|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
5-430 |
0e+00 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 719.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07087 2 ELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:cd07087 82 RVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd07087 162 VEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 245 APDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDktQGAVLIGGERDRADLYIPPTVL-D 323
Cdd:cd07087 242 APDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLD--DGKVVIGGQVDKEERYIAPTILdD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFG 403
Cdd:cd07087 320 VSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFG 399
|
410 420
....*....|....*....|....*..
gi 32566756 404 GVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07087 400 GVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
5-447 |
0e+00 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 659.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07132 2 EAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:cd07132 82 PVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd07132 162 VLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 245 APDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDKtqGAVLIGGERDRADLYIPPTVL-D 323
Cdd:cd07132 242 APDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSG--GKVAIGGQTDEKERYIAPTVLtD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFG 403
Cdd:cd07132 320 VKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFG 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 32566756 404 GVGVSGMGRYRGKYGFDTFTHEKSVLHRGFFGESLLAARYPPLS 447
Cdd:cd07132 400 GVGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
5-456 |
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: 622.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07136 2 SLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:cd07136 82 RVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd07136 162 VEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 245 APDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDktQGAVLIGGERDRADLYIPPTVLD- 323
Cdd:cd07136 242 APDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLD--NGKIVFGGNTDRETLYIEPTILDn 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFG 403
Cdd:cd07136 320 VTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 32566756 404 GVGVSGMGRYRGKYGFDTFTHEKSVLHRGFFGEslLAARYPPlSQQKLDQMRR 456
Cdd:cd07136 400 GVGNSGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPP-YKGKKKKLKK 449
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
7-459 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 596.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPTHV 86
Cdd:PTZ00381 13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 87 EKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVN 166
Cdd:PTZ00381 93 DTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 167 GGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAP 246
Cdd:PTZ00381 173 GGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 247 DYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDKTQGAVLIGGERDRADLYIPPTVL-DVE 325
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGKVVYGGEVDIENKYVAPTIIvNPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 326 KSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFGGV 405
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 32566756 406 GVSGMGRYRGKYGFDTFTHEKSVLHRGFFGESLLAARYPPLSQQKLDQMRRLTG 459
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSWVLSFLLK 466
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
2-430 |
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: 594.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 2 AFTELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWV 81
Cdd:cd07135 6 EIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 82 KPTHVEKT-FTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESK 160
Cdd:cd07135 86 KDEKVKDGpLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 161 YVTVVNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCG 240
Cdd:cd07135 166 AFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 241 QTCLAPDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDKTQGAVLIGGERDRADLYIPPT 320
Cdd:cd07135 246 QICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTKGKVVIGGEMDEATRFIPPT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 321 -VLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDT 399
Cdd:cd07135 326 iVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDN 405
|
410 420 430
....*....|....*....|....*....|.
gi 32566756 400 LPFGGVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07135 406 APFGGVGDSGYGAYHGKYGFDTFTHERTVVK 436
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
5-429 |
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: 517.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07134 2 RVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:cd07134 82 RVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd07134 162 FEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 245 APDYILVNSTVKPKLVAAIRKYVNEFYGED--VKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGERDRADLYIPP 319
Cdd:cd07134 242 APDYVFVHESVKDAFVEHLKAEIEKFYGKDaaRKASPDLARIVNDRHFDRLKGLLDDAvaKGAkVEFGGQFDAAQRYIAP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 320 TVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVD 398
Cdd:cd07134 322 TVLtNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNP 401
|
410 420 430
....*....|....*....|....*....|.
gi 32566756 399 TLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07134 402 NLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
4-430 |
1.04e-175 |
|
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: 500.47 E-value: 1.04e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 4 TELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDL-RRRHESTEILEIGMTIQEIDYFLKNIDDWVK 82
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 83 PT--HVEKTFTTAldKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESK 160
Cdd:cd07133 81 PSrrHVGLLFLPA--KAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 161 YVTVVNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCG 240
Cdd:cd07133 159 EVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 241 QTCLAPDYILVNSTVKPKLVAAIRKYVNEFYGeDVKASKDYARMINQRHFDRISGLLD--KTQGAVLI----GGERDRAD 314
Cdd:cd07133 239 QTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEdaRAKGARVIelnpAGEDFAAT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 315 LYIPPT-VLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLM 393
Cdd:cd07133 318 RKLPPTlVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLL 397
|
410 420 430
....*....|....*....|....*....|....*..
gi 32566756 394 HITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07133 398 HVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPVFK 434
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
5-429 |
4.42e-171 |
|
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: 488.84 E-value: 4.42e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07137 3 RLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:cd07137 83 KVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNC-GQTC 243
Cdd:cd07137 163 IEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQAC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 244 LAPDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGERDRADLYIPPT- 320
Cdd:cd07137 243 IAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDdpSVADKIVHGGERDEKNLYIEPTi 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 321 VLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTL 400
Cdd:cd07137 323 LLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTL 402
|
410 420
....*....|....*....|....*....
gi 32566756 401 PFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07137 403 PFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
5-457 |
3.53e-152 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 442.63 E-value: 3.53e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:PLN02203 10 GSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMAPK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 85 HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTV 164
Cdd:PLN02203 90 KAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 165 VNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVE---DDADIDISAKRIAWGKWLNC-G 240
Cdd:PLN02203 170 IEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSCaG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 241 QTCLAPDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGERDRADLYIP 318
Cdd:PLN02203 250 QACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKdpRVAASIVHGGSIDEKKLFIE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 319 PTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITV 397
Cdd:PLN02203 330 PTILlNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQYAC 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 398 DTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVLHRGFFGEslLAARYPPLSQQKLDQMRRL 457
Cdd:PLN02203 410 DSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTE--FEFRYPPWNDFKLGFLRLV 467
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
5-429 |
1.12e-135 |
|
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: 398.50 E-value: 1.12e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEIlEIGMTIQEIDYFLKNIDDWVKPT 84
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 85 HVEKTFTTALdkpVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESK-YVT 163
Cdd:cd07078 81 IPSPDPGELA---IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPgVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 164 VVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQ 241
Cdd:cd07078 158 VVTGDGDEVGAALasHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 242 TCLAPDYILVNSTVKPKLVAAIRKYVNEFYGED-VKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRAD--L 315
Cdd:cd07078 238 VCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEdaKAEGAkLLCGGKRLEGGkgY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 316 YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMH 394
Cdd:cd07078 318 FVPPTVLtDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVG 397
|
410 420 430
....*....|....*....|....*....|....*
gi 32566756 395 iTVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07078 398 -AEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
6-462 |
5.96e-127 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 378.23 E-value: 5.96e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 6 LVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPTH 85
Cdd:PLN02174 15 LVTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 86 VEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVV 165
Cdd:PLN02174 95 AKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 166 NGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKW-LNCGQTCL 244
Cdd:PLN02174 175 EGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 245 APDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDKTQGA--VLIGGERDRADLYIPPTV- 321
Cdd:PLN02174 255 SPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEVSdkIVYGGEKDRENLKIAPTIl 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 322 LDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLP 401
Cdd:PLN02174 335 LDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLP 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566756 402 FGGVGVSGMGRYRGKYGFDTFTHEKSVLHRGFFGESllAARYPPLSQQKLDQMRRLTGKRI 462
Cdd:PLN02174 415 FGGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDS--AVRYPPYSRGKLRLLKALVDSNI 473
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
8-429 |
2.63e-111 |
|
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: 333.81 E-value: 2.63e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 8 ETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEIlEIGMTIQEIDYFLKNIDDWVKPTHVE 87
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 88 KTFTTALdkpVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESK-YVTVVN 166
Cdd:cd06534 80 PDPGGEA---YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPgVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 167 GGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd06534 157 GGGDEVGAALlsHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 245 APDYILVNSTVKPKLVAAIRkyvnefygedvkaskdyarminqrhfdrisglldktqgavliggerdradlyippTVL-D 323
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV-------------------------------------------------------TVLvD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHiTVDTLPFG 403
Cdd:cd06534 262 VDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIG-VGPEAPFG 340
|
410 420
....*....|....*....|....*.
gi 32566756 404 GVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd06534 341 GVKNSGIGREGGPYGLEEYTRTKTVV 366
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
7-428 |
1.36e-106 |
|
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: 325.93 E-value: 1.36e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAvwkdlrrrhestEILEIGMTIQE--------IDYF----- 73
Cdd:COG1012 49 VAAARAAFPAWAATPPAERAAILLRAADLLEERREELAAL------------LTLETGKPLAEargevdraADFLryyag 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 74 -LKNIDDWVKPTHVEKTFTtaldkpVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL 152
Cdd:COG1012 117 eARRLYGETIPSDAPGTRA------YVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 153 I-----PKyfesKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADID 225
Cdd:COG1012 191 LeeaglPA----GVLNVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 226 ISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQG 302
Cdd:COG1012 267 AAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIEdaVAEG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 303 A-VLIGGERDRAD--LYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLL 378
Cdd:COG1012 347 AeLLTGGRRPDGEggYFVEPTVLaDVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVA 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 32566756 379 NETSSGGVTVNDVLMHiTVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:COG1012 427 RRLEAGMVWINDGTTG-AVPQAPFGGVKQSGIGREGGREGLEEYTETKTV 475
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
7-428 |
1.58e-96 |
|
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: 299.06 E-value: 1.58e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRR-RHESTEilEIGMTIQEIDYF---LKNIDDWVK 82
Cdd:pfam00171 35 IAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKpLAEARG--EVDRAIDVLRYYaglARRLDGETL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 83 P-THVEKTFTTaldkpvieKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLI-----PKy 156
Cdd:pfam00171 113 PsDPGRLAYTR--------REPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFeeaglPA- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 157 fesKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWG 234
Cdd:pfam00171 184 ---GVLNVVTGSGAEVGEALveHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 235 KWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER 310
Cdd:pfam00171 261 AFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVEdaKEEGAkLLTGGEA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 311 DRAD-LYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTV 388
Cdd:pfam00171 341 GLDNgYFVEPTVLaNVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWI 420
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 32566756 389 NDVLMhITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:pfam00171 421 NDYTT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
18-430 |
3.59e-90 |
|
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: 282.57 E-value: 3.59e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 18 ETKPVKFRKQQLLKLKKFIEENREALSEAVWKDL-RRRHESTeiLEIGMTIQEIDYFLKNIDDWVKPTHVEKTFTTALDK 96
Cdd:cd07099 35 AALGVEGRAQRLLRWKRALADHADELAELLHAETgKPRADAG--LEVLLALEAIDWAARNAPRVLAPRKVPTGLLMPNKK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 97 PVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSEL----SENVAATFEKLIPkyfESKYVTVVNGGIPET 172
Cdd:cd07099 113 ATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVtplvGELLAEAWAAAGP---PQGVLQVVTGDGATG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 173 TDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVN 252
Cdd:cd07099 190 AALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 253 STVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRAD-LYIPPTVL-DVEK 326
Cdd:cd07099 270 ESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRRHVDdaVAKGAkALTGGARSNGGgPFYEPTVLtDVPH 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 327 SDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFGGVG 406
Cdd:cd07099 350 DMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVK 429
|
410 420
....*....|....*....|....
gi 32566756 407 VSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07099 430 DSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
25-429 |
3.98e-76 |
|
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: 246.44 E-value: 3.98e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 25 RKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPTHVEKTFTTALDKPVIEKDPK 104
Cdd:cd07098 42 RRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 105 GVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFES-----KYVTVVNGgIPETTDLLKE- 178
Cdd:cd07098 122 GVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLAAcghdpDLVQLVTC-LPETAEALTSh 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 179 -RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKP 257
Cdd:cd07098 201 pVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 258 KLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLL--DKTQGAVLI-GGER-----DRADLYIPPTVL-DVEKS 327
Cdd:cd07098 281 KLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVadAVEKGARLLaGGKRyphpeYPQGHYFPPTLLvDVTPD 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 328 DPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFGGVGV 407
Cdd:cd07098 361 MKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKG 440
|
410 420
....*....|....*....|..
gi 32566756 408 SGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07098 441 SGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
98-428 |
2.47e-74 |
|
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: 241.57 E-value: 2.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 98 VIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----IPKyfesKYVTVVNGGIPET 172
Cdd:cd07103 112 LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELaeeagLPA----GVLNVVTGSPAEI 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 173 TDLLKERFD--HILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYIL 250
Cdd:cd07103 188 GEALCASPRvrKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIY 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 251 VNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER-DRADLYIPPTVL-DV 324
Cdd:cd07103 268 VHESIYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALVEdaVAKGAkVLTGGKRlGLGGYFYEPTVLtDV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 325 EKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLmhITVDTLPFGG 404
Cdd:cd07103 348 TDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGL--ISDAEAPFGG 425
|
330 340
....*....|....*....|....
gi 32566756 405 VGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07103 426 VKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
25-426 |
8.09e-71 |
|
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: 231.65 E-value: 8.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 25 RKQQLLKLKKFIEENREALseAVWkdLRRRHESTEI---LEIGMTIQEIDY---FLKNIDDWVKPTHVEKTFTTAldkpv 98
Cdd:cd07104 24 RAAILRKAAEILEERRDEI--ADW--LIRESGSTRPkaaFEVGAAIAILREaagLPRRPEGEILPSDVPGKESMV----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 99 iEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATfekLIPKYFE-----SKYVTVVNGGIPETT 173
Cdd:cd07104 95 -RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGL---LIAEIFEeaglpKGVLNVVPGGGSEIG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 174 DLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILV 251
Cdd:cd07104 171 DALVEhpRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 252 NSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGERDraDLYIPPTVL-DVEK 326
Cdd:cd07104 251 HESVYDEFVEKLVAKAKALpVGDPRDPDTVIGPLINERQVDRVHAIVEDAvaAGArLLTGGTYE--GLFYQPTVLsDVTP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 327 SDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlmhiTVD---TLPFG 403
Cdd:cd07104 329 DMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQ----TVNdepHVPFG 404
|
410 420
....*....|....*....|...
gi 32566756 404 GVGVSGMGRYRGKYGFDTFTHEK 426
Cdd:cd07104 405 GVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
25-430 |
1.67e-69 |
|
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: 228.75 E-value: 1.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 25 RKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPTHVE--KTFTTaldkpVIEKD 102
Cdd:cd07092 43 RSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFRFFAGAARTLEGPAAGEylPGHTS-----MIRRE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVNGGIPETTDLL--KERF 180
Cdd:cd07092 118 PIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALvaHPRV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 181 DHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLV 260
Cdd:cd07092 198 RMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 261 AAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDKT-QGA-VLIGGER-DRADLYIPPTVL-DVEKSDPFMHDEI 335
Cdd:cd07092 278 AALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVERApAHArVLTGGRRaEGPGYFYEPTVVaGVAQDDEIVQEEI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 336 FGPVLpiiTVQSFS---ESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlmHITVDT-LPFGGVGVSGMG 411
Cdd:cd07092 358 FGPVV---TVQPFDdedEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPLAAeMPHGGFKQSGYG 431
|
410
....*....|....*....
gi 32566756 412 RYRGKYGFDTFTHEKSVLH 430
Cdd:cd07092 432 KDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
7-428 |
4.80e-69 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 227.83 E-value: 4.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLknidDWVKpTHV 86
Cdd:cd07093 25 VAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIPRAAANFRFFA----DYIL-QLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 87 EKTFTTALD-KPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESKYVTV 164
Cdd:cd07093 100 GESYPQDGGaLNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAgLPPGVVNV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 165 VNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQT 242
Cdd:cd07093 180 VHGFGPEAGAALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 243 CLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRAD---- 314
Cdd:cd07093 260 CLAGSRILVQRSIYDEFLERFVERAKALkVGDPLDPDTEVGPLISKEHLEKVLGYVElaRAEGAtILTGGGRPELPdleg 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 315 -LYIPPTVL-DVEKSDPFMHDEIFGPVLpiiTVQSFSESLEYIA---DGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN 389
Cdd:cd07093 340 gYFVEPTVItGLDNDSRVAQEEIFGPVV---TVIPFDDEEEAIElanDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVN 416
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 32566756 390 DVLMHitvD-TLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07093 417 CWLVR---DlRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
98-428 |
1.02e-68 |
|
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: 226.30 E-value: 1.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 98 VIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELS----ENVAATFEKL-IPKyfesKYVTVVNGG---I 169
Cdd:cd07105 93 MVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSprthWLIGRVFHEAgLPK----GVLNVVTHSpedA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 170 PETTDLLkerFDH-----ILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCL 244
Cdd:cd07105 169 PEVVEAL---IAHpavrkVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICM 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 245 APDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKdyarMINQRHFDRISGLLDKTQ--GAVLIGGERDR---ADLYIPP 319
Cdd:cd07105 246 STERIIVHESIADEFVEKLKAAAEKLFAGPVVLGS----LVSAAAADRVKELVDDALskGAKLVVGGLADespSGTSMPP 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 320 TVLD-VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHitvD 398
Cdd:cd07105 322 TILDnVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVH---D 398
|
330 340 350
....*....|....*....|....*....|..
gi 32566756 399 --TLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07105 399 epTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
7-428 |
1.64e-66 |
|
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: 221.27 E-value: 1.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETK--PVKFRKQQLLKLKKFIEENREALSEavwkdlrrrhesTEILEIGMTIQEI-----------DYF 73
Cdd:cd07114 25 VAAARAAFEGGAWRklTPTERGKLLRRLADLIEANAEELAE------------LETRDNGKLIRETraqvrylaewyRYY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 74 ---LKNIDDWVKPTHVEKTFTTALDKPViekdpkGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFE 150
Cdd:cd07114 93 aglADKIEGAVIPVDKGDYLNFTRREPL------GVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 151 KLIPKY-FESKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDIS 227
Cdd:cd07114 167 KLAEEAgFPPGVVNVVTGFGPETGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 228 AKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA- 303
Cdd:cd07114 247 VNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIrVGDPLDPETQMGPLATERQLEKVERYVAraREEGAr 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 304 VLIGGER-DRADL----YIPPTVL-DVEKSDPFMHDEIFGPVLpiiTVQSFSESLEYIA---DGEKPLAAYIFTRNEAKV 374
Cdd:cd07114 327 VLTGGERpSGADLgagyFFEPTILaDVTNDMRIAQEEVFGPVL---SVIPFDDEEEAIAlanDSEYGLAAGIWTRDLARA 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 32566756 375 KRLLNETSSGGVTVNDvlMHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07114 404 HRVARAIEAGTVWVNT--YRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
101-428 |
3.31e-66 |
|
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: 220.18 E-value: 3.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESKYVTVVNGGIPETTDLLKE- 178
Cdd:cd07109 115 REPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGLGAEAGAALVAh 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 179 -RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKP 257
Cdd:cd07109 195 pGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 258 KLVAAIRKYVNEF---YGEDvkaSKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRADL----YIPPTVLD-VEK 326
Cdd:cd07109 275 EVLERLVERFRALrvgPGLE---DPDLGPLISAKQLDRVEGFVAraRARGArIVAGGRIAEGAPaggyFVAPTLLDdVPP 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 327 SDPFMHDEIFGPVLPIITVQSFSESLEyIADG-EKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDtLPFGGV 405
Cdd:cd07109 352 DSRLAQEEIFGPVLAVMPFDDEAEAIA-LANGtDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAGGGIE-LPFGGV 429
|
330 340
....*....|....*....|...
gi 32566756 406 GVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07109 430 KKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
7-428 |
9.66e-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: 219.44 E-value: 9.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKdlrrrhESTEIL-----EIGMTIQEIDYFLKN---ID 78
Cdd:cd07088 41 VDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVE------EQGKTLslarvEVEFTADYIDYMAEWarrIE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 79 DWVKPTHVEKtfttalDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----I 153
Cdd:cd07088 115 GEIIPSDRPN------ENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELvdeagL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 154 PKyfesKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRI 231
Cdd:cd07088 189 PA----GVLNIVTGRGSVVGDALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 232 AWGKWLNCGQTCLAPDYILVNSTVKP----KLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-V 304
Cdd:cd07088 265 VDSRIINCGQVCTCAERVYVHEDIYDefmeKLVEKMKAVK---VGDPFDAATDMGPLVNEAALDKVEEMVERAveAGAtL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 305 LIGGERDRAD--LYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNET 381
Cdd:cd07088 342 LTGGKRPEGEkgYFYEPTVLtNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNEL 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 32566756 382 SSGGVTVN----DVL--MHitvdtlpfGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07088 422 EFGETYINrenfEAMqgFH--------AGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
7-428 |
6.53e-64 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 214.96 E-value: 6.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETK-PVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFlkniDDWVKPTH 85
Cdd:cd07144 51 VKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYY----AGWADKIQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 86 vEKTFTTALDK-PVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESKYVT 163
Cdd:cd07144 127 -GKTIPTSPNKlAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 164 VVNGGIPETTDLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQ 241
Cdd:cd07144 206 IIPGYGAVAGSALAEHpdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 242 TCLAPDYILVNSTVKPKLVAAIRKYVNEFYGEDVKASKD--YARMINQRHFDRISGLLD--KTQGAVLI-GGERDRADL- 315
Cdd:cd07144 286 NCTATSRIYVQESIYDKFVEKFVEHVKQNYKVGSPFDDDtvVGPQVSKTQYDRVLSYIEkgKKEGAKLVyGGEKAPEGLg 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 316 ---YIPPTV-LDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDV 391
Cdd:cd07144 366 kgyFIPPTIfTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSS 445
|
410 420 430
....*....|....*....|....*....|....*...
gi 32566756 392 LM-HITVdtlPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07144 446 NDsDVGV---PFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
7-428 |
7.19e-64 |
|
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: 214.77 E-value: 7.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGE--TKPVKFRKQQLLKLKKFIEENREALS--EAV--WKDLRrrhESTEIlEIGMTIQEIDYF---LKNI 77
Cdd:cd07091 47 VKAARAAFETGWwrKMDPRERGRLLNKLADLIERDRDELAalESLdnGKPLE---ESAKG-DVALSIKCLRYYagwADKI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 78 DDWVKPTHVEKTFTTaldkpviEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY- 156
Cdd:cd07091 123 QGKTIPIDGNFLAYT-------RREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAg 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 157 FESKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADIDISAKRIAW 233
Cdd:cd07091 196 FPPGVVNIVPGFGPTAGAAISShmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 234 GKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGE 309
Cdd:cd07091 276 GIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIEsgKKEGAtLLTGGE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 310 R-DRADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVT 387
Cdd:cd07091 356 RhGSKGYFIQPTVFtDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVW 435
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 32566756 388 VN--DVLMHitvdTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07091 436 VNtyNVFDA----AVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
7-428 |
2.83e-63 |
|
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: 212.58 E-value: 2.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTG--ETKPVKFRKQQLLKLKKFIEENREALseAVWkdlrrrhestEILEIGMTIQ----EIDYflkNIDDW 80
Cdd:cd07118 25 VAAARKAFDKGpwPRMSGAERAAVLLKVADLIRARRERL--ALI----------ETLESGKPISqargEIEG---AADLW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 81 ------VKPTHVEkTFTTALDK--PVIEKDPKGVVLIISPWNYPVsMILLPMVP-AIAAGNTVVIKPSELSEnvAATF-- 149
Cdd:cd07118 90 ryaaslARTLHGD-SYNNLGDDmlGLVLREPIGVVGIITPWNFPF-LILSQKLPfALAAGCTVVVKPSEFTS--GTTLml 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 150 -EKLIPKYFESKYVTVVNG-----GIPETTDllkERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDAD 223
Cdd:cd07118 166 aELLIEAGLPAGVVNIVTGygatvGQAMTEH---PDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 224 IDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAI----RKYVnefYGEDVKASKDYARMINQRHFDRISGLLD- 298
Cdd:cd07118 243 LDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVvarsRKVR---VGDPLDPETKVGAIINEAQLAKITDYVDa 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 299 -KTQGA-VLIGGERD--RADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAK 373
Cdd:cd07118 320 gRAEGAtLLLGGERLasAAGLFYQPTIFtDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 32566756 374 VKRLLNETSSGGVTVNDVLmhitvDT---LPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07118 400 ALTVARRIRAGTVWVNTFL-----DGspeLPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
17-428 |
1.00e-62 |
|
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: 211.03 E-value: 1.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 17 GETKPVKfRKQQLLKLKKFIEENREALSEAVwkdlrrrhesteILEIGMTIQEIDY-------FLKNIDDWVK------- 82
Cdd:cd07150 38 AATTPSE-RERILLKAAEIMERRADDLIDLL------------IDEGGSTYGKAWFettftpeLLRAAAGECRrvrgetl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 83 PTHVEKTFTTALdkpvieKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----IPKyf 157
Cdd:cd07150 105 PSDSPGTVSMSV------RRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEImeeagLPK-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 158 esKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGK 235
Cdd:cd07150 177 --GVFNVVTGGGAEVGDELvdDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 236 WLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDK--TQGAVLIGGERdR 312
Cdd:cd07150 255 FMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKRQVEDavAKGAKLLTGGK-Y 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 313 ADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDV 391
Cdd:cd07150 334 DGNFYQPTVLtDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDP 413
|
410 420 430
....*....|....*....|....*....|....*....
gi 32566756 392 LMH--ITVdtlPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07150 414 TILdeAHV---PFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
7-428 |
2.13e-62 |
|
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: 210.37 E-value: 2.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYF---LKNIDDWVKP 83
Cdd:cd07115 25 VAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVPRAADTFRYYagwADKIEGEVIP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 84 thVEKTFTTALdkpviEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESKYV 162
Cdd:cd07115 105 --VRGPFLNYT-----VREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 163 TVVNGGIPETTDLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCG 240
Cdd:cd07115 178 NVVTGFGEVAGAALVEHpdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 241 QTCLAPDYILVNSTVKPK----LVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRA 313
Cdd:cd07115 258 QMCTAGSRLLVHESIYDEflerFTSLARSLR---PGDPLDPKTQMGPLVSQAQFDRVLDYVDvgREEGArLLTGGKRPGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 314 D-LYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEyIADG-EKPLAAYIFTRNEAKVKRLLNETSSGGVTVNd 390
Cdd:cd07115 335 RgFFVEPTIFaAVPPEMRIAQEEIFGPVVSVMRFRDEEEALR-IANGtEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN- 412
|
410 420 430
....*....|....*....|....*....|....*....
gi 32566756 391 vlMHITVDT-LPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07115 413 --TYNRFDPgSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
5-428 |
3.22e-62 |
|
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: 209.79 E-value: 3.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAV-WKDLRRRHESTEilEIGMTIQEIDYFLKNIDDWVKP 83
Cdd:cd07102 22 AALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELtWQMGRPIAQAGG--EIRGMLERARYMISIAEEALAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 84 THVEKTfttALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELS----ENVAATF-EKLIPKyfe 158
Cdd:cd07102 100 IRVPEK---DGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTplcgERFAAAFaEAGLPE--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 159 sKYVTVVNGGIPETTDLLKE-RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWL 237
Cdd:cd07102 174 -GVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 238 NCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRA 313
Cdd:cd07102 253 NSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIAdaIAKGArALIDGALFPE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 314 DL----YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTV 388
Cdd:cd07102 333 DKaggaYLAPTVLtNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFM 412
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 32566756 389 N--DVlmhitVD-TLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07102 413 NrcDY-----LDpALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
7-428 |
1.03e-61 |
|
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: 208.61 E-value: 1.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTG---ETKPVKfRKQQLLKLKKFIEENREALseAVWKDLRRRHESTEIL--EIGMTIQEIDYFLKNID--- 78
Cdd:cd07112 30 VAAARRAFESGvwsRLSPAE-RKAVLLRLADLIEAHRDEL--ALLETLDMGKPISDALavDVPSAANTFRWYAEAIDkvy 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 79 DWVKPTHVEktfTTALdkpvIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----I 153
Cdd:cd07112 107 GEVAPTGPD---ALAL----ITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 154 PKyfesKYVTVVNGGIPETTDLLKER--FDHILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDA-DIDISAK 229
Cdd:cd07112 180 PA----GVLNVVPGFGHTAGEALGLHmdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 230 RIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VL 305
Cdd:cd07112 256 AAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKpGDPLDPATRMGALVSEAHFDKVLGYIEsgKAEGArLV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 306 IGGERDRAD---LYIPPTVLD-VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNET 381
Cdd:cd07112 336 AGGKRVLTEtggFFVEPTVFDgVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRL 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 32566756 382 SSGGVTVNdvlmhiTVD----TLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07112 416 RAGTVWVN------CFDegdiTTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
70-428 |
1.29e-61 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 209.16 E-value: 1.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 70 IDYFL---KNIDDWVKPTHVEKTFTTALDKPViekdpkGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVA 146
Cdd:PLN02278 130 LEYFAeeaKRVYGDIIPSPFPDRRLLVLKQPV------GVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 147 ATFEKL-----IPkyfeSKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVE 219
Cdd:PLN02278 204 LAAAELalqagIP----PGVLNVVMGDAPEIGDALlaSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 220 DDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD 298
Cdd:PLN02278 280 DDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVESHVQ 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 299 K--TQGA-VLIGGERDRADL-YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAK 373
Cdd:PLN02278 360 DavSKGAkVLLGGKRHSLGGtFYEPTVLgDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQR 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 32566756 374 VKRLLNETSSGGVTVNDVLmhITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:PLN02278 440 AWRVSEALEYGIVGVNEGL--ISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
99-431 |
1.35e-61 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 208.61 E-value: 1.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 99 IEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVNGGIPETTDLL-- 176
Cdd:PRK13473 134 IRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALvg 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 177 KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVK 256
Cdd:PRK13473 214 HPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 257 PKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDKTQGA----VLIGGER-DRADLYIPPTVL-DVEKSDP 329
Cdd:PRK13473 294 DDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFVERAKALghirVVTGGEApDGKGYYYEPTLLaGARQDDE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 330 FMHDEIFGPVLpiiTVQSFS---ESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlmHIT-VDTLPFGGV 405
Cdd:PRK13473 374 IVQREVFGPVV---SVTPFDdedQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNT---HFMlVSEMPHGGQ 447
|
330 340
....*....|....*....|....*.
gi 32566756 406 GVSGMGRYRGKYGFDTFTHEKSVLHR 431
Cdd:PRK13473 448 KQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
25-428 |
1.59e-61 |
|
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: 207.77 E-value: 1.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 25 RKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEIlEIGMTIQEIDYFLKNIddwVKPTHVEKTFTTaldKPVIEKDPK 104
Cdd:cd07106 43 RRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-EVGGAVAWLRYTASLD---LPDEVIEDDDTR---RVELRRKPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 105 GVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVNGGiPETTDLLKE--RFDH 182
Cdd:cd07106 116 GVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGG-DELGPALTShpDIRK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 183 ILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAA 262
Cdd:cd07106 195 ISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 263 IRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER-DRADLYIPPTVL-DVEKSDPFMHDEIF 336
Cdd:cd07106 275 LVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEdaKAKGAkVLAGGEPlDGPGYFIPPTIVdDPPEGSRIVDEEQF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 337 GPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN---DVLMHItvdtlPFGGVGVSGMGRY 413
Cdd:cd07106 355 GPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINthgALDPDA-----PFGGHKQSGIGVE 429
|
410
....*....|....*
gi 32566756 414 RGKYGFDTFTHEKSV 428
Cdd:cd07106 430 FGIEGLKEYTQTQVI 444
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
14-428 |
1.94e-59 |
|
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: 201.53 E-value: 1.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 14 FRTGETKPVKFRKQQLLKLKKFIEENREALSEAVwkdlrrrhesteILEIGMTI----QEI-------DYFLKNIDDWVK 82
Cdd:cd07100 12 FLAWRKTSFAERAALLRKLADLLRERKDELARLI------------TLEMGKPIaearAEVekcawicRYYAENAEAFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 83 PTHVEktftTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPK--YFESK 160
Cdd:cd07100 80 DEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREagFPEGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 161 YVTVVNGGiPETTDLLK-ERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNC 239
Cdd:cd07100 156 FQNLLIDS-DQVEAIIAdPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 240 GQTCLAPDYILVNSTV----KPKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGER-D 311
Cdd:cd07100 235 GQSCIAAKRFIVHEDVydefLEKFVEAMAALK---VGDPMDEDTDLGPLARKDLRDELHEQVEEAvaAGAtLLLGGKRpD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 312 RADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEyIA-DGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN 389
Cdd:cd07100 312 GPGAFYPPTVLtDVTPGMPAYDEELFGPVAAVIKVKDEEEAIA-LAnDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 32566756 390 DvlmHITVDT-LPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07100 391 G---MVKSDPrLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
7-428 |
4.18e-59 |
|
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: 202.19 E-value: 4.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRrhestEILEIGMTIQEIdyflknID--DWVKPT 84
Cdd:cd07131 43 VEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGK-----PLAEGRGDVQEA------IDmaQYAAGE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 85 hVEKTFTTALDKPVIEKD------PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATF-EKLIPKYF 157
Cdd:cd07131 112 -GRRLFGETVPSELPNKDamtrrqPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLvELFAEAGL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 158 ESKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGK 235
Cdd:cd07131 191 PPGVVNVVHGRGEEVGEALVEhpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 236 WLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER- 310
Cdd:cd07131 271 FGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLNYNEigKEEGAtLLLGGERl 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 311 DRADL----YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGG 385
Cdd:cd07131 351 TGGGYekgyFVEPTVFtDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGI 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 32566756 386 VTVNDVLMHITVDtLPFGGVGVSGMG-RYRGKYGFDTFTHEKSV 428
Cdd:cd07131 431 TYVNAPTIGAEVH-LPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
21-428 |
9.30e-59 |
|
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: 9.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 21 PVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPTHV-EKTFTTALDKPVI 99
Cdd:cd07089 40 DAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSFPWEFDLpVPALRGGPGRRVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 100 EKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPS--------ELSENVAATFeklIPKyfesKYVTVVNGGIPE 171
Cdd:cd07089 120 RREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPApdtplsalLLGEIIAETD---LPA----GVVNVVTGSDNA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 172 TTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYI 249
Cdd:cd07089 193 VGEALTTdpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 250 LVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER-DRAD--LYIPPTVL 322
Cdd:cd07089 273 LVPRSRYDEVVEALAAAFEALpVGDPADPGTVMGPLISAAQRDRVEGYIArgRDEGArLVTGGGRpAGLDkgFYVEPTLF 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 323 -DVEKSDPFMHDEIFGPVLPIITVQSFSESLEyIA-DGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlMHITVDTl 400
Cdd:cd07089 353 aDVDNDMRIAQEEIFGPVLVVIPYDDDDEAVR-IAnDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGG-GGYGPDA- 429
|
410 420
....*....|....*....|....*...
gi 32566756 401 PFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07089 430 PFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
25-430 |
1.60e-58 |
|
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: 200.22 E-value: 1.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 25 RKQQLLKLKKFIEENREALSEAvwkdLRRRHESTEI---LEIGMT---IQEIDYFLKNIDDWVKPTHVEktfttalDKP- 97
Cdd:cd07151 56 RAEILEKAAQILEERRDEIVEW----LIRESGSTRIkanIEWGAAmaiTREAATFPLRMEGRILPSDVP-------GKEn 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 98 VIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSElseNVAATFEKLIPKYFESK-----YVTVVNGGIPET 172
Cdd:cd07151 125 RVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPAS---DTPITGGLLLAKIFEEAglpkgVLNVVVGAGSEI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 173 TDLLKE----RFdhILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDY 248
Cdd:cd07151 202 GDAFVEhpvpRL--ISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 249 ILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGERDraDLYIPPTVL-D 323
Cdd:cd07151 280 IIVHEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIEQAveEGAtLLVGGEAE--GNVLEPTVLsD 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlmhITVD---TL 400
Cdd:cd07151 358 VTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIND----QPVNdepHV 433
|
410 420 430
....*....|....*....|....*....|..
gi 32566756 401 PFGGVGVSGMGRYRGKYGFDTFTHEK--SVLH 430
Cdd:cd07151 434 PFGGEKNSGLGRFNGEWALEEFTTDKwiSVQH 465
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
11-430 |
1.21e-57 |
|
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: 198.30 E-value: 1.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 11 RKYFRTGE--TKPVKFRKQQLLKLKKFIEENREALSEavwkdlrrrhesTEILEIGMTIQEIDYflkNIDDWVkptHVEK 88
Cdd:cd07119 45 RRAFDSGEwpHLPAQERAALLFRIADKIREDAEELAR------------LETLNTGKTLRESEI---DIDDVA---NCFR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 89 TFTTALDKP-------------VIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPK 155
Cdd:cd07119 107 YYAGLATKEtgevydvpphvisRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 156 Y-FESKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIA 232
Cdd:cd07119 187 AgLPAGVVNLVTGSGATVGAELAEspDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQAL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 233 WGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLI-GG 308
Cdd:cd07119 267 NGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIkLGNGLDADTEMGPLVSAEHREKVLSYIQlgKEEGARLVcGG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 309 ER-DRADL----YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETS 382
Cdd:cd07119 347 KRpTGDELakgyFVEPTIFdDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLR 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 32566756 383 SGGVTVNDvlMHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07119 427 AGTVWIND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHINI 472
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
2-430 |
1.33e-57 |
|
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: 197.53 E-value: 1.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 2 AFTELVETQRKYFRTgetkPVKFRKQQLLKLKKFIEENREALSeavwkDL-------RRRHESTEILEIGMTIQeidYFL 74
Cdd:cd07101 23 AFARARAAQRAWAAR----PFAERAAVFLRFHDLVLERRDELL-----DLiqletgkARRHAFEEVLDVAIVAR---YYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 75 KNIDDWVKPTHVEKTFTTaLDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVA-ATFEKLI 153
Cdd:cd07101 91 RRAERLLKPRRRRGAIPV-LTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTAlWAVELLI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 154 PKYFESKYVTVVNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAW 233
Cdd:cd07101 170 EAGLPRDLWQVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 234 GKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGER 310
Cdd:cd07101 250 ACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVDdaVAKGATVLAGGR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 311 DRADL---YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGV 386
Cdd:cd07101 330 ARPDLgpyFYEPTVLtGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTV 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 32566756 387 TVND--VLMHITVDTlPFGGVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07101 410 NVNEgyAAAWASIDA-PMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
103-424 |
2.19e-57 |
|
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: 196.75 E-value: 2.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSenvAATFEKLIPKYFE-----SKYVTVVNGGiPETTDLLK 177
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRT---PVSGGVVIARLFEeaglpAGVLHVLPGG-ADAGEALV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 178 E--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTV 255
Cdd:cd07152 186 EdpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 256 KPKLVAA-IRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLDKTQGA---VLIGGERDraDLYIPPTVL-DVEKSDPF 330
Cdd:cd07152 266 ADAYTAKlAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAgarLEAGGTYD--GLFYRPTVLsGVKPGMPA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 331 MHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlmhiTVD---TLPFGGVGV 407
Cdd:cd07152 344 FDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVNdepHNPFGGMGA 419
|
330
....*....|....*...
gi 32566756 408 SGMG-RYRGKYGFDTFTH 424
Cdd:cd07152 420 SGNGsRFGGPANWEEFTQ 437
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
38-430 |
5.35e-57 |
|
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: 196.18 E-value: 5.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 38 ENREALSEAVWKDLRRRHE---STEILEIG------------MTIQEIDYFLKNIDDWvkpthvekTFTTALDKPVIEKD 102
Cdd:cd07138 58 EERAALLERIAEAYEARADelaQAITLEMGapitlaraaqvgLGIGHLRAAADALKDF--------EFEERRGNSLVVRE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLI-----PK-YFeskyvTVVNGGIPETTDLL 176
Cdd:cd07138 130 PIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILdeaglPAgVF-----NLVNGDGPVVGEAL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 177 KE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNST 254
Cdd:cd07138 205 SAhpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 255 VKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDK--TQGAVLIGGERDRAD-----LYIPPTVL-DVe 325
Cdd:cd07138 285 RYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIQKgiEEGARLVAGGPGRPEglergYFVKPTVFaDV- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 326 ksDPFM---HDEIFGPVLPIITVQSFSESLEyIA-DGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHItvdTLP 401
Cdd:cd07138 364 --TPDMtiaREEIFGPVLSIIPYDDEDEAIA-IAnDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP---GAP 437
|
410 420
....*....|....*....|....*....
gi 32566756 402 FGGVGVSGMGRYRGKYGFDTFTHEKSVLH 430
Cdd:cd07138 438 FGGYKQSGNGREWGRYGLEEFLEVKSIQG 466
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
7-428 |
1.06e-56 |
|
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: 195.83 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTgeTKPVKF----RKQQLLKLKKFIEENREALSeavwkdlrrrheSTEILEIGMTIQEIDYF--------L 74
Cdd:cd07143 50 VEVAHAAFET--DWGLKVsgskRGRCLSKLADLMERNLDYLA------------SIEALDNGKTFGTAKRVdvqasadtF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 75 KNIDDWVKPTH------VEKTFTTALDKPViekdpkGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAAT 148
Cdd:cd07143 116 RYYGGWADKIHgqvietDIKKLTYTRHEPI------GVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 149 FEKLIPKY-FESKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADI 224
Cdd:cd07143 190 MTKLIPEAgFPPGVINVVSGYGRTCGNAISShmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 225 DISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQ 301
Cdd:cd07143 270 ESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLkVGDPFAEDTFQGPQVSQIQYERIMSYIEsgKAE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 302 GA-VLIGGERDRADLY-IPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLL 378
Cdd:cd07143 350 GAtVETGGKRHGNEGYfIEPTIFtDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVA 429
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 32566756 379 NETSSGGVTVNDV-LMHITVdtlPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07143 430 NALKAGTVWVNCYnLLHHQV---PFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
5-426 |
1.16e-54 |
|
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: 189.87 E-value: 1.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEIlEIGMTIQEIDYF---LKNIDDWV 81
Cdd:cd07145 25 EAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV-EVERTIRLFKLAaeeAKVLRGET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 82 KPthVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESK 160
Cdd:cd07145 104 IP--VDAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 161 YVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLN 238
Cdd:cd07145 182 VINVVTGYGSEVGDEIvtNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFEN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 239 CGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDK--TQGA-VLIGGERDRAD 314
Cdd:cd07145 262 AGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVNDavEKGGkILYGGKRDEGS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 315 lYIPPTVLDVEKSD-PFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlM 393
Cdd:cd07145 342 -FFPPTVLENDTPDmIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDS-T 419
|
410 420 430
....*....|....*....|....*....|...
gi 32566756 394 HITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEK 426
Cdd:cd07145 420 RFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEK 452
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
101-428 |
9.16e-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: 187.42 E-value: 9.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATF-EKLIPKYFESKYVTVVNGGIPETTDLLKE- 178
Cdd:cd07149 121 REPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLaELLLEAGLPKGALNVVTGSGETVGDALVTd 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 179 -RFDHILYTGCPPVAKIIMTAAAkhLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVK- 256
Cdd:cd07149 201 pRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYd 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 257 ---PKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRAdlYIPPTVL-DVEKSDP 329
Cdd:cd07149 279 eflERFVAATKKLV---VGDPLDEDTDVGPMISEAEAERIEEWVEeaVEGGArLLTGGKRDGA--ILEPTVLtDVPPDMK 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 330 FMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlMHITVDTLPFGGVGVSG 409
Cdd:cd07149 354 VVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDS-STFRVDHMPYGGVKESG 432
|
330
....*....|....*....
gi 32566756 410 MGRYRGKYGFDTFTHEKSV 428
Cdd:cd07149 433 TGREGPRYAIEEMTEIKLV 451
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
29-389 |
1.34e-53 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 185.71 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 29 LLKLKKFIEENREALSEAVWKDLRRRHESTEIlEIGMTIQEIDYflknIDDWVKPTHVEktfTTALDKP----VIEKDPK 104
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEV-EVAFTADYIDY----MAEWARRYEGE---IIQSDRPgeniLLFKRAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 105 GVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYV-TVVNGGIPETTDLL--KERFD 181
Cdd:PRK10090 73 GVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVfNLVLGRGETVGQELagNPKVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 182 HILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVA 261
Cdd:PRK10090 153 MVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 262 AIRKYVNEF-YGEDVKASK-DYARMINQRHFDRISGLLDKT--QGA-VLIGGERDRAD-LYIPPTVL-DVEKSDPFMHDE 334
Cdd:PRK10090 233 RLGEAMQAVqFGNPAERNDiAMGPLINAAALERVEQKVARAveEGArVALGGKAVEGKgYYYPPTLLlDVRQEMSIMHEE 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 32566756 335 IFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN 389
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
5-428 |
1.46e-53 |
|
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: 186.87 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 5 ELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAV-------WKDLRRrhestEILEIGMTIQEIDYFLKNI 77
Cdd:cd07094 25 EALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIaceggkpIKDARV-----EVDRAIDTLRLAAEEAERI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 78 DDWVKPTHVEKTFTTALdkPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLI-PKY 156
Cdd:cd07094 100 RGEEIPLDATQGSDNRL--AWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 157 FESKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKhlTPVTLELGGKCPVVVEDDADIDISAKRIAWG 234
Cdd:cd07094 178 VPEGVLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 235 KWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDK--TQGAVLI-GGER 310
Cdd:cd07094 256 GFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLkVGDPLDEDTDVGPLISEEAAERVERWVEEavEAGARLLcGGER 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 311 DRADLYipPTVLDVEKSDPFM-HDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN 389
Cdd:cd07094 336 DGALFK--PTVLEDVPRDTKLsTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVN 413
|
410 420 430
....*....|....*....|....*....|....*....
gi 32566756 390 DVlMHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07094 414 DS-SAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
99-428 |
2.37e-53 |
|
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: 186.30 E-value: 2.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 99 IEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATF-EKLIPKYFESKYVTVVNGGIPETTDLLK 177
Cdd:cd07147 119 VRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILgEVLAETGLPKGAFSVLPCSRDDADLLVT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 178 -ERFDHILYTGCPPVAKIIMTAAAKHltPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTV- 255
Cdd:cd07147 199 dERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVy 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 256 ---KPKLVAAIRKYVNefyGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGERDRADLYipPTVL-DVEKSD 328
Cdd:cd07147 277 defKSRLVARVKALKT---GDPKDDATDVGPMISESEAERVEGWVNEAvdAGAkLLTGGKRDGALLE--PTILeDVPPDM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 329 PFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlMHITVDTLPFGGVGVS 408
Cdd:cd07147 352 EVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDV-PTFRVDHMPYGGVKDS 430
|
330 340
....*....|....*....|
gi 32566756 409 GMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07147 431 GIGREGVRYAIEEMTEPRLL 450
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
101-428 |
2.45e-53 |
|
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: 186.69 E-value: 2.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLI-----PKyfeskyvTVVN---GGIPET 172
Cdd:cd07097 133 REPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILeeaglPA-------GVFNlvmGSGSEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 173 TDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYIL 250
Cdd:cd07097 206 GQALVEhpDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 251 VNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLI-GGER-DRAD--LYIPPTVL- 322
Cdd:cd07097 286 VTEGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIEiaRSEGAKLVyGGERlKRPDegYYLAPALFa 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 323 DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN----DVLMHitvd 398
Cdd:cd07097 366 GVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlptaGVDYH---- 441
|
330 340 350
....*....|....*....|....*....|.
gi 32566756 399 tLPFGGVGVSGMG-RYRGKYGFDTFTHEKSV 428
Cdd:cd07097 442 -VPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
40-429 |
2.74e-53 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 186.24 E-value: 2.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 40 REALSEAVWKDL-----------------RRRHESTEI--LEIGMTI------------QEIDYFLKNIDDWVKPTHVEk 88
Cdd:cd07139 46 RRAFDNGPWPRLspaeraavlrrladaleARADELARLwtAENGMPIswsrraqgpgpaALLRYYAALARDFPFEERRP- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 89 tfTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSE--------LSENVAatfEKLIPKyfesK 160
Cdd:cd07139 125 --GSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPetpldaylLAEAAE---EAGLPP----G 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 161 YVTVVNGGIpETTDLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLN 238
Cdd:cd07139 196 VVNVVPADR-EVGEYLVRHpgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 239 CGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDK--TQGAVLI-GGERdRAD 314
Cdd:cd07139 275 NGQVCVALTRILVPRSRYDEVVEALAAAVAALkVGDPLDPATQIGPLASARQRERVEGYIAKgrAEGARLVtGGGR-PAG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 315 L----YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEyIA-DGEKPLAAYIFTRNEAKVKRLLNETSSGGVTV 388
Cdd:cd07139 354 LdrgwFVEPTLFaDVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR-IAnDSDYGLSGSVWTADVERGLAVARRIRTGTVGV 432
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 32566756 389 NdvlmHITVD-TLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07139 433 N----GFRLDfGAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
7-431 |
1.42e-52 |
|
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: 184.57 E-value: 1.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRT--GETKPVKfRKQQLLKLKKFIEENREALSEavwkdlrrrhesTEILEIGMTIQ-----EIDY---FLKN 76
Cdd:cd07113 43 VASAWRAFVSawAKTTPAE-RGRILLRLADLIEQHGEELAQ------------LETLCSGKSIHlsrafEVGQsanFLRY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 77 IDDWVkpTHVE-KTFTTALDKPVIE-------KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSE----N 144
Cdd:cd07113 110 FAGWA--TKINgETLAPSIPSMQGErytaftrREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPltllR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 145 VA--ATfEKLIPkyfeSKYVTVVNGgipeTTDLLKERFDH-----ILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVV 217
Cdd:cd07113 188 VAelAK-EAGIP----DGVLNVVNG----KGAVGAQLISHpdvakVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 218 VEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGL 296
Cdd:cd07113 259 FLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 297 LDKTQGA---VLIGGER-DRADLYIPPT-VLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNE 371
Cdd:cd07113 339 LDDARAEgdeIVRGGEAlAGEGYFVQPTlVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNL 418
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566756 372 AKVKRLLNETSSGGVTVNdvlMHITVD-TLPFGGVGVSGMGRYRGKYGFDTFTHEKSVLHR 431
Cdd:cd07113 419 SKALRYIPRIEAGTVWVN---MHTFLDpAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
7-429 |
2.29e-52 |
|
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: 184.08 E-value: 2.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRT-GETKPVKfRKQQLLKLKKFIEENREALSEA-VW---KDLRrrhESTEIlEIGMTIQEIDYF-------- 73
Cdd:cd07559 44 VDAAHEAFKTwGKTSVAE-RANILNKIADRIEENLELLAVAeTLdngKPIR---ETLAA-DIPLAIDHFRYFagviraqe 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 74 --LKNIDdwvkpthvEKTFTTALDKPViekdpkGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSE----NVAA 147
Cdd:cd07559 119 gsLSEID--------EDTLSYHFHEPL------GVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPlsilVLME 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 148 TFEKLIPKyfesKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDA--- 222
Cdd:cd07559 185 LIGDLLPK----GVVNVVTGFGSEAGKPLAShpRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFFDDAmda 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 223 --DIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVA-AIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD- 298
Cdd:cd07559 261 ddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIErAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDi 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 299 -KTQGA-VLIGGER------DRADLYIPPTVLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRN 370
Cdd:cd07559 341 gKEEGAeVLTGGERltlgglDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRD 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 32566756 371 EAKVKRLLNETSSGGVTVNdvLMHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07559 421 INRALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNIL 477
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
9-428 |
2.64e-52 |
|
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: 183.31 E-value: 2.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 9 TQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVwkdlrrRHESTEIL-----EIGMTIQEIDYFLKNIddwvkp 83
Cdd:cd07120 28 ARRAFDETDWAHDPRLRARVLLELADAFEANAERLARLL------ALENGKILgearfEISGAISELRYYAGLA------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 84 thvEKTFTTALD-KP----VIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIP--KY 156
Cdd:cd07120 96 ---RTEAGRMIEpEPgsfsLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAeiPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 157 FESKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWG 234
Cdd:cd07120 173 LPAGVVNLFTESGSEGAAHLVAspDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 235 KWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVnefygEDVK------ASKDYARMINQRHFDRISGLLDK--TQGA--V 304
Cdd:cd07120 253 LTIFAGQFCMAGSRVLVQRSIADEVRDRLAARL-----AAVKvgpgldPASDMGPLIDRANVDRVDRMVERaiAAGAevV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 305 LIGG---ERDRADLYIPPTVLDVEKSD-PFMHDEIFGPVLpiiTVQSFSESLEYIA---DGEKPLAAYIFTRNEAKVKRL 377
Cdd:cd07120 328 LRGGpvtEGLAKGAFLRPTLLEVDDPDaDIVQEEIFGPVL---TLETFDDEAEAVAlanDTDYGLAASVWTRDLARAMRV 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 32566756 378 LNETSSGGVTVNDvlmHITV-DTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07120 405 ARAIRAGTVWIND---WNKLfAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
7-429 |
4.45e-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: 182.94 E-value: 4.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDL-RRRHESTeiLEIGMTIQEIDYFLKNIDDWvkPTH 85
Cdd:cd07110 25 VRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNgKPLDEAA--WDVDDVAGCFEYYADLAEQL--DAK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 86 VEKTFTTALD--KPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSE---LSENVAATF--EKLIPKyfe 158
Cdd:cd07110 101 AERAVPLPSEdfKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEltsLTELELAEIaaEAGLPP--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 159 sKYVTVVNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKW 236
Cdd:cd07110 178 -GVLNVVTGTGDEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 237 LNCGQTCLAPDYILVNSTVK----PKLVAAIRKY-VNEFYGEDVkaskDYARMINQRHFDRISGLLD--KTQGAVLIGGE 309
Cdd:cd07110 257 WNNGQICSATSRLLVHESIAdaflERLATAAEAIrVGDPLEEGV----RLGPLVSQAQYEKVLSFIArgKEEGARLLCGG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 310 RDRADL----YIPPTVL-DVEKSDPFMHDEIFGPVLpiiTVQSFSESLEYIA---DGEKPLAAYIFTRNEAKVKRLLNET 381
Cdd:cd07110 333 RRPAHLekgyFIAPTVFaDVPTDSRIWREEIFGPVL---CVRSFATEDEAIAlanDSEYGLAAAVISRDAERCDRVAEAL 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 32566756 382 SSGGVTVNDVlmHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07110 410 EAGIVWINCS--QPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
101-429 |
5.22e-52 |
|
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: 182.56 E-value: 5.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSE----NVAATFEKLIPkyfeSKYVTVVNGGIPETTDLL 176
Cdd:cd07108 115 REPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPlavlLLAEILAQVLP----AGVLNVITGYGEECGAAL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 177 KER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKR-IAWGKWLNCGQTCLAPDYILVNS 253
Cdd:cd07108 191 VDHpdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGaIAGMRFTRQGQSCTAGSRLFVHE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 254 TVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD---KTQGA-VLIGGE-----RDRADLYIPPTVL- 322
Cdd:cd07108 271 DIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDlglSTSGAtVLRGGPlpgegPLADGFFVQPTIFs 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 323 DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlMHITVDTLPF 402
Cdd:cd07108 351 GVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQ--GGGQQPGQSY 428
|
330 340
....*....|....*....|....*...
gi 32566756 403 GGVGVSGMGRYRGKYG-FDTFTHEKSVL 429
Cdd:cd07108 429 GGFKQSGLGREASLEGmLEHFTQKKTVN 456
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
2-428 |
6.46e-52 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 183.93 E-value: 6.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 2 AFTELVETQRKYFRTgetkPVKFRKQQLLKLKKFIEENREALSeavwkDL-------RRRHESTEILEIGMTIqeiDYFL 74
Cdd:PRK09407 59 AFARARAAQRAWAAT----PVRERAAVLLRFHDLVLENREELL-----DLvqletgkARRHAFEEVLDVALTA---RYYA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 75 KNIDDWVKPTHVEKTFTTaLDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKP-SELSENVAATFEKLI 153
Cdd:PRK09407 127 RRAPKLLAPRRRAGALPV-LTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPdSQTPLTALAAVELLY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 154 PKYFESKYVTVVNGGIPETTDLLKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAW 233
Cdd:PRK09407 206 EAGLPRDLWQVVTGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 234 GKWLNCGQTCLAPDYILVNSTVKPKLVaaiRKYVNEFYGEDVKASKDY-ARM---INQRHFDRISGLLD--KTQGA-VLI 306
Cdd:PRK09407 286 ACFSNAGQLCISIERIYVHESIYDEFV---RAFVAAVRAMRLGAGYDYsADMgslISEAQLETVSAHVDdaVAKGAtVLA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 307 GGeRDRADL---YIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETS 382
Cdd:PRK09407 363 GG-KARPDLgplFYEPTVLtGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIR 441
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 32566756 383 SGGVTVND--VLMHITVDTlPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:PRK09407 442 AGTVNVNEgyAAAWGSVDA-PMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
96-428 |
2.43e-51 |
|
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: 180.63 E-value: 2.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 96 KPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIpkyFES----KYVTVVNGGIPE 171
Cdd:cd07146 113 KIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLL---YEAglppDMLSVVTGEPGE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 172 TTDLL--KERFDHILYTGCPPVAKIIM-TAAAKHLTpvtLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDY 248
Cdd:cd07146 190 IGDELitHPDVDLVTFTGGVAVGKAIAaTAGYKRQL---LELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKR 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 249 ILVNSTV----KPKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGERDRADLYipPTV 321
Cdd:cd07146 267 ILVHESVadefVDLLVEKSAALV---VGDPMDPATDMGTVIDEEAAIQIENRVEEAiaQGArVLLGNQRQGALYA--PTV 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 322 LD-VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlMHITVDTL 400
Cdd:cd07146 342 LDhVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEV-PGFRSELS 420
|
330 340
....*....|....*....|....*....
gi 32566756 401 PFGGVGVSGMGRYRG-KYGFDTFTHEKSV 428
Cdd:cd07146 421 PFGGVKDSGLGGKEGvREAMKEMTNVKTY 449
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
101-428 |
1.42e-50 |
|
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: 179.47 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESKYVTVVNGGIPETTDLLKER 179
Cdd:cd07141 143 HEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSH 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 180 --FDHILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVK 256
Cdd:cd07141 223 pdIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 257 PKLVA-AIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVL-IGGER--DRAdLYIPPTVL-DVEKSDP 329
Cdd:cd07141 303 DEFVKrSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIEsgKKEGAKLeCGGKRhgDKG-YFIQPTVFsDVTDDMR 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 330 FMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNdVLMHITVDTlPFGGVGVSG 409
Cdd:cd07141 382 IAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN-CYNVVSPQA-PFGGYKMSG 459
|
330
....*....|....*....
gi 32566756 410 MGRYRGKYGFDTFTHEKSV 428
Cdd:cd07141 460 NGRELGEYGLQEYTEVKTV 478
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
7-429 |
4.65e-50 |
|
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: 178.03 E-value: 4.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIddwvkptHV 86
Cdd:cd07117 44 VKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVI-------RA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 87 EKTFTTALDK---PVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSE----NVAATFEKLIPKyfes 159
Cdd:cd07117 117 EEGSANMIDEdtlSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSlsllELAKIIQDVLPK---- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 160 KYVTVVNGGIPETTDLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWL 237
Cdd:cd07117 193 GVVNIVTGKGSKSGEYLLNHpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 238 NCGQTCLAPDYILVNSTVKPKLVAA-IRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER--- 310
Cdd:cd07117 273 NQGQVCCAGSRIFVQEGIYDEFVAKlKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDiaKEEGAkILTGGHRlte 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 311 DRAD--LYIPPTVLDVEKSD-PFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVT 387
Cdd:cd07117 353 NGLDkgFFIEPTLIVNVTNDmRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVW 432
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 32566756 388 VNdvLMHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07117 433 VN--TYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIY 472
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
7-429 |
5.27e-50 |
|
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: 177.69 E-value: 5.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGE--TKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLknidDWVKPT 84
Cdd:cd07142 47 VKAARKAFDEGPwpRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQARYAEVPLAARLFRYYA----GWADKI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 85 HVEktfTTALDKPVIE---KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKY-FESK 160
Cdd:cd07142 123 HGM---TLPADGPHHVytlHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 161 YVTVVNGGIPETTDLLKERF--DHILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWL 237
Cdd:cd07142 200 VLNIVTGFGPTAGAAIASHMdvDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 238 NCGQTCLAPDYILVNSTVKPKLV-AAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLI-GGER-DR 312
Cdd:cd07142 280 NQGQCCCAGSRTFVHESIYDEFVeKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEhgKEEGATLItGGDRiGS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 313 ADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN-- 389
Cdd:cd07142 360 KGYYIQPTIFsDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcy 439
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 32566756 390 DVLmhitVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07142 440 DVF----DASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
25-426 |
1.71e-48 |
|
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: 173.46 E-value: 1.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 25 RKQQLLKLKKFIEENREALSEavwkdlrrrhesTEILEIGMTIQEIDYflKNIDDWVKPTHVEKTFTTALDKPVIE---- 100
Cdd:TIGR01804 59 RGRILRRAADLIRERNEELAK------------LETLDTGKTLQETIV--ADMDSGADVFEFFAGLAPALNGEIIPlggp 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 101 ------KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVA-ATFEKLIPKYFESKYVTVVNGGIPETT 173
Cdd:TIGR01804 125 sfaytiREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTAlKVAEIMEEAGLPKGVFNVVQGDGAEVG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 174 DLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILV 251
Cdd:TIGR01804 205 PLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 252 NSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRAD-----LYIPPTVL 322
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIEkgKAEGAtLATGGGRPENVglqngFFVEPTVF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 323 -DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlMHITVDTLP 401
Cdd:TIGR01804 365 aDCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEAP 442
|
410 420
....*....|....*....|....*
gi 32566756 402 FGGVGVSGMGRYRGKYGFDTFTHEK 426
Cdd:TIGR01804 443 FGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
18-431 |
2.19e-48 |
|
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: 173.14 E-value: 2.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 18 ETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEIlEIGMTIQEIDYF---LKNID-DWVKPTHVEKTFTTa 93
Cdd:cd07082 56 PTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALK-EVDRTIDYIRDTieeLKRLDgDSLPGDWFPGTKGK- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 94 ldKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPselsenvaATFEKLIP----KYFES-----KYVTV 164
Cdd:cd07082 134 --IAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKP--------ATQGVLLGiplaEAFHDagfpkGVVNV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 165 VNGGIPETTDLLKE--RFDHILYTGCPPVAKIIMTAAAKhlTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQT 242
Cdd:cd07082 204 VTGRGREIGDPLVThgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 243 CLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGERDRADLYIPP 319
Cdd:cd07082 282 CTAIKRVLVHESVADELVELLKEEVAKLkVGMPWDNGVDITPLIDPKSADFVEGLIDdaVAKGATVLNGGGREGGNLIYP 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 320 TVLDVEKSDpfM---HDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHiT 396
Cdd:cd07082 362 TLLDPVTPD--MrlaWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQR-G 438
|
410 420 430
....*....|....*....|....*....|....*
gi 32566756 397 VDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVLHR 431
Cdd:cd07082 439 PDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
99-428 |
6.03e-47 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 169.91 E-value: 6.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 99 IEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELS-----ENVAATFEKLIPkyfeSKYVTVVNGGIPETT 173
Cdd:PLN02467 147 VLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELAsvtclELADICREVGLP----PGVLNVVTGLGTEAG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 174 DLLKE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILV 251
Cdd:PLN02467 223 APLAShpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLV 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 252 NSTVKPKLVAAIRKYVnefygEDVKASKDYAR------MINQRHFDRISGLLD--KTQGA-VLIGGERD---RADLYIPP 319
Cdd:PLN02467 303 HERIASEFLEKLVKWA-----KNIKISDPLEEgcrlgpVVSEGQYEKVLKFIStaKSEGAtILCGGKRPehlKKGFFIEP 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 320 TVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNdvLMHITVD 398
Cdd:PLN02467 378 TIItDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN--CSQPCFC 455
|
330 340 350
....*....|....*....|....*....|
gi 32566756 399 TLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:PLN02467 456 QAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
100-428 |
7.38e-47 |
|
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: 168.64 E-value: 7.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 100 EKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSenvAATFEKLIPKYFE----SKYVTVVNGGiPETTDL 175
Cdd:cd07090 113 RREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFT---PLTALLLAEILTEaglpDGVFNVVQGG-GETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 176 LKERFD--HILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDiSAKRIA-WGKWLNCGQTCLAPDYILVN 252
Cdd:cd07090 189 LCEHPDvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLE-NAVNGAmMANFLSQGQVCSNGTRVFVQ 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 253 STVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGERDRADL------YIPPTVL 322
Cdd:cd07090 268 RSIKDEFTERLVERTKKIrIGDPLDEDTQMGALISEEHLEKVLGYIEsaKQEGAkVLCGGERVVPEDglengfYVSPCVL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 323 -DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlMHITVDTLP 401
Cdd:cd07090 348 tDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVEVP 425
|
330 340
....*....|....*....|....*..
gi 32566756 402 FGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07090 426 FGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
25-429 |
3.52e-46 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 168.08 E-value: 3.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 25 RKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDwvkpTHVEKTFTTALDKPVIEKDPK 104
Cdd:PLN02766 84 RGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADK----IHGETLKMSRQLQGYTLKEPI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 105 GVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSE---LSENVAATFEKL--IPkyfeSKYVTVVNGGIPETTDLLKER 179
Cdd:PLN02766 160 GVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEqtpLSALFYAHLAKLagVP----DGVINVVTGFGPTAGAAIASH 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 180 FD--HILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVN---- 252
Cdd:PLN02766 236 MDvdKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQegiy 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 253 STVKPKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGERDRAD--LYIPPTVL-DVEKS 327
Cdd:PLN02766 316 DEFVKKLVEKAKDWV---VGDPFDPRARQGPQVDKQQFEKILSYIEhgKREGATLLTGGKPCGDkgYYIEPTIFtDVTED 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 328 DPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNdvlMHITVDT-LPFGGVG 406
Cdd:PLN02766 393 MKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYFAFDPdCPFGGYK 469
|
410 420
....*....|....*....|...
gi 32566756 407 VSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:PLN02766 470 MSGFGRDQGMDALDKYLQVKSVV 492
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
103-428 |
1.06e-45 |
|
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: 166.20 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESK-----YVTVVNGGiPETTDLLK 177
Cdd:cd07086 133 PLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNglppgVVNLVTGG-GDGGELLV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 178 --ERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTV 255
Cdd:cd07086 212 hdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 256 KPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER-DRAD--LYIPPTVLDVEK-S 327
Cdd:cd07086 292 YDEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNAIEiaKSQGGtVLTGGKRiDGGEpgNYVEPTIVTGVTdD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 328 DPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSS--GGVTVNdvlmhitVDT------ 399
Cdd:cd07086 372 ARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGSdcGIVNVN-------IPTsgaeig 444
|
330 340
....*....|....*....|....*....
gi 32566756 400 LPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07086 445 GAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
100-428 |
1.23e-44 |
|
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: 162.93 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 100 EKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVNGGIPETTDLLKER 179
Cdd:cd07107 113 LREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALVRH 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 180 FD--HILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWG---KWlnCGQTCLAPDYILVNST 254
Cdd:cd07107 193 PDvkRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGmnfTW--CGQSCGSTSRLFVHES 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 255 VKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLI--GGERDRADL----YIPPTVL-DV 324
Cdd:cd07107 271 IYDEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIDsaKREGARLVtgGGRPEGPALeggfYVEPTVFaDV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 325 EKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITvdTLPFGG 404
Cdd:cd07107 351 TPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFL--GAPFGG 428
|
330 340
....*....|....*....|....
gi 32566756 405 VGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07107 429 VKNSGIGREECLEELLSYTQEKNV 452
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
25-429 |
2.56e-41 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 155.35 E-value: 2.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 25 RKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLknidDWVKPTHvekTFTTALDKP---VIEK 101
Cdd:PLN02466 121 RSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYA----GWADKIH---GLTVPADGPhhvQTLH 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 102 DPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSE---LSENVAATF--EKLIPkyfeSKYVTVVNGGIPETTDLL 176
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEqtpLSALYAAKLlhEAGLP----PGVLNVVSGFGPTAGAAL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 177 KERF--DHILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNS 253
Cdd:PLN02466 270 ASHMdvDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 254 TVKPKLVA-----AIRKYVnefyGEDVKASKDYARMINQRHFDRISGLLDK--TQGAVLI-GGER-DRADLYIPPTVL-D 323
Cdd:PLN02466 350 RVYDEFVEkakarALKRVV----GDPFKKGVEQGPQIDSEQFEKILRYIKSgvESGATLEcGGDRfGSKGYYIQPTVFsN 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 324 VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN--DVLmhitvD-TL 400
Cdd:PLN02466 426 VQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVF-----DaAI 500
|
410 420
....*....|....*....|....*....
gi 32566756 401 PFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:PLN02466 501 PFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
25-428 |
6.09e-41 |
|
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: 153.42 E-value: 6.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 25 RKQQLLKLKKFIEENREAL-------SEAVWKDLRRRHesteileIGMTIQEIDYFLKNID---------DWVKPTHVeK 88
Cdd:cd07140 69 RGRLMYRLADLMEEHQEELatiesldSGAVYTLALKTH-------VGMSIQTFRYFAGWCDkiqgktipiNQARPNRN-L 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 89 TFTtaldkpviEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----IPKyfeskyvT 163
Cdd:cd07140 141 TLT--------KREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtvkagFPK-------G 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 164 VVNgGIPETTDLLKERF-DH-----ILYTGCPPVAKIIMTAAAK-HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKW 236
Cdd:cd07140 206 VIN-ILPGSGSLVGQRLsDHpdvrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 237 LNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDK--TQGAVLI-GGER-D 311
Cdd:cd07140 285 FNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLVEYCERgvKEGATLVyGGKQvD 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 312 RADLYIPPTVL-DVEKSDPFMHDEIFGPVLpiiTVQSFSES-----LEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGG 385
Cdd:cd07140 365 RPGFFFEPTVFtDVEDHMFIAKEESFGPIM---IISKFDDGdvdgvLQRANDTEYGLASGVFTKDINKALYVSDKLEAGT 441
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 32566756 386 VTVN-----DVlmhitvdTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07140 442 VFVNtynktDV-------AAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
7-428 |
1.51e-40 |
|
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: 151.90 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWK-----------DLRRRHESTEiLEIGMTIQEIDYFLK 75
Cdd:cd07085 44 VAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLehgktladargDVLRGLEVVE-FACSIPHLLKGEYLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 76 NIddwvkpthvektfTTALDKpVIEKDPKGVVLIISPWNYPVsMILLPMVP-AIAAGNTVVIKPSELSENVAATFEKLIP 154
Cdd:cd07085 123 NV-------------ARGIDT-YSYRQPLGVVAGITPFNFPA-MIPLWMFPmAIACGNTFVLKPSERVPGAAMRLAELLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 155 kyfESKY----VTVVNGGIPETTDLLkerfDH-----ILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADID 225
Cdd:cd07085 188 ---EAGLpdgvLNVVHGGKEAVNALL----DHpdikaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 226 ISAKRIAWGKWLNCGQTCLA-PDYILVNSTVK---PKLVAAIRKY-VNEFYGEDVkaskDYARMINQRHFDRISGLLDK- 299
Cdd:cd07085 261 QTANALVGAAFGAAGQRCMAlSVAVAVGDEADewiPKLVERAKKLkVGAGDDPGA----DMGPVISPAAKERIEGLIESg 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 300 -TQGA-VLIGGERDRADLY-----IPPTVLD-VEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNE 371
Cdd:cd07085 337 vEEGAkLVLDGRGVKVPGYengnfVGPTILDnVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSG 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32566756 372 AKVKRLLNETSSGGVTVN-----DVLMHitvdtlPFGGVGVS--GMGRYRGKYGFDTFTHEKSV 428
Cdd:cd07085 417 AAARKFQREVDAGMVGINvpipvPLAFF------SFGGWKGSffGDLHFYGKDGVRFYTQTKTV 474
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
103-409 |
1.82e-40 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 152.40 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSmILLPM-VPAIAAGNTVVIKPSELSENVAATF-----EKLIPKyfeskyvTVVN---GGIPETT 173
Cdd:PRK03137 171 PLGVGVVISPWNFPFA-IMAGMtLAAIVAGNTVLLKPASDTPVIAAKFvevleEAGLPA-------GVVNfvpGSGSEVG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 174 DLL----KERFdhILYTGCPPVAKIIMTAAAK------HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTC 243
Cdd:PRK03137 243 DYLvdhpKTRF--ITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKC 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 244 LAPDYILVNSTVKPKLVAAIRKYVNEFygeDVKASKDYARM---INQRHFDRISGLLD--KTQGAVLIGGERDRAD-LYI 317
Cdd:PRK03137 321 SACSRAIVHEDVYDEVLEKVVELTKEL---TVGNPEDNAYMgpvINQASFDKIMSYIEigKEEGRLVLGGEGDDSKgYFI 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 318 PPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHIT 396
Cdd:PRK03137 398 QPTIFaDVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAI 477
|
330
....*....|...
gi 32566756 397 VDTLPFGGVGVSG 409
Cdd:PRK03137 478 VGYHPFGGFNMSG 490
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
103-428 |
3.11e-40 |
|
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: 151.61 E-value: 3.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSmILLPM-VPAIAAGNTVVIKPSELSENVAATFEKLIpkyFESKY----VTVVNGGIPETTDLLK 177
Cdd:cd07124 166 PLGVGAVISPWNFPLA-ILAGMtTAALVTGNTVVLKPAEDTPVIAAKLVEIL---EEAGLppgvVNFLPGPGEEVGDYLV 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 178 E--RFDHILYTGCPPVAKIIMTAAAK------HLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYI 249
Cdd:cd07124 242 EhpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRV 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 250 LVNSTVK----PKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGERDRADL---YIPPT 320
Cdd:cd07124 322 IVHESVYdeflERLVERTKALK---VGDPEDPEVYMGPVIDKGARDRIRRYIEigKSEGRLLLGGEVLELAAegyFVQPT 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 321 VL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNdvlMHIT--- 396
Cdd:cd07124 399 IFaDVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN---RKITgal 475
|
330 340 350
....*....|....*....|....*....|....*
gi 32566756 397 VDTLPFGGVGVSGMGRYRGkyGFDT---FTHEKSV 428
Cdd:cd07124 476 VGRQPFGGFKMSGTGSKAG--GPDYllqFMQPKTV 508
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
7-428 |
4.68e-40 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 150.82 E-value: 4.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGE---TKPVKfRKQQLLKLKKFIEENREALSeavwkdlrrrhesteILEIGMTIQEIDYFLKniDDWVKP 83
Cdd:PRK09847 63 VSAARGVFERGDwslSSPAK-RKAVLNKLADLMEAHAEELA---------------LLETLDTGKPIRHSLR--DDIPGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 84 THVEKTFTTALDK-------------PVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFE 150
Cdd:PRK09847 125 ARAIRWYAEAIDKvygevattsshelAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 151 KLIPKY-FESKYVTVVNGGIPETTDLLKER--FDHILYTGCPPVAKIIMT-AAAKHLTPVTLELGGKCP-VVVEDDADID 225
Cdd:PRK09847 205 GLAKEAgLPDGVLNVVTGFGHEAGQALSRHndIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSAnIVFADCPDLQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 226 ISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQG 302
Cdd:PRK09847 285 QAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIRegESKG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 303 AVLIGGERDRADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNET 381
Cdd:PRK09847 365 QLLLDGRNAGLAAAIGPTIFvDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRL 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 32566756 382 SSGGVTV---NDVLMhitvdTLPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:PRK09847 445 KAGSVFVnnyNDGDM-----TVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
17-429 |
3.94e-38 |
|
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: 145.29 E-value: 3.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 17 GETKPVKfRKQQLLKLKKFIEENREALSEA-VWKDLRRRHESTEIlEIGMTIQEIDYFLKNIddwvkptHVEKTFTTALD 95
Cdd:cd07116 55 GKTSVAE-RANILNKIADRMEANLEMLAVAeTWDNGKPVRETLAA-DIPLAIDHFRYFAGCI-------RAQEGSISEID 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 96 KPVIE---KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYVTVVNGGIPET 172
Cdd:cd07116 126 ENTVAyhfHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 173 TDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCP------VVVEDDADIDISAKRIAWGKwLNCGQTCL 244
Cdd:cd07116 206 GKPLasSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniffadVMDADDAFFDKALEGFVMFA-LNQGEVCT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 245 APDYILVNSTVKPKLVA-AIRKyvnefygedVKASK-----DYARMI----NQRHFDRISGLLD--KTQGA-VLIGGERD 311
Cdd:cd07116 285 CPSRALIQESIYDRFMErALER---------VKAIKqgnplDTETMIgaqaSLEQLEKILSYIDigKEEGAeVLTGGERN 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 312 RAD------LYIPPTVLDVEKSDPFmHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGG 385
Cdd:cd07116 356 ELGgllgggYYVPTTFKGGNKMRIF-QEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGR 434
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 32566756 386 VTVNdvLMHITVDTLPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:cd07116 435 VWTN--CYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 476
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
95-422 |
7.09e-38 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 144.66 E-value: 7.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 95 DKPVIE-KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----IPKyfesKYVTVVNGG 168
Cdd:PRK11241 137 DKRLIViKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELairagIPA----GVFNVVTGS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 169 IPETTDLLKER--FDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAP 246
Cdd:PRK11241 213 AGAVGGELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 247 DYILVNSTVKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHF----DRISGLLDKtqGA-VLIGGE-RDRADLYIPP 319
Cdd:PRK11241 293 NRLYVQDGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVakveEHIADALEK--GArVVCGGKaHELGGNFFQP 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 320 TVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLmhITVD 398
Cdd:PRK11241 371 TILvDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI--ISNE 448
|
330 340
....*....|....*....|....
gi 32566756 399 TLPFGGVGVSGMGRYRGKYGFDTF 422
Cdd:PRK11241 449 VAPFGGIKASGLGREGSKYGIEDY 472
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
102-418 |
2.06e-36 |
|
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: 140.61 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 102 DPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLI-----PKyfesKYVTVVNGGiPETTDLL 176
Cdd:cd07111 146 KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICaeaglPP----GVLNIVTGN-GSFGSAL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 177 KE--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNST 254
Cdd:cd07111 221 ANhpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQES 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 255 VKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLI--GGERDRADLYIPPT-VLDVEKSD 328
Cdd:cd07111 301 VAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEegRAEGADVFqpGADLPSKGPFYPPTlFTNVPPAS 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 329 PFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlmHITVD-TLPFGGVGV 407
Cdd:cd07111 381 RIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING---HNLFDaAAGFGGYRE 457
|
330
....*....|.
gi 32566756 408 SGMGRYRGKYG 418
Cdd:cd07111 458 SGFGREGGKEG 468
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
7-431 |
2.47e-36 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 140.79 E-value: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALseavwkdlrrrhESTEILEIGMTIQE--------IDYFLKNID 78
Cdd:cd07083 61 LEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRREL------------IATLTYEVGKNWVEaiddvaeaIDFIRYYAR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 79 DWVK---PTHVEKTFTTALDKPVIEkdPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENV-AATFEKLIP 154
Cdd:cd07083 129 AALRlryPAVEVVPYPGEDNESFYV--GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVgYKVFEIFHE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 155 KYFESKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLT------PVTLELGGKCPVVVEDDADIDI 226
Cdd:cd07083 207 AGFPPGVVQFLPGVGEEVGAYLteHERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFEL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 227 SAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLD--KTQGA 303
Cdd:cd07083 287 VVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEhgKNEGQ 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 304 VLIGGERDRADLY-IPPTVLD-VEKSDPFMHDEIFGPVLPIITVQS--FSESLEYIADGEKPLAAYIFTRNEAKVKRLLN 379
Cdd:cd07083 367 LVLGGKRLEGEGYfVAPTVVEeVPPKARIAQEEIFGPVLSVIRYKDddFAEALEVANSTPYGLTGGVYSRKREHLEEARR 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 32566756 380 ETSSGGVTVNDVLMHITVDTLPFGGVGVSGMGRYRGKYGFDT-FTHEKSVLHR 431
Cdd:cd07083 447 EFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTGGPHYLRrFLEMKAVAER 499
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
7-420 |
4.29e-33 |
|
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: 130.47 E-value: 4.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAV--------WkdlrrrhESTEilEIGMTIQEIDYFLKNID 78
Cdd:cd07095 6 VAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLIsretgkplW-------EAQT--EVAAMAGKIDISIKAYH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 79 DWVKPTHVEKTFTTAldkpVIEKDPKGVVLIISPWNYPVSmilLP---MVPAIAAGNTVVIKPSELSENVAA-TFEKLIP 154
Cdd:cd07095 77 ERTGERATPMAQGRA----VLRHRPHGVMAVFGPFNFPGH---LPnghIVPALLAGNTVVFKPSELTPAVAElMVELWEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 155 KYFESKYVTVVNGGiPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHltP---VTLELGGKCPVVVEDDADIDISAK 229
Cdd:cd07095 150 AGLPPGVLNLVQGG-RETGEALaaHEGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 230 RIAWGKWLNCGQTCLAPDYILVNSTVK-----PKLVAAIRKY-VNEFYGEDvkaskdyARMINQRHFDRISGLLDKTQGA 303
Cdd:cd07095 227 LIVQSAFLTAGQRCTCARRLIVPDGAVgdaflERLVEAAKRLrIGAPDAEP-------PFMGPLIIAAAAARYLLAQQDL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 304 VLIGGE-------RDRADLYIPPTVLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKR 376
Cdd:cd07095 300 LALGGEpllamerLVAGTAFLSPGIIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFER 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 32566756 377 LLNETSSGGVTVNDVLMHITvDTLPFGGVGVSGMGRYRGKYGFD 420
Cdd:cd07095 380 FLARIRAGIVNWNRPTTGAS-STAPFGGVGLSGNHRPSAYYAAD 422
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
101-429 |
9.23e-33 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 130.39 E-value: 9.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAAtfeKLIPKYFES---KYVTVVNGGIPETTDLLK 177
Cdd:PRK13252 140 REPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTAL---KLAEIYTEAglpDGVFNVVQGDGRVGAWLT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 178 E--RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDiSAKRIAW-GKWLNCGQTCLAPDYILVNST 254
Cdd:PRK13252 217 EhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLD-RAADIAMlANFYSSGQVCTNGTRVFVQKS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 255 VKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER-DRADL----YIPPTVL-DV 324
Cdd:PRK13252 296 IKAAFEARLLERVERIRiGDPMDPATNFGPLVSFAHRDKVLGYIEkgKAEGArLLCGGERlTEGGFangaFVAPTVFtDC 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 325 EKSDPFMHDEIFGPVLPIITvqsFSESLEYIA---DGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVN-----DVLMhit 396
Cdd:PRK13252 376 TDDMTIVREEIFGPVMSVLT---FDDEDEVIAranDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINtwgesPAEM--- 449
|
330 340 350
....*....|....*....|....*....|...
gi 32566756 397 vdtlPFGGVGVSGMGRYRGKYGFDTFTHEKSVL 429
Cdd:PRK13252 450 ----PVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
103-430 |
3.80e-32 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 127.93 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPK--YFESKYVTVVNGGIPETTDLLKERF 180
Cdd:PRK09406 123 PLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRagFPDGCFQTLLVGSGAVEAILRDPRV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 181 DHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTV----K 256
Cdd:PRK09406 203 AAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVydafA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 257 PKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLIGGER-DRADLYIPPTVL-DVEKSDPFM 331
Cdd:PRK09406 283 EKFVARMAALR---VGDPTDPDTDVGPLATEQGRDEVEKQVDDAvaAGAtILCGGKRpDGPGWFYPPTVItDITPDMRLY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 332 HDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDvlMHITVDTLPFGGVGVSGMG 411
Cdd:PRK09406 360 TEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING--MTVSYPELPFGGVKRSGYG 437
|
330
....*....|....*....
gi 32566756 412 RYRGKYGFDTFTHEKSVLH 430
Cdd:PRK09406 438 RELSAHGIREFCNIKTVWI 456
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
82-428 |
4.46e-31 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 124.97 E-value: 4.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 82 KPTHVEKtfttalDKPVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPselSENVAATFEkLIPKYFESK- 160
Cdd:PRK13968 111 EPTLVEN------QQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKH---APNVMGCAQ-LIAQVFKDAg 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 161 -------YVTVVNGGIPETTDllKERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAW 233
Cdd:PRK13968 181 ipqgvygWLNADNDGVSQMIN--DSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 234 GKWLNCGQTCLAPDYILVNSTVKP----KLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDKT--QGA-VLI 306
Cdd:PRK13968 259 GRYQNTGQVCAAAKRFIIEEGIASafteRFVAAAAALK---MGDPRDEENALGPMARFDLRDELHHQVEATlaEGArLLL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 307 GGER-DRADLYIPPTVL-DVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSG 384
Cdd:PRK13968 336 GGEKiAGAGNYYAPTVLaNVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECG 415
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 32566756 385 GVTVNDvlmHITVDT-LPFGGVGVSGMGRYRGKYGFDTFTHEKSV 428
Cdd:PRK13968 416 GVFING---YCASDArVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
101-411 |
1.85e-27 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 115.24 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSElSENVAA--TFEKLIPKYFESKYVTVVNGGIPETTDLLKE 178
Cdd:PLN00412 156 KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPT-QGAVAAlhMVHCFHLAGFPKGLISCVTGKGSEIGDFLTM 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 179 R--FDHILYTGCPPVAKIIMTAAakhLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVK 256
Cdd:PLN00412 235 HpgVNCISFTGGDTGIAISKKAG---MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 257 PKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGAVLIGGERDRADLyIPPTVLDVEKSDpfMH-- 332
Cdd:PLN00412 312 DALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMdaKEKGATFCQEWKREGNL-IWPLLLDNVRPD--MRia 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 333 -DEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHiTVDTLPFGGVGVSGMG 411
Cdd:PLN00412 389 wEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPAR-GPDHFPFQGLKDSGIG 467
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
101-411 |
2.89e-27 |
|
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: 114.05 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 101 KDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSE---LS--ENVAATFEKLIPKYFESKYVTVVNGGIPETTDl 175
Cdd:cd07148 122 REPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALatpLSclAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTD- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 176 lkERFDHILYTGCPPVAKIIMTAAAKHlTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVN--- 252
Cdd:cd07148 201 --PRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPaei 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 253 -STVKPKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDK--TQGA-VLIGGERDRADLYIPPTVLDVEKSD 328
Cdd:cd07148 278 aDDFAQRLAAAAEKLV---VGDPTDPDTEVGPLIRPREVDRVEEWVNEavAAGArLLCGGKRLSDTTYAPTVLLDPPRDA 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 329 PFMHDEIFGPVlpiITVQSFSESLEYIADGEK-PLA--AYIFTRNEAKVKRLLNETSSGGVTVNDvlmHIT--VDTLPFG 403
Cdd:cd07148 355 KVSTQEIFGPV---VCVYSYDDLDEAIAQANSlPVAfqAAVFTKDLDVALKAVRRLDATAVMVND---HTAfrVDWMPFA 428
|
....*...
gi 32566756 404 GVGVSGMG 411
Cdd:cd07148 429 GRRQSGYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
99-411 |
1.01e-26 |
|
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: 113.06 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 99 IEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKL-----IPKyfesKYVTVVNG-GIPET 172
Cdd:cd07125 163 LELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELlheagVPR----DVLQLVPGdGEEIG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 173 TDLLK-ERFDHILYTGCPPVAKIIMTAAAKH---LTPVTLELGGKCPVVVEDDADIDISAKRI---AWGkwlNCGQTCLA 245
Cdd:cd07125 239 EALVAhPRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPEQAVKDVvqsAFG---SAGQRCSA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 246 PDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQRHFDRISGLLDKTQGAVLIGGERDRADL---YIPPTV 321
Cdd:cd07125 316 LRLLYLQEEIAERFIEMLKGAMASLkVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGngyFVAPGI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 322 LDVEKSDpFMHDEIFGPVLPIITVQSF--SESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVlmhIT--- 396
Cdd:cd07125 396 IEIVGIF-DLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRN---ITgai 471
|
330
....*....|....*
gi 32566756 397 VDTLPFGGVGVSGMG 411
Cdd:cd07125 472 VGRQPFGGWGLSGTG 486
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
103-389 |
3.67e-26 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 111.14 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPV------SMIllpmvpAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYV-----TVVNGGIPE 171
Cdd:cd07130 132 PLGVVGVITAFNFPVavwgwnAAI------ALVCGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLpgaiaSLVCGGADV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 172 TTDLLK-ERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYIL 250
Cdd:cd07130 206 GEALVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 251 VNSTVKPKLVAAIRK-YVNEFYGEDVKASKDYARMINQRHFDRISGLLD--KTQGA-VLIGGER-DRADLYIPPTVLDVE 325
Cdd:cd07130 286 VHESIYDEVLERLKKaYKQVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEeaKSQGGtVLFGGKViDGPGNYVEPTIVEGL 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32566756 326 KSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSS--GGVTVN 389
Cdd:cd07130 366 SDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVN 431
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
103-411 |
1.36e-21 |
|
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: 97.67 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAA-TFEKLIPKYFESKYVTVVNG-----GIPETTDll 176
Cdd:TIGR01238 160 SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYrAVELMQEAGFPAGTIQLLPGrgadvGAALTSD-- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 177 kERFDHILYTGCPPVAKIIMTAAAKHL---TPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNS 253
Cdd:TIGR01238 238 -PRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 254 TVKPKLVAAIRKYVNEF-YGEDVKASKDYARMINQ-------RHFDRISGLLDKTQGAVLIGGERDRADLYIPPTVLDVE 325
Cdd:TIGR01238 317 DVADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDAeakqnllAHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLFELD 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 326 KSDPfMHDEIFGPVLPIITVQS--FSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPFG 403
Cdd:TIGR01238 397 DIAE-LSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFG 475
|
....*...
gi 32566756 404 GVGVSGMG 411
Cdd:TIGR01238 476 GQGLSGTG 483
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
3-431 |
8.70e-21 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 95.58 E-value: 8.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 3 FTELVETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVW----KDLRRRH----ESTEILE--IGMTIQEIDY 72
Cdd:PLN02419 153 FKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITteqgKTLKDSHgdifRGLEVVEhaCGMATLQMGE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 73 FLKNIDDWVKPTHVektfttaldkpvieKDPKGVVLIISPWNYPvSMILLPMVP-AIAAGNTVVIKPSELSENVAATFEK 151
Cdd:PLN02419 233 YLPNVSNGVDTYSI--------------REPLGVCAGICPFNFP-AMIPLWMFPvAVTCGNTFILKPSEKDPGASVILAE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 152 LIPKYFESKYVTVVNGGIPETTDLL--KERFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAK 229
Cdd:PLN02419 298 LAMEAGLPDGVLNIVHGTNDTVNAIcdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLN 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 230 RIAWGKWLNCGQTCLAPDYILVNSTVKP---KLVAAIrKYVNEFYGEDVKAskDYARMINQRHFDRISGLLDK--TQGAV 304
Cdd:PLN02419 378 ALLAAGFGAAGQRCMALSTVVFVGDAKSwedKLVERA-KALKVTCGSEPDA--DLGPVISKQAKERICRLIQSgvDDGAK 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 305 LIGGERD------RADLYIPPTVLDVEKSD-PFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRL 377
Cdd:PLN02419 455 LLLDGRDivvpgyEKGNFIGPTILSGVTPDmECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKF 534
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 32566756 378 LNETSSGGVTVNdVLMHITVDTLPFGGVGVSGMG--RYRGKYGFDTFTHEKSVLHR 431
Cdd:PLN02419 535 QMDIEAGQIGIN-VPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQIKLVTQK 589
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
103-412 |
2.30e-18 |
|
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: 87.29 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKP----SELSENVAATFEK--LIPkyfeSKYVTVVNGGIPETTDLL 176
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPhtavSIVMQIMVRLLHYagLLP----PEDVTLINGDGKTMQALL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 177 KE-RFDHILYTGCPPVAKIImtAAAKHLTPVTLELGGKCPVVVEDDAD-IDISAKRIAWGKWLNCGQTCLAPDYILVNST 254
Cdd:cd07084 176 LHpNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPEN 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 255 -----VKPKLVAAIRKYVNEFYGEDVKASKDYARMINQRHFD-----RISGLLDKTQGAVLIGGERDRADLYIPPTVLDv 324
Cdd:cd07084 254 wsktpLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMENLlgsvlLFSGKELKNHSIPSIYGACVASALFVPIDEIL- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 325 eKSDPFMHDEIFGPVLPIITVQSFSES--LEYIADGEKPLAAYIFTRNEAKVKRLLNETSSGGVTVNDVLMHITVDTLPF 402
Cdd:cd07084 333 -KTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVAPNQN 411
|
330
....*....|
gi 32566756 403 GGVGVSGMGR 412
Cdd:cd07084 412 HGGGPAADPR 421
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
87-409 |
2.47e-18 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 87.32 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 87 EKTFTTALDKPVIEKDPKGVVLIISPWNYPVSmilLP---MVPAIAAGNTVVIKPSELSENVAATFEKL-----IPKyfe 158
Cdd:PRK09457 118 EKRSEMADGAAVLRHRPHGVVAVFGPYNFPGH---LPnghIVPALLAGNTVVFKPSELTPWVAELTVKLwqqagLPA--- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 159 sKYVTVVNGGIPETTDLLKER-FDHILYTGCPPVAKIIMTAAAKHltP---VTLELGGKCPVVVEDDADIDISAKRIAWG 234
Cdd:PRK09457 192 -GVLNLVQGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQS 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 235 KWLNCGQTCLAPDYILVNSTVK-----PKLVAAIRKY-VNEFYGE---------DVKASKdyaRMIN-QRHfdrisgLLD 298
Cdd:PRK09457 269 AFISAGQRCTCARRLLVPQGAQgdaflARLVAVAKRLtVGRWDAEpqpfmgaviSEQAAQ---GLVAaQAQ------LLA 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 299 KTqGAVLIGGERDRADL-YIPPTVLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRL 377
Cdd:PRK09457 340 LG-GKSLLEMTQLQAGTgLLTPGIIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQF 418
|
330 340 350
....*....|....*....|....*....|..
gi 32566756 378 LNETSSGGVTVNDVLMHITvDTLPFGGVGVSG 409
Cdd:PRK09457 419 LLEIRAGIVNWNKPLTGAS-SAAPFGGVGASG 449
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
105-409 |
2.39e-14 |
|
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: 75.32 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 105 GVVLIISPWNYPVSMILLPMVPAIAaGNTVVIKPSelSENVAATFekLIPKYFESKYVT--VVN---GGIPETTD--LLK 177
Cdd:cd07123 172 GFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPS--DTAVLSNY--LVYKILEEAGLPpgVINfvpGDGPVVGDtvLAS 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 178 ERFDHILYTGCPPVAKIIMTAAAKHLT-----P-VTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLA------ 245
Cdd:cd07123 247 PHLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAasrayv 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 246 PDYILvnSTVKPKLVAAIRKYVnefYGEDVKASKDYARMINQRHFDRISGLLDKTQGA----VLIGGERDRADLY-IPPT 320
Cdd:cd07123 327 PESLW--PEVKERLLEELKEIK---MGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpeaeIIAGGKCDDSVGYfVEPT 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 321 VldVEKSDP---FMHDEIFGPVLpiiTVQ-----SFSESLEYIAD-GEKPLAAYIFTRNEAKVKRLLNE--TSSGGVTVN 389
Cdd:cd07123 402 V--IETTDPkhkLMTEEIFGPVL---TVYvypdsDFEETLELVDTtSPYALTGAIFAQDRKAIREATDAlrNAAGNFYIN 476
|
330 340
....*....|....*....|
gi 32566756 390 DVLMHITVDTLPFGGVGVSG 409
Cdd:cd07123 477 DKPTGAVVGQQPFGGARASG 496
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
102-424 |
2.80e-14 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 74.87 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 102 DPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFESKYV-----TVVNGGIPETTDLL 176
Cdd:PLN02315 153 NPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLpgaifTSFCGGAEIGEAIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 177 KE-RFDHILYTGCPPVAKIIMTAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTV 255
Cdd:PLN02315 233 KDtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 256 KPKLVAA-IRKYVNEFYGEDVKASKDYARM---INQRHFDRISGLLDKTQGAVLIGGER-DRADLYIPPTVLDVEKSDPF 330
Cdd:PLN02315 313 YDDVLEQlLTVYKQVKIGDPLEKGTLLGPLhtpESKKNFEKGIEIIKSQGGKILTGGSAiESEGNFVQPTIVEISPDADV 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 331 MHDEIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKRLLNETSS--GGVTVNdvlmhitvdtLP------- 401
Cdd:PLN02315 393 VKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVN----------IPtngaeig 462
|
330 340
....*....|....*....|....*
gi 32566756 402 --FGGVGVSGMGRYRGKYGFDTFTH 424
Cdd:PLN02315 463 gaFGGEKATGGGREAGSDSWKQYMR 487
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
103-411 |
3.97e-13 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 72.15 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLipkYFESkyvtvvngGIPE----------- 171
Cdd:PRK11904 684 GRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKL---LHEA--------GIPKdvlqllpgdga 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 172 ------TTDllkERFDHILYTGCPPVAKII-MTAAAKHLTPVTL--ELGGKCPVVVEDDA-------DIDISAKRIAwgk 235
Cdd:PRK11904 753 tvgaalTAD---PRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQNAMIVDSTAlpeqvvdDVVTSAFRSA--- 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 236 wlncGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-------YGEDV-----KASKDyarMINqRHFDRIsglldkTQGA 303
Cdd:PRK11904 827 ----GQRCSALRVLFVQEDIADRVIEMLKGAMAELkvgdprlLSTDVgpvidAEAKA---NLD-AHIERM------KREA 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 304 VLI-----GGERDRADlYIPPTVLDVEKSDpFMHDEIFGPVLPIITVQSF--SESLEYIADGEKPLAAYIFTRNEAKVKR 376
Cdd:PRK11904 893 RLLaqlplPAGTENGH-FVAPTAFEIDSIS-QLEREVFGPILHVIRYKASdlDKVIDAINATGYGLTLGIHSRIEETADR 970
|
330 340 350
....*....|....*....|....*....|....*
gi 32566756 377 LLNETSSGGVTVNDVLMHITVDTLPFGGVGVSGMG 411
Cdd:PRK11904 971 IADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
103-411 |
1.17e-12 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 70.77 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIpkyfeskyvtvVNGGIPE-TTDLL----- 176
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRIL-----------LEAGVPAgVVQLLpgrge 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 177 --------KERFDHILYTGCPPVAKIIMTAAAKHL------TPVTLELGGKCPVVVEDDA-------DIDISAKRIAwgk 235
Cdd:PRK11809 837 tvgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSAlteqvvaDVLASAFDSA--- 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 236 wlncGQTCLAPDYILVNSTVKPKLVAAIRKYVNEF-YGEDVKASKDYARMIN-------QRHfdrISGLLDK----TQgA 303
Cdd:PRK11809 914 ----GQRCSALRVLCLQDDVADRTLKMLRGAMAECrMGNPDRLSTDIGPVIDaeakaniERH---IQAMRAKgrpvFQ-A 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 304 VLIGGERDRADLYIPPTVLDVEKSDPfMHDEIFGPVLPIITVQS--FSESLEYIADGEKPLAAYIFTRNEAKVKRLLNET 381
Cdd:PRK11809 986 ARENSEDWQSGTFVPPTLIELDSFDE-LKREVFGPVLHVVRYNRnqLDELIEQINASGYGLTLGVHTRIDETIAQVTGSA 1064
|
330 340 350
....*....|....*....|....*....|
gi 32566756 382 SSGGVTVNDVLMHITVDTLPFGGVGVSGMG 411
Cdd:PRK11809 1065 HVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
103-411 |
4.74e-11 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 65.66 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIpkyFESkyvtvvngGIPETT-DLL----- 176
Cdd:PRK11905 676 PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLL---HEA--------GVPKDAlQLLpgdgr 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 177 --------KERFDHILYTGCPPVAKIIMTAAAKHLT-PVTL--ELGGKCPVVVEDDA-------DIDISAKRIAwgkwln 238
Cdd:PRK11905 745 tvgaalvaDPRIAGVMFTGSTEVARLIQRTLAKRSGpPVPLiaETGGQNAMIVDSSAlpeqvvaDVIASAFDSA------ 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 239 cGQTCLAPDYILVNSTVKPKLVAAIRKYVNEFY-GEDVKASKDYARMINQRHFDRISGLLD--KTQGAVL----IGGERD 311
Cdd:PRK11905 819 -GQRCSALRVLCLQEDVADRVLTMLKGAMDELRiGDPWRLSTDVGPVIDAEAQANIEAHIEamRAAGRLVhqlpLPAETE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 312 RAdLYIPPTVLDVEK-SDpfMHDEIFGPVLPIITVQSfSESLEYIAD------GekpLAAYIFTRNEAKVKRLLNETSSG 384
Cdd:PRK11905 898 KG-TFVAPTLIEIDSiSD--LEREVFGPVLHVVRFKA-DELDRVIDDinatgyG---LTFGLHSRIDETIAHVTSRIRAG 970
|
330 340
....*....|....*....|....*..
gi 32566756 385 GVTVNDVLMHITVDTLPFGGVGVSGMG 411
Cdd:PRK11905 971 NIYVNRNIIGAVVGVQPFGGEGLSGTG 997
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
7-370 |
8.54e-11 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 63.80 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYFRtgetKPVKFRKQQLLKLKKFIEENREALSEAvwkdlrrrhestEILEIGMTIQEiDYFLKNIDDWVKPTHV 86
Cdd:cd07121 14 KAAQKQYRK----CTLADREKIIEAIREALLSNAEELAEM------------AVEETGMGRVE-DKIAKNHLAAEKTPGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 87 EKTFTTAL--DK--PVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFES--- 159
Cdd:cd07121 77 EDLTTTAWsgDNglTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEagg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 160 --KYVTVVNGGIPETTDLLkerFDH-----ILYTGCPPVAKIIMTAAAKhltpvtlELG---GKCPVVVEDDADIDISAK 229
Cdd:cd07121 157 pdNLVVTVEEPTIETTNEL---MAHpdinlLVVTGGPAVVKAALSSGKK-------AIGagaGNPPVVVDETADIEKAAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 230 RIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYvNEFYGEDVKASKDYARMINQRHFDRIS-GLLDKTQGAVLigg 308
Cdd:cd07121 227 DIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRN-GAYVLNDEQAEQLLEVVLLTNKGATPNkKWVGKDASKIL--- 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32566756 309 erDRADLYIPPT----VLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPL--AAYIFTRN 370
Cdd:cd07121 303 --KAAGIEVPADirliIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKN 368
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
50-377 |
1.92e-09 |
|
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: 59.59 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 50 DLRRRHESTEILEIGMTIQEiDYFLKNIDDWVKPTHVEKTFTT----ALDKP---VIEKDPKGVVLIISPWNYPVSMILL 122
Cdd:cd07081 36 DARIDLAKLAVSETGMGRVE-DKVIKNHFAAEYIYNVYKDEKTcgvlTGDENggtLIIAEPIGVVASITPSTNPTSTVIF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 123 PMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYF------ESKYVTVVNGGIPETTDLLKE-RFDHILYTGCPPVAKii 195
Cdd:cd07081 115 KSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAvaagapENLIGWIDNPSIELAQRLMKFpGIGLLLATGGPAVVK-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 196 mtAAAKHLTPVTLELGGKCPVVVEDDADIDISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVaairkyvnefygedv 275
Cdd:cd07081 193 --AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVM--------------- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 276 kaskdyaRMINQRHFDRISG-LLDKTQGAVLIGGERDR-------------ADLYIPPT-------VLDVEKSDPFMHdE 334
Cdd:cd07081 256 -------RLFEGQGAYKLTAeELQQVQPVILKNGDVNRdivgqdaykiaaaAGLKVPQEtriligeVTSLAEHEPFAH-E 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 32566756 335 IFGPVLPIITVQSFSESLE----YIADGEKPLAAYIFTRNEAKVKRL 377
Cdd:cd07081 328 KLSPVLAMYRAANFADADAkalaLKLEGGCGHTSAMYSDNIKAIENM 374
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
103-390 |
4.92e-09 |
|
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: 58.44 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PK-GVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIpkyfeskyvtVVNGGIPE---------T 172
Cdd:cd07128 143 PRrGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDI----------VESGLLPEgalqlicgsV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 173 TDLLK--ERFDHILYTGCPPVAKIIMT--AAAKHLTPVTLE--------LGgkcPVVVEDDADIDISAKRIAWGKWLNCG 240
Cdd:cd07128 213 GDLLDhlGEQDVVAFTGSAATAAKLRAhpNIVARSIRFNAEadslnaaiLG---PDATPGTPEFDLFVKEVAREMTVKAG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 241 QTCLAPDYILVNS----TVKPKLVAAIRKYVnefYG----EDVK----ASKDyarminQRHfDRISGLLDKTQGAVLIGG 308
Cdd:cd07128 290 QKCTAIRRAFVPEarvdAVIEALKARLAKVV---VGdprlEGVRmgplVSRE------QRE-DVRAAVATLLAEAEVVFG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 309 ERDRADL---------YIPPTVLDVEKSD--PFMHD-EIFGPVLPIITVQSFSESLEYIADGEKPLAAYIFTRNEAKVKR 376
Cdd:cd07128 360 GPDRFEVvgadaekgaFFPPTLLLCDDPDaaTAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARE 439
|
330
....*....|....*.
gi 32566756 377 LLNETSS--GGVTVND 390
Cdd:cd07128 440 LVLGAAPyhGRLLVLN 455
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
127-394 |
7.38e-09 |
|
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: 57.94 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 127 AIAAGNTVVIK--PS--ELSENVAATFEKLIPKY-FESKYVTVVNGGIPET-TDLLKerfdH-----ILYTGCPPVAKII 195
Cdd:cd07129 131 ALAAGCPVVVKahPAhpGTSELVARAIRAALRATgLPAGVFSLLQGGGREVgVALVK----HpaikaVGFTGSRRGGRAL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 196 MTAAAKHLT--PVTLELGGKCPVVV------EDDADIdisAKRIAWGKWLNCGQTCLAPDYILV-NSTVKPKLVAAIRKY 266
Cdd:cd07129 207 FDAAAARPEpiPFYAELGSVNPVFIlpgalaERGEAI---AQGFVGSLTLGAGQFCTNPGLVLVpAGPAGDAFIAALAEA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 267 VNEFYGedvkaskdyARMIN---QRHFDR-ISGLLDKTQGAVLIGGERDRADLYIPPTVLDVEKS----DPFMHDEIFGP 338
Cdd:cd07129 284 LAAAPA---------QTMLTpgiAEAYRQgVEALAAAPGVRVLAGGAAAEGGNQAAPTLFKVDAAaflaDPALQEEVFGP 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32566756 339 VLPIITVQSFSE------SLE-------YIADGEKPLAAYIFTRNEAKVKRLLNetsSG---GVTVNDVLMH 394
Cdd:cd07129 355 ASLVVRYDDAAEllavaeALEgqltatiHGEEDDLALARELLPVLERKAGRLLF---NGwptGVEVCPAMVH 423
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
8-383 |
1.96e-08 |
|
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: 56.46 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 8 ETQRKYFRTGETKPVKFRKQQLLKLKKFIEENREALSEAVWKDLRRRHESTEILEIGMTIQEIDYFLKNIDDWVKPT--- 84
Cdd:cd07077 1 ESAKNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITasv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 85 -HVEKTFTTALDKPVIEKDPKGVVLIISPWNYPVSMILLPMVpAIAAGNTVVIKPSELSE--NVAAT--FEKLIPKYFES 159
Cdd:cd07077 81 gHIQDVLLPDNGETYVRAFPIGVTMHILPSTNPLSGITSALR-GIATRNQCIFRPHPSAPftNRALAllFQAADAAHGPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 160 KYV-TVVNGGIPETTDLLK-ERFDHILYTGCPPVAKiimtAAAKH--LTPVTLELGGKCPVVVEDDADIDISAKRIAWGK 235
Cdd:cd07077 160 ILVlYVPHPSDELAEELLShPKIDLIVATGGRDAVD----AAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 236 WLNcGQTCLAPDYILVNSTVKPKLvaairkyvnefygedvkaskdyarminqrhFDRIsglldKTQGAVliggerDRADL 315
Cdd:cd07077 236 FFD-QNACASEQNLYVVDDVLDPL------------------------------YEEF-----KLKLVV------EGLKV 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32566756 316 YIPPTVLDVE---KSDPFMHDEiFGPVLPIITVQSFSESLE----YIADGEKPLAAYIFTRNEAKVKRLLN--ETSS 383
Cdd:cd07077 274 PQETKPLSKEttpSFDDEALES-MTPLECQFRVLDVISAVEnawmIIESGGGPHTRCVYTHKINKVDDFVQyiDTAS 349
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
103-411 |
2.65e-08 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 56.48 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 103 PKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIpkyFESkyvtvvngGIPE----------- 171
Cdd:COG4230 680 GRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLL---HEA--------GVPAdvlqllpgdge 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 172 ------TTDllkERFDHILYTGCPPVAKII-MTAAAKHLTPVTL--ELGGKCPVVVedD---------ADIDISAkriaw 233
Cdd:COG4230 749 tvgaalVAD---PRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIV--DssalpeqvvDDVLASA----- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 234 gkWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYVNE-------FYGEDV-----KASKDyarMInQRHFDRIsglldKTQ 301
Cdd:COG4230 819 --FDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAElrvgdpaDLSTDVgpvidAEARA---NL-EAHIERM-----RAE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 302 GAVLIGGERDRAD---LYIPPTVLDVEKSDpFMHDEIFGPVLPIITVQsfSESLEYIAD-----GekplaaY-----IFT 368
Cdd:COG4230 888 GRLVHQLPLPEECangTFVAPTLIEIDSIS-DLEREVFGPVLHVVRYK--ADELDKVIDainatG------YgltlgVHS 958
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 32566756 369 RNEAKVKRLLNETSSGGVTVNdvlMHIT---VDTLPFGGVGVSGMG 411
Cdd:COG4230 959 RIDETIDRVAARARVGNVYVN---RNIIgavVGVQPFGGEGLSGTG 1001
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
7-377 |
9.41e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 54.52 E-value: 9.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 7 VETQRKYfrtgETKPVKFRKQQLLKLKKFIEENREALSEAVWKdlrrrhesteilEIGMTIQEiDYFLKNIDDWVKPTHV 86
Cdd:PRK15398 46 KVAQQRY----QQKSLAMRQRIIDAIREALLPHAEELAELAVE------------ETGMGRVE-DKIAKNVAAAEKTPGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 87 EKTFTTAL--DK--PVIEKDPKGVVLIISPWNYPVSMILLPMVPAIAAGNTVVIKPSELSENVAATFEKLIPKYFES--- 159
Cdd:PRK15398 109 EDLTTEALtgDNglTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAagg 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 160 --KYVTVVNGGIPETTDLLkerFDH-----ILYTGCPPVAKIIMT-------AAAkhltpvtlelgGKCPVVVEDDADID 225
Cdd:PRK15398 189 peNLVVTVAEPTIETAQRL---MKHpgialLVVTGGPAVVKAAMKsgkkaigAGA-----------GNPPVVVDETADIE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 226 ISAKRIAWGKWLNCGQTCLAPDYILVNSTVKPKLVAAIRKYvnefyGedvkaskdyARMINQRHFDRISGLLDKTQGAV- 304
Cdd:PRK15398 255 KAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKN-----G---------AVLLTAEQAEKLQKVVLKNGGTVn 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 305 --LIGGER----DRADLYIPPT----VLDVEKSDPFMHDEIFGPVLPIITVQSFSESLEYIADGEKPL--AAYIFTRNea 372
Cdd:PRK15398 321 kkWVGKDAakilEAAGINVPKDtrllIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRN-- 398
|
....*
gi 32566756 373 kVKRL 377
Cdd:PRK15398 399 -VDNL 402
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
83-389 |
1.01e-07 |
|
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: 54.41 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 83 PTHVEKTFTtaldkPViekdPKGVVLIIS-----PWN-YPvsmillPMVPAIAAGNTVVIKPSE-----LSENVAATFEK 151
Cdd:cd07127 182 PLAMEKTFT-----VV----PRGVALVIGcstfpTWNgYP------GLFASLATGNPVIVKPHPaailpLAITVQVAREV 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 152 LIPKYFESKYVTVVNGGIPEttDLLKERFDH-----ILYTGCPPVAKIIMTAAAKHLtpVTLELGGKCPVVVEDDADIDI 226
Cdd:cd07127 247 LAEAGFDPNLVTLAADTPEE--PIAQTLATRpevriIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 227 SAKRIAWGKWLNCGQTCLAPDYILV--------NSTVKPKLVAA-IRKYVNEFYGEDVKASKDYARMINQRHFDRISgll 297
Cdd:cd07127 323 MLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtdDGRKSFDEVAAdLAAAIDGLLADPARAAALLGAIQSPDTLARIA--- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566756 298 DKTQGAVLIGGERDRADLYIP------PTVLDVEKSDPFMHD-EIFGPVLPIITVQSFSESLE---YIADGEKPLAAYIF 367
Cdd:cd07127 400 EARQLGEVLLASEAVAHPEFPdarvrtPLLLKLDASDEAAYAeERFGPIAFVVATDSTDHSIElarESVREHGAMTVGVY 479
|
330 340 350
....*....|....*....|....*....|..
gi 32566756 368 TRNEAKVKRL----------LNETSSGGVTVN 389
Cdd:cd07127 480 STDPEVVERVqeaaldagvaLSINLTGGVFVN 511
|
|
| |
