----GSTVAIGGD-CDE 310
Cdd:cd07092 254 YNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDtEMGPLNSAAQRERVAGFVErapaHARVLTGGRrAEG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 311 SECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDc 390
Cdd:cd07092 334 PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT- 412
|
410 420 430
....*....|....*....|....*....|....*.
gi 47086741 391 mvHFTL-SDLPFGGVGYSGTGRYHGKYSFDQVSHLR 425
Cdd:cd07092 413 --HIPLaAEMPHGGFKQSGYGKDLSIYALEDYTRIK 446
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
103-419 |
3.12e-53 |
|
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: 186.46 E-value: 3.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 103 EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSShtASVMELMSLYLDSE----MYQVVTGGVPETQELLKQ 178
Cdd:cd07144 143 EPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTP--LSLLYFANLVKEAGfppgVVNIIPGYGAVAGSALAE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 179 R--FDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQ 256
Cdd:cd07144 221 HpdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIY 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 257 DRVIDEIQKCIKEFYTI----DPKTFEdyGRIINRRHFKRIMALLE-----GSTVAIGG----DCDESECYIAPTVLRDV 323
Cdd:cd07144 301 DKFVEKFVEHVKQNYKVgspfDDDTVV--GPQVSKTQYDRVLSYIEkgkkeGAKLVYGGekapEGLGKGYFIPPTIFTDV 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 324 KPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALL---ANDCMVHftlsdLP 400
Cdd:cd07144 379 PQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWinsSNDSDVG-----VP 453
|
330
....*....|....*....
gi 47086741 401 FGGVGYSGTGRYHGKYSFD 419
Cdd:cd07144 454 FGGFKMSGIGRELGEYGLE 472
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
41-420 |
1.03e-52 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 185.28 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 41 AADITNALRK--DLYKsANSTQLFEILGLE---------GEINLAVSKLaEWAAP---RPVNKNLLTISDD--VFLQPEP 104
Cdd:PLN02278 83 ASERSKILRRwyDLII-ANKEDLAQLMTLEqgkplkeaiGEVAYGASFL-EYFAEeakRVYGDIIPSPFPDrrLLVLKQP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 105 LGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVMELMSLY--LDSEMYQVVTGGVPETQELL----KQ 178
Cdd:PLN02278 161 VGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQagIPPGVLNVVMGDAPEIGDALlaspKV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 179 RfdHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDR 258
Cdd:PLN02278 241 R--KITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 259 VIDEIQKCIKEFYT---IDPKTfeDYGRIINRRHFKRIM-----ALLEGSTVAIGGD-CDESECYIAPTVLRDVKPASKV 329
Cdd:PLN02278 319 FAEAFSKAVQKLVVgdgFEEGV--TQGPLINEAAVQKVEshvqdAVSKGAKVLLGGKrHSLGGTFYEPTVLGDVTEDMLI 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 330 MQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLSdlPFGGVGYSGT 409
Cdd:PLN02278 397 FREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGGVKQSGL 474
|
410
....*....|.
gi 47086741 410 GRYHGKYSFDQ 420
Cdd:PLN02278 475 GREGSKYGIDE 485
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
6-426 |
2.31e-52 |
|
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: 183.66 E-value: 2.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKS--------ANSTQLFEILG-----LEGE-I 71
Cdd:cd07090 23 LAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPieearvdiDSSADCLEYYAglaptLSGEhV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 72 NLAVSKLAewaaprpvnknlltisddvFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVme 151
Cdd:cd07090 103 PLPGGSFA-------------------YTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALL-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 152 LMSLY----LDSEMYQVVTGGvPETQELLKQRFD--HIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIR 225
Cdd:cd07090 162 LAEILteagLPDGVFNVVQGG-GETGQLLCEHPDvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 226 IACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPkTFED--YGRIINRRHFKRIMALL-----E 298
Cdd:cd07090 241 NAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDP-LDEDtqMGALISEEHLEKVLGYIesakqE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 299 GSTVAIGGDCDESEC------YIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKV 372
Cdd:cd07090 320 GAKVLCGGERVVPEDglengfYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 47086741 373 IKQMISETSSGALLANDcmvhFTLS--DLPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:cd07090 400 AHRVIAQLQAGTCWINT----YNISpvEVPFGGYKQSGFGRENGTAALEHYTQLKT 451
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
6-425 |
2.98e-52 |
|
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: 183.32 E-value: 2.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDlyksaNSTQLFEilgleGEINLA--------VSK 77
Cdd:cd07110 23 AAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARD-----NGKPLDE-----AAWDVDdvagcfeyYAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 78 LAEwaAPRPVNKNLLTISDDVF---LQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvMELMS 154
Cdd:cd07110 93 LAE--QLDAKAERAVPLPSEDFkarVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTE--LELAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 155 LYLDSEM----YQVVTGGVPETQELLKQ--RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIAC 228
Cdd:cd07110 169 IAAEAGLppgvLNVVTGTGDEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 229 RRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALL-----EGSTV 302
Cdd:cd07110 249 EWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGvRLGPLVSQAQYEKVLSFIargkeEGARL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 303 AIGG---DCDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISE 379
Cdd:cd07110 329 LCGGrrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEA 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 47086741 380 TSSGALLANDCMVHFTlsDLPFGGVGYSGTGRYHGKYSFDQVSHLR 425
Cdd:cd07110 409 LEAGIVWINCSQPCFP--QAPWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
6-419 |
3.55e-51 |
|
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: 180.25 E-value: 3.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKER--------AADITNALRK----DLYKSANSTQLFEilGLEGEI-- 71
Cdd:cd07108 23 RAVAAAKAAFPEWAATPARERGKLLARIADALEARseelarllALETGNALRTqarpEAAVLADLFRYFG--GLAGELkg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 72 -NLavsklaewaaprPVNKNLLTISddvflQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM 150
Cdd:cd07108 101 eTL------------PFGPDVLTYT-----VREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 151 -ELMSLYLDSEMYQVVTGGVPETQELLKQR--FDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSP--CYIDKNCDIR 225
Cdd:cd07108 164 aEILAQVLPAGVLNVITGYGEECGAALVDHpdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPmiVFPDADLDDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 226 IAcRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDP---KTfeDYGRIINRRHFKRIMALLE---- 298
Cdd:cd07108 244 VD-GAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPldeAT--DIGAIISEKQFAKVCGYIDlgls 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 299 --GSTVAIGG-----DCDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKK 371
Cdd:cd07108 321 tsGATVLRGGplpgeGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 47086741 372 VIKQMISETSSGALLANDCMVhfTLSDLPFGGVGYSGTGRyhgKYSFD 419
Cdd:cd07108 401 RALRAAHALEAGWVQVNQGGG--QQPGQSYGGFKQSGLGR---EASLE 443
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
6-429 |
5.02e-51 |
|
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: 180.58 E-value: 5.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTG--RSKSLDYRIKQLKNLSRFIKERAADIT--------NALRKDLYKSANSTQLFEILGlegeinlav 75
Cdd:cd07119 39 RAIAAARRAFDSGewPHLPAQERAALLFRIADKIREDAEELArletlntgKTLRESEIDIDDVANCFRYYA--------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 76 sKLAEWAAPRPVNKNLLTISDDVflqPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA-SVMELMS 154
Cdd:cd07119 110 -GLATKETGEVYDVPPHVISRTV---REPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTiALFELIE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 155 -LYLDSEMYQVVTGGVPETQELL--KQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRI 231
Cdd:cd07119 186 eAGLPAGVVNLVTGSGATVGAELaeSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 232 TWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYT---IDPKTfeDYGRIINRRHFKRIMALL-----EGSTVA 303
Cdd:cd07119 266 LNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLgngLDADT--EMGPLVSAEHREKVLSYIqlgkeEGARLV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 304 IGGD-CDESEC----YIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMIS 378
Cdd:cd07119 344 CGGKrPTGDELakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVAR 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 47086741 379 ETSSGALLANDcmVHFTLSDLPFGGVGYSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:cd07119 424 RLRAGTVWIND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
104-425 |
6.93e-51 |
|
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: 179.03 E-value: 6.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 104 PLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM--ELMSLY-LDSEMYQVVTGGvPETQELL--KQ 178
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVViaRLFEEAgLPAGVLHVLPGG-ADAGEALveDP 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 179 RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDR 258
Cdd:cd07152 189 NVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 259 VIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALLE-----GSTVAIGGDCDeSECYiAPTVLRDVKPASKVMQE 332
Cdd:cd07152 269 YTAKLAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIVDdsvaaGARLEAGGTYD-GLFY-RPTVLSGVKPGMPAFDE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 333 EIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCmvhfTLSD---LPFGGVGYSGT 409
Cdd:cd07152 347 EIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVNDephNPFGGMGASGN 422
|
330
....*....|....*..
gi 47086741 410 G-RYHGKYSFDQVSHLR 425
Cdd:cd07152 423 GsRFGGPANWEEFTQWQ 439
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
7-425 |
1.24e-50 |
|
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: 179.24 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAAD------------ITNALRKDLYKSANSTQLFEIL--GLEGEIn 72
Cdd:TIGR01804 40 AIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEElakletldtgktLQETIVADMDSGADVFEFFAGLapALNGEI- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 73 lavsklaewaAPRPvnknlltISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA-SVME 151
Cdd:TIGR01804 119 ----------IPLG-------GPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTAlKVAE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 152 LMS-LYLDSEMYQVVTGGVPETQELLKQR--FDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIAC 228
Cdd:TIGR01804 182 IMEeAGLPKGVFNVVQGDGAEVGPLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 229 RRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALL-----EGSTV 302
Cdd:TIGR01804 262 DGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEAtEMGPLISAAHRDKVLSYIekgkaEGATL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 303 AIGGDCDESE-----CYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMI 377
Cdd:TIGR01804 342 ATGGGRPENVglqngFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVA 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 47086741 378 SETSSGALLANDcmVHFTLSDLPFGGVGYSGTGRYHGKYSFDQVSHLR 425
Cdd:TIGR01804 422 DQLEAGTVWINT--YNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
7-414 |
2.50e-49 |
|
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: 175.46 E-value: 2.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTG--RSKSLDYRIKQLKNLSRFIKERAADITNALRKD----LYKSANSTQLFEILGLEGEINLAVSklAE 80
Cdd:cd07139 41 AVAAARRAFDNGpwPRLSPAERAAVLRRLADALEARADELARLWTAEngmpISWSRRAQGPGPAALLRYYAALARD--FP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 81 WAAPRPVnknlLTISDDVFLQpEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSShtasvmelMSLYLDSE 160
Cdd:cd07139 119 FEERRPG----SGGGHVLVRR-EPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETP--------LDAYLLAE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 161 MYQ----------VVTGGVPETQELLKQ-RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACR 229
Cdd:cd07139 186 AAEeaglppgvvnVVPADREVGEYLVRHpGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 230 RITWGKYLNCGQTCIAPDYILCESSIQDRVIDeiqkCIKEFYT-------IDPKTFedYGRIINRRHFKRI-----MALL 297
Cdd:cd07139 266 GLVPASLMNNGQVCVALTRILVPRSRYDEVVE----ALAAAVAalkvgdpLDPATQ--IGPLASARQRERVegyiaKGRA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 298 EGSTVAIGG-DCDESE--CYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSK---- 370
Cdd:cd07139 340 EGARLVTGGgRPAGLDrgWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVergl 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 47086741 371 KVIKQMisetSSGALLANDCMVHFTlsdLPFGGVGYSGTGRYHG 414
Cdd:cd07139 420 AVARRI----RTGTVGVNGFRLDFG---APFGGFKQSGIGREGG 456
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
7-421 |
3.99e-49 |
|
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: 174.87 E-value: 3.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADIT-----------NALRKDLYKSANSTQLFE--ILGLEGEiNL 73
Cdd:cd07107 24 AVAAARAAFPEWRATTPLERARMLRELATRLREHAEELAlidaldcgnpvSAMLGDVMVAAALLDYFAglVTELKGE-TI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 74 AVSklaewaaPRPVNKNLLtisddvflqpEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-EL 152
Cdd:cd07107 103 PVG-------GRNLHYTLR----------EPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLaEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 153 MSLYLDSEMYQVVTGGVPETQELLKQRFD--HIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRR 230
Cdd:cd07107 166 AREVLPPGVFNILPGDGATAGAALVRHPDvkRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 231 ITWG-KYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYT---IDPKTfeDYGRIINRRHFKRIM-----ALLEGST 301
Cdd:cd07107 246 AVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVgdpTDPAT--TMGPLVSRQQYDRVMhyidsAKREGAR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 302 VAIGGDCDESE-----CYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQM 376
Cdd:cd07107 324 LVTGGGRPEGPaleggFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRT 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 47086741 377 ISETSSGALLANDCMVHFTlsDLPFGGVGYSGTGRYHGK---YSFDQV 421
Cdd:cd07107 404 ARRVEAGYVWINGSSRHFL--GAPFGGVKNSGIGREECLeelLSYTQE 449
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
7-410 |
5.08e-49 |
|
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: 175.87 E-value: 5.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLknlsrfikERAADItnaLRKDLYKsANSTQLFEI----LGLEGEINLAVSKLaEWA 82
Cdd:cd07124 74 AVQAARAAFPTWRRTPPEERARLL--------LRAAAL---LRRRRFE-LAAWMVLEVgknwAEADADVAEAIDFL-EYY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 83 A------------PRPVNKNLLTIsddvflqpEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAS-V 149
Cdd:cd07124 141 AremlrlrgfpveMVPGEDNRYVY--------RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAkL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 150 MELM-SLYLDSEMYQVVTGgvpETQELLKQRFDH-----IFYTGNSTVGKLVMEAAS------HHLTPVTLELGGKSPCY 217
Cdd:cd07124 213 VEILeEAGLPPGVVNFLPG---PGEEVGDYLVEHpdvrfIAFTGSREVGLRIYERAAkvqpgqKWLKRVIAEMGGKNAII 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 218 IDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDY-GRIINRRHFKRIMAL 296
Cdd:cd07124 290 VDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYmGPVIDKGARDRIRRY 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 297 LE----GSTVAIGGDCDESEC---YIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSS 369
Cdd:cd07124 370 IEigksEGRLLLGGEVLELAAegyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRS 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 47086741 370 KKVIKQMISETSSGALLAN-DCM-----VHftlsdlPFGGVGYSGTG 410
Cdd:cd07124 450 PEHLERARREFEVGNLYANrKITgalvgRQ------PFGGFKMSGTG 490
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
7-429 |
5.18e-49 |
|
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: 174.95 E-value: 5.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEI-LGLEGEINLAVSKLAEWAAPR 85
Cdd:cd07117 43 AVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIpLAADHFRYFAGVIRAEEGSAN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 86 PVNKNLLTIsddvfLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSevSSHTASVMELMSLY---LDSEMY 162
Cdd:cd07117 123 MIDEDTLSI-----VLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPS--STTSLSLLELAKIIqdvLPKGVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 163 QVVTGGVPETQELLKQR--FDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCG 240
Cdd:cd07117 196 NIVTGKGSKSGEYLLNHpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 241 QTCIAPDYILCESSIQDRVIDEIQ---KCIKEFYTIDPKTfeDYGRIINRRHFKRIM-----ALLEGSTVAIGG------ 306
Cdd:cd07117 276 QVCCAGSRIFVQEGIYDEFVAKLKekfENVKVGNPLDPDT--QMGAQVNKDQLDKILsyvdiAKEEGAKILTGGhrlten 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 307 DCDESEcYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALL 386
Cdd:cd07117 354 GLDKGF-FIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVW 432
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 47086741 387 ANdcMVHFTLSDLPFGGVGYSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:cd07117 433 VN--TYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
7-426 |
5.32e-49 |
|
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: 173.92 E-value: 5.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLfeilglegEINLAVSKLAEWAAprp 86
Cdd:cd07105 5 AVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGF--------NVDLAAGMLREAAS--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 87 vnknlLTISDDVFLQP------------EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHT----ASVM 150
Cdd:cd07105 74 -----LITQIIGGSIPsdkpgtlamvvkEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRThwliGRVF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 151 E--------LMSLYLDSEMyqvvtggVPETQELLkqrFDH-----IFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCY 217
Cdd:cd07105 149 HeaglpkgvLNVVTHSPED-------APEVVEAL---IAHpavrkVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 218 IDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTfedyGRIINRRHFKRIMALL 297
Cdd:cd07105 219 VLEDADLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL----GSLVSAAAADRVKELV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 298 E-----GSTVAIGG--DCDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSK 370
Cdd:cd07105 295 DdalskGAKLVVGGlaDESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDL 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 47086741 371 KVIKQMISETSSGALLANDCMVHftlsD---LPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:cd07105 375 ARALAVAKRIESGAVHINGMTVH----DeptLPHGGVKSSGYGRFNGKWGIDEFTETKW 429
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
101-429 |
2.05e-48 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 173.13 E-value: 2.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 101 QPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA-SVMELMSLYLDSE-----MYQVVTGGVpETQE 174
Cdd:cd07086 130 QWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAiAVTKILAEVLEKNglppgVVNLVTGGG-DGGE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 175 LLK--QRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCE 252
Cdd:cd07086 209 LLVhdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVH 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 253 SSIQDRVIDEIQKCIKEFyTI----DPKTFedYGRIINRRHFKRIMALLE-----GSTVAIGG---DCDESECYIAPTVL 320
Cdd:cd07086 289 ESVYDEFLERLVKAYKQV-RIgdplDEGTL--VGPLINQAAVEKYLNAIEiaksqGGTVLTGGkriDGGEPGNYVEPTIV 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 321 RDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANdcmVHFTLS--- 397
Cdd:cd07086 366 TGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSDCGIVN---VNIPTSgae 442
|
330 340 350
....*....|....*....|....*....|...
gi 47086741 398 -DLPFGGVGYSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:cd07086 443 iGGAFGGEKETGGGRESGSDAWKQYMRRSTCTI 475
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
7-416 |
5.45e-48 |
|
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: 171.10 E-value: 5.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKnlsrfikeRAADItnaLRKdlyksaNSTQLFEILGLE---------GEINLaVSK 77
Cdd:cd07100 4 ALDRAHAAFLAWRKTSFAERAALLR--------KLADL---LRE------RKDELARLITLEmgkpiaearAEVEK-CAW 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 78 LAEW--------AAPRPVNknllTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASV 149
Cdd:cd07100 66 ICRYyaenaeafLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 150 MElmSLYLDS----EMYQVVTGGVPETQELLK-QRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDI 224
Cdd:cd07100 142 IE--ELFREAgfpeGVFQNLLIDSDQVEAIIAdPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 225 RIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYT---IDPKTF----------EDYGRIINRrhfk 291
Cdd:cd07100 220 DKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVgdpMDEDTDlgplarkdlrDELHEQVEE---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 292 rimALLEGSTVAIGGDCDESE-CYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSK 370
Cdd:cd07100 296 ---AVAAGATLLLGGKRPDGPgAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDL 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 47086741 371 KVIKQMISETSSGALLANDcmvhFTLSD--LPFGGVGYSGTGRYHGKY 416
Cdd:cd07100 373 ERAERVARRLEAGMVFING----MVKSDprLPFGGVKRSGYGRELGRF 416
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
6-430 |
8.16e-47 |
|
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: 169.07 E-value: 8.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTG---RSKSLDYRIKQLKNLSRFIkERAADITNALrkdlyKSANSTQLFEILGLeGEINLAVSKL---A 79
Cdd:cd07141 48 KAVKAARAAFKLGspwRTMDASERGRLLNKLADLI-ERDRAYLASL-----ETLDNGKPFSKSYL-VDLPGAIKVLryyA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 80 EWAaprpvNKNL-LTISDD----VFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvmelms 154
Cdd:cd07141 121 GWA-----DKIHgKTIPMDgdffTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTA------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 155 LYLDSEMYQ---------VVTGGVPETQELLKQR--FDHIFYTGNSTVGKLVMEAASH-HLTPVTLELGGKSPCYIDKNC 222
Cdd:cd07141 189 LYLASLIKEagfppgvvnVVPGYGPTAGAAISSHpdIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 223 DIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVID---EIQKCIKEFYTIDPKTFEdyGRIINRRHFKRIMALL-- 297
Cdd:cd07141 269 DLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKrsvERAKKRVVGNPFDPKTEQ--GPQIDEEQFKKILELIes 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 298 ---EGSTVAIGGD-CDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFssSKKVI 373
Cdd:cd07141 347 gkkEGAKLECGGKrHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVF--TKDID 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47086741 374 KQMiseTSSGALLAN----DCMVHFTlSDLPFGGVGYSGTGRYHGKYSFDQVSHLRSCLIK 430
Cdd:cd07141 425 KAI---TFSNALRAGtvwvNCYNVVS-PQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
37-420 |
1.30e-46 |
|
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: 168.25 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 37 IKERAADITNAlRKD-----LYKSANSTqlfeILGLEGEINLAVSKLAEWA--APRPVNKNLLTISDD----VFlqPEPL 105
Cdd:cd07151 59 ILEKAAQILEE-RRDeivewLIRESGST----RIKANIEWGAAMAITREAAtfPLRMEGRILPSDVPGkenrVY--REPL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 106 GVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHT-----ASVMELMSlyLDSEMYQVVTGGVPEtqelLKQRF 180
Cdd:cd07151 132 GVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITgglllAKIFEEAG--LPKGVLNVVVGAGSE----IGDAF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 181 -DH-----IFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESS 254
Cdd:cd07151 206 vEHpvprlISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHED 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 255 IQDRVIDEIQKCIKEFYT---IDPKTFedYGRIINRRHFKRIMALLE-----GSTVAIGGDCDESecYIAPTVLRDVKPA 326
Cdd:cd07151 286 VYDEFVEKFVERVKALPYgdpSDPDTV--VGPLINESQVDGLLDKIEqaveeGATLLVGGEAEGN--VLEPTVLSDVTND 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 327 SKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHfTLSDLPFGGVGY 406
Cdd:cd07151 362 MEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVN-DEPHVPFGGEKN 440
|
410
....*....|....
gi 47086741 407 SGTGRYHGKYSFDQ 420
Cdd:cd07151 441 SGLGRFNGEWALEE 454
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
7-411 |
2.25e-46 |
|
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: 167.22 E-value: 2.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNAL-----------RKDLYKSANSTQL--FEILGLEGEInl 73
Cdd:cd07094 26 ALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIaceggkpikdaRVEVDRAIDTLRLaaEEAERIRGEE-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 74 avsklaewaaprpVNKNLLTISDD--VFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvME 151
Cdd:cd07094 104 -------------IPLDATQGSDNrlAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSA--LE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 152 LMSLYLDS----EMYQVVTGGVPETQELL--KQRFDHIFYTGNSTVGKLVMEAAShhLTPVTLELGGKSPCYIDKNCDIR 225
Cdd:cd07094 169 LAKILVEAgvpeGVLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAG--GKRIALELGGNAPVIVDRDADLD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 226 IACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRI-----MALLEG 299
Cdd:cd07094 247 AAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDtDVGPLISEEAAERVerwveEAVEAG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 300 STVAIGGDCDESECYiaPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISE 379
Cdd:cd07094 327 ARLLCGGERDGALFK--PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEK 404
|
410 420 430
....*....|....*....|....*....|..
gi 47086741 380 TSSGALLANDCmVHFTLSDLPFGGVGYSGTGR 411
Cdd:cd07094 405 LEVGGVMVNDS-SAFRTDWMPFGGVKESGVGR 435
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
2-419 |
2.84e-46 |
|
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: 167.43 E-value: 2.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 2 SREQL--AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKS--------ANSTQLF-----EILG 66
Cdd:cd07097 35 SAEDAdaAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTlpeargevTRAGQIFryyagEALR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 67 LEGEInlavsklaewaAPrPVNKNLltisdDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHT 146
Cdd:cd07097 115 LSGET-----------LP-STRPGV-----EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPAS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 147 ASVM-ELMSLY-LDSEMYQVVTG-GVPETQELLK-QRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNC 222
Cdd:cd07097 178 AWALvEILEEAgLPAGVFNLVMGsGSEVGQALVEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 223 DIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQ---KCIKEFYTIDPKTfeDYGRIINRRHFKRIMALL-- 297
Cdd:cd07097 258 DLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVertKALKVGDALDEGV--DIGPVVSERQLEKDLRYIei 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 298 ---EGSTVAIGGDCDESEC---YIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKK 371
Cdd:cd07097 336 arsEGAKLVYGGERLKRPDegyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLK 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 47086741 372 VIKQMISETSSGallandcMVHFTLS------DLPFGGVGYSGTG-RYHGKYSFD 419
Cdd:cd07097 416 HATHFKRRVEAG-------VVMVNLPtagvdyHVPFGGRKGSSYGpREQGEAALE 463
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
6-426 |
5.82e-46 |
|
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: 166.94 E-value: 5.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLT--GRSKSLDYRIKQLKNLSRFIkERAADITNALrkdlyKSANSTQLFEILGlEGEINLAVSKL---AE 80
Cdd:cd07143 48 IAVEVAHAAFETdwGLKVSGSKRGRCLSKLADLM-ERNLDYLASI-----EALDNGKTFGTAK-RVDVQASADTFryyGG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 81 WAaprpvNKNL-LTISDDV----FLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvMELMSL 155
Cdd:cd07143 121 WA-----DKIHgQVIETDIkkltYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSA--LYMTKL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 156 Y----LDSEMYQVVTGGVPETQELLKQ--RFDHIFYTGNSTVGKLVMEAASH-HLTPVTLELGGKSPCYIDKNCDIRIAC 228
Cdd:cd07143 194 IpeagFPPGVINVVSGYGRTCGNAISShmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 229 RRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDP---KTFEdyGRIINRRHFKRIMALLE-----GS 300
Cdd:cd07143 274 VWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPfaeDTFQ--GPQVSQIQYERIMSYIEsgkaeGA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 301 TVAIGGDCDESECY-IAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISE 379
Cdd:cd07143 352 TVETGGKRHGNEGYfIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANA 431
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 47086741 380 TSSGALLANdC--MVHFtlsDLPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:cd07143 432 LKAGTVWVN-CynLLHH---QVPFGGYKQSGIGRELGEYALENYTQIKA 476
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
30-383 |
7.32e-46 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 164.91 E-value: 7.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 30 LKNLSRFIKERAADITNALRKDLYKsanstqlfeILGL-EGEINLAVSKL---AEWA---------APRPvNKNLLtisd 96
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGK---------IQQLaEVEVAFTADYIdymAEWArryegeiiqSDRP-GENIL---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 97 dVFLQPepLGVVLIIGAWNYP---IAVTLQPlvgAIAAGNAVVVKPSEVSSHTAsvMELMSLY----LDSEMYQVVTGGV 169
Cdd:PRK10090 67 -LFKRA--LGVTTGILPWNFPfflIARKMAP---ALLTGNTIVIKPSEFTPNNA--IAFAKIVdeigLPKGVFNLVLGRG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 170 PET-QELLK-QRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPD 247
Cdd:PRK10090 139 ETVgQELAGnPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 248 YILCESSIQDRVIDEIQKCIKEFYTIDPKTFE--DYGRIINRRHFKRIMALL-----EGSTVAIGGDCDESECYI-APTV 319
Cdd:PRK10090 219 RVYVQKGIYDQFVNRLGEAMQAVQFGNPAERNdiAMGPLINAAALERVEQKVaraveEGARVALGGKAVEGKGYYyPPTL 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086741 320 LRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSG 383
Cdd:PRK10090 299 LLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFG 362
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
6-419 |
2.98e-45 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 165.29 E-value: 2.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTGRSKSLD-----YRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQ--------LFEIL-----GL 67
Cdd:PLN02467 49 AAVEAARKAFKRNKGKDWArttgaVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAwdmddvagCFEYYadlaeAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 68 EGEINLAVSklaewaaprpvnknLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA 147
Cdd:PLN02467 129 DAKQKAPVS--------------LPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTC 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 148 svMELMSLY----LDSEMYQVVTGGVPETQELLKQ--RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKN 221
Cdd:PLN02467 195 --LELADICrevgLPPGVLNVVTGLGTEAGAPLAShpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 222 CDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPktFED---YGRIINRRHFKRIMALL- 297
Cdd:PLN02467 273 VDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDP--LEEgcrLGPVVSEGQYEKVLKFIs 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 298 ----EGSTVAIGGDCDE---SECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSK 370
Cdd:PLN02467 351 taksEGATILCGGKRPEhlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDL 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 47086741 371 KVIKQMISETSSGALLANDCMVHFTlsDLPFGGVGYSGTGRYHGKYSFD 419
Cdd:PLN02467 431 ERCERVSEAFQAGIVWINCSQPCFC--QAPWGGIKRSGFGRELGEWGLE 477
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
7-409 |
3.74e-45 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 165.11 E-value: 3.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKS--------ANSTQLFEILGLEgeinlavskL 78
Cdd:PRK03137 78 AMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPwaeadadtAEAIDFLEYYARQ---------M 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 79 AEWAAPRPVNKnllTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAS-VMELM-SLY 156
Cdd:PRK03137 149 LKLADGKPVES---RPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAkFVEVLeEAG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 157 LDSEMYQVVTGGVPETQELL----KQRFdhIFYTGNSTVGKLVMEAASH------HLTPVTLELGGKSPCYIDKNCDIRI 226
Cdd:PRK03137 226 LPAGVVNFVPGSGSEVGDYLvdhpKTRF--ITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 227 ACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDYGRIINRRHFKRIMALLE-----GST 301
Cdd:PRK03137 304 AAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEigkeeGRL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 302 VAiGGDCDESECY-IAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISET 380
Cdd:PRK03137 384 VL-GGEGDDSKGYfIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREF 462
|
410 420 430
....*....|....*....|....*....|....*
gi 47086741 381 SSGALLAN-DCM-----VHftlsdlPFGGVGYSGT 409
Cdd:PRK03137 463 HVGNLYFNrGCTgaivgYH------PFGGFNMSGT 491
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
98-410 |
4.37e-45 |
|
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: 163.68 E-value: 4.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 98 VFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSshTASVMELMSLYLDS----EMYQVVTGGVPETQ 173
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKT--PLSAIYLADLLYEAglppDMLSVVTGEPGEIG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 174 ELLKQ--RFDHIFYTGNSTVGKLVMEAASHHLTpvTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILC 251
Cdd:cd07146 192 DELIThpDVDLVTFTGGVAVGKAIAATAGYKRQ--LLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILV 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 252 ESSIQDRVIDEIQKCIKEFYTIDP-KTFEDYGRIINR---RHFKRIM--ALLEGSTVAIGGDCDESecYIAPTVLRDVKP 325
Cdd:cd07146 270 HESVADEFVDLLVEKSAALVVGDPmDPATDMGTVIDEeaaIQIENRVeeAIAQGARVLLGNQRQGA--LYAPTVLDHVPP 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 326 ASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDcMVHFTLSDLPFGGVG 405
Cdd:cd07146 348 DAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNE-VPGFRSELSPFGGVK 426
|
....*
gi 47086741 406 YSGTG 410
Cdd:cd07146 427 DSGLG 431
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
104-415 |
2.10e-44 |
|
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: 162.09 E-value: 2.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 104 PLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVMelMSLYLDS----EMYQVVTGGVPETQELLKQR 179
Cdd:cd07101 118 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWA--VELLIEAglprDLWQVVTGPGSEVGGAIVDN 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 180 FDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRV 259
Cdd:cd07101 196 ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEF 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 260 IDEIQKCIKEF-----YTIDPktfeDYGRIINRRHFKRIMALLE-----GSTVAIGGDC--DESECYIAPTVLRDVKPAS 327
Cdd:cd07101 276 VRRFVARTRALrlgaaLDYGP----DMGSLISQAQLDRVTAHVDdavakGATVLAGGRArpDLGPYFYEPTVLTGVTEDM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 328 KVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMV-HFTLSDLPFGGVGY 406
Cdd:cd07101 352 ELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAaAWASIDAPMGGMKD 431
|
....*....
gi 47086741 407 SGTGRYHGK 415
Cdd:cd07101 432 SGLGRRHGA 440
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
6-426 |
2.34e-44 |
|
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: 162.28 E-value: 2.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTG---------RSKSLdYRIKQLknLSRFIKERAAditnalrkdlYKSANSTQLFEIlGLEGEINLAVs 76
Cdd:cd07142 45 RAVKAARKAFDEGpwprmtgyeRSRIL-LRFADL--LEKHADELAA----------LETWDNGKPYEQ-ARYAEVPLAA- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 77 KLAEWAAPRPVNKNLLTISDD----VFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVMEL 152
Cdd:cd07142 110 RLFRYYAGWADKIHGMTLPADgphhVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 153 MSLY--LDSEMYQVVTGGVPETQELLKQRF--DHIFYTGNSTVGKLVMEAASH-HLTPVTLELGGKSPCYIDKNCDIRIA 227
Cdd:cd07142 190 LAAEagLPDGVLNIVTGFGPTAGAAIASHMdvDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 228 CRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDP-KTFEDYGRIINRRHFKRIMALL-----EGST 301
Cdd:cd07142 270 VELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPfRKGVEQGPQVDKEQFEKILSYIehgkeEGAT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 302 VAIGGDCDESECY-IAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISET 380
Cdd:cd07142 350 LITGGDRIGSKGYyIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRAL 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 47086741 381 SSGALLANdCMVHFTlSDLPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:cd07142 430 KAGTVWVN-CYDVFD-ASIPFGGYKMSGIGREKGIYALNNYLQVKA 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
55-414 |
2.23e-43 |
|
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: 159.05 E-value: 2.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 55 SANSTQLFEILGLE---------GEINLAVSKLAEWAA-PRPVNKNLLTISDDVF--LQPEPLGVVLIIGAWNYPIAVTL 122
Cdd:cd07120 56 EANAERLARLLALEngkilgearFEISGAISELRYYAGlARTEAGRMIEPEPGSFslVLREPMGVAGIIVPWNSPVVLLV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 123 QPLVGAIAAGNAVVVKP-SEVSSHTASVMELMS--LYLDSEMYQVVTGGVPETQELL--KQRFDHIFYTGNSTVGKLVME 197
Cdd:cd07120 136 RSLAPALAAGCTVVVKPaGQTAQINAAIIRILAeiPSLPAGVVNLFTESGSEGAAHLvaSPDVDVISFTGSTATGRAIMA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 198 AASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQK---CIKEFYTID 274
Cdd:cd07120 216 AAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAArlaAVKVGPGLD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 275 PKTfeDYGRIINRRHFKRIMALLE-----GSTVAI-GGDCDESEC---YIAPTVLRDVKPASKVMQEEIFGPILPIVTVN 345
Cdd:cd07120 296 PAS--DMGPLIDRANVDRVDRMVEraiaaGAEVVLrGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFD 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47086741 346 GLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFtlSDLPFGGVGYSGTGRYHG 414
Cdd:cd07120 374 DEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWINDWNKLF--AEAEEGGYRQSGLGRLHG 440
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
6-426 |
2.72e-43 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 159.99 E-value: 2.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTGR----SKSLDYRIkqlknLSRFikeraADITNALRKDLYK--SANSTQLFEiLGLEGEINLAVSKLA 79
Cdd:PLN02766 62 LAVKAAREAFDHGPwprmSGFERGRI-----MMKF-----ADLIEEHIEELAAldTIDAGKLFA-LGKAVDIPAAAGLLR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 80 EWA-APRPVNKNLLTISDDV--FLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvmeLMSLY 156
Cdd:PLN02766 131 YYAgAADKIHGETLKMSRQLqgYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSA----LFYAH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 157 LDSE------MYQVVTGGVPETQELLKQRFD--HIFYTGNSTVGKLVMEAAS-HHLTPVTLELGGKSPCYIDKNCDIRIA 227
Cdd:PLN02766 207 LAKLagvpdgVINVVTGFGPTAGAAIASHMDvdKVSFTGSTEVGRKIMQAAAtSNLKQVSLELGGKSPLLIFDDADVDMA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 228 CRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPktFE---DYGRIINRRHFKRIMALL-----EG 299
Cdd:PLN02766 287 VDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP--FDpraRQGPQVDKQQFEKILSYIehgkrEG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 300 STVAIGGD-CDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMIS 378
Cdd:PLN02766 365 ATLLTGGKpCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSR 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 47086741 379 ETSSGALLANdCMVHFTlSDLPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:PLN02766 445 SIRAGTIWVN-CYFAFD-PDCPFGGYKMSGFGRDQGMDALDKYLQVKS 490
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
99-430 |
3.15e-43 |
|
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: 159.14 E-value: 3.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 99 FLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA-SVMELMS-LYLDSEMYQVVTGGVPETQELL 176
Cdd:cd07113 137 FTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLlRVAELAKeAGIPDGVLNVVNGKGAVGAQLI 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 177 KQ-RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSI 255
Cdd:cd07113 217 SHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSK 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 256 QDRVIDEIQKCIKEFYT---IDPKTFedYGRIINRRHFKRI-----MALLEGSTVAIGGDCDESECY-IAPTVLRDVKPA 326
Cdd:cd07113 297 FDELVTKLKQALSSFQVgspMDESVM--FGPLANQPHFDKVcsyldDARAEGDEIVRGGEALAGEGYfVQPTLVLARSAD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 327 SKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANdcMVHFTLSDLPFGGVGY 406
Cdd:cd07113 375 SRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN--MHTFLDPAVPFGGMKQ 452
|
330 340
....*....|....*....|....
gi 47086741 407 SGTGRYHGKYSFDQVSHLRSCLIK 430
Cdd:cd07113 453 SGIGREFGSAFIDDYTELKSVMIR 476
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
104-457 |
1.30e-41 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 155.81 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 104 PLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA-SVMELmsLY---LDSEMYQVVTGGVPETQELLKQR 179
Cdd:PRK09407 154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTAlAAVEL--LYeagLPRDLWQVVTGPGPVVGTALVDN 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 180 FDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRV 259
Cdd:PRK09407 232 ADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEF 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 260 IDEIQKCIKEF-----YTIDPktfeDYGRIINRRHFKRIMALLE-----GSTVAIGGDC--DESECYIAPTVLRDVKPAS 327
Cdd:PRK09407 312 VRAFVAAVRAMrlgagYDYSA----DMGSLISEAQLETVSAHVDdavakGATVLAGGKArpDLGPLFYEPTVLTGVTPDM 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 328 KVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDC-MVHFTLSDLPFGGVGY 406
Cdd:PRK09407 388 ELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGyAAAWGSVDAPMGGMKD 467
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 47086741 407 SGTGRYHG-----KYSFDQ-VSHLRsclikKLNMEAVNQMRYPphtteklRWARVLL 457
Cdd:PRK09407 468 SGLGRRHGaegllKYTESQtIATQR-----VLPLAPPPGMPYE-------KYAKLML 512
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
104-429 |
1.00e-40 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 151.63 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 104 PLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvMELMSLYLDSEM----YQVVTGGVPETQELLK-Q 178
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSA--LILGEVLAETGLpkgaFSVLPCSRDDADLLVTdE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 179 RFDHIFYTGNSTVGKLVMEAASHHltPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDR 258
Cdd:cd07147 201 RIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 259 VIDEIQKCIKEFYTIDPK---TFedYGRIINRRHFKRIM-----ALLEGSTVAIGGDCDESecYIAPTVLRDVKPASKVM 330
Cdd:cd07147 279 FKSRLVARVKALKTGDPKddaTD--VGPMISESEAERVEgwvneAVDAGAKLLTGGKRDGA--LLEPTILEDVPPDMEVN 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 331 QEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDcMVHFTLSDLPFGGVGYSGTG 410
Cdd:cd07147 355 CEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIND-VPTFRVDHMPYGGVKDSGIG 433
|
330
....*....|....*....
gi 47086741 411 RYHGKYSFDQVSHLRSCLI 429
Cdd:cd07147 434 REGVRYAIEEMTEPRLLVI 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
103-423 |
1.20e-39 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 149.29 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 103 EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMSLYLDSEMYQVVTGGVPETQELL--KQR 179
Cdd:PRK13473 137 DPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLaELAADILPPGVLNVVTGRGATVGDALvgHPK 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 180 FDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRV 259
Cdd:PRK13473 217 VRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 260 ID---EIQKCIKEFYTIDPKTfeDYGRIINRRHFKRIMALLE------GSTVAIGG-DCDESECYIAPTVLRDVKPASKV 329
Cdd:PRK13473 297 VAklaAAVATLKVGDPDDEDT--ELGPLISAAHRDRVAGFVErakalgHIRVVTGGeAPDGKGYYYEPTLLAGARQDDEI 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 330 MQEEIFGPILPIVTVNGLKEAIEFINDREKPLAlyvfSS--SKKVIKQM--ISETSSGALLANDcmvHFTL-SDLPFGGV 404
Cdd:PRK13473 375 VQREVFGPVVSVTPFDDEDQAVRWANDSDYGLA----SSvwTRDVGRAHrvSARLQYGCTWVNT---HFMLvSEMPHGGQ 447
|
330 340
....*....|....*....|..
gi 47086741 405 GYSGTGRYHGKYSFD---QVSH 423
Cdd:PRK13473 448 KQSGYGKDMSLYGLEdytVVRH 469
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
102-429 |
2.67e-39 |
|
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: 148.37 E-value: 2.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 102 PEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSShtASVMELMSLYLD---SEMYQVVTGGVPETQELL-- 176
Cdd:cd07116 134 HEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTP--ASILVLMELIGDllpPGVVNVVNGFGLEAGKPLas 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 177 KQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSP------------CYIDKNCD--IRIAcrritwgkyLNCGQT 242
Cdd:cd07116 212 SKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniffadvmdaddAFFDKALEgfVMFA---------LNQGEV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 243 CIAPDYILCESSIQDRVID---EIQKCIKEFYTIDPKTFedYGRIINRRHFKRIMALL-----EGSTVAIGGD-----CD 309
Cdd:cd07116 283 CTCPSRALIQESIYDRFMEralERVKAIKQGNPLDTETM--IGAQASLEQLEKILSYIdigkeEGAEVLTGGErnelgGL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 310 ESECYIAPTVlrdVKPASK--VMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLA 387
Cdd:cd07116 361 LGGGYYVPTT---FKGGNKmrIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWT 437
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 47086741 388 NdCMvHFTLSDLPFGGVGYSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:cd07116 438 N-CY-HLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
1-411 |
2.67e-39 |
|
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: 148.10 E-value: 2.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 1 MSREQL--AVQQARKAFL-TGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQ-------------LFEI 64
Cdd:cd07082 35 LSALEIleAAETAYDAGRgWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALkevdrtidyirdtIEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 65 LGLEGEinlavSKLAEWAaprPVNKNLLTIsddvfLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSE--- 141
Cdd:cd07082 115 KRLDGD-----SLPGDWF---PGTKGKIAQ-----VRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATqgv 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 142 -VSSHTASVMELMSLylDSEMYQVVTGGVPETQELL--KQRFDHIFYTGNSTVGKLVMEAasHHLTPVTLELGGKSPCYI 218
Cdd:cd07082 182 lLGIPLAEAFHDAGF--PKGVVNVVTGRGREIGDPLvtHGRIDVISFTGSTEVGNRLKKQ--HPMKRLVLELGGKDPAIV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 219 DKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPktFEDYGRI---INRRHFKRIMA 295
Cdd:cd07082 258 LPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMP--WDNGVDItplIDPKSADFVEG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 296 LLE-----GSTVAIGGDcDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSK 370
Cdd:cd07082 336 LIDdavakGATVLNGGG-REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDI 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 47086741 371 KVIKQMISETSSGALLAND-CMV---HFtlsdlPFGGVGYSGTGR 411
Cdd:cd07082 415 NKARKLADALEVGTVNINSkCQRgpdHF-----PFLGRKDSGIGT 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
7-411 |
3.42e-39 |
|
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: 148.41 E-value: 3.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYR-----IKQLKNLSRFIKERAADI---------TNALRKDLYKSANSTQLF-----EILGL 67
Cdd:cd07140 48 AVAAAKEAFENGEWGKMNARdrgrlMYRLADLMEEHQEELATIesldsgavyTLALKTHVGMSIQTFRYFagwcdKIQGK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 68 EGEINLAvsklaewaapRPvNKNLltisddVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA 147
Cdd:cd07140 128 TIPINQA----------RP-NRNL------TLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 148 svMELMSLYLDSEMYQVVTGGVPETQELLKQRF-DH-----IFYTGNSTVGKLVME-AASHHLTPVTLELGGKSPCYIDK 220
Cdd:cd07140 191 --LKFAELTVKAGFPKGVINILPGSGSLVGQRLsDHpdvrkLGFTGSTPIGKHIMKsCAVSNLKKVSLELGGKSPLIIFA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 221 NCDIRIACRRITWGKYLNCGQTCIAPDYILCESSIQD----RVIDEIQKcikefYTI-DP-KTFEDYGRIINRRHFKRIM 294
Cdd:cd07140 269 DCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDefvrRVVEEVKK-----MKIgDPlDRSTDHGPQNHKAHLDKLV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 295 -----ALLEGSTVAIGG-DCDESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNG--LKEAIEFINDREKPLALYVF 366
Cdd:cd07140 344 eycerGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVF 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 47086741 367 ssSKKVIKQM-ISEtssgALLANDCMVH-FTLSDL--PFGGVGYSGTGR 411
Cdd:cd07140 424 --TKDINKALyVSD----KLEAGTVFVNtYNKTDVaaPFGGFKQSGFGK 466
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
103-426 |
4.40e-39 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 148.10 E-value: 4.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 103 EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvMELMSLYLDSEM----YQVVTG-GvpETQELLK 177
Cdd:PRK13252 141 EPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTA--LKLAEIYTEAGLpdgvFNVVQGdG--RVGAWLT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 178 Q--RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSI 255
Cdd:PRK13252 217 EhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 256 QDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALL-----EGSTVAIGG-----DCDESECYIAPTVLRDVK 324
Cdd:PRK13252 297 KAAFEARLLERVERIRIGDPMDPAtNFGPLVSFAHRDKVLGYIekgkaEGARLLCGGerlteGGFANGAFVAPTVFTDCT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 325 PASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSS----KKVIKQmisetssgaLLANDCMV-HFTLS-- 397
Cdd:PRK13252 377 DDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADlsraHRVIHQ---------LEAGICWInTWGESpa 447
|
330 340
....*....|....*....|....*....
gi 47086741 398 DLPFGGVGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:PRK13252 448 EMPVGGYKQSGIGRENGIATLEHYTQIKS 476
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
96-410 |
8.35e-39 |
|
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: 147.34 E-value: 8.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 96 DDVFLQPepLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSS-HTASVMELM-SLYLDSEMYQVVTGGVPETQ 173
Cdd:cd07083 148 NESFYVG--LGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVvVGYKVFEIFhEAGFPPGVVQFLPGVGEEVG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 174 ELL--KQRFDHIFYTGNSTVGKLVMEAAS------HHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIA 245
Cdd:cd07083 226 AYLteHERIRGINFTGSLETGKKIYEAAArlapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 246 PDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALLE----GSTVAIGGDCDESECY-IAPTV 319
Cdd:cd07083 306 ASRLILTQGAYEPVLERLLKRAERLSVGPPEENGtDLGPVIDAEQEAKVLSYIEhgknEGQLVLGGKRLEGEGYfVAPTV 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 320 LRDVKPASKVMQEEIFGPILPIVTV--NGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLS 397
Cdd:cd07083 386 VEEVPPKARIAQEEIFGPVLSVIRYkdDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVG 465
|
330
....*....|...
gi 47086741 398 DLPFGGVGYSGTG 410
Cdd:cd07083 466 VQPFGGFKLSGTN 478
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
103-429 |
1.01e-38 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 146.96 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 103 EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvMELMSLY----LDSEMYQVVTG-GVPETQEL-L 176
Cdd:PRK09847 156 EPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSA--IRLAGLAkeagLPDGVLNVVTGfGHEAGQALsR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 177 KQRFDHIFYTGNSTVGK-LVMEAASHHLTPVTLELGGKSPCYIDKNC-DIRIACRRITWGKYLNCGQTCIAPDYILCESS 254
Cdd:PRK09847 234 HNDIDAIAFTGSTRTGKqLLKDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEES 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 255 IQDRVIDEIQKCIKEF---YTIDPKTfeDYGRIINRRHFKRIMALLEG----STVAIGGDCDESECYIAPTVLRDVKPAS 327
Cdd:PRK09847 314 IADEFLALLKQQAQNWqpgHPLDPAT--TMGTLIDCAHADSVHSFIREgeskGQLLLDGRNAGLAAAIGPTIFVDVDPNA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 328 KVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDcmvhFTLSDL--PFGGVG 405
Cdd:PRK09847 392 SLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN----YNDGDMtvPFGGYK 467
|
330 340
....*....|....*....|....
gi 47086741 406 YSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:PRK09847 468 QSGNGRDKSLHALEKFTELKTIWI 491
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
97-419 |
2.30e-38 |
|
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: 145.74 E-value: 2.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 97 DVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSE-VSShtaSVMELMSLYLDSEM----YQVVTGGVPE 171
Cdd:cd07085 129 DTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSErVPG---AAMRLAELLQEAGLpdgvLNVVHGGKEA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 172 TQELLkqrfDH-----IFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAP 246
Cdd:cd07085 206 VNALL----DHpdikaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMAL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 247 DYILCESSIQDRVIDEIQKCIKEF---YTIDPKTfeDYGRIINRRHFKRIMALL-----EGSTVAIGG-DCDESEC---- 313
Cdd:cd07085 282 SVAVAVGDEADEWIPKLVERAKKLkvgAGDDPGA--DMGPVISPAAKERIEGLIesgveEGAKLVLDGrGVKVPGYengn 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 314 YIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGallandcMV- 392
Cdd:cd07085 360 FVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAG-------MVg 432
|
330 340 350
....*....|....*....|....*....|....*....
gi 47086741 393 ----------HFtlsdlPFGGVGYS--GTGRYHGKYSFD 419
Cdd:cd07085 433 invpipvplaFF-----SFGGWKGSffGDLHFYGKDGVR 466
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
7-419 |
1.82e-37 |
|
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: 142.41 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLfEILGLEGEINLAVSKLAEWAAPRp 86
Cdd:cd07095 5 AVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQT-EVAAMAGKIDISIKAYHERTGER- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 87 vnkNLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEvssHTASVMELM-SLY----LDSEM 161
Cdd:cd07095 83 ---ATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSE---LTPAVAELMvELWeeagLPPGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 162 YQVVTGGVPETQELLKQ-RFDHIFYTGNSTVGKLVMEAASHHltP---VTLELGGKSPCYIDKNCDIRIACRRITWGKYL 237
Cdd:cd07095 157 LNLVQGGRETGEALAAHeGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 238 NCGQTC-IAPDYILCESSIQDRVIDEIQKCIKEfYTIDPKTFED--YGRIINRRHFKRiMALLEGSTVAIGGDC------ 308
Cdd:cd07095 235 TAGQRCtCARRLIVPDGAVGDAFLERLVEAAKR-LRIGAPDAEPpfMGPLIIAAAAAR-YLLAQQDLLALGGEPllamer 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 309 -DESECYIAPTVLrDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLA 387
Cdd:cd07095 313 lVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNW 391
|
410 420 430
....*....|....*....|....*....|..
gi 47086741 388 NDcMVHFTLSDLPFGGVGYSGTGRYHGKYSFD 419
Cdd:cd07095 392 NR-PTTGASSTAPFGGVGLSGNHRPSAYYAAD 422
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
6-415 |
3.85e-37 |
|
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: 142.53 E-value: 3.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 6 LAVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQlfeilglEGEINLAVSKL---AEWA 82
Cdd:cd07111 63 AAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESR-------DCDIPLVARHFyhhAGWA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 83 aprpvnknllTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVM-ELMS-LYLDSE 160
Cdd:cd07111 136 ----------QLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFaEICAeAGLPPG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 161 MYQVVTGGVPETQELLKQ-RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNC 239
Cdd:cd07111 206 VLNIVTGNGSFGSALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 240 GQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDP--KTFeDYGRIINRRHFKRIMALLE-----GSTV-AIGGDCDES 311
Cdd:cd07111 286 GQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPldKAI-DMGAIVDPAQLKRIRELVEegraeGADVfQPGADLPSK 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 312 ECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDcm 391
Cdd:cd07111 365 GPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING-- 442
|
410 420
....*....|....*....|....*.
gi 47086741 392 vhFTLSD--LPFGGVGYSGTGRYHGK 415
Cdd:cd07111 443 --HNLFDaaAGFGGYRESGFGREGGK 466
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
103-417 |
8.64e-34 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 133.78 E-value: 8.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 103 EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvMELMSLYLDSEM----YQVVTGGVPETQELLKQ 178
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSA--LYAAKLLHEAGLppgvLNVVSGFGPTAGAALAS 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 179 RF--DHIFYTGNSTVGKLVME-AASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSI 255
Cdd:PLN02466 272 HMdvDKLAFTGSTDTGKIVLElAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 256 QDRVIDEIQKCIKEFYTIDP-KTFEDYGRIINRRHFKRIMALLE-----GSTVAIGGDCDESECY-IAPTVLRDVKPASK 328
Cdd:PLN02466 352 YDEFVEKAKARALKRVVGDPfKKGVEQGPQIDSEQFEKILRYIKsgvesGATLECGGDRFGSKGYyIQPTVFSNVQDDML 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 329 VMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANdCMVHFTLSdLPFGGVGYSG 408
Cdd:PLN02466 432 IAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN-CFDVFDAA-IPFGGYKMSG 509
|
....*....
gi 47086741 409 TGRYHGKYS 417
Cdd:PLN02466 510 IGREKGIYS 518
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
5-411 |
4.05e-33 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 130.75 E-value: 4.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 5 QLAVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSanstqlfeILGLEGEINLAVSkLAEWAA- 83
Cdd:PRK13968 32 ENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKP--------INQARAEVAKSAN-LCDWYAe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 84 -------PRPVnknlLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSevSSHTASVMELMSLY 156
Cdd:PRK13968 103 hgpamlkAEPT----LVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA--PNVMGCAQLIAQVF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 157 LDSEMYQVVTGGVPETQELLKQ-----RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRI 231
Cdd:PRK13968 177 KDAGIPQGVYGWLNADNDGVSQmindsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 232 TWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDYGRIINR------RHFKRIMALLEGSTVAIG 305
Cdd:PRK13968 257 VAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARfdlrdeLHHQVEATLAEGARLLLG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 306 GDCDESEC-YIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGA 384
Cdd:PRK13968 337 GEKIAGAGnYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGG 416
|
410 420
....*....|....*....|....*....
gi 47086741 385 LLANDcmvhFTLSD--LPFGGVGYSGTGR 411
Cdd:PRK13968 417 VFING----YCASDarVAFGGVKKSGFGR 441
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-419 |
2.86e-30 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 123.09 E-value: 2.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERaaditnalRKDLYKSANSTQLFEILGLEGEINLAVSKLaEWAAPRP 86
Cdd:PRK11241 53 AIDAANRALPAWRALTAKERANILRRWFNLMMEH--------QDDLARLMTLEQGKPLAEAKGEISYAASFI-EWFAEEG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 87 ------------VNKNLLTISddvflqpEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA-SVMELM 153
Cdd:PRK11241 124 kriygdtipghqADKRLIVIK-------QPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSAlALAELA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 154 SLY-LDSEMYQVVTGGVPETQELLKQR--FDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRR 230
Cdd:PRK11241 197 IRAgIPAGVFNVVTGSAGAVGGELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 231 ITWGKYLNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDpkTFED---YGRIINRRHFKRIM-----ALLEGSTV 302
Cdd:PRK11241 277 ALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGD--GLEKgvtIGPLIDEKAVAKVEehiadALEKGARV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 303 AIGGDCDESE-CYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETS 381
Cdd:PRK11241 355 VCGGKAHELGgNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALE 434
|
410 420 430
....*....|....*....|....*....|....*...
gi 47086741 382 SGALLANDCMVHFTLSdlPFGGVGYSGTGRYHGKYSFD 419
Cdd:PRK11241 435 YGIVGINTGIISNEVA--PFGGIKASGLGREGSKYGIE 470
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
101-390 |
3.04e-27 |
|
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: 114.23 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 101 QPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA-SVMELMSLYLDS-----EMYQVVTGGVPETQE 174
Cdd:cd07130 129 QWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAiAVTKIVARVLEKnglpgAIASLVCGGADVGEA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 175 LLK-QRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCES 253
Cdd:cd07130 209 LVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHE 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 254 SIQDRVIDEIQKCIKEFYTIDPktFED---YGRIINRRHFKRIMALLE-----GSTVAIGGD-CDESECYIAPTVLRdVK 324
Cdd:cd07130 289 SIYDEVLERLKKAYKQVRIGDP--LDDgtlVGPLHTKAAVDNYLAAIEeaksqGGTVLFGGKvIDGPGNYVEPTIVE-GL 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47086741 325 PASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSgallanDC 390
Cdd:cd07130 366 SDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGS------DC 425
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
100-410 |
4.35e-27 |
|
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: 114.21 E-value: 4.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 100 LQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVmeLMSLYLDS----EMYQVVTG-GVPETQE 174
Cdd:cd07125 163 LELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAAR--AVELLHEAgvprDVLQLVPGdGEEIGEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 175 LLKQ-RFDHIFYTGNSTVGKLVMEA---ASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYIL 250
Cdd:cd07125 241 LVAHpRIDGVIFTGSTETAKLINRAlaeRDGPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLY 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 251 CESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALL-----EGSTVAIGGDCDESECYIAPTVLRDVK 324
Cdd:cd07125 321 LQEEIAERFIEMLKGAMASLKVGDPWDLStDVGPLIDKPAGKLLRAHTelmrgEAWLIAPAPLDDGNGYFVAPGIIEIVG 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 325 paSKVMQEEIFGPILPIVTVNG--LKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLSDLPFG 402
Cdd:cd07125 401 --IFDLTTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFG 478
|
....*...
gi 47086741 403 GVGYSGTG 410
Cdd:cd07125 479 GWGLSGTG 486
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
7-411 |
1.95e-26 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 111.97 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALR----KDLYKSANstqlfEILGLEGEINLAVSKLAEwa 82
Cdd:PRK09457 42 AVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIAretgKPLWEAAT-----EVTAMINKIAISIQAYHE-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 83 apRPVNKNLLTISDDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVMelMSLYLDS--- 159
Cdd:PRK09457 115 --RTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELT--VKLWQQAglp 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 160 -EMYQVVTGGVPETQELLKQR-FDHIFYTGNSTVGKLVMEAASHHltP---VTLELGGKSPCYIDKNCDIRIACRRITWG 234
Cdd:PRK09457 191 aGVLNLVQGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 235 KYLNCGQTCIAPDYILCESSIQ-DRVIDEIQKCIKEF----YTIDPKTFedYGRIINRRHFKRIMALlEGSTVAIGGDC- 308
Cdd:PRK09457 269 AFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLtvgrWDAEPQPF--MGAVISEQAAQGLVAA-QAQLLALGGKSl 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 309 ------DESECYIAPTVLrDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSS 382
Cdd:PRK09457 346 lemtqlQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRA 424
|
410 420
....*....|....*....|....*....
gi 47086741 383 GALLANDCMVHFTlSDLPFGGVGYSGTGR 411
Cdd:PRK09457 425 GIVNWNKPLTGAS-SAAPFGGVGASGNHR 452
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
103-410 |
6.77e-25 |
|
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: 107.30 E-value: 6.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 103 EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTA--SVMELMSLYLDSEMYQVVTGGVPETQELLK--Q 178
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAyrAVELMQEAGFPAGTIQLLPGRGADVGAALTsdP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 179 RFDHIFYTGNSTVGKLVMEA-ASHHLTPVTL--ELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESSI 255
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTlAQREDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 256 QDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALLE-----GSTVAIGGDCDESEC----YIAPTV--LRDV 323
Cdd:TIGR01238 319 ADRVLTMIQGAMQELKVGVPHLLTtDVGPVIDAEAKQNLLAHIEhmsqtQKKIAQLTLDDSRACqhgtFVAPTLfeLDDI 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 324 KPaskvMQEEIFGPILPIVTVNG--LKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFTLSDLPF 401
Cdd:TIGR01238 399 AE----LSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPF 474
|
....*....
gi 47086741 402 GGVGYSGTG 410
Cdd:TIGR01238 475 GGQGLSGTG 483
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
99-410 |
7.98e-25 |
|
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: 106.73 E-value: 7.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 99 FLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSevSSHTASVMELMSLyldsemyqVVTGGVPE------- 171
Cdd:cd07148 119 FTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA--LATPLSCLAFVDL--------LHEAGLPEgwcqavp 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 172 ----TQELL--KQRFDHIFYTGNSTVG-KLVMEAASHhlTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCI 244
Cdd:cd07148 189 cenaVAEKLvtDPRVAFFSFIGSARVGwMLRSKLAPG--TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 245 APDYILCESSIQDRVIDEIQKCIKEFYT---IDPKTfeDYGRIINRRHFKRIM-----ALLEGSTVAIGGDCDESECYiA 316
Cdd:cd07148 267 SVQRVFVPAEIADDFAQRLAAAAEKLVVgdpTDPDT--EVGPLIRPREVDRVEewvneAVAAGARLLCGGKRLSDTTY-A 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 317 PTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDcmvH--F 394
Cdd:cd07148 344 PTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND---HtaF 420
|
330
....*....|....*.
gi 47086741 395 TLSDLPFGGVGYSGTG 410
Cdd:cd07148 421 RVDWMPFAGRRQSGYG 436
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
7-356 |
3.82e-24 |
|
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: 104.96 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTQLFEILGLE-GEINLAVSKLAEWAAPR 85
Cdd:TIGR01722 43 AVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDVARGLEvVEHACGVNSLLKGETST 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 86 PVNKNLltisdDVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvMELMSLYLDSEM---- 161
Cdd:TIGR01722 123 QVATRV-----DVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAA--VKLAELFSEAGApdgv 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 162 YQVVTGGVPETQELLKQ-RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCG 240
Cdd:TIGR01722 196 LNVVHGDKEAVDRLLEHpDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 241 QTCIAPDYILCESSIqDRVIDEIQKCIKEFyTIDPKT--FEDYGRIINRRHFKRIMALL-----EGSTVAIGG-----DC 308
Cdd:TIGR01722 276 QRCMAISAAVLVGAA-DEWVPEIRERAEKI-RIGPGDdpGAEMGPLITPQAKDRVASLIaggaaEGAEVLLDGrgykvDG 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 47086741 309 DESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFIND 356
Cdd:TIGR01722 354 YEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINA 401
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
98-418 |
6.54e-23 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 100.97 E-value: 6.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 98 VFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKpsevssHTASVMElMSLYLdSEMYQvvTGGVPET--QEL 175
Cdd:PRK09406 117 AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLK------HASNVPQ-TALYL-ADLFR--RAGFPDGcfQTL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 176 L-----------KQRFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCI 244
Cdd:PRK09406 187 LvgsgaveailrDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCI 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 245 APDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHFKRIMALLE-----GSTVAIGGD-CDESECYIAP 317
Cdd:PRK09406 267 AAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDtDVGPLATEQGRDEVEKQVDdavaaGATILCGGKrPDGPGWFYPP 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 318 TVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANDCMVHFtlS 397
Cdd:PRK09406 347 TVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSY--P 424
|
330 340
....*....|....*....|....
gi 47086741 398 DLPFGGVGYSGTGRY---HGKYSF 418
Cdd:PRK09406 425 ELPFGGVKRSGYGRElsaHGIREF 448
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
104-429 |
9.98e-23 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 101.06 E-value: 9.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 104 PLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVK--PSE------VSSHTASVMELMSLylDSEMYQVVTGGVPETQEL 175
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKgaPTTplitiaMTKLVAEVLEKNNL--PGAIFTSFCGGAEIGEAI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 176 LKQ-RFDHIFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYILCESS 254
Cdd:PLN02315 232 AKDtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHES 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 255 IQDRVIDEIQKCIKEFYTIDPKtfeDYGRIINRRHFKRIMALLE---------GSTVAIGGDCDESEC-YIAPTVLrDVK 324
Cdd:PLN02315 312 IYDDVLEQLLTVYKQVKIGDPL---EKGTLLGPLHTPESKKNFEkgieiiksqGGKILTGGSAIESEGnFVQPTIV-EIS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 325 PASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGALLANdcmvhftlSDLP---- 400
Cdd:PLN02315 388 PDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVN--------VNIPtnga 459
|
330 340 350
....*....|....*....|....*....|....
gi 47086741 401 -----FGGVGYSGTGRYHGKYSFDQVSHLRSCLI 429
Cdd:PLN02315 460 eiggaFGGEKATGGGREAGSDSWKQYMRRSTCTI 493
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
26-410 |
3.94e-22 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 99.06 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 26 RIKQLKNLSRFIKERAADITNALRKDLYKSAN--------STQLFEILGLEGEINLAVSKLAEwAAPRPVN-KNLLTISD 96
Cdd:PLN00412 77 RAELLHKAAAILKEHKAPIAECLVKEIAKPAKdavtevvrSGDLISYTAEEGVRILGEGKFLV-SDSFPGNeRNKYCLTS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 97 DVflqpePLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKP---SEVSS-HTASVMELMSlyLDSEMYQVVTGGVPET 172
Cdd:PLN00412 156 KI-----PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPptqGAVAAlHMVHCFHLAG--FPKGLISCVTGKGSEI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 173 QELLKQR--FDHIFYTGNSTvGKLVMEAAShhLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYIL 250
Cdd:PLN00412 229 GDFLTMHpgVNCISFTGGDT-GIAISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 251 CESSIQDRVIDEIQKCIKEFYTIDPKTFEDYGRIINRRHFKRIMALLEGSTVAIGGDCDE---SECYIAPTVLRDVKPAS 327
Cdd:PLN00412 306 VMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEwkrEGNLIWPLLLDNVRPDM 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 328 KVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSS-KKVIkqMISET-SSGALLANDCMV----HFtlsdlPF 401
Cdd:PLN00412 386 RIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDiNKAI--LISDAmETGTVQINSAPArgpdHF-----PF 458
|
....*....
gi 47086741 402 GGVGYSGTG 410
Cdd:PLN00412 459 QGLKDSGIG 467
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
104-411 |
1.32e-19 |
|
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: 91.15 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 104 PLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKP-SEVSSHTASVMELM--SLYLDSEMYQVVTGGVPETQELLKQ-R 179
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPhTAVSIVMQIMVRLLhyAGLLPPEDVTLINGDGKTMQALLLHpN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 180 FDHIFYTGNSTVGKLVmeAASHHLTPVTLELGGKSPCYIDKNCD-IRIACRRITWGKYLNCGQTCIAPDYILCESSIQDR 258
Cdd:cd07084 180 PKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWSKT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 259 -VIDEIQ----KCIKEFYTIDPKTFEDY-GRIINRRHFKRIMALLEGSTV-AIGGDCDESECyIAPTVLRDVKPA---SK 328
Cdd:cd07084 258 pLVEKLKallaRRKLEDLLLGPVQTFTTlAMIAHMENLLGSVLLFSGKELkNHSIPSIYGAC-VASALFVPIDEIlktYE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 329 VMQEEIFGPILPIVTVNGLKEA--IEFINDREKPLALYVFSSSKKVIKQMISET-SSGALLANDcMVHFTLSDLPFGGVG 405
Cdd:cd07084 337 LVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLwVAGRTYAIL-RGRTGVAPNQNHGGG 415
|
....*.
gi 47086741 406 YSGTGR 411
Cdd:cd07084 416 PAADPR 421
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
112-409 |
3.10e-18 |
|
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: 87.26 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 112 GAWNypiAVTLQPLVG-----------AIAA---------GNAVVVKPSEVSSHTAS-VMELMSLY-LDSEMYQVVTGGV 169
Cdd:cd07123 160 GVWN---RLEYRPLEGfvyavspfnftAIGGnlagapalmGNVVLWKPSDTAVLSNYlVYKILEEAgLPPGVINFVPGDG 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 170 PE-TQELLKQR-FDHIFYTGNSTVGKLVMEAASHHLT-----P-VTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQ 241
Cdd:cd07123 237 PVvGDTVLASPhLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQ 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 242 TCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDPKTFEDY-GRIINRRHFKRIMALLE------GSTVAIGGDCDESECY 314
Cdd:cd07123 317 KCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFmGAVIDEKAFDRIKGYIDhaksdpEAEIIAGGKCDDSVGY 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 315 -IAPTVLRDVKPASKVMQEEIFGPILpivTV-----NGLKEAIEFINDREkPLALY--VFSSSKKVIKQM---------- 376
Cdd:cd07123 397 fVEPTVIETTDPKHKLMTEEIFGPVL---TVyvypdSDFEETLELVDTTS-PYALTgaIFAQDRKAIREAtdalrnaagn 472
|
330 340 350
....*....|....*....|....*....|....*
gi 47086741 377 --ISETSSGALLANDcmvhftlsdlPFGGVGYSGT 409
Cdd:cd07123 473 fyINDKPTGAVVGQQ----------PFGGARASGT 497
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
7-426 |
7.68e-18 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 86.34 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 7 AVQQARKAFLTGRSKSLDYRIKQLKNLSRFIKER----AADITNALRKDLyKSANSTQLFEILGLEGEINLAVSKLAEWa 82
Cdd:PLN02419 156 AVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNmdklAMNITTEQGKTL-KDSHGDIFRGLEVVEHACGMATLQMGEY- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 83 aprpvnknLLTISD--DVFLQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEvSSHTASVMeLMSLYLDSE 160
Cdd:PLN02419 234 --------LPNVSNgvDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSE-KDPGASVI-LAELAMEAG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 161 MYQVVTGGVPETQELLKQRFDH-----IFYTGNSTVGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGK 235
Cdd:PLN02419 304 LPDGVLNIVHGTNDTVNAICDDediraVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 236 YLNCGQTCIAPDYILC---ESSIQDRVIdEIQKCIKEFYTIDPKTfeDYGRIINRRHFKRI------------MALLEGS 300
Cdd:PLN02419 384 FGAAGQRCMALSTVVFvgdAKSWEDKLV-ERAKALKVTCGSEPDA--DLGPVISKQAKERIcrliqsgvddgaKLLLDGR 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 301 TVAIGGDcdESECYIAPTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISET 380
Cdd:PLN02419 461 DIVVPGY--EKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDI 538
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 47086741 381 SSGALLANdCMVHFTLSDLPFGG--VGYSGTGRYHGKYSFDQVSHLRS 426
Cdd:PLN02419 539 EAGQIGIN-VPIPVPLPFFSFTGnkASFAGDLNFYGKAGVDFFTQIKL 585
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
104-410 |
5.73e-13 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 71.54 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 104 PLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVMelMSLYLDSemyqvvtgGVPE-TQELL------ 176
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQA--VRILLEA--------GVPAgVVQLLpgrget 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 177 -------KQRFDHIFYTGNSTVGKLVMEAASHHL------TPVTLELGGKSPCYIDKNC-------DIrIAcrritwGKY 236
Cdd:PRK11809 838 vgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSAlteqvvaDV-LA------SAF 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 237 LNCGQTCIAPDyILC-ESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINR-------RHFKRIMAllEGSTV---AI 304
Cdd:PRK11809 911 DSAGQRCSALR-VLClQDDVADRTLKMLRGAMAECRMGNPDRLStDIGPVIDAeakanieRHIQAMRA--KGRPVfqaAR 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 305 GGDCDESE-CYIAPTV--LRDVKPaskvMQEEIFGPILPIV--TVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISE 379
Cdd:PRK11809 988 ENSEDWQSgTFVPPTLieLDSFDE----LKREVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGS 1063
|
330 340 350
....*....|....*....|....*....|.
gi 47086741 380 TSSGALLANDCMVHFTLSDLPFGGVGYSGTG 410
Cdd:PRK11809 1064 AHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
103-410 |
1.44e-11 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 67.20 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 103 EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSShtasvmeLMSLYLDSEMYQVvtgGVPET--QELL---- 176
Cdd:PRK11905 675 KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTP-------LIAARAVRLLHEA---GVPKDalQLLPgdgr 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 177 --------KQRFDHIFYTGNSTVGKLVMEA-ASHHLTPVTL--ELGGkspcyidKNCDI-------RIACRRITWGKYLN 238
Cdd:PRK11905 745 tvgaalvaDPRIAGVMFTGSTEVARLIQRTlAKRSGPPVPLiaETGG-------QNAMIvdssalpEQVVADVIASAFDS 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 239 CGQTCIAPDyILC-ESSIQDRVIDEIQKCIKEFYTIDP---KTfeDYGRIINRRHFKRIMALLEGST--------VAIGG 306
Cdd:PRK11905 818 AGQRCSALR-VLClQEDVADRVLTMLKGAMDELRIGDPwrlST--DVGPVIDAEAQANIEAHIEAMRaagrlvhqLPLPA 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 307 DCDESEcYIAPTVLRdVKPASkVMQEEIFGPILPIVTV--NGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGA 384
Cdd:PRK11905 895 ETEKGT-FVAPTLIE-IDSIS-DLEREVFGPVLHVVRFkaDELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGN 971
|
330 340
....*....|....*....|....*.
gi 47086741 385 LLANDCMVHFTLSDLPFGGVGYSGTG 410
Cdd:PRK11905 972 IYVNRNIIGAVVGVQPFGGEGLSGTG 997
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
100-410 |
2.87e-08 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 56.36 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 100 LQPEPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTAsvMELMSLYLDSemyqvvtgGVPET------- 172
Cdd:PRK11904 680 LRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIA--AEAVKLLHEA--------GIPKDvlqllpg 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 173 ------QELLKQ-RFDHIFYTGNSTVGKLVMEA-ASHHLTPVTL--ELGGKSPCYIDKN------CD--IRIACRritwg 234
Cdd:PRK11904 750 dgatvgAALTADpRIAGVAFTGSTETARIINRTlAARDGPIVPLiaETGGQNAMIVDSTalpeqvVDdvVTSAFR----- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 235 kylNCGQTCIAPDYILCESSIQDRVIDEIQKCIKEFYTIDP---KTfeDYGRIINRRHFKRIMALLEGST--------VA 303
Cdd:PRK11904 825 ---SAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPrllST--DVGPVIDAEAKANLDAHIERMKrearllaqLP 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 304 IGGDCDESeCYIAPTVLRdvKPASKVMQEEIFGPILPIVTVN--GLKEAIEFINDREKPLALYVFSSSKKVIKQMISETS 381
Cdd:PRK11904 900 LPAGTENG-HFVAPTAFE--IDSISQLEREVFGPILHVIRYKasDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVR 976
|
330 340
....*....|....*....|....*....
gi 47086741 382 SGALLANDCMVHFTLSDLPFGGVGYSGTG 410
Cdd:PRK11904 977 VGNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
103-141 |
5.58e-08 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 55.71 E-value: 5.58e-08
10 20 30
....*....|....*....|....*....|....*....
gi 47086741 103 EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSE 141
Cdd:COG4230 679 RGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAE 717
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
106-389 |
5.97e-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: 54.97 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 106 GVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPSEVSSHTASVMelMSLYLDSEM-----YQVVTGGVPETQELLkQRF 180
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAV--VKDIVESGLlpegaLQLICGSVGDLLDHL-GEQ 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 181 DHIFYTGNSTVG-KL-VMEAASHHLTPVTLELGGKSPCYI--DKNCD-------IRIACRRITwgkyLNCGQTCIAPDYI 249
Cdd:cd07128 223 DVVAFTGSAATAaKLrAHPNIVARSIRFNAEADSLNAAILgpDATPGtpefdlfVKEVAREMT----VKAGQKCTAIRRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 250 LCESSIQDRVIDEIQKCIKEFYTIDPKTFE-DYGRIINRRHF----KRIMALLEGSTVAIGGDCDESE--------CYIA 316
Cdd:cd07128 299 FVPEARVDAVIEALKARLAKVVVGDPRLEGvRMGPLVSREQRedvrAAVATLLAEAEVVFGGPDRFEVvgadaekgAFFP 378
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47086741 317 PTVLRDVKP--ASKVMQEEIFGPILPIVTVNGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSS--GALLAND 389
Cdd:cd07128 379 PTLLLCDDPdaATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPyhGRLLVLN 455
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
104-376 |
7.33e-08 |
|
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: 54.79 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 104 PLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPsevssHTASVME-----------LMSLYLDSEMYQVV--TGGVP 170
Cdd:cd07127 193 PRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKP-----HPAAILPlaitvqvarevLAEAGFDPNLVTLAadTPEEP 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 171 ETQEL-LKQRFDHIFYTGNSTVGKLVMEAASHHLtpVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYI 249
Cdd:cd07127 268 IAQTLaTRPEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 250 LC-ESSIQ--------DRVIDEIQKCIKEFYTIDPKTFEDYGRIINRRHFKRImalleGSTVAIGGDCDESECYI----- 315
Cdd:cd07127 346 YVpRDGIQtddgrksfDEVAADLAAAIDGLLADPARAAALLGAIQSPDTLARI-----AEARQLGEVLLASEAVAhpefp 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47086741 316 -----APTVLRDVKPASKVMQEEIFGPILPIVTVNGLKEAIEFIND--REK-PLALYVFSSSKKVIKQM 376
Cdd:cd07127 421 darvrTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgAMTVGVYSTDPEVVERV 489
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
102-265 |
3.12e-07 |
|
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: 52.49 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 102 PEPLGVVL-IIGAWNyPIAVTLQPLVGAIAAGNAVVVKPS----EVSSHTASVM--ELMSLYLDSEMYQVVTG-GVPETQ 173
Cdd:cd07122 93 AEPVGVIAaLIPSTN-PTSTAIFKALIALKTRNAIIFSPHprakKCSIEAAKIMreAAVAAGAPEGLIQWIEEpSIELTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 174 ELLKQR-FDHIFYTGnstvGKLVMEAASHHLTPVtleLG---GKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDYI 249
Cdd:cd07122 172 ELMKHPdVDLILATG----GPGMVKAAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSV 244
|
170
....*....|....*.
gi 47086741 250 LCESSIQDRVIDEIQK 265
Cdd:cd07122 245 IVDDEIYDEVRAELKR 260
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
11-263 |
2.20e-06 |
|
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: 49.91 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 11 ARKAFLTGRSKSLDYRIKQLKNLSRFIKERAADITNALRKDLYKSANSTqlfeILGLEGEINLAVSKLAEWAA-----PR 85
Cdd:cd07077 3 AKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSL----IANWIAMMGCSESKLYKNIDtergiTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 86 PVNKNLLTISDDVFL---QPEPLGVVLIIGAWNYPIAVTLQPLVGaIAAGNAVVVKPSEVSSHTASVMELMSLYLDS--- 159
Cdd:cd07077 79 SVGHIQDVLLPDNGEtyvRAFPIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALALLFQAADAahg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 160 --EMYQVV-TGGVPETQELLKQ-RFDHIFYTGNSTVGKLVMEAASHhlTPVTLELGGKSPCYIDKNCDIRIACRRITWGK 235
Cdd:cd07077 158 pkILVLYVpHPSDELAEELLSHpKIDLIVATGGRDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASGSVHDSK 235
|
250 260
....*....|....*....|....*...
gi 47086741 236 YLNcGQTCIAPDYILCESSIQDRVIDEI 263
Cdd:cd07077 236 FFD-QNACASEQNLYVVDDVLDPLYEEF 262
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
104-355 |
2.66e-06 |
|
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: 49.85 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 104 PLGVVLIIGAWNYPIAVTLqplVG-----AIAAGNAVVVKPSevSSHTAS---VMELMSLYLD-SEM----YQVVTGGVP 170
Cdd:cd07129 105 PLGPVAVFGASNFPLAFSV---AGgdtasALAAGCPVVVKAH--PAHPGTselVARAIRAALRaTGLpagvFSLLQGGGR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 171 ET-QELLKqrfdH-----IFYTGNSTVGKLVMEAASHHLT--PVTLELGGKSPCYIDKNcdiRIACRRITWGK------Y 236
Cdd:cd07129 180 EVgVALVK----HpaikaVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFILPG---ALAERGEAIAQgfvgslT 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 237 LNCGQTCIAPDYILC-ESSIQDRVIDEIQKCIKEFYT---IDPKTFEDYGRIINRrhfkriMALLEGSTVAIGGDCDESE 312
Cdd:cd07129 253 LGAGQFCTNPGLVLVpAGPAGDAFIAALAEALAAAPAqtmLTPGIAEAYRQGVEA------LAAAPGVRVLAGGAAAEGG 326
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 47086741 313 CYIAPTVLR---DVKPASKVMQEEIFGPILPIVTVNGLKEAIEFIN 355
Cdd:cd07129 327 NQAAPTLFKvdaAAFLADPALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
103-264 |
1.67e-05 |
|
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: 47.26 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 103 EPLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKPsevssHTASvMELMSLYLDSEMYQVVTGGVPE----------- 171
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSP-----HPRA-KKVTQRAATLLLQAAVAAGAPEnligwidnpsi 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 172 --TQELLKQ-RFDHIFYTGnstvGKLVMEAASHHLTPVTLELGGKSPCYIDKNCDIRIACRRITWGKYLNCGQTCIAPDY 248
Cdd:cd07081 168 elAQRLMKFpGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQS 243
|
170
....*....|....*.
gi 47086741 249 ILCESSIQDRVIDEIQ 264
Cdd:cd07081 244 VIVVDSVYDEVMRLFE 259
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
104-387 |
6.30e-05 |
|
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: 45.56 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 104 PLGVVLIIGAWNYPIAVTLQPLVGAIAAGNAVVVKpseVSSHTASVME-LMSLYLD-----SEMYQVVTGGVPETQELLK 177
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLK---VDSKVSVVMEqFLRLLHLcgmpaTDVDLIHSDGPTMNKILLE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 178 QRFDHIFYTGNSTV---------GKLVMEAASHH---LTPVTLELGgkspcYIDKNCDiriacrritWGKYLNCGQTCIA 245
Cdd:cd07126 219 ANPRMTLFTGSSKVaerlalelhGKVKLEDAGFDwkiLGPDVSDVD-----YVAWQCD---------QDAYACSGQKCSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 246 PDYILC-ESSIQDRVIDEIQKCIK----EFYTIDPKTFEDYGRIINrrHFKRIMAlLEGSTVAIGG----DCDESECY-- 314
Cdd:cd07126 285 QSILFAhENWVQAGILDKLKALAEqrklEDLTIGPVLTWTTERILD--HVDKLLA-IPGAKVLFGGkpltNHSIPSIYga 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086741 315 IAPTV----LRDVKPAS--KVMQEEIFGPiLPIVTV---NGLKEAIEFINDREKPLALYVFSSSKKVIKQMISETSSGAL 385
Cdd:cd07126 362 YEPTAvfvpLEEIAIEEnfELVTTEVFGP-FQVVTEykdEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTT 440
|
..
gi 47086741 386 LA 387
Cdd:cd07126 441 YA 442
|
|
| |
