|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
5-447 |
0e+00 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 873.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 5 SEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAAD 84
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 85 EPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYP 164
Cdd:cd07132 81 EPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 165 VINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTC 244
Cdd:cd07132 161 VVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 245 VAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVAYGGTGDAATRYIAPTILTDV 324
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 325 DPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFGG 404
Cdd:cd07132 321 KPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 22907049 405 VGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDEGLKVRYPPSP 447
Cdd:cd07132 401 VGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
5-430 |
0e+00 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 748.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 5 SEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAAD 84
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 85 EPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYP 164
Cdd:cd07087 81 RRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 165 VINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTC 244
Cdd:cd07087 161 VVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 245 VAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVAYGGTGDAATRYIAPTILTDV 324
Cdd:cd07087 241 IAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 325 DPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFGG 404
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGG 400
|
410 420
....*....|....*....|....*.
gi 22907049 405 VGNSGMGSYHGKKSFETFSHRRSCLV 430
Cdd:cd07087 401 VGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
5-450 |
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: 672.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 5 SEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAAD 84
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 85 EPVeKTPQTQQ-DELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLY 163
Cdd:cd07136 81 KRV-KTPLLNFpSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 164 PVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQT 243
Cdd:cd07136 160 AVVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 244 CVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVAYGGTGDAATRYIAPTILTD 323
Cdd:cd07136 240 CVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 324 VDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFG 403
Cdd:cd07136 320 VTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFG 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 22907049 404 GVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDegLKVRYPPSPAKM 450
Cdd:cd07136 400 GVGNSGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPPYKGKK 444
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
2-445 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 640.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 2 SKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEW 81
Cdd:PTZ00381 7 EIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKD 161
Cdd:PTZ00381 87 LKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 162 LYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSG 241
Cdd:PTZ00381 167 YVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 242 QTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIE--GQKVAYGGTGDAATRYIAPT 319
Cdd:PTZ00381 247 QTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDIENKYVAPT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 320 ILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHS 399
Cdd:PTZ00381 327 IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPN 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 22907049 400 LPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDEGLKVRYPP 445
Cdd:PTZ00381 407 LPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPP 452
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
1-427 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 622.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 1 MSKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPE 80
Cdd:cd07135 4 LDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 81 WAADEPVEKTPQTQQ-DELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLD 159
Cdd:cd07135 84 WAKDEKVKDGPLAFMfGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 KDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMN 239
Cdd:cd07135 164 PDAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 240 SGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIE--GQKVAYGGTGDAATRYIA 317
Cdd:cd07135 244 AGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDttKGKVVIGGEMDEATRFIP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 318 PTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITL 397
Cdd:cd07135 324 PTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGV 403
|
410 420 430
....*....|....*....|....*....|
gi 22907049 398 HSLPFGGVGNSGMGSYHGKKSFETFSHRRS 427
Cdd:cd07135 404 DNAPFGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
12-430 |
0e+00 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 531.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 12 RAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAADEPVEKTP 91
Cdd:cd07134 8 QAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 92 QTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVP 171
Cdd:cd07134 88 LLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 172 ETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYIL 251
Cdd:cd07134 168 VAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 252 CDPSIQNQIVEKLKKSLKEFYGEDA--KKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTGDAATRYIAPTILTDV 324
Cdd:cd07134 248 VHESVKDAFVEHLKAEIEKFYGKDAarKASPDLARIVNDRHFDRLKGLLDdavakGAKVEFGGQFDAAQRYIAPTVLTNV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 325 DPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHItLHS-LPFG 403
Cdd:cd07134 328 TPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHF-LNPnLPFG 406
|
410 420
....*....|....*....|....*..
gi 22907049 404 GVGNSGMGSYHGKKSFETFSHRRSCLV 430
Cdd:cd07134 407 GVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
4-430 |
0e+00 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 528.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAA 83
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 DEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLY 163
Cdd:cd07137 81 PEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 164 PVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKF-MNSGQ 242
Cdd:cd07137 161 KVIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 243 TCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVA----YGGTGDAATRYIAP 318
Cdd:cd07137 241 ACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVAdkivHGGERDEKNLYIEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 319 TILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLH 398
Cdd:cd07137 321 TILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAID 400
|
410 420 430
....*....|....*....|....*....|..
gi 22907049 399 SLPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 430
Cdd:cd07137 401 TLPFGGVGESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
9-427 |
4.21e-172 |
|
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: 489.69 E-value: 4.21e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 9 KRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLhknEWNAYYE----EVVYVLEEIEYMIQKLPEWAAD 84
Cdd:cd07133 5 ERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADF---GHRSRHEtllaEILPSIAGIKHARKHLKKWMKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 85 EPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYP 164
Cdd:cd07133 82 SRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 165 VINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTC 244
Cdd:cd07133 162 VVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 245 VAPDYILCDPSIQNQIVEKLKKSLKEFYGeDAKKSRDYGRIISARHFQRVMGLIE-----GQKV---AYGGTGDAATRYI 316
Cdd:cd07133 242 VAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEdarakGARVielNPAGEDFAATRKL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 317 APTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHIT 396
Cdd:cd07133 321 PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVA 400
|
410 420 430
....*....|....*....|....*....|.
gi 22907049 397 LHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 427
Cdd:cd07133 401 QDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-445 |
3.86e-161 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 463.81 E-value: 3.86e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 1 MSKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPE 80
Cdd:PLN02203 5 GETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 81 WAADE----PVEKTPQTQQdelyIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQ 156
Cdd:PLN02203 85 WMAPKkaklPLVAFPATAE----VVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 157 YLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVD---KNCDLDVACRRIA 233
Cdd:PLN02203 161 YLDSKAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 234 WGKFMN-SGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEGQKVA----YGGT 308
Cdd:PLN02203 241 GGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAasivHGGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 309 GDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAA 388
Cdd:PLN02203 321 IDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTF 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 22907049 389 NDVIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDegLKVRYPP 445
Cdd:PLN02203 401 NDAIIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTE--FEFRYPP 455
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
6-430 |
2.84e-155 |
|
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: 447.04 E-value: 2.84e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 6 EAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWnAYYEEVVYVLEEIEYMIQKLPEWAADE 85
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 86 PVEKTPQTQqdeLYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYP 164
Cdd:cd07078 81 IPSPDPGEL---AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 165 VINGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQ 242
Cdd:cd07078 158 VVTGDGDEVGAALasHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 243 TCVAPDYILCDPSIQNQIVEKLKKSLKEFYGED-AKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGT--GDAATR 314
Cdd:cd07078 238 VCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEdakaeGAKLLCGGKrlEGGKGY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 315 YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVH 394
Cdd:cd07078 318 FVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVG 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 22907049 395 ITLHsLPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 430
Cdd:cd07078 398 AEPS-APFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
5-445 |
7.34e-136 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 399.42 E-value: 7.34e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 5 SEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAAD 84
Cdd:PLN02174 13 SILVTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 85 EPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYP 164
Cdd:PLN02174 93 EKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 165 VINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKF-MNSGQT 243
Cdd:PLN02174 173 VVEGAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 244 CVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIE----GQKVAYGGTGDAATRYIAPT 319
Cdd:PLN02174 253 CISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 320 ILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHS 399
Cdd:PLN02174 333 ILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHT 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 22907049 400 LPFGGVGNSGMGSYHGKKSFETFSHRRSCLVRPLMNDEGlkVRYPP 445
Cdd:PLN02174 413 LPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSA--VRYPP 456
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
9-430 |
1.40e-123 |
|
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: 363.86 E-value: 1.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 9 KRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWnAYYEEVVYVLEEIEYMIQKLPEWAADEPVE 88
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGPELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 89 KTPQTqqdELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVIN 167
Cdd:cd06534 80 PDPGG---EAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 168 GGVPET-TELLK-ERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCV 245
Cdd:cd06534 157 GGGDEVgAALLShPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 246 APDYILCDPSIQNQIVEKLKkslkefygedakksrdygriisarhfqrvmgliegqkvayggtgdaatryiapTILTDVD 325
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV-----------------------------------------------------TVLVDVD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 326 PQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHsLPFGGV 405
Cdd:cd06534 264 PDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-APFGGV 342
|
410 420
....*....|....*....|....*
gi 22907049 406 GNSGMGSYHGKKSFETFSHRRSCLV 430
Cdd:cd06534 343 KNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
6-427 |
1.86e-121 |
|
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: 362.52 E-value: 1.86e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 6 EAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYyEEVVYVLEEIEYMIqklpEWAADE 85
Cdd:COG1012 47 AAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEAR-GEVDRAADFLRYYA----GEARRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 86 PVEKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLY 163
Cdd:COG1012 122 YGETIPSDAPGTRaYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 164 PVINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSG 241
Cdd:COG1012 202 NVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 242 QTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGT--GDAAT 313
Cdd:COG1012 282 QRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIedavaEGAELLTGGRrpDGEGG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 314 RYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIV 393
Cdd:COG1012 362 YFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTT 441
|
410 420 430
....*....|....*....|....*....|....
gi 22907049 394 HITLHsLPFGGVGNSGMGSYHGKKSFETFSHRRS 427
Cdd:COG1012 442 GAVPQ-APFGGVKQSGIGREGGREGLEEYTETKT 474
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
6-427 |
1.46e-109 |
|
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: 331.42 E-value: 1.46e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 6 EAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEevvyvleeIEYMIQKLpEWAADE 85
Cdd:pfam00171 33 AAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGE--------VDRAIDVL-RYYAGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 86 PV----EKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDK 160
Cdd:pfam00171 104 ARrldgETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 161 DLYPVINGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFM 238
Cdd:pfam00171 184 GVLNVVTGSGAEVGEALveHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 239 NSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGTGDAA 312
Cdd:pfam00171 264 NAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 313 T-RYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDV 391
Cdd:pfam00171 344 NgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDY 423
|
410 420 430
....*....|....*....|....*....|....*.
gi 22907049 392 IVhITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 427
Cdd:pfam00171 424 TT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
4-430 |
2.14e-105 |
|
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: 320.32 E-value: 2.14e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKnEWNAYYEEVVYVLEEIEYMIQKLPEWAA 83
Cdd:cd07099 20 VAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGK-PRADAGLEVLLALEAIDWAARNAPRVLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 DEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSEL----SENMASLLATIIPqylD 159
Cdd:cd07099 99 PRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVtplvGELLAEAWAAAGP---P 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 KDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMN 239
Cdd:cd07099 176 QGVLQVVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 240 SGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGG---TGD 310
Cdd:cd07099 256 AGQTCISVERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRRHVDdavakGAKALTGGarsNGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 311 AatRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAND 390
Cdd:cd07099 336 G--PFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSIND 413
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 22907049 391 VIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 430
Cdd:cd07099 414 VLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
4-436 |
1.09e-82 |
|
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: 262.24 E-value: 1.09e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAA 83
Cdd:cd07098 20 VDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 DEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYL----- 158
Cdd:cd07098 100 PESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLaacgh 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 159 DKDLYPVINGgVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGK 236
Cdd:cd07098 180 DPDLVQLVTC-LPETAEALTShpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 237 FMNSGQTCVAPDYILCDPSIQNQIVEKLKK---SLKEFYGEDakKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG- 307
Cdd:cd07098 259 FQSSGQNCIGIERVIVHEKIYDKLLEILTDrvqALRQGPPLD--GDVDVGAMISPARFDRLEELVadaveKGARLLAGGk 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 308 ----TGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSS 383
Cdd:cd07098 337 ryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLET 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 22907049 384 GGVAANDVIVHITLHSLPFGGVGNSGMGSYHGKKSFetfshRRSCLVRPLMND 436
Cdd:cd07098 417 GMVAINDFGVNYYVQQLPFGGVKGSGFGRFAGEEGL-----RGLCNPKSVTED 464
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
4-426 |
3.63e-77 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 247.06 E-value: 3.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAAD----LHKNEWnayyeevvyvleEIEYMIQKLP 79
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIREsgstRPKAAF------------EVGAAIAILR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 80 EwAADEPVEKTPQTQQDEL-----YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLL-ATI 153
Cdd:cd07104 70 E-AAGLPRRPEGEILPSDVpgkesMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiAEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 154 IPQY-LDKDLYPVINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACR 230
Cdd:cd07104 149 FEEAgLPKGVLNVVPGGGSEIGDALVEhpRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 231 RIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLK---KSLKefYGEDAKKSRDYGRIISARHFQRVMGLIE-----GQK 302
Cdd:cd07104 229 AAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVakaKALP--VGDPRDPDTVIGPLINERQVDRVHAIVEdavaaGAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 303 VAYGGTGDAatRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN-DKVIKkmIAET 381
Cdd:cd07104 307 LLTGGTYEG--LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDlERAMA--FAER 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 22907049 382 S-SGGVAANDVIVHITLHSlPFGGVGNSGMGSYHGKKSFETFSHRR 426
Cdd:cd07104 383 LeTGMVHINDQTVNDEPHV-PFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
3-427 |
2.40e-75 |
|
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: 242.92 E-value: 2.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 3 KISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEwnAYY-EEVVYVLEEIEYMIQKLPEW 81
Cdd:cd07102 19 AVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPI--AQAgGEIRGMLERARYMISIAEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADEPVEKTPQTqqdELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELS----ENMASLLATI-IPq 156
Cdd:cd07102 97 LADIRVPEKDGF---ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTplcgERFAAAFAEAgLP- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 157 yldKDLYPVINGGVPETTELLKE-RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWG 235
Cdd:cd07102 173 ---EGVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 236 KFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGG-- 307
Cdd:cd07102 250 AFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIAdaiakGARALIDGal 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 308 --TGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGG 385
Cdd:cd07102 330 fpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGT 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 22907049 386 VAAN--DVIVhitlHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 427
Cdd:cd07102 410 VFMNrcDYLD----PALAWTGVKDSGRGVTLSRLGYDQLTRPKS 449
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
4-423 |
5.55e-75 |
|
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: 242.09 E-value: 5.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYmiqkLPEWAA 83
Cdd:cd07093 21 VDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIPRAAANFRF----FADYIL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 DEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIpqyLDKDLY 163
Cdd:cd07093 97 QLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELA---NEAGLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 164 P----VINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKF 237
Cdd:cd07093 174 PgvvnVVHGFGPEAGAALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 238 MNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGTGDA 311
Cdd:cd07093 254 SNNGEVCLAGSRILVQRSIYDEFLERFVERAKALkVGDPLDPDTEVGPLISKEHLEKVLGYVelaraEGATILTGGGRPE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 312 ATR-----YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGV 386
Cdd:cd07093 334 LPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTV 413
|
410 420 430
....*....|....*....|....*....|....*...
gi 22907049 387 AANDVIV-HITlhsLPFGGVGNSGMGSYHGKKSFETFS 423
Cdd:cd07093 414 WVNCWLVrDLR---TPFGGVKASGIGREGGDYSLEFYT 448
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
7-389 |
3.48e-74 |
|
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: 240.24 E-value: 3.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 7 AVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYyEEVVYVLEEIEYMIqklpEWAADEP 86
Cdd:cd07088 40 AVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLAR-VEVEFTADYIDYMA----EWARRIE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 87 VEKTPQTQQDE-LYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYP 164
Cdd:cd07088 115 GEIIPSDRPNEnIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 165 VINGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQ 242
Cdd:cd07088 195 IVTGRGSVVGDALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 243 TCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTGDAATR-- 314
Cdd:cd07088 275 VCTCAERVYVHEDIYDEFMEKLVEKMKAVkVGDPFDAATDMGPLVNEAALDKVEEMVEraveaGATLLTGGKRPEGEKgy 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22907049 315 YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAN 389
Cdd:cd07088 355 FYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYIN 429
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
6-412 |
5.28e-73 |
|
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: 236.56 E-value: 5.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 6 EAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKnEWNAYYEEVVYVLEEIEymiqklpeWAADE 85
Cdd:cd07103 23 AAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGK-PLAEARGEVDYAASFLE--------WFAEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 86 PVE--------KTPQTQQdelYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY 157
Cdd:cd07103 94 ARRiygrtipsPAPGKRI---LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 158 -LDKDLYPVINGGVPETTELLKERFD--HILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAW 234
Cdd:cd07103 171 gLPAGVLNVVTGSPAEIGEALCASPRvrKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 235 GKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGT 308
Cdd:cd07103 251 SKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALVEdavakGAKVLTGGK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 309 GDAAT-RYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVA 387
Cdd:cd07103 331 RLGLGgYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVG 410
|
410 420
....*....|....*....|....*
gi 22907049 388 ANDVIvhITLHSLPFGGVGNSGMGS 412
Cdd:cd07103 411 INTGL--ISDAEAPFGGVKESGLGR 433
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
4-427 |
1.85e-72 |
|
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: 235.60 E-value: 1.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSG-RTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWa 82
Cdd:cd07089 21 VDAAIAAARRAFDTGdWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 83 aDEPVEKTPQTQQDELY---IHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIpqyLD 159
Cdd:cd07089 100 -PWEFDLPVPALRGGPGrrvVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEII---AE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 KDLYP-VIN---GGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIA 233
Cdd:cd07089 176 TDLPAgVVNvvtGSDNAVGEALTTdpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 234 WGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG 307
Cdd:cd07089 256 GVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGDPADPGTVMGPLISAAQRDRVEGYIargrdEGARLVTGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 308 ---TGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSG 384
Cdd:cd07089 336 grpAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTG 415
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 22907049 385 GVAANDviVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 427
Cdd:cd07089 416 SVGING--GGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
4-422 |
2.22e-72 |
|
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: 236.15 E-value: 2.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTR-PLQFRIQQLEALQRLIqEQEQELVGAL-AADLHKnewnAYYEEVVYVLEEIEYMIQKLPEW 81
Cdd:cd07144 47 VDKAVKAARKAFESWWSKvTGEERGELLDKLADLV-EKNRDLLAAIeALDSGK----PYHSNALGDLDEIIAVIRYYAGW 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AaDEPVEKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LD 159
Cdd:cd07144 122 A-DKIQGKTIPTSPNKLaYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 KDLYPVINGGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKF 237
Cdd:cd07144 201 PGVVNIIPGYGAVAGSALAEHpdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 238 MNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFY--GEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGT-- 308
Cdd:cd07144 281 YNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEkgkkeGAKLVYGGEka 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 309 --GDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGV 386
Cdd:cd07144 361 peGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMV 440
|
410 420 430
....*....|....*....|....*....|....*....
gi 22907049 387 ---AANDVIVHItlhslPFGGVGNSGMGSYHGKKSFETF 422
Cdd:cd07144 441 winSSNDSDVGV-----PFGGFKMSGIGRELGEYGLETY 474
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
4-420 |
4.14e-71 |
|
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: 231.74 E-value: 4.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSG--RTRPLQfRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYyEEVVYVLEEIEY---MIQKL 78
Cdd:cd07109 21 VDRAVQAARRAFESGwlRLSPAE-RGRLLLRIARLIREHADELARLESLDTGKPLTQAR-ADVEAAARYFEYyggAADKL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 79 PEwaadepvEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY- 157
Cdd:cd07109 99 HG-------ETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAg 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 158 LDKDLYPVINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWG 235
Cdd:cd07109 172 LPAGALNVVTGLGAEAGAALVAhpGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 236 KFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF---YGEDakkSRDYGRIISARHFQRVMGLIE-----GQKVAYGG 307
Cdd:cd07109 252 IIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALrvgPGLE---DPDLGPLISAKQLDRVEGFVArararGARIVAGG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 308 T--GDAATR--YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSS 383
Cdd:cd07109 329 RiaEGAPAGgyFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRA 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 22907049 384 GGVAAND------VivhitlhSLPFGGVGNSGmgsyHGK-KSFE 420
Cdd:cd07109 409 GQVFVNNygagggI-------ELPFGGVKKSG----HGReKGLE 441
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
6-426 |
3.52e-70 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 229.52 E-value: 3.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 6 EAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEeVVYVLEEIEYmiqklpewAADE 85
Cdd:cd07150 25 RAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE-TTFTPELLRA--------AAGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 86 PVEKTPQTQQDEL-----YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LD 159
Cdd:cd07150 96 CRRVRGETLPSDSpgtvsMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 KDLYPVINGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKF 237
Cdd:cd07150 176 KGVFNVVTGGGAEVGDELvdDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 238 MNSGQTCVAPDYILCDPSIQNQIVEKL---KKSLKefYGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTG 309
Cdd:cd07150 256 MHQGQICMSASRIIVEEPVYDEFVKKFvarASKLK--VGDPRDPDTVIGPLISPRQVERIKRQVEdavakGAKLLTGGKY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 310 DAatRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAN 389
Cdd:cd07150 334 DG--NFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHIN 411
|
410 420 430
....*....|....*....|....*....|....*..
gi 22907049 390 DVIVHITLHsLPFGGVGNSGMGSYHGKKSFETFSHRR 426
Cdd:cd07150 412 DPTILDEAH-VPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
7-422 |
4.20e-70 |
|
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: 229.70 E-value: 4.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 7 AVKRARAAFSS-GRTrPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAADE 85
Cdd:cd07138 41 AVAAARRAFPAwSAT-SVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 86 PVEKTpqtqqdelYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYP 164
Cdd:cd07138 120 RRGNS--------LVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 165 VINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQ 242
Cdd:cd07138 192 LVNGDGPVVGEALSAhpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 243 TCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGTG--DAATR 314
Cdd:cd07138 272 SCNAPTRMLVPRSRYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIqkgieEGARLVAGGPGrpEGLER 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 315 --YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVI 392
Cdd:cd07138 352 gyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAA 431
|
410 420 430
....*....|....*....|....*....|
gi 22907049 393 VHItlhSLPFGGVGNSGMGSYHGKKSFETF 422
Cdd:cd07138 432 FNP---GAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
4-423 |
3.16e-69 |
|
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: 3.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSS-GRTRPLQFRIQQLEALQrLIQEQEQELVGALAADLHKNEWNAYYEevvyvleeIEYMIQKLPEWA 82
Cdd:cd07105 2 ADQAVEAAAAAFPAwSKTPPSERRDILLKAAD-LLESRRDEFIEAMMEETGATAAWAGFN--------VDLAAGMLREAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 83 A---DEPVEKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIipqYL 158
Cdd:cd07105 73 SlitQIIGGSIPSDKPGTLaMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRV---FH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 159 DKDLYP-VIN------GGVPETTELLkerFDH-----ILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLD 226
Cdd:cd07105 150 EAGLPKgVLNvvthspEDAPEVVEAL---IAHpavrkVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 227 VACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKsrdyGRIISARHFQRVMGLIE-----GQ 301
Cdd:cd07105 227 AAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL----GSLVSAAAADRVKELVDdalskGA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 302 KVAYGGTGD--AATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIA 379
Cdd:cd07105 303 KLVVGGLADesPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAK 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 22907049 380 ETSSGGVAANDVIVHITlHSLPFGGVGNSGMGSYHGKKSFETFS 423
Cdd:cd07105 383 RIESGAVHINGMTVHDE-PTLPHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
4-411 |
2.30e-66 |
|
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: 219.51 E-value: 2.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGR-TRPLQfRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYM---IQKLP 79
Cdd:cd07092 21 VDAAVAAAHAAFPSWRrTTPAE-RSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFRFFagaARTLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 80 EWAADEPVEKTpqtqqdELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLD 159
Cdd:cd07092 100 GPAAGEYLPGH------TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 KDLYPVINGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKF 237
Cdd:cd07092 174 PGVVNVVCGGGASAGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGY 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 238 MNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE----GQKVAYGG-TGDA 311
Cdd:cd07092 254 YNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVErapaHARVLTGGrRAEG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 312 ATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDv 391
Cdd:cd07092 334 PGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT- 412
|
410 420
....*....|....*....|.
gi 22907049 392 ivHITLHS-LPFGGVGNSGMG 411
Cdd:cd07092 413 --HIPLAAeMPHGGFKQSGYG 431
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
6-416 |
2.91e-65 |
|
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: 216.24 E-value: 2.91e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 6 EAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEeVVYVLEEIEYMIQ-KLPEWAAD 84
Cdd:cd07106 23 QAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFE-VGGAVAWLRYTASlDLPDEVIE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 85 EPVEKTpqtqqdeLYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYP 164
Cdd:cd07106 102 DDDTRR-------VELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 165 VINGGvPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQ 242
Cdd:cd07106 175 VVSGG-DELGPALTShpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 243 TCVAPDYILCDPSIQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGTGDAATRY- 315
Cdd:cd07106 254 VCAAIKRLYVHESIYDEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEdakakGAKVLAGGEPLDGPGYf 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 316 IAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAN---DVI 392
Cdd:cd07106 334 IPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINthgALD 413
|
410 420
....*....|....*....|....
gi 22907049 393 VHItlhslPFGGVGNSGMGSYHGK 416
Cdd:cd07106 414 PDA-----PFGGHKQSGIGVEFGI 432
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
4-427 |
8.38e-65 |
|
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: 215.49 E-value: 8.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSG---RTRPLQfRIQQLEALQRLIQEQEQELVGALAADLHKnewnayyeevvyVLEEIEYMIQKLPE 80
Cdd:cd07114 21 VDRAVAAARAAFEGGawrKLTPTE-RGKLLRRLADLIEANAEELAELETRDNGK------------LIRETRAQVRYLAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 81 W------AADE------PVEKtpqtqQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMA 147
Cdd:cd07114 88 WyryyagLADKiegaviPVDK-----GDYLnFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 148 SLLATIIPQY-LDKDLYPVINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCD 224
Cdd:cd07114 163 LELAKLAEEAgFPPGVVNVVTGFGPETGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 225 LDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLK---KSLKefYGEDAKKSRDYGRIISARHFQRVMGLI--- 298
Cdd:cd07114 243 LDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVaraRAIR--VGDPLDPETQMGPLATERQLEKVERYVara 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 299 --EGQKVAYGG-----TGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSND 371
Cdd:cd07114 321 reEGARVLTGGerpsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 22907049 372 KVIKKMIAETSSGGVAANDviVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 427
Cdd:cd07114 401 ARAHRVARAIEAGTVWVNT--YRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKS 454
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
4-411 |
1.40e-63 |
|
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: 212.84 E-value: 1.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSG--RTRPLQFRIQQLEALQRLIqEQEQELVGALAA-DLHKNEWNAYYEEVVYVLEEIEYmiqklpe 80
Cdd:cd07091 43 VDAAVKAARAAFETGwwRKMDPRERGRLLNKLADLI-ERDRDELAALESlDNGKPLEESAKGDVALSIKCLRY------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 81 WA--ADEPVEKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPqy 157
Cdd:cd07091 115 YAgwADKIQGKTIPIDGNFLaYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIK-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 158 ldKDLYP-----VINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVAC 229
Cdd:cd07091 193 --EAGFPpgvvnIVPGFGPTAGAAISShmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 230 RRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLI-----EGQKV 303
Cdd:cd07091 271 EWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIesgkkEGATL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 304 AYGGT--GDAATrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAET 381
Cdd:cd07091 351 LTGGErhGSKGY-FIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRAL 429
|
410 420 430
....*....|....*....|....*....|.
gi 22907049 382 SSGGVAAND-VIVHitlHSLPFGGVGNSGMG 411
Cdd:cd07091 430 KAGTVWVNTyNVFD---AAVPFGGFKQSGFG 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
7-411 |
3.48e-63 |
|
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: 211.31 E-value: 3.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 7 AVKRARAAFSSG---RTRPLQfRIQQLEALQRLIQEQEQELvgAL--AADLHKNEWNAYYEEVVYVLEEIEYMIQklpew 81
Cdd:cd07112 29 AVAAARRAFESGvwsRLSPAE-RKAVLLRLADLIEAHRDEL--ALleTLDMGKPISDALAVDVPSAANTFRWYAE----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADEPVEKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI-----IP 155
Cdd:cd07112 101 AIDKVYGEVAPTGPDALaLITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 156 qyldKDLYPVINGGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNC-DLDVACRR 231
Cdd:cd07112 181 ----AGVLNVVPGFGHTAGEALGLHmdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 232 IAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDA-KKSRDYGRIISARHFQRVMGLI-----EGQKVAY 305
Cdd:cd07112 257 AAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPlDPATRMGALVSEAHFDKVLGYIesgkaEGARLVA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 306 GGTGDAATR---YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETS 382
Cdd:cd07112 337 GGKRVLTETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLR 416
|
410 420 430
....*....|....*....|....*....|....
gi 22907049 383 SGGVAAN-----DVIVhitlhslPFGGVGNSGMG 411
Cdd:cd07112 417 AGTVWVNcfdegDITT-------PFGGFKQSGNG 443
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
103-430 |
6.75e-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: 210.27 E-value: 6.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 103 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELLKE-- 179
Cdd:cd07118 118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMTEhp 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 180 RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQ 259
Cdd:cd07118 198 DVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 260 IVEKLK-KSLKEFYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG--TGDAATRYIAPTILTDVDPQSPVM 331
Cdd:cd07118 278 FVAAVVaRSRKVRVGDPLDPETKVGAIINEAQLAKITDYVdagraEGATLLLGGerLASAAGLFYQPTIFTDVTPDMAIA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 332 QEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN-DKVIkKMIAETSSGGVAANDVIVhiTLHSLPFGGVGNSGM 410
Cdd:cd07118 358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDiDTAL-TVARRIRAGTVWVNTFLD--GSPELPFGGFKQSGI 434
|
330 340
....*....|....*....|
gi 22907049 411 GSYHGKKSFETFSHRRSCLV 430
Cdd:cd07118 435 GRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
1-431 |
9.46e-63 |
|
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: 209.85 E-value: 9.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 1 MSKISEAVKRARAAFSS-GRTRPLQfRIQQLEALQRLIQEQEQELVGALAADLHKnewnAYYE---EVVYVLEEIEYMIQ 76
Cdd:cd07090 18 AEDVDLAVKSAKAAQKEwSATSGME-RGRILRKAADLLRERNDEIARLETIDNGK----PIEEarvDIDSSADCLEYYAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 77 KLPEWAAdepvEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQ 156
Cdd:cd07090 93 LAPTLSG----EHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 157 Y-LDKDLYPVINGGvPETTELLKERFD--HILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIA 233
Cdd:cd07090 169 AgLPDGVFNVVQGG-GETGQLLCEHPDvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 234 WGKFMNSGQTCVAPDYILCDPSIQNQIVEKL-KKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG 307
Cdd:cd07090 248 MANFLSQGQVCSNGTRVFVQRSIKDEFTERLvERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIesakqEGAKVLCGG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 308 T------GDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAET 381
Cdd:cd07090 328 ErvvpedGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 22907049 382 SSGGVAANDviVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVR 431
Cdd:cd07090 408 QAGTCWINT--YNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVE 455
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
7-430 |
1.06e-62 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 209.91 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 7 AVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEwAADEP 86
Cdd:cd07108 24 AVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVLADLFRYFGGLAGE-LKGET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 87 VEKTPQTQQdelYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVI 166
Cdd:cd07108 103 LPFGPDVLT---YTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 167 NGGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRR-IAWGKFMNSGQT 243
Cdd:cd07108 180 TGYGEECGAALVDHpdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGaIAGMRFTRQGQS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 244 CVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE------GQKVAYGGTGDAATR-- 314
Cdd:cd07108 260 CTAGSRLFVHEDIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDlglstsGATVLRGGPLPGEGPla 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 315 ---YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDv 391
Cdd:cd07108 340 dgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQ- 418
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 22907049 392 iVHITLHSLPFGGVGNSGMG---SYHGkkSFETFSHRRSCLV 430
Cdd:cd07108 419 -GGGQQPGQSYGGFKQSGLGreaSLEG--MLEHFTQKKTVNI 457
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
6-411 |
2.11e-62 |
|
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: 208.99 E-value: 2.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 6 EAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNewnayyeeVVYVLEEIEYMIQKLpEWAADE 85
Cdd:cd07149 25 KAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKP--------IKDARKEVDRAIETL-RLSAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 86 ---------PVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQ 156
Cdd:cd07149 96 akrlagetiPFDASPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 157 -YLDKDLYPVINGGVPET-TELLK-ERFDHILYTGSTGVGKIIMTAAAkhLTPVTLELGGKSPCYVDKNCDLDVACRRIA 233
Cdd:cd07149 176 aGLPKGALNVVTGSGETVgDALVTdPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 234 WGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGG 307
Cdd:cd07149 254 SGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLvVGDPLDEDTDVGPMISEAEAERIEEWVEeavegGARLLTGG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 308 TGDAAtrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVA 387
Cdd:cd07149 334 KRDGA--ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVM 411
|
410 420
....*....|....*....|....*...
gi 22907049 388 ANDV----IVHitlhsLPFGGVGNSGMG 411
Cdd:cd07149 412 INDSstfrVDH-----MPYGGVKESGTG 434
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-412 |
4.66e-62 |
|
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: 208.64 E-value: 4.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 6 EAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELvgalAADLHKNEWNAYYEEVvyvlEEIEYMIQKLPEWAA-- 83
Cdd:cd07097 41 AAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEEL----ARLLTREEGKTLPEAR----GEVTRAGQIFRYYAGea 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 -DEPVEKTPQTQQD-ELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQyldkd 161
Cdd:cd07097 113 lRLSGETLPSTRPGvEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEE----- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 162 lypvinGGVPETT-------------ELLK-ERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDV 227
Cdd:cd07097 188 ------AGLPAGVfnlvmgsgsevgqALVEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 228 ACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLK---KSLKefYGEDAKKSRDYGRIISARHFQRVMGLI-----E 299
Cdd:cd07097 262 AVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVertKALK--VGDALDEGVDIGPVVSERQLEKDLRYIeiarsE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 300 GQKVAYGG---TGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKK 376
Cdd:cd07097 340 GAKLVYGGerlKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATH 419
|
410 420 430
....*....|....*....|....*....|....*.
gi 22907049 377 MIAETSSGGVAANDVIVHITLHsLPFGGVGNSGMGS 412
Cdd:cd07097 420 FKRRVEAGVVMVNLPTAGVDYH-VPFGGRKGSSYGP 454
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
7-427 |
6.04e-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: 207.68 E-value: 6.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 7 AVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYmiqkLPEWAADEP 86
Cdd:cd07115 24 AVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVPRAADTFRY----YAGWADKIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 87 VEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPV 165
Cdd:cd07115 100 GEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 166 INGGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQT 243
Cdd:cd07115 180 VTGFGEVAGAALVEHpdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 244 CVAPDYILCDPSIQNQIVEKL---KKSLKefYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGTGDAATR- 314
Cdd:cd07115 260 CTAGSRLLVHESIYDEFLERFtslARSLR--PGDPLDPKTQMGPLVSQAQFDRVLDYVdvgreEGARLLTGGKRPGARGf 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 315 YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdvIVH 394
Cdd:cd07115 338 FVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYN 415
|
410 420 430
....*....|....*....|....*....|...
gi 22907049 395 ITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 427
Cdd:cd07115 416 RFDPGSPFGGYKQSGFGREMGREALDEYTEVKS 448
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
4-426 |
7.52e-62 |
|
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: 207.15 E-value: 7.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALA----ADLHKNEWnayyeevvyvleEIEYMIQKLP 79
Cdd:cd07152 15 VDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVresgSIRPKAGF------------EVGAAIGELH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 80 EWAAdepvekTPQTQQDELYIHSE---------PLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKP---SELSENMa 147
Cdd:cd07152 83 EAAG------LPTQPQGEILPSAPgrlslarrvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPdprTPVSGGV- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 148 sLLATIIPQY-LDKDLYPVINGGvPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCD 224
Cdd:cd07152 156 -VIARLFEEAgLPAGVLHVLPGG-ADAGEALVEdpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 225 LDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE---- 299
Cdd:cd07152 234 LDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLpVGDPATGQVALGPLINARQLDRVHAIVDdsva 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 300 -GQKVAYGGTGDAatRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMI 378
Cdd:cd07152 314 aGARLEAGGTYDG--LFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 22907049 379 AETSSGGVAANDVIVHITLHSlPFGGVGNSGMGSYHG-KKSFETFSHRR 426
Cdd:cd07152 392 DRLRTGMLHINDQTVNDEPHN-PFGGMGASGNGSRFGgPANWEEFTQWQ 439
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
6-412 |
2.04e-61 |
|
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: 207.85 E-value: 2.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 6 EAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNewnaYYEEVVYVLEEIEYMiqklpEWAADE 85
Cdd:cd07124 73 AAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKN----WAEADADVAEAIDFL-----EYYARE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 86 PVEKTPQTQQDELYIHS----EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIpqyLDKD 161
Cdd:cd07124 144 MLRLRGFPVEMVPGEDNryvyRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEIL---EEAG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 162 LYP-VIN--GGVPET-----TELLKERFdhILYTGSTGVGKIIMTAAAK------HLTPVTLELGGKSPCYVDKNCDLDV 227
Cdd:cd07124 221 LPPgVVNflPGPGEEvgdylVEHPDVRF--IAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDE 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 228 ACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLK---KSLKefYGEDAKKSRDYGRIISARHFQRVMGLIE----G 300
Cdd:cd07124 299 AAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVertKALK--VGDPEDPEVYMGPVIDKGARDRIRRYIEigksE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 301 QKVAYGGTGDA-ATR--YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKM 377
Cdd:cd07124 377 GRLLLGGEVLElAAEgyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERA 456
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 22907049 378 IAETSSGGVAAND------VIVHitlhslPFGGVGNSGMGS 412
Cdd:cd07124 457 RREFEVGNLYANRkitgalVGRQ------PFGGFKMSGTGS 491
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
4-419 |
1.17e-60 |
|
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: 203.85 E-value: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHK--NEWNAYYEEVVYVLEeieYMIQKLPEW 81
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKpiAEARAEVEKCAWICR---YYAENAEAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADEPVEktpqTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDK 160
Cdd:cd07100 78 LADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAgFPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 161 DLYPVINGGVPETTELLK-ERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMN 239
Cdd:cd07100 154 GVFQNLLIDSDQVEAIIAdPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 240 SGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGT---GD 310
Cdd:cd07100 234 AGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALkVGDPMDEDTDLGPLARKDLRDELHEQVEeavaaGATLLLGGKrpdGP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 311 AAtrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAND 390
Cdd:cd07100 314 GA--FYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFING 391
|
410 420 430
....*....|....*....|....*....|..
gi 22907049 391 VIVhiTLHSLPFGGVGNSGMG---SYHGKKSF 419
Cdd:cd07100 392 MVK--SDPRLPFGGVKRSGYGrelGRFGIREF 421
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
4-422 |
4.95e-60 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 203.77 E-value: 4.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKnEWNAYYEEVVYVLEEIEymiqklpeWAA 83
Cdd:PLN02278 64 TNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGK-PLKEAIGEVAYGASFLE--------YFA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 DEPV----EKTPQTQQD-ELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI----- 153
Cdd:PLN02278 135 EEAKrvygDIIPSPFPDrRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELalqag 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 154 IPQyldkDLYPVINGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRR 231
Cdd:PLN02278 215 IPP----GVLNVVMGDAPEIGDALlaSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 232 IAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAY 305
Cdd:PLN02278 291 ALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVESHVqdavsKGAKVLL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 306 GGT--GDAATRYiAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSS 383
Cdd:PLN02278 371 GGKrhSLGGTFY-EPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEY 449
|
410 420 430
....*....|....*....|....*....|....*....
gi 22907049 384 GGVAANDVIvhITLHSLPFGGVGNSGMGSYHGKKSFETF 422
Cdd:PLN02278 450 GIVGVNEGL--ISTEVAPFGGVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
4-416 |
2.30e-59 |
|
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: 201.00 E-value: 2.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYyEEVVYVLEEIEYMIQKLPEWAA 83
Cdd:cd07101 20 VEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF-EEVLDVAIVARYYARRAERLLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 DE------PVektpQTQQDELYihsEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSelSENMASLLATI---I 154
Cdd:cd07101 99 PRrrrgaiPV----LTRTTVNR---RPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD--SQTALTALWAVellI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 155 PQYLDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAW 234
Cdd:cd07101 170 EAGLPRDLWQVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 235 GKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGT 308
Cdd:cd07101 250 ACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVDdavakGATVLAGGR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 309 G--DAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGV 386
Cdd:cd07101 330 ArpDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTV 409
|
410 420 430
....*....|....*....|....*....|..
gi 22907049 387 AANDVIVhITLHSL--PFGGVGNSGMGSYHGK 416
Cdd:cd07101 410 NVNEGYA-AAWASIdaPMGGMKDSGLGRRHGA 440
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
97-423 |
3.30e-59 |
|
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: 200.99 E-value: 3.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 97 ELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLL-ATIIPQY-LDKDLYPVINGGVPETT 174
Cdd:cd07151 123 ENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLlAKIFEEAgLPKGVLNVVVGAGSEIG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 175 ELLKE----RFdhILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYI 250
Cdd:cd07151 203 DAFVEhpvpRL--ISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 251 LCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIEgQKVAYGGT----GDAATRYIAPTILTDVD 325
Cdd:cd07151 281 IVHEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIE-QAVEEGATllvgGEAEGNVLEPTVLSDVT 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 326 PQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHsLPFGGV 405
Cdd:cd07151 360 NDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPH-VPFGGE 438
|
330
....*....|....*...
gi 22907049 406 GNSGMGSYHGKKSFETFS 423
Cdd:cd07151 439 KNSGLGRFNGEWALEEFT 456
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
4-422 |
1.08e-58 |
|
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: 199.72 E-value: 1.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSG--RTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIqklpEW 81
Cdd:cd07139 38 VDAAVAAARRAFDNGpwPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGPGPAALLRYYA----AL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADEPVEKTPQTQQ-DELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQyldK 160
Cdd:cd07139 114 ARDFPFEERRPGSGgGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEE---A 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 161 DLYP----VINGGVpETTELLKER--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAW 234
Cdd:cd07139 191 GLPPgvvnVVPADR-EVGEYLVRHpgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 235 GKFMNSGQTCVAPDYILCDPSIQNQIVEKLK---KSLKefYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYG 306
Cdd:cd07139 270 ASLMNNGQVCVALTRILVPRSRYDEVVEALAaavAALK--VGDPLDPATQIGPLASARQRERVEGYIakgraEGARLVTG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 307 GTGDAA-TR--YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSND----KVIKKMia 379
Cdd:cd07139 348 GGRPAGlDRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVerglAVARRI-- 425
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 22907049 380 etSSGGVAANDVIVHItlhSLPFGGVGNSGMGSYHGKKSFETF 422
Cdd:cd07139 426 --RTGTVGVNGFRLDF---GAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
2-427 |
1.40e-58 |
|
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: 199.50 E-value: 1.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 2 SKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNewnaYYEEVVYVLEEIEyMIQklpeW 81
Cdd:cd07131 37 SDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKP----LAEGRGDVQEAID-MAQ----Y 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADEPVEKTPQTQQDEL-----YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSElsenMASLLATIIPQ 156
Cdd:cd07131 108 AAGEGRRLFGETVPSELpnkdaMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAE----DTPACALKLVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 157 YLDKDLYP--VIN---GGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVAC 229
Cdd:cd07131 184 LFAEAGLPpgVVNvvhGRGEEVGEALVEhpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 230 RRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKV 303
Cdd:cd07131 264 EGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLNYNeigkeEGATL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 304 AYGG---TGDAATR--YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMI 378
Cdd:cd07131 344 LLGGerlTGGGYEKgyFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRAR 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 22907049 379 AETSSGGVAANDVIVHITLHsLPFGGVGNSGMGSYH-GKKSFETFSHRRS 427
Cdd:cd07131 424 RDLEAGITYVNAPTIGAEVH-LPFGGVKKSGNGHREaGTTALDAFTEWKA 472
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
6-423 |
4.61e-58 |
|
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: 4.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 6 EAVKRARAAFSSG--RTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYE--EVVYVLEEIEYMIQKlpew 81
Cdd:cd07119 39 RAIAAARRAFDSGewPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDidDVANCFRYYAGLATK---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADEPVEKTPQTQQdelYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDK 160
Cdd:cd07119 115 ETGEVYDVPPHVIS---RTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 161 DLYPVINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFM 238
Cdd:cd07119 192 GVVNLVTGSGATVGAELAEspDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 239 NSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF---YGEDAkkSRDYGRIISARHFQRVMGLI-----EGQKVAYGG--- 307
Cdd:cd07119 272 NAGQVCSAGSRLLVEESIHDKFVAALAERAKKIklgNGLDA--DTEMGPLVSAEHREKVLSYIqlgkeEGARLVCGGkrp 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 308 TGDAATR--YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGG 385
Cdd:cd07119 350 TGDELAKgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGT 429
|
410 420 430
....*....|....*....|....*....|....*...
gi 22907049 386 VAANDviVHITLHSLPFGGVGNSGMGSYHGKKSFETFS 423
Cdd:cd07119 430 VWIND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
2-411 |
5.80e-58 |
|
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: 197.57 E-value: 5.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 2 SKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAAD----LHKNEWN--------AYYEEVVYVLE 69
Cdd:cd07110 19 EDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDngkpLDEAAWDvddvagcfEYYADLAEQLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 70 eieymiQKLPEwAADEPVEktpqtqQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASL 149
Cdd:cd07110 99 ------AKAER-AVPLPSE------DFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 150 LATIIPQY-LDKDLYPVINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLD 226
Cdd:cd07110 166 LAEIAAEAgLPPGVLNVVTGTGDEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 227 VACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EG 300
Cdd:cd07110 246 KAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIrVGDPLEEGVRLGPLVSQAQYEKVLSFIargkeEG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 301 QKVAYGGTGDAATR---YIAPTILTDVDPQSPVMQEEIFGPVLpivCVRSL---EEAIQFINQREKPLALYMFSSNDKVI 374
Cdd:cd07110 326 ARLLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVL---CVRSFateDEAIALANDSEYGLAAAVISRDAERC 402
|
410 420 430
....*....|....*....|....*....|....*..
gi 22907049 375 KKMIAETSSGGVAANdvIVHITLHSLPFGGVGNSGMG 411
Cdd:cd07110 403 DRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSGIG 437
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
6-411 |
2.02e-57 |
|
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: 196.03 E-value: 2.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 6 EAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKnewnAYYEEVVyvleEIEYMIQKLpEWAADE 85
Cdd:cd07145 25 EAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGK----PIKQSRV----EVERTIRLF-KLAAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 86 ---------PVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQ 156
Cdd:cd07145 96 akvlrgetiPVDAYEYNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 157 Y-LDKDLYPVINGGVPET-TELLK-ERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIA 233
Cdd:cd07145 176 AgLPPGVINVVTGYGSEVgDEIVTnPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 234 WGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG 307
Cdd:cd07145 256 RGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVndaveKGGKILYGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 308 TGDAATrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVA 387
Cdd:cd07145 336 KRDEGS-FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVV 414
|
410 420
....*....|....*....|....
gi 22907049 388 ANDViVHITLHSLPFGGVGNSGMG 411
Cdd:cd07145 415 INDS-TRFRWDNLPFGGFKKSGIG 437
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
30-384 |
5.69e-57 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 193.41 E-value: 5.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 30 LEALQRLIQEQEQELVGALAADLHKNEWNAYYEeVVYVLEEIEYMiqklPEWAADEPVEKTPQTQQDE-LYIHSEPLGVV 108
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVE-VAFTADYIDYM----AEWARRYEGEIIQSDRPGEnILLFKRALGVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 109 LVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELL--KERFDHIL 185
Cdd:PRK10090 76 TGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELagNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 186 YTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLK 265
Cdd:PRK10090 156 MTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 266 KSLKEF-YGEDAKKSR-DYGRIISARHFQRVMGLI-----EGQKVAYGGTGDAATRYI-APTILTDVDPQSPVMQEEIFG 337
Cdd:PRK10090 236 EAMQAVqFGNPAERNDiAMGPLINAAALERVEQKVaraveEGARVALGGKAVEGKGYYyPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 22907049 338 PVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSG 384
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFG 362
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
99-415 |
1.44e-56 |
|
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: 193.73 E-value: 1.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 99 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVINGGVPETTELL 177
Cdd:cd07146 115 FTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 178 --KERFDHILYTGSTGVGKIIM-TAAAKHLTpvtLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDP 254
Cdd:cd07146 195 itHPDVDLVTFTGGVAVGKAIAaTAGYKRQL---LELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 255 SIQNQIVEKL-KKSLKEFYGEDAKKSRDYGRIIS---ARHFQ-RVMGLIE-GQKVAYGGTGDAAtrYIAPTILTDVDPQS 328
Cdd:cd07146 272 SVADEFVDLLvEKSAALVVGDPMDPATDMGTVIDeeaAIQIEnRVEEAIAqGARVLLGNQRQGA--LYAPTVLDHVPPDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 329 PVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDViVHITLHSLPFGGVGNS 408
Cdd:cd07146 350 ELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEV-PGFRSELSPFGGVKDS 428
|
....*..
gi 22907049 409 GMGSYHG 415
Cdd:cd07146 429 GLGGKEG 435
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
7-424 |
1.11e-55 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 192.64 E-value: 1.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 7 AVKRARAAFSSGRTR-----PLQFRIQQLEALQRLIQEQEQELVGALAAD----LHKNEWNA--------YYEEVVYVLE 69
Cdd:PLN02467 50 AVEAARKAFKRNKGKdwartTGAVRAKYLRAIAAKITERKSELAKLETLDcgkpLDEAAWDMddvagcfeYYADLAEALD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 70 EIEYMIQKLPewaadepvektpqTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELsenmASL 149
Cdd:PLN02467 130 AKQKAPVSLP-------------METFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSEL----ASV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 150 ----LATIIPQY-LDKDLYPVINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKN 222
Cdd:PLN02467 193 tcleLADICREVgLPPGVLNVVTGLGTEAGAPLAShpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 223 CDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI--- 298
Cdd:PLN02467 273 VDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIkISDPLEEGCRLGPVVSEGQYEKVLKFIsta 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 299 --EGQKVAYGGT---GDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKV 373
Cdd:PLN02467 353 ksEGATILCGGKrpeHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLER 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 22907049 374 IKKMIAETSSGGVAANdvIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSH 424
Cdd:PLN02467 433 CERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSGFGRELGEWGLENYLS 481
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
4-427 |
1.57e-55 |
|
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: 191.25 E-value: 1.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAF-SSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYyEEVVYVLEEIEYMIQKLPEWA 82
Cdd:cd07082 40 ILEAAETAYDAGrGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL-KEVDRTIDYIRDTIEELKRLD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 83 ADE-PVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDK 160
Cdd:cd07082 119 GDSlPGDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 161 DLYPVINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKhlTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFM 238
Cdd:cd07082 199 GVVNVVTGRGREIGDPLVThgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 239 NSGQTCVAPDYILCDPSIQNQIVEKLKK---SLKEFYGEDA---------KKSRDYgriisarhfqrVMGLIE-----GQ 301
Cdd:cd07082 277 YSGQRCTAIKRVLVHESVADELVELLKEevaKLKVGMPWDNgvditplidPKSADF-----------VEGLIDdavakGA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 302 KVAYGGTGDAATrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAET 381
Cdd:cd07082 346 TVLNGGGREGGN-LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADAL 424
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 22907049 382 SSGGVAANDVIVHITLHsLPFGGVGNSGMGSYHGKKSFETFSHRRS 427
Cdd:cd07082 425 EVGTVNINSKCQRGPDH-FPFLGRKDSGIGTQGIGDALRSMTRRKG 469
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
4-415 |
5.20e-55 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 191.25 E-value: 5.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYyEEVVYVLEEIEYMIQKLPEWAA 83
Cdd:PRK09407 56 VEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAF-EEVLDVALTARYYARRAPKLLA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 DE------PVektpQTQQDELYIhsePLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSelSENMASLLATIIPQY 157
Cdd:PRK09407 135 PRrragalPV----LTKTTELRQ---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPD--SQTPLTALAAVELLY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 158 ---LDKDLYPVINGGVPETTELLKERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAW 234
Cdd:PRK09407 206 eagLPRDLWQVVTGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 235 GKFMNSGQTCVAPDYILCDPSIQNQIVEKL---KKSLKefYGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYG 306
Cdd:PRK09407 286 ACFSNAGQLCISIERIYVHESIYDEFVRAFvaaVRAMR--LGAGYDYSADMGSLISEAQLETVSAHVDdavakGATVLAG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 307 GTG--DAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSG 384
Cdd:PRK09407 364 GKArpDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAG 443
|
410 420 430
....*....|....*....|....*....|...
gi 22907049 385 GVAANDVIVhITLHSL--PFGGVGNSGMGSYHG 415
Cdd:PRK09407 444 TVNVNEGYA-AAWGSVdaPMGGMKDSGLGRRHG 475
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
7-431 |
9.38e-55 |
|
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: 188.74 E-value: 9.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 7 AVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLhKNEWNAYYEEVVYVLEEIEYMIQKLPEWAAdep 86
Cdd:cd07107 24 AVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDC-GNPVSAMLGDVMVAAALLDYFAGLVTELKG--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 87 vEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVI 166
Cdd:cd07107 100 -ETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 167 NGGVPETTELLKERFD--HILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGkfMN---SG 241
Cdd:cd07107 179 PGDGATAGAALVRHPDvkRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAG--MNftwCG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 242 QTCVAPDYILCDPSIQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG---TGDAA 312
Cdd:cd07107 257 QSCGSTSRLFVHESIYDEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIdsakrEGARLVTGGgrpEGPAL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 313 TR--YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAND 390
Cdd:cd07107 337 EGgfYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWING 416
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 22907049 391 VIVHITlhSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVR 431
Cdd:cd07107 417 SSRHFL--GAPFGGVKNSGIGREECLEELLSYTQEKNVNVR 455
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
6-412 |
1.60e-54 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 189.76 E-value: 1.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 6 EAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNeWNayyEEVVYVLEEI---EYMIQKLPEWA 82
Cdd:PRK03137 77 KAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKP-WA---EADADTAEAIdflEYYARQMLKLA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 83 ADEPVEKTPQTQQDELYIhsePLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKD 161
Cdd:PRK03137 153 DGKPVESRPGEHNRYFYI---PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 162 LYPVINGGVPETTELL----KERFdhILYTGSTGVGKIIMTAAAK------HLTPVTLELGGKSPCYVDKNCDLDVACRR 231
Cdd:PRK03137 230 VVNFVPGSGSEVGDYLvdhpKTRF--ITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAES 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 232 IAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYG 306
Cdd:PRK03137 308 IVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEigkeeGRLVLGG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 307 GTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGV 386
Cdd:PRK03137 388 EGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNL 467
|
410 420 430
....*....|....*....|....*....|..
gi 22907049 387 AAND------VIVHitlhslPFGGVGNSGMGS 412
Cdd:PRK03137 468 YFNRgctgaiVGYH------PFGGFNMSGTDS 493
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
4-411 |
1.12e-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: 186.10 E-value: 1.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEevvyVLEEIEYMiqKLpewAA 83
Cdd:cd07094 23 AEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVE----VDRAIDTL--RL---AA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 DE---------PVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATII 154
Cdd:cd07094 94 EEaerirgeeiPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 155 -PQYLDKDLYPVINGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKhlTPVTLELGGKSPCYVDKNCDLDVACRR 231
Cdd:cd07094 174 vEAGVPEGVLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 232 IAWGKFMNSGQTCVAPDYILcdpsiqnqIVEKLKKSLKEFYGEDAKKSR---------DYGRIISARHFQRVMGLIE--- 299
Cdd:cd07094 252 LAKGGFYHAGQVCISVQRIY--------VHEELYDEFIEAFVAAVKKLKvgdpldedtDVGPLISEEAAERVERWVEeav 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 300 --GQKVAYGGTGDAATRYiaPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKM 377
Cdd:cd07094 324 eaGARLLCGGERDGALFK--PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKA 401
|
410 420 430
....*....|....*....|....*....|....
gi 22907049 378 IAETSSGGVAANDViVHITLHSLPFGGVGNSGMG 411
Cdd:cd07094 402 AEKLEVGGVMVNDS-SAFRTDWMPFGGVKESGVG 434
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
4-431 |
1.24e-53 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 186.58 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSgrTRPLQFR-IQQLEALQRLIQ--EQEQELVGALAA-DLHKNEWNAYYEEVVYVLEEIEYMiqklP 79
Cdd:cd07143 46 VDIAVEVAHAAFET--DWGLKVSgSKRGRCLSKLADlmERNLDYLASIEAlDNGKTFGTAKRVDVQASADTFRYY----G 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 80 EWAaDEPVEKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY- 157
Cdd:cd07143 120 GWA-DKIHGQVIETDIKKLtYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAg 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 158 LDKDLYPVINGGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVACRRIAW 234
Cdd:cd07143 199 FPPGVINVVSGYGRTCGNAISShmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAY 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 235 GKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGGT 308
Cdd:cd07143 279 GIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLkVGDPFAEDTFQGPQVSQIQYERIMSYIEsgkaeGATVETGGK 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 309 --GDAATrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGV 386
Cdd:cd07143 359 rhGNEGY-FIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTV 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 22907049 387 AANDV-IVHitlHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLVR 431
Cdd:cd07143 438 WVNCYnLLH---HQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
92-430 |
1.88e-53 |
|
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: 186.01 E-value: 1.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 92 QTQQDELYIH-SEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGV 170
Cdd:cd07559 123 EIDEDTLSYHfHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 171 PETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYV-----DKNCDLDVACRRIAWGKFMNSGQT 243
Cdd:cd07559 203 SEAGKPLAShpRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFAFNQGEV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 244 CVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG-----TGDAA 312
Cdd:cd07559 283 CTCPSRALVQESIYDEFIERAVERFEAIkVGNPLDPETMMGAQVSKDQLEKILSYVdigkeEGAEVLTGGerltlGGLDK 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 313 TRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdvi 392
Cdd:cd07559 363 GYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--- 439
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 22907049 393 vhiTLHSLP----FGGVGNSGMGSYHGKKSFETFSHRRSCLV 430
Cdd:cd07559 440 ---CYHQYPahapFGGYKKSGIGRETHKMMLDHYQQTKNILV 478
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
4-412 |
2.64e-52 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 182.80 E-value: 2.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSS-GRTRPLQfRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYM---IQKLP 79
Cdd:PRK13473 41 VDAAVAAADAAFPEwSQTTPKE-RAEALLKLADAIEENADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFagaARCLE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 80 EWAADEPVEKtpQTQqdelYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIpqyld 159
Cdd:PRK13473 120 GKAAGEYLEG--HTS----MIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELA----- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 KDLYP--VIN---GGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRI 232
Cdd:PRK13473 189 ADILPpgVLNvvtGRGATVGDALvgHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 233 AWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLK---KSLKefYGEDAKKSRDYGRIISARHFQRVMGLIE---GQK---- 302
Cdd:PRK13473 269 RTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAaavATLK--VGDPDDEDTELGPLISAAHRDRVAGFVErakALGhirv 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 303 VAYGGTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETS 382
Cdd:PRK13473 347 VTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQ 426
|
410 420 430
....*....|....*....|....*....|.
gi 22907049 383 SGGVAANDvivHITLHS-LPFGGVGNSGMGS 412
Cdd:PRK13473 427 YGCTWVNT---HFMLVSeMPHGGQKQSGYGK 454
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
4-427 |
3.27e-52 |
|
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: 182.69 E-value: 3.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSG---RTRPLQfRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMiqklPE 80
Cdd:cd07142 43 VDRAVKAARKAFDEGpwpRMTGYE-RSRILLRFADLLEKHADELAALETWDNGKPYEQARYAEVPLAARLFRYY----AG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 81 WAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LD 159
Cdd:cd07142 118 WADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 KDLYPVINGGVPETTELLKERF--DHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGK 236
Cdd:cd07142 198 DGVLNIVTGFGPTAGAAIASHMdvDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFAL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 237 FMNSGQTCVAPDYILCDPSIQNQIVEKLK-KSLKEFYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG--T 308
Cdd:cd07142 278 FFNQGQCCCAGSRTFVHESIYDEFVEKAKaRALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIehgkeEGATLITGGdrI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 309 GDAATrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAA 388
Cdd:cd07142 358 GSKGY-YIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWV 436
|
410 420 430
....*....|....*....|....*....|....*....
gi 22907049 389 NdvIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRS 427
Cdd:cd07142 437 N--CYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKA 473
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
88-423 |
3.39e-51 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 179.62 E-value: 3.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 88 EKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVI 166
Cdd:TIGR01804 117 EIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 167 NGGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTC 244
Cdd:TIGR01804 197 QGDGAEVGPLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVC 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 245 VAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG-------TGDA 311
Cdd:TIGR01804 277 SNGTRVFVHKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIekgkaEGATLATGGgrpenvgLQNG 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 312 AtrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDv 391
Cdd:TIGR01804 357 F--FVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT- 433
|
330 340 350
....*....|....*....|....*....|..
gi 22907049 392 iVHITLHSLPFGGVGNSGMGSYHGKKSFETFS 423
Cdd:TIGR01804 434 -YNLYPAEAPFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
4-423 |
2.56e-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: 177.54 E-value: 2.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSG---RTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYmiqkLPE 80
Cdd:cd07141 46 VDKAVKAARAAFKLGspwRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRY----YAG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 81 WAaDEPVEKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQyld 159
Cdd:cd07141 122 WA-DKIHGKTIPMDGDFFtYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKE--- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 kDLYP--VIN---GGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVACRR 231
Cdd:cd07141 198 -AGFPpgVVNvvpGYGPTAGAAISSHpdIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 232 IAWGKFMNSGQTCVAPDYILCDPSIQNQIVEK-LKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAY 305
Cdd:cd07141 277 AHEALFFNMGQCCCAGSRTFVQESIYDEFVKRsVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIesgkkEGAKLEC 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 306 GGT--GDAATrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN-DKVIkkmiaeTS 382
Cdd:cd07141 357 GGKrhGDKGY-FIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDiDKAI------TF 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 22907049 383 SGGVAANDVIV----HITLHSlPFGGVGNSGMGSYHGKKSFETFS 423
Cdd:cd07141 430 SNALRAGTVWVncynVVSPQA-PFGGYKMSGNGRELGEYGLQEYT 473
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
2-430 |
7.15e-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: 176.49 E-value: 7.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 2 SKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLpew 81
Cdd:cd07117 38 ADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVI--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADEpvEKTPQTQQDELYI-HSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDK 160
Cdd:cd07117 115 RAEE--GSANMIDEDTLSIvLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 161 DLYPVINGGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFM 238
Cdd:cd07117 193 GVVNIVTGKGSKSGEYLLNHpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 239 NSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG----- 307
Cdd:cd07117 273 NQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVkVGNPLDPDTQMGAQVNKDQLDKILSYVdiakeEGAKILTGGhrlte 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 308 TGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVA 387
Cdd:cd07117 353 NGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVW 432
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 22907049 388 ANdvIVHITLHSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 430
Cdd:cd07117 433 VN--TYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYI 473
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
104-430 |
2.21e-49 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 175.06 E-value: 2.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 104 PLGVVLVIGTWNYPF-----NLTIqpmvgAIAAGNSVVLKPSELsenmASLLATIIPQYL-----DKDLYP----VINGG 169
Cdd:cd07086 133 PLGVVGVITAFNFPVavpgwNAAI-----ALVCGNTVVWKPSET----TPLTAIAVTKILaevleKNGLPPgvvnLVTGG 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 170 VpETTELLK--ERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAP 247
Cdd:cd07086 204 G-DGGELLVhdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTT 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 248 DYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGG---TGDAATRYIAP 318
Cdd:cd07086 283 RRLIVHESVYDEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNAIEiaksqGGTVLTGGkriDGGEPGNYVEP 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 319 TILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN-DKVIKKMIAETSSGGvaandvIVHITL 397
Cdd:cd07086 363 TIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDlREAFRWLGPKGSDCG------IVNVNI 436
|
330 340 350
....*....|....*....|....*....|....*....
gi 22907049 398 HS------LPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 430
Cdd:cd07086 437 PTsgaeigGAFGGEKETGGGRESGSDAWKQYMRRSTCTI 475
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
4-411 |
8.08e-49 |
|
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: 172.82 E-value: 8.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHK--NEWNAyyeEVVYVLEEIEymiqklpeW 81
Cdd:cd07147 23 IEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKpiKDARG---EVARAIDTFR--------I 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADE---------PVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLAT 152
Cdd:cd07147 92 AAEEatriygevlPLDISARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 153 II-PQYLDKDLYPVINGGVPETTELLK-ERFDHILYTGSTGVGKIIMTAAAKHltPVTLELGGKSPCYVDKNCDLDVACR 230
Cdd:cd07147 172 VLaETGLPKGAFSVLPCSRDDADLLVTdERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFAAQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 231 RIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKL---KKSLKEfyGEDAKKSRDYGRIISARHFQRVMGLIE-----GQK 302
Cdd:cd07147 250 RIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLvarVKALKT--GDPKDDATDVGPMISESEAERVEGWVNeavdaGAK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 303 VAYGGTGDAATryIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETS 382
Cdd:cd07147 328 LLTGGKRDGAL--LEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELE 405
|
410 420
....*....|....*....|....*....
gi 22907049 383 SGGVAANDVIVhITLHSLPFGGVGNSGMG 411
Cdd:cd07147 406 VGGVVINDVPT-FRVDHMPYGGVKDSGIG 433
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
100-423 |
1.87e-48 |
|
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: 172.14 E-value: 1.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 100 IHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQ--YLDKDLYPVINGGVPETTELL 177
Cdd:cd07120 113 VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEipSLPAGVVNLFTESGSEGAAHL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 178 KE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 255
Cdd:cd07120 193 VAspDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 256 IQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE------GQKVAYGGTGD---AATRYIAPTILTDVD 325
Cdd:cd07120 273 IADEVRDRLAARLAAVkVGPGLDPASDMGPLIDRANVDRVDRMVEraiaagAEVVLRGGPVTeglAKGAFLRPTLLEVDD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 326 PQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDvivHITLHS-LPFGG 404
Cdd:cd07120 353 PDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND---WNKLFAeAEEGG 429
|
330
....*....|....*....
gi 22907049 405 VGNSGMGSYHGKKSFETFS 423
Cdd:cd07120 430 YRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
1-426 |
8.47e-48 |
|
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: 170.78 E-value: 8.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 1 MSKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYyEEVVYVLEEIEYMIQkLPE 80
Cdd:cd07085 37 AEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADAR-GDVLRGLEVVEFACS-IPH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 81 WAADEPVEKTpQTQQDELYIHsEPLGVVLVIGTWNYPF--NLTIQPMvgAIAAGNSVVLKPSELSENMASLLATIIPQY- 157
Cdd:cd07085 115 LLKGEYLENV-ARGIDTYSYR-QPLGVVAGITPFNFPAmiPLWMFPM--AIACGNTFVLKPSERVPGAAMRLAELLQEAg 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 158 LDKDLYPVINGGVPETTELLkerfDH-----ILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRI 232
Cdd:cd07085 191 LPDGVLNVVHGGKEAVNALL----DHpdikaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANAL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 233 AWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLK---KSLKEFYGEDAKKsrDYGRIISARHFQRVMGLI-----EGQKVA 304
Cdd:cd07085 267 VGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVeraKKLKVGAGDDPGA--DMGPVISPAAKERIEGLIesgveEGAKLV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 305 YGGTGDAATRY-----IAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIA 379
Cdd:cd07085 345 LDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQR 424
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 22907049 380 ETSSGGVAANdVIVHITLHSLPFGGVGNSGMGSYH--GKKSFETFSHRR 426
Cdd:cd07085 425 EVDAGMVGIN-VPIPVPLAFFSFGGWKGSFFGDLHfyGKDGVRFYTQTK 472
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
4-416 |
1.05e-47 |
|
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: 170.65 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMiqklPEWAa 83
Cdd:cd07111 61 VDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHH----AGWA- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 depvektpQTQQDELYIHsEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQyldKDLY 163
Cdd:cd07111 136 --------QLLDTELAGW-KPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAE---AGLP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 164 P-VIN--GGVPETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFM 238
Cdd:cd07111 204 PgVLNivTGNGSFGSALANhpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWF 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 239 NSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIEGQKvAYGG----TGDAAT 313
Cdd:cd07111 284 NQGQVCCAGSRLLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGAdvfqPGADLP 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 314 R---YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAND 390
Cdd:cd07111 363 SkgpFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING 442
|
410 420 430
....*....|....*....|....*....|.
gi 22907049 391 vivhitlHSL-----PFGGVGNSGMGSYHGK 416
Cdd:cd07111 443 -------HNLfdaaaGFGGYRESGFGREGGK 466
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
2-415 |
5.57e-47 |
|
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: 169.30 E-value: 5.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 2 SKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNeWNAYYEEVVYVLEEIEYMIQKLPEW 81
Cdd:cd07083 55 AEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKN-WVEAIDDVAEAIDFIRYYARAALRL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADEPVEKTPQTQQDELYIhsEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSElsenMASLLATIIPQYLDKD 161
Cdd:cd07083 134 RYPAVEVVPYPGEDNESFY--VGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAE----DAVVVGYKVFEIFHEA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 162 LYP--VINGgVPETTELL------KERFDHILYTGSTGVGKIIMTAAAKHLT------PVTLELGGKSPCYVDKNCDLDV 227
Cdd:cd07083 208 GFPpgVVQF-LPGVGEEVgaylteHERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFEL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 228 ACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQ 301
Cdd:cd07083 287 VVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEhgkneGQ 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 302 KVAYGGTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSSNDKVIKKMIA 379
Cdd:cd07083 367 LVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDddFAEALEVANSTPYGLTGGVYSRKREHLEEARR 446
|
410 420 430
....*....|....*....|....*....|....*.
gi 22907049 380 ETSSGGVAANDVIVHITLHSLPFGGVGNSGMGSYHG 415
Cdd:cd07083 447 EFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
103-431 |
3.83e-46 |
|
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: 166.46 E-value: 3.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 103 EPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSE----NMASLL--ATIIPQYLDkdlypVINGGVPETTEL 176
Cdd:cd07113 141 EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPltllRVAELAkeAGIPDGVLN-----VVNGKGAVGAQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 177 LKE-RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPS 255
Cdd:cd07113 216 ISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRS 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 256 IQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGGTGDAATRY-IAPTILTDVDPQS 328
Cdd:cd07113 296 KFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEALAGEGYfVQPTLVLARSADS 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 329 PVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdviVHITLH-SLPFGGVGN 407
Cdd:cd07113 376 RLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDpAVPFGGMKQ 452
|
330 340
....*....|....*....|....
gi 22907049 408 SGMGSYHGKKSFETFSHRRSCLVR 431
Cdd:cd07113 453 SGIGREFGSAFIDDYTELKSVMIR 476
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
4-423 |
2.25e-45 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 164.68 E-value: 2.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSG---RTRPLQfRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQklpe 80
Cdd:PRK09847 59 IDRAVSAARGVFERGdwsLSSPAK-RKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDDIPGAARAIRWYAE---- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 81 wAADEPVEKTPQTQQDEL-YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-L 158
Cdd:PRK09847 134 -AIDKVYGEVATTSSHELaMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 159 DKDLYPVINGGVPETTELLKER--FDHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNC-DLDVACRRIAW 234
Cdd:PRK09847 213 PDGVLNVVTGFGHEAGQALSRHndIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 235 GKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLIEG----QKVAYGGTG 309
Cdd:PRK09847 293 GIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIREgeskGQLLLDGRN 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 310 DAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAAN 389
Cdd:PRK09847 373 AGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVN 452
|
410 420 430
....*....|....*....|....*....|....*....
gi 22907049 390 -----DVIVhitlhslPFGGVGNSGMGSYHGKKSFETFS 423
Cdd:PRK09847 453 nyndgDMTV-------PFGGYKQSGNGRDKSLHALEKFT 484
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
4-409 |
8.59e-44 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 158.97 E-value: 8.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAyyeevvyvLEEIEYMIQK--LPEW 81
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA--------QTEVAAMAGKidISIK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADEPV-EKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATII-PQYLD 159
Cdd:cd07095 74 AYHERTgERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 KDLYPVINGGVPETTELL-KERFDHILYTGSTGVGKIIMTAAAKHltP---VTLELGGKSPCYVDKNCDLDVACRRIAWG 235
Cdd:cd07095 154 PGVLNLVQGGRETGEALAaHEGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 236 KFMNSGQTCV-APDYILCDPSIQNQIVEKLKKSLKEFY--GEDAKKSRDYGRIISA------RHFQRVMGLiEGQKVAYG 306
Cdd:cd07095 232 AFLTAGQRCTcARRLIVPDGAVGDAFLERLVEAAKRLRigAPDAEPPFMGPLIIAAaaarylLAQQDLLAL-GGEPLLAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 307 GTGDAATRYIAPTILtDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGV 386
Cdd:cd07095 311 ERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIV 389
|
410 420
....*....|....*....|....*
gi 22907049 387 AANdviVHITLHS--LPFGGVGNSG 409
Cdd:cd07095 390 NWN---RPTTGASstAPFGGVGLSG 411
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
7-435 |
6.70e-43 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 158.06 E-value: 6.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 7 AVKRARAAFSSGR-TRPLQF-RIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQklpewAAD 84
Cdd:PLN02766 63 AVKAAREAFDHGPwPRMSGFeRGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAG-----AAD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 85 E-PVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKD-L 162
Cdd:PLN02766 138 KiHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDgV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 163 YPVINGGVPETTELLKERFD--HILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMN 239
Cdd:PLN02766 218 INVVTGFGPTAGAAIASHMDvdKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYN 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 240 SGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSR-DYGRIISARHFQRVMGLI-----EGQKVAYGG--TGDA 311
Cdd:PLN02766 298 KGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRaRQGPQVDKQQFEKILSYIehgkrEGATLLTGGkpCGDK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 312 ATrYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVikkmiAETSSGGVAANDV 391
Cdd:PLN02766 378 GY-YIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDV-----ANTVSRSIRAGTI 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 22907049 392 IVHITL---HSLPFGGVGNSGMGSYHGKKSFETFSHRRScLVRPLMN 435
Cdd:PLN02766 452 WVNCYFafdPDCPFGGYKMSGFGRDQGMDALDKYLQVKS-VVTPLYN 497
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
4-435 |
7.24e-43 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 158.43 E-value: 7.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSG---RTRPLQfRIQQLEALQRLIQEQEQELvGALAAdlhkneWNA--YYEEVVYVleEIEYMIQKL 78
Cdd:PLN02466 97 VNRAVAAARKAFDEGpwpKMTAYE-RSRILLRFADLLEKHNDEL-AALET------WDNgkPYEQSAKA--ELPMFARLF 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 79 PEWA--ADE------PVEKTPQTQQdelyIHsEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSE---LSENMA 147
Cdd:PLN02466 167 RYYAgwADKihgltvPADGPHHVQT----LH-EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEqtpLSALYA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 148 SLL---ATIIPQYLDkdlypVINGGVPETTELLKERF--DHILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDK 221
Cdd:PLN02466 242 AKLlheAGLPPGVLN-----VVSGFGPTAGAALASHMdvDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 222 NCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLK-KSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIE- 299
Cdd:PLN02466 317 DADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKaRALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKs 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 300 ----GQKVAYGGtGDAATR--YIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKV 373
Cdd:PLN02466 397 gvesGATLECGG-DRFGSKgyYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDT 475
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22907049 374 IKKMIAETSSGGVAAN--DVIVhitlHSLPFGGVGNSGMGSYHGKKSFETFSHRRScLVRPLMN 435
Cdd:PLN02466 476 ANTLSRALRVGTVWVNcfDVFD----AAIPFGGYKMSGIGREKGIYSLNNYLQVKA-VVTPLKN 534
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
99-430 |
6.72e-42 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 155.04 E-value: 6.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 99 YIHSEPLGVVLVIGTWNYPfnltIQ-------PmvgAIAAGNSVVLKPSELSENMASLLATIIPQY-LDKDLYPVING-G 169
Cdd:PRK13252 137 YTRREPLGVCAGIGAWNYP----IQiacwksaP---ALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVVQGdG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 170 vpETTELLKE--RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAP 247
Cdd:PRK13252 210 --RVGAWLTEhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNG 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 248 DYILCDPSIQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG---TGDAATR--YI 316
Cdd:PRK13252 288 TRVFVQKSIKAAFEARLLERVERIRiGDPMDPATNFGPLVSFAHRDKVLGYIekgkaEGARLLCGGerlTEGGFANgaFV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 317 APTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN----DKVIKKMIAET----SSGGVAA 388
Cdd:PRK13252 368 APTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADlsraHRVIHQLEAGIcwinTWGESPA 447
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 22907049 389 ndvivhitlhSLPFGGVGNSGMGSYHGKKSFETFSHRRSCLV 430
Cdd:PRK13252 448 ----------EMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
99-411 |
8.72e-38 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 143.79 E-value: 8.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 99 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSenmaSLLATIIPQYLDKDLYP--VINGgVPETTEL 176
Cdd:cd07140 142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVT----PLTALKFAELTVKAGFPkgVINI-LPGSGSL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 177 LKERF-DH-----ILYTGSTGVGKIIMTAAAK-HLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDY 249
Cdd:cd07140 217 VGQRLsDHpdvrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 250 ILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVM-----GLIEGQKVAYGGTG-DAATRYIAPTILT 322
Cdd:cd07140 297 LFVEESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLVeycerGVKEGATLVYGGKQvDRPGFFFEPTVFT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 323 DVDPQSPVMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSsndKVIKKmiAETSSGGVAANDVIVHI---TL 397
Cdd:cd07140 377 DVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFT---KDINK--ALYVSDKLEAGTVFVNTynkTD 451
|
330
....*....|....
gi 22907049 398 HSLPFGGVGNSGMG 411
Cdd:cd07140 452 VAAPFGGFKQSGFG 465
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
2-411 |
1.98e-37 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 142.31 E-value: 1.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 2 SKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYyEEVVYVLEEIEYMIQKLPEW 81
Cdd:PRK13968 29 DDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVAKSANLCDWYAEHGPAM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADEP--VEktpqTQQdeLYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQY-L 158
Cdd:PRK13968 108 LKAEPtlVE----NQQ--AVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAgI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 159 DKDLYPVINGGVPETTELLKE-RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKF 237
Cdd:PRK13968 182 PQGVYGWLNADNDGVSQMINDsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 238 MNSGQTCVAPDYILCDPSIQNQIVEKL---KKSLKefYGEDAKKSRDYGRIisAR-------HFQRVMGLIEGQKVAYGG 307
Cdd:PRK13968 262 QNTGQVCAAAKRFIIEEGIASAFTERFvaaAAALK--MGDPRDEENALGPM--ARfdlrdelHHQVEATLAEGARLLLGG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 308 TGDA-ATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGV 386
Cdd:PRK13968 338 EKIAgAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGV 417
|
410 420 430
....*....|....*....|....*....|
gi 22907049 387 -----AANDVIVhitlhslPFGGVGNSGMG 411
Cdd:PRK13968 418 fingyCASDARV-------AFGGVKKSGFG 440
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
70-422 |
1.72e-36 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 140.04 E-value: 1.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 70 EIEYMIQKLpEWAADEPV----EKTPQTQQDE-LYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSE 144
Cdd:PRK11241 108 EISYAASFI-EWFAEEGKriygDTIPGHQADKrLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 145 NMASLLATI-----IPqyldKDLYPVINGGVPET-TELLKERFDHIL-YTGSTGVGKIIMTAAAKHLTPVTLELGGKSPC 217
Cdd:PRK11241 187 FSALALAELairagIP----AGVFNVVTGSAGAVgGELTSNPLVRKLsFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPF 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 218 YVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFY-GEDAKKSRDYGRIISARHFQRVMG 296
Cdd:PRK11241 263 IVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 297 LIE-----GQKVAYGGTGDA-ATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN 370
Cdd:PRK11241 343 HIAdalekGARVVCGGKAHElGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARD 422
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 22907049 371 DKVIKKMIAETSSGGVAANDVIvhITLHSLPFGGVGNSGMGSYHGKKSFETF 422
Cdd:PRK11241 423 LSRVFRVGEALEYGIVGINTGI--ISNEVAPFGGIKASGLGREGSKYGIEDY 472
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
4-411 |
7.06e-35 |
|
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: 135.79 E-value: 7.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEevvyVLEEIEY-------MIQ 76
Cdd:cd07125 71 VDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAE----VREAIDFcryyaaqARE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 77 KLPEWAADEPVEKTPQtqqdelyIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATI--- 153
Cdd:cd07125 147 LFSDPELPGPTGELNG-------LELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELlhe 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 154 --IPQYLdkdLYPVINGGVPETTELLK-ERFDHILYTGSTGVGKIIMTAAAKH---LTPVTLELGGKSPCYVDKNCDLDV 227
Cdd:cd07125 220 agVPRDV---LQLVPGDGEEIGEALVAhPRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPEQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 228 ACRRIAWGKFMNSGQTCVAPDyILCdpsIQNQIVEKLKKSLKefygeDAKKS----------RDYGRIISARHFQRVMGL 297
Cdd:cd07125 297 AVKDVVQSAFGSAGQRCSALR-LLY---LQEEIAERFIEMLK-----GAMASlkvgdpwdlsTDVGPLIDKPAGKLLRAH 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 298 IE---GQK--VAYGGTGDAATRYIAPTILTDVDpqSPVMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSSN 370
Cdd:cd07125 368 TElmrGEAwlIAPAPLDDGNGYFVAPGIIEIVG--IFDLTTEVFGPILHVIRFKAedLDEAIEDINATGYGLTLGIHSRD 445
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 22907049 371 DKVIKKMIAETSSGGVAANDVIVHITLHSLPFGGVGNSGMG 411
Cdd:cd07125 446 EREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTG 486
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
99-430 |
6.08e-34 |
|
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: 132.96 E-value: 6.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 99 YIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELL- 177
Cdd:cd07116 131 YHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLa 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 178 -KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSP--CYVDKNCDLDVACRRIAWGKFM---NSGQTCVAPDYIL 251
Cdd:cd07116 211 sSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniFFADVMDADDAFFDKALEGFVMfalNQGEVCTCPSRAL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 252 CDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLI-----EGQKVAYGG-----TGDAATRYIAPTI 320
Cdd:cd07116 291 IQESIYDRFMERALERVKAIkQGNPLDTETMIGAQASLEQLEKILSYIdigkeEGAEVLTGGernelGGLLGGGYYVPTT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 321 LTDVDpQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdvIVHITLHSL 400
Cdd:cd07116 371 FKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLYPAHA 447
|
330 340 350
....*....|....*....|....*....|
gi 22907049 401 PFGGVGNSGMGSYHGKKSFETFSHRRSCLV 430
Cdd:cd07116 448 AFGGYKQSGIGRENHKMMLDHYQQTKNLLV 477
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
4-419 |
1.77e-32 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 128.32 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIqEQEQELVGALAADLHKNEWNAYYEEVVYVLEEIEYMIQKLPEWAA 83
Cdd:PRK09406 25 VDAAIARAHARFRDYRTTTFAQRARWANAAADLL-EAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEHAEALLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 DEPVEkTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPselsenmasllATIIPQ---YLDk 160
Cdd:PRK09406 104 DEPAD-AAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH-----------ASNVPQtalYLA- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 161 DLYPviNGGVPE---TTELL----------KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDV 227
Cdd:PRK09406 171 DLFR--RAGFPDgcfQTLLVgsgaveailrDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 228 ACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQ 301
Cdd:PRK09406 249 AAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALrVGDPTDPDTDVGPLATEQGRDEVEKQVDdavaaGA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 302 KVAYGGTG-DAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAE 380
Cdd:PRK09406 329 TILCGGKRpDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDD 408
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 22907049 381 TSSGGVAANDVIVhiTLHSLPFGGVGNSGMG---SYHGKKSF 419
Cdd:PRK09406 409 LEAGQVFINGMTV--SYPELPFGGVKRSGYGrelSAHGIREF 448
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
2-412 |
3.43e-32 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 127.95 E-value: 3.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 2 SKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYyEEVVYVLEEIEYmiqklpew 81
Cdd:PLN00412 53 EEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAV-TEVVRSGDLISY-------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 82 AADEPV-----------EKTPQTQQDELYIHSE-PLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSelSENMASL 149
Cdd:PLN00412 124 TAEEGVrilgegkflvsDSFPGNERNKYCLTSKiPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPP--TQGAVAA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 150 LATI-------IPqyldKDLYPVINGGVPETTELLKER--FDHILYTG-STGvgkiIMTAAAKHLTPVTLELGGKSPCYV 219
Cdd:PLN00412 202 LHMVhcfhlagFP----KGLISCVTGKGSEIGDFLTMHpgVNCISFTGgDTG----IAISKKAGMVPLQMELGGKDACIV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 220 DKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIE 299
Cdd:PLN00412 274 LEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVM 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 300 GQKvAYGGTgdAATRY------IAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN-DK 372
Cdd:PLN00412 354 DAK-EKGAT--FCQEWkregnlIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDiNK 430
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 22907049 373 VIkkMIAET-SSGGVAANDVIVHITLHsLPFGGVGNSGMGS 412
Cdd:PLN00412 431 AI--LISDAmETGTVQINSAPARGPDH-FPFQGLKDSGIGS 468
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
3-414 |
1.83e-31 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 125.76 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 3 KISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYyEEVVYVLEEIEYmiqklpewA 82
Cdd:TIGR01722 39 EVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDAL-GDVARGLEVVEH--------A 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 83 ADEPV----EKTPQTQQD-ELYIHSEPLGVVLVIGTWNYP--FNLTIQPMvgAIAAGNSVVLKPSELSENMASLLATIIP 155
Cdd:TIGR01722 110 CGVNSllkgETSTQVATRvDVYSIRQPLGVCAGITPFNFPamIPLWMFPI--AIACGNTFVLKPSEKVPSAAVKLAELFS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 156 QY-LDKDLYPVINGGVPETTELLKE-RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIA 233
Cdd:TIGR01722 188 EAgAPDGVLNVVHGDKEAVDRLLEHpDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 234 WGKFMNSGQTCVAPDYILCDPSIQN---QIVEKLKKsLKEFYGEDAkkSRDYGRIISARHFQRVMGLI-----EGQKVAY 305
Cdd:TIGR01722 268 GAAYGAAGQRCMAISAAVLVGAADEwvpEIRERAEK-IRIGPGDDP--GAEMGPLITPQAKDRVASLIaggaaEGAEVLL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 306 GGTGDAATRY-----IAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAE 380
Cdd:TIGR01722 345 DGRGYKVDGYeegnwVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHE 424
|
410 420 430
....*....|....*....|....*....|....*
gi 22907049 381 TSSGGVAANDVI-VHITLHSlpFGGVGNSGMGSYH 414
Cdd:TIGR01722 425 IEVGQVGVNVPIpVPLPYFS--FTGWKDSFFGDHH 457
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
2-411 |
2.79e-31 |
|
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: 124.84 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 2 SKISEAVKRARAAF-SSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKnewnAYYEEVVYVLEEIEYMiqklpE 80
Cdd:cd07148 21 AAIDKALDTAHALFlDRNNWLPAHERIAILERLADLMEERADELALLIAREGGK----PLVDAKVEVTRAIDGV-----E 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 81 WAADE---------PVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSelSENMASLLA 151
Cdd:cd07148 92 LAADElgqlggreiPMGLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA--LATPLSCLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 152 TIipqyldkDLypVINGGVPE-----------TTELL--KERFDHILYTGSTGVGKIIMTAAAKHlTPVTLELGGKSPCY 218
Cdd:cd07148 170 FV-------DL--LHEAGLPEgwcqavpcenaVAEKLvtDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 219 VDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKL-KKSLKEFYGEDAKKSRDYGRIISARHFQRVMGL 297
Cdd:cd07148 240 VDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLaAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 298 IE-----GQKVAYGGTGDAATRYiAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDK 372
Cdd:cd07148 320 VNeavaaGARLLCGGKRLSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLD 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 22907049 373 VIKKMIAETSSGGVAANDvivhitlHS------LPFGGVGNSGMG 411
Cdd:cd07148 399 VALKAVRRLDATAVMVND-------HTafrvdwMPFAGRRQSGYG 436
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
4-409 |
1.62e-30 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 123.14 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYyEEVVYVLEEIEYMIQKLPEwaa 83
Cdd:PRK09457 39 VDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAA-TEVTAMINKIAISIQAYHE--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 depveKTPQTQQD----ELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIipqYLD 159
Cdd:PRK09457 115 -----RTGEKRSEmadgAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKL---WQQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 KDLYP-VIN--GGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHltP---VTLELGGKSPCYVDKNCDLDVACRR 231
Cdd:PRK09457 187 AGLPAgVLNlvQGGRETGKALaaHPDIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 232 IAWGKFMNSGQTCVAPDYILCDPSIQNQ-IVEKLKKSLKEF-YGE-DAKKSRDYGRIISARHFQrvmGLIEGQK--VAYG 306
Cdd:PRK09457 265 IIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLtVGRwDAEPQPFMGAVISEQAAQ---GLVAAQAqlLALG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 307 GTG-------DAATRYIAPTILtDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIA 379
Cdd:PRK09457 342 GKSllemtqlQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLL 420
|
410 420 430
....*....|....*....|....*....|
gi 22907049 380 ETSSGGVAANDVIVHITlHSLPFGGVGNSG 409
Cdd:PRK09457 421 EIRAGIVNWNKPLTGAS-SAAPFGGVGASG 449
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
100-370 |
4.75e-29 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 118.85 E-value: 4.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 100 IHSE-----------PLGVVLVIGTWNYP-----FNLTIqpmvgAIAAGNSVVLKPSELsenmASLLA----TIIPQYLD 159
Cdd:cd07130 117 IPSErpghrmmeqwnPLGVVGVITAFNFPvavwgWNAAI-----ALVCGNVVVWKPSPT----TPLTAiavtKIVARVLE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 K-----DLYPVINGGVPETTELLK-ERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIA 233
Cdd:cd07130 188 KnglpgAIASLVCGGADVGEALVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 234 WGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGG 307
Cdd:cd07130 268 FAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVrIGDPLDDGTLVGPLHTKAAVDNYLAAIEeaksqGGTVLFGG 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22907049 308 TG-DAATRYIAPTILTdVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSN 370
Cdd:cd07130 348 KViDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTD 410
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
4-415 |
4.36e-27 |
|
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: 113.47 E-value: 4.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEevvyVLEEIEYMiqklpEWAA 83
Cdd:TIGR01238 76 VQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAE----VREAVDFC-----RYYA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 DEPVEKTPQTQqdelyihSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQyldkdly 163
Cdd:TIGR01238 147 KQVRDVLGEFS-------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQE------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 164 pvinGGVPETT-ELL-------------KERFDHILYTGSTGVGKIIMTAAAKHL---TPVTLELGGKSPCYVDKNCDLD 226
Cdd:TIGR01238 213 ----AGFPAGTiQLLpgrgadvgaaltsDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 227 VACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMGLIEG----Q 301
Cdd:TIGR01238 289 QVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDAEAKQNLLAHIEHmsqtQ 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 302 KVAYGGTGDAATR-----YIAPTI--LTDVDPqspvMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSSNDK 372
Cdd:TIGR01238 369 KKIAQLTLDDSRAcqhgtFVAPTLfeLDDIAE----LSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSRIET 444
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 22907049 373 VIKKMIAETSSGGVAANDVIVHITLHSLPFGGVGNSGMGSYHG 415
Cdd:TIGR01238 445 TYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
7-427 |
1.98e-24 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 106.37 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 7 AVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYyEEVVYVLEEIEYMIQKlpewAADEP 86
Cdd:PLN02419 156 AVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSH-GDIFRGLEVVEHACGM----ATLQM 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 87 VEKTPQTQQD-ELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYPV 165
Cdd:PLN02419 231 GEYLPNVSNGvDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLN 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 166 INGGVPETTELL--KERFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQT 243
Cdd:PLN02419 311 IVHGTNDTVNAIcdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQR 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 244 CVAPDYILC---DPSIQNQIVEKlKKSLKEFYGedAKKSRDYGRIISARHFQRVMGLIE-----GQKVAYGG-----TGD 310
Cdd:PLN02419 391 CMALSTVVFvgdAKSWEDKLVER-AKALKVTCG--SEPDADLGPVISKQAKERICRLIQsgvddGAKLLLDGrdivvPGY 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 311 AATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANd 390
Cdd:PLN02419 468 EKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN- 546
|
410 420 430
....*....|....*....|....*....|....*....
gi 22907049 391 VIVHITLHSLPFGGVGNSGMG--SYHGKKSFETFSHRRS 427
Cdd:PLN02419 547 VPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQIKL 585
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
104-430 |
2.67e-22 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 99.14 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 104 PLGVVLVIGTWNYP-----FNLTIqpmvgAIAAGNSVVLKPSELSENMASLLATIIPQYLDKDLYP-----VINGGVPET 173
Cdd:PLN02315 154 PLGIVGVITAFNFPcavlgWNACI-----ALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNNLPgaiftSFCGGAEIG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 174 TELLKE-RFDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILC 252
Cdd:PLN02315 229 EAIAKDtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 253 DPSIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRI---ISARHFQRVMGLIEGQ--KVAYGGTG-DAATRYIAPTILtDVD 325
Cdd:PLN02315 309 HESIYDDVLEQLLTVYKQVkIGDPLEKGTLLGPLhtpESKKNFEKGIEIIKSQggKILTGGSAiESEGNFVQPTIV-EIS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 326 PQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANdviVHITLHSL----P 401
Cdd:PLN02315 388 PDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSDCGIVN---VNIPTNGAeiggA 464
|
330 340
....*....|....*....|....*....
gi 22907049 402 FGGVGNSGMGSYHGKKSFETFSHRRSCLV 430
Cdd:PLN02315 465 FGGEKATGGGREAGSDSWKQYMRRSTCTI 493
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
97-340 |
6.06e-22 |
|
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: 98.43 E-value: 6.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 97 ELYiHSEPLGVVlvIGTWN---Y-----------PFNLTiqpmvgAIAA---------GNSVVLKPSelseNMASLLATI 153
Cdd:cd07123 148 ELY-AQQPLSSP--AGVWNrleYrplegfvyavsPFNFT------AIGGnlagapalmGNVVLWKPS----DTAVLSNYL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 154 IPQYLDKDLYP--VIN---GGVPETTE--LLKERFDHILYTGSTGVGKIIMTAAAKHLT-----P-VTLELGGKSPCYVD 220
Cdd:cd07123 215 VYKILEEAGLPpgVINfvpGDGPVVGDtvLASPHLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVH 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 221 KNCDLDVACRRIAWGKFMNSGQTCVAPD--YIlcdP-SIQNQIVEKLKKSLKEF-YGEDAKKSRDYGRIISARHFQRVMG 296
Cdd:cd07123 295 PSADVDSLVTATVRGAFEYQGQKCSAASraYV---PeSLWPEVKERLLEELKEIkMGDPDDFSNFMGAVIDEKAFDRIKG 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 22907049 297 LIE------GQKVAYGGTGDAATRY-IAPTILTDVDPQSPVMQEEIFGPVL 340
Cdd:cd07123 372 YIDhaksdpEAEIIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFGPVL 422
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
84-415 |
1.52e-21 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 96.54 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 DEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKP----SELSENMASLL--ATIIPQy 157
Cdd:cd07084 80 HEPGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPhtavSIVMQIMVRLLhyAGLLPP- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 158 ldkDLYPVINGGVPETTELLKE-RFDHILYTGSTGVGKIImtAAAKHLTPVTLELGGKSPCYVDKNCD-LDVACRRIAWG 235
Cdd:cd07084 159 ---EDVTLINGDGKTMQALLLHpNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQD 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 236 KFMNSGQTCVAPDYILC--DPSIQnQIVEKLKkslkefygEDAKKSRDYGRIISARHFQRVMGLIE------GQKVAYGG 307
Cdd:cd07084 234 MTACSGQKCTAQSMLFVpeNWSKT-PLVEKLK--------ALLARRKLEDLLLGPVQTFTTLAMIAhmenllGSVLLFSG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 308 T----GDAATRY---IAPTILTDVDP---QSPVMQEEIFGPVLPIVCVRSLEEA--IQFINQREKPLALYMFSSNDKVIK 375
Cdd:cd07084 305 KelknHSIPSIYgacVASALFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQ 384
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 22907049 376 KMIAETSSGGVAandviVHITLhslpfgGVGNSGMGSYHG 415
Cdd:cd07084 385 ELIGNLWVAGRT-----YAILR------GRTGVAPNQNHG 413
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
4-411 |
9.72e-17 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 82.99 E-value: 9.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAYYEevvyVLEEIEYmiqkLPEWAA 83
Cdd:PRK11905 592 VERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAE----VREAVDF----LRYYAA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 84 DepVEKTPQTQQdelyihSEPLGVVLVIGTWNYPfnLTI---QpMVGAIAAGNSVVLKPSELSENMASLLATIIPQyldk 160
Cdd:PRK11905 664 Q--ARRLLNGPG------HKPLGPVVCISPWNFP--LAIftgQ-IAAALVAGNTVLAKPAEQTPLIAARAVRLLHE---- 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 161 dlypvinGGVPETT-ELL-------------KERFDHILYTGSTGVGKIIMTAAAKHLT-PVTL--ELGGKSPCYVDKNC 223
Cdd:PRK11905 729 -------AGVPKDAlQLLpgdgrtvgaalvaDPRIAGVMFTGSTEVARLIQRTLAKRSGpPVPLiaETGGQNAMIVDSSA 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 224 DLDVACRRIAWGKFMNSGQTCVAPDyILCdpsIQNQIVEK----LKKSLKEFY-GEDAKKSRDYGRIISA-------RHF 291
Cdd:PRK11905 802 LPEQVVADVIASAFDSAGQRCSALR-VLC---LQEDVADRvltmLKGAMDELRiGDPWRLSTDVGPVIDAeaqanieAHI 877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 292 QRVMGliEGQKVAYGGTGDAATR--YIAPTILtDVDPQSpVMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMF 367
Cdd:PRK11905 878 EAMRA--AGRLVHQLPLPAETEKgtFVAPTLI-EIDSIS-DLEREVFGPVLHVVRFKAdeLDRVIDDINATGYGLTFGLH 953
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 22907049 368 SSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFGGVGNSGMG 411
Cdd:PRK11905 954 SRIDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTG 997
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
104-411 |
4.45e-16 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 81.17 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 104 PLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIpqyldkdlypvINGGVPE-TTELL----- 177
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRIL-----------LEAGVPAgVVQLLpgrge 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 178 --------KERFDHILYTGSTGVGKIIMTAAAKHL------TPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQT 243
Cdd:PRK11809 837 tvgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQR 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 244 CVAPDyILCdpsIQNQIVEK----LKKSLKEF-YGEDAKKSRDYGRIISA-------RHFQRVMGliEGQKV---AYGGT 308
Cdd:PRK11809 917 CSALR-VLC---LQDDVADRtlkmLRGAMAECrMGNPDRLSTDIGPVIDAeakanieRHIQAMRA--KGRPVfqaARENS 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 309 GDAAT-RYIAPTI--LTDVDPqspvMQEEIFGPVLPIVCVRS--LEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSS 383
Cdd:PRK11809 991 EDWQSgTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNRnqLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHV 1066
|
330 340
....*....|....*....|....*...
gi 22907049 384 GGVAANDVIVHITLHSLPFGGVGNSGMG 411
Cdd:PRK11809 1067 GNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
68-387 |
1.29e-11 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 66.35 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 68 LEEIEYMIQKLPEWAADEPVEKtPQTQQDELYI----HSEPLGVVLVIG-----TWN-YPfnltiqPMVGAIAAGNSVVL 137
Cdd:cd07127 154 LEAVAYAWREMSRIPPTAEWEK-PQGKHDPLAMektfTVVPRGVALVIGcstfpTWNgYP------GLFASLATGNPVIV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 138 KPSElsenmasllATIIPQYL--------------DKDLYPVI--NGGVPETTEL-LKERFDHILYTGSTGVGKIIMTAA 200
Cdd:cd07127 227 KPHP---------AAILPLAItvqvarevlaeagfDPNLVTLAadTPEEPIAQTLaTRPEVRIIDFTGSNAFGDWLEANA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 201 AKHLtpVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCdPS--IQN--------QIVEKLKKSLKE 270
Cdd:cd07127 298 RQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYV-PRdgIQTddgrksfdEVAADLAAAIDG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 271 FYGEDAKKSRDYG---------RIISARHFQRVmgLIEGQKVAYGGTGDAATRyiAPTILTDVDPQSPVMQEEIFGPVLP 341
Cdd:cd07127 375 LLADPARAAALLGaiqspdtlaRIAEARQLGEV--LLASEAVAHPEFPDARVR--TPLLLKLDASDEAAYAEERFGPIAF 450
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 22907049 342 IVCVRSLEEAIQFINQ--REK-PLALYMFSSNDKVIKKMIAETSSGGVA 387
Cdd:cd07127 451 VVATDSTDHSIELAREsvREHgAMTVGVYSTDPEVVERVQEAALDAGVA 499
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
4-411 |
1.53e-11 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 66.89 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNA------------YYeevvyvleei 71
Cdd:COG4230 595 VEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAiaevreavdfcrYY---------- 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 72 eymiqklpewaADEpVEKTPQTQQdelyiHSEPLGVVLVIGTWNYPfnLTI---QpMVGAIAAGNSVVLKPSElsenMAS 148
Cdd:COG4230 665 -----------AAQ-ARRLFAAPT-----VLRGRGVFVCISPWNFP--LAIftgQ-VAAALAAGNTVLAKPAE----QTP 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 149 LLATIIPQYLDKdlypvinGGVP-----------ETT--ELLK-ERFDHILYTGSTGVGKII-MTAAAKHLTPVTL--EL 211
Cdd:COG4230 721 LIAARAVRLLHE-------AGVPadvlqllpgdgETVgaALVAdPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaET 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 212 GGKSPCYVD------KNCDlDVacrrIAwGKFMNSGQTCVAPDyILCdpsIQNQIVEK----LKKSLKEF-YGEDAKKSR 280
Cdd:COG4230 794 GGQNAMIVDssalpeQVVD-DV----LA-SAFDSAGQRCSALR-VLC---VQEDIADRvlemLKGAMAELrVGDPADLST 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 281 DYGRIISA-------RHFQRVMGliEGQKVAYGGTGDAATR--YIAPTI--LTDVDpqspVMQEEIFGPVLPIVCVRS-- 347
Cdd:COG4230 864 DVGPVIDAearanleAHIERMRA--EGRLVHQLPLPEECANgtFVAPTLieIDSIS----DLEREVFGPVLHVVRYKAde 937
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22907049 348 LEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFGGVGNSGMG 411
Cdd:COG4230 938 LDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTG 1001
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
4-411 |
1.37e-10 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 63.68 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVgAL------------------AADLHKnewnaYYEEVV 65
Cdd:PRK11904 587 VEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELI-ALcvreagktlqdaiaevreAVDFCR-----YYAAQA 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 66 yvlEEIEYMIQKLPewaadepvekTPQTQQDELYIHsePLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSElsen 145
Cdd:PRK11904 661 ---RRLFGAPEKLP----------GPTGESNELRLH--GRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAE---- 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 146 MASLLATIIPQYLDKdlypvinGGVPETT-ELL-------------KERFDHILYTGSTGVGKII-MTAAAKHLTPVTL- 209
Cdd:PRK11904 722 QTPLIAAEAVKLLHE-------AGIPKDVlQLLpgdgatvgaaltaDPRIAGVAFTGSTETARIInRTLAARDGPIVPLi 794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 210 -ELGGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDyILCdpsIQNQIVEK----LKKSLKEF-YGEDAKKSRDYG 283
Cdd:PRK11904 795 aETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALR-VLF---VQEDIADRviemLKGAMAELkVGDPRLLSTDVG 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 284 RIISARHFQRVMGLIE----GQKVAYGGTGDAATR---YIAPTI--LTDVDpqspVMQEEIFGPVLPIVCVRS--LEEAI 352
Cdd:PRK11904 871 PVIDAEAKANLDAHIErmkrEARLLAQLPLPAGTEnghFVAPTAfeIDSIS----QLEREVFGPILHVIRYKAsdLDKVI 946
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 22907049 353 QFINQREKPLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFGGVGNSGMG 411
Cdd:PRK11904 947 DAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
104-359 |
2.53e-10 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 62.17 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 104 PLGVVLVIGTWNYPFNLTIqpmVG-----AIAAGNSVVLK--PS--ELSEnmasLLATIIPQYLDKDLYP-----VINGG 169
Cdd:cd07129 105 PLGPVAVFGASNFPLAFSV---AGgdtasALAAGCPVVVKahPAhpGTSE----LVARAIRAALRATGLPagvfsLLQGG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 170 VPET-TELLKerfdH-----ILYTGSTGVGKIIMTAAAKHLT--PVTLELGGKSPCYVDKNCdldVACRRIAWGK-F--- 237
Cdd:cd07129 178 GREVgVALVK----HpaikaVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFILPGA---LAERGEAIAQgFvgs 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 238 --MNSGQTCVAPDYILcdpSIQNQIVEKLKKSLKEFYGEDAKksrdyGRIIS---ARHFQRVMGLIEGQK----VAYGGT 308
Cdd:cd07129 251 ltLGAGQFCTNPGLVL---VPAGPAGDAFIAALAEALAAAPA-----QTMLTpgiAEAYRQGVEALAAAPgvrvLAGGAA 322
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 22907049 309 GDAATRYiAPTILTdVDPQS----PVMQEEIFGPVLPIVCVRSLEEAIQFINQRE 359
Cdd:cd07129 323 AEGGNQA-APTLFK-VDAAAfladPALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
88-377 |
1.09e-08 |
|
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: 56.89 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 88 EKTPQT-QQDELY---IHSEPLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMASLLATIIPQYL----- 158
Cdd:cd07081 75 EKTCGVlTGDENGgtlIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAvaaga 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 159 DKDLYPVINGGVPETTELL--KERFDHILYTGSTGVGKiimtAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGK 236
Cdd:cd07081 155 PENLIGWIDNPSIELAQRLmkFPGIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 237 FMNSGQTCVAPDYILCDPSIQNQIVEKLK-KSLKEFYGEDAKKSRDYgrIISARHFQR-VMGLIEGQKVAYGGTGDAATR 314
Cdd:cd07081 231 TFDNGVICASEQSVIVVDSVYDEVMRLFEgQGAYKLTAEELQQVQPV--ILKNGDVNRdIVGQDAYKIAAAAGLKVPQET 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22907049 315 YIAPTILTDVDPQSPVMQEEIfGPVLPIVCVRSLEEAIqfinqrEKPLALY----------MFSSNDKVIKKM 377
Cdd:cd07081 309 RILIGEVTSLAEHEPFAHEKL-SPVLAMYRAANFADAD------AKALALKleggcghtsaMYSDNIKAIENM 374
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
87-270 |
7.94e-07 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 51.07 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 87 VEKTPQT---QQDELYIHSEPLGVVLVIGTWNYPFnLTIQPMVGAIAAGNSVVLKPSELSENMASLLA----TIIPQYLD 159
Cdd:cd07077 80 VGHIQDVllpDNGETYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALAllfqAADAAHGP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 160 KDLYPVINGGVPETTE-LLK-ERFDHILYTGSTGVGKiimtAAAKH--LTPVTLELGGKSPCYVDKNCDLDVACRRIAWG 235
Cdd:cd07077 159 KILVLYVPHPSDELAEeLLShPKIDLIVATGGRDAVD----AAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDS 234
|
170 180 190
....*....|....*....|....*....|....*
gi 22907049 236 KFMNsGQTCVAPDYILCDPSIQNQIVEKLKKSLKE 270
Cdd:cd07077 235 KFFD-QNACASEQNLYVVDDVLDPLYEEFKLKLVV 268
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
103-376 |
1.50e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 50.18 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 103 EPLGVVL-VIGTWNyP-----FNLTIqpmvgAIAAGNSVVLKPS----ELSENMASLL-ATIIPQYLDKDLYPVI-NGGV 170
Cdd:cd07122 94 EPVGVIAaLIPSTN-PtstaiFKALI-----ALKTRNAIIFSPHprakKCSIEAAKIMrEAAVAAGAPEGLIQWIeEPSI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 171 PETTELLK-ERFDHILYTGSTGVGKiimtAAAKHLTPVtleLG---GKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVA 246
Cdd:cd07122 168 ELTQELMKhPDVDLILATGGPGMVK----AAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICAS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 247 PDYILCDPSIQNQIVEKLKKS----LKEfygEDAKKSRDY---------GRII--SARHFQRVMGLiegqKVAYGgtgda 311
Cdd:cd07122 241 EQSVIVDDEIYDEVRAELKRRgayfLNE---EEKEKLEKAlfddggtlnPDIVgkSAQKIAELAGI----EVPED----- 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22907049 312 aTRYIAPTIlTDVDPQSPVMQEEIFgPVLPIVCVRSLEEAIqfinqrEKPLALYMF----------SSNDKVIKK 376
Cdd:cd07122 309 -TKVLVAEE-TGVGPEEPLSREKLS-PVLAFYRAEDFEEAL------EKARELLEYggaghtavihSNDEEVIEE 374
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
94-380 |
2.13e-06 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 49.75 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 94 QQDELYIHSEPLGVVLVIGTWNYPFnLTIQPMVGAIAAGNSVVLKPSELSENMAS-LLATIIPQYLDKDLYPVI-----N 167
Cdd:pfam05893 78 PTKPSYEKAFPPGLVFHVLSGNVPL-LPVMSILMGLLVKNVNLLKVSSSDPFTAAaLLASFADLDPTHPLADSLsvvywD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 168 GGVPETTELLKERFDHILYTGstgvGKIIMTAAAKHLTPVT--LELGGK-SPCYVDKNCDLDVACRRIAWGKFMNSGQTC 244
Cdd:pfam05893 157 GGSTQLEDLIVANADVVIAWG----GEDAINAIRECLKPGKqwIDFGAKiSFAVVDREAALDKAAERAADDICVFDQQAC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 245 VAPDYILCDPSIQNQI---VEKLKKSLK---EFYgEDAKKSRDYG-RIISARHFQRV-MGLIEGQKVaYGGTGDAATryi 316
Cdd:pfam05893 233 LSPQTVFVESDDKITPdefAERLAAALAkraRIL-PKAVLDIDEAaKISSDRAECKLdYAFAGERGV-WSDFHQRWT--- 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22907049 317 apTILTDVDPQSPvmqeEIFGPVLPIVCVRSLEEAIQFINQREKPL---ALYMFSSNDKVIKKMIAE 380
Cdd:pfam05893 308 --VIWSDGQEELN----SPLNRTVNVVPVPSLSDVVRYVSENRTYLqtcGLAPYSGRLPYLDRKLAL 368
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
106-383 |
7.89e-06 |
|
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: 48.03 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 106 GVVLVIGTWNYPfnltIQPMVGAIA----AGNSVVLKPSELSENMASLLATIIpqyLDKDLYP-----VINGGVPETTEL 176
Cdd:cd07128 146 GVAVHINAFNFP----VWGMLEKFApallAGVPVIVKPATATAYLTEAVVKDI---VESGLLPegalqLICGSVGDLLDH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 177 LKERfDHILYTGSTGVGKIIMT--AAAKHLTPVTLE--------LGgksPCYVDKNCDLDVACRRIAWGKFMNSGQTCVA 246
Cdd:cd07128 219 LGEQ-DVVAFTGSAATAAKLRAhpNIVARSIRFNAEadslnaaiLG---PDATPGTPEFDLFVKEVAREMTVKAGQKCTA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 247 PDYILCDPSIQNQIVEKLKKSL-KEFYGEDAKKSRDYGRIISARHFQRVMG----LIEGQKVAYGGTGDAATR------- 314
Cdd:cd07128 295 IRRAFVPEARVDAVIEALKARLaKVVVGDPRLEGVRMGPLVSREQREDVRAavatLLAEAEVVFGGPDRFEVVgadaekg 374
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22907049 315 -YIAPTILT--DVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAETSS 383
Cdd:cd07128 375 aFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAP 446
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
104-307 |
1.64e-05 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 47.11 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 104 PLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKP----SELSENMASLLATIIPQYLDKDLypvINGGVPETTELLKE 179
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVdskvSVVMEQFLRLLHLCGMPATDVDL---IHSDGPTMNKILLE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 180 -RFDHILYTGSTGV---------GKIIMTAAA---KHLTPVTLELGgkspcYVDKNCDLDV-ACrriawgkfmnSGQTCV 245
Cdd:cd07126 219 aNPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQDAyAC----------SGQKCS 283
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22907049 246 APDYILCDPS-IQNQIVEKLKKSLKEFYGEDAK----KSRDYGRIISarHFQRVMGlIEGQKVAYGG 307
Cdd:cd07126 284 AQSILFAHENwVQAGILDKLKALAEQRKLEDLTigpvLTWTTERILD--HVDKLLA-IPGAKVLFGG 347
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
4-352 |
1.20e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 44.12 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 4 ISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELvGALAAdlhknewnayyeevvyvlEE-----IEYMIQKL 78
Cdd:PRK15398 38 VDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEEL-AELAV------------------EEtgmgrVEDKIAKN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 79 pEWAAdepvEKTPQTQQ--------DE---LYIHSePLGVVLVIGTWNYPFNLTIQPMVGAIAAGNSVVLKPSELSENMA 147
Cdd:PRK15398 99 -VAAA----EKTPGVEDlttealtgDNgltLIEYA-PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 148 SLLATIIPQYLDKDLYP-----VINGGVPETTELLkerFDH-----ILYTGSTGVGKIIMT-------AAAkhltpvtle 210
Cdd:PRK15398 173 LRAIELLNEAIVAAGGPenlvvTVAEPTIETAQRL---MKHpgialLVVTGGPAVVKAAMKsgkkaigAGA--------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 211 lgGKSPCYVDKNCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNQIV----------------EKLKKSL------ 268
Cdd:PRK15398 241 --GNPPVVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMrlmekngavlltaeqaEKLQKVVlknggt 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 269 --KEFYGEDAKKsrdygriisarhfqrvmgLIEgqkvAYGGTGDAATRyiapTILTDVDPQSPVMQEEIFGPVLPIVCVR 346
Cdd:PRK15398 319 vnKKWVGKDAAK------------------ILE----AAGINVPKDTR----LLIVETDANHPFVVTELMMPVLPVVRVK 372
|
....*.
gi 22907049 347 SLEEAI 352
Cdd:PRK15398 373 DVDEAI 378
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
240-427 |
3.85e-04 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 42.77 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 240 SGQTCVAPDYILCDPSIQNQIVEKLKKSL-KEFYGEDAKKSRDYGRIISARHFQRVM----GLIEGQKVAYGGTG----- 309
Cdd:PRK11903 292 SGQKCTAIRRIFVPEALYDAVAEALAARLaKTTVGNPRNDGVRMGPLVSRAQLAAVRaglaALRAQAEVLFDGGGfalvd 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22907049 310 -DAATRY-IAPTIL--TDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREKPLALYMFSSNDKVIKKMIAE--TSS 383
Cdd:PRK11903 372 aDPAVAAcVGPTLLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALElaDSH 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22907049 384 GGVAA--NDVIVHITLHS--LP---FGGVGNSGMGSYHGKKSFETFSHRRS 427
Cdd:PRK11903 452 GRVHVisPDVAALHTGHGnvMPqslHGGPGRAGGGEELGGLRALAFYHRRS 502
|
|
| |
