|
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: 845.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 5 EDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAISQAEVDLALRNLRSWMKD 84
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 85 EKVSKNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFA 164
Cdd:cd07132 81 EPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 165 VVLGGPQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 244
Cdd:cd07132 161 VVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 245 VAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCGRVAIGGQSDEGERYIAPTVLVDV 324
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 325 QETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTLSSLPFGG 404
Cdd:cd07132 321 KPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958646404 405 VGTSGMGRYHGKFSFDTFSNQRACLLRSPGMEKINDLRYPPYT 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 ... |
8-429 |
0e+00 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 700.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 8 LQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAISQAEVDLALRNLRSWMKDEKV 87
Cdd:cd07087 4 VARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 88 SKNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFAVVL 167
Cdd:cd07087 84 SVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 168 GGPQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAP 247
Cdd:cd07087 164 GGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 248 DYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQET 327
Cdd:cd07087 244 DYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSPD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 328 EPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTLSSLPFGGVGT 407
Cdd:cd07087 324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGN 403
|
410 420
....*....|....*....|..
gi 1958646404 408 SGMGRYHGKFSFDTFSNQRACL 429
Cdd:cd07087 404 SGMGAYHGKAGFDTFSHLKSVL 425
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
5-454 |
0e+00 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 641.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 5 EDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAISQAEVDLALRNLRSWMKD 84
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 85 EKVSKNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFA 164
Cdd:cd07136 81 KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 165 VVLGGPQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 244
Cdd:cd07136 161 VVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 245 VAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCGRVAIGGQSDEGERYIAPTVLVDV 324
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 325 QETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTLSSLPFGG 404
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958646404 405 VGTSGMGRYHGKFSFDTFSNQRACLLRSPGMEkiNDLRYPPYTSRNLRVL 454
Cdd:cd07136 401 VGNSGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPPYKGKKKKLK 448
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
5-459 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 630.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 5 EDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAISQAEVDLALRNLRSWMKD 84
Cdd:PTZ00381 10 PPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 85 EKVSKNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFA 164
Cdd:PTZ00381 90 EKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 165 VVLGGPQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 244
Cdd:PTZ00381 170 VIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTC 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 245 VAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGC--GRVAIGGQSDEGERYIAPTVLV 322
Cdd:PTZ00381 250 VAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDhgGKVVYGGEVDIENKYVAPTIIV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 323 DVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTLSSLPF 402
Cdd:PTZ00381 330 NPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPF 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958646404 403 GGVGTSGMGRYHGKFSFDTFSNQRACLLRSPGMEKINDLRYPPYTSRNLRVLLVAME 459
Cdd:PTZ00381 410 GGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSWVLSFLLK 466
|
|
| 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: 580.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 1 MDSFEDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAISQAEVDLALRNLRS 80
Cdd:cd07135 4 LDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 81 WMKDEKVSKNLATQ-LDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLD 159
Cdd:cd07135 84 WAKDEKVKDGPLAFmFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 160 QSCFAVVLGGPQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 239
Cdd:cd07135 164 PDAFQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 240 AGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGC--GRVAIGGQSDEGERYIA 317
Cdd:cd07135 244 AGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTtkGKVVIGGEMDEATRFIP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 318 PTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTL 397
Cdd:cd07135 324 PTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGV 403
|
410 420 430
....*....|....*....|....*....|
gi 1958646404 398 SSLPFGGVGTSGMGRYHGKFSFDTFSNQRA 427
Cdd:cd07135 404 DNAPFGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
8-429 |
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: 516.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 8 LQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAISQAEVDLALRNLRSWMKDEKV 87
Cdd:cd07137 5 VRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPEKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 88 SKNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFAVVL 167
Cdd:cd07137 85 KTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 168 GGPQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRY-FNAGQTCVA 246
Cdd:cd07137 165 GGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 247 PDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCGRVAI----GGQSDEGERYIAPTVLV 322
Cdd:cd07137 245 PDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADkivhGGERDEKNLYIEPTILL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 323 DVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTLSSLPF 402
Cdd:cd07137 325 DPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPF 404
|
410 420
....*....|....*....|....*..
gi 1958646404 403 GGVGTSGMGRYHGKFSFDTFSNQRACL 429
Cdd:cd07137 405 GGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
12-429 |
1.13e-180 |
|
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: 512.16 E-value: 1.13e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAG-------RTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAISQAEVDLALRNLRSWMKD 84
Cdd:cd07134 1 RRVFAAQqahalalRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 85 EKVSKNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFA 164
Cdd:cd07134 81 KRVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 165 VVLGGPQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 244
Cdd:cd07134 161 VFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 245 VAPDYVLCSQEMQERLVPALQNAITRFYGDNPQT--SPNLGRIINQKHFERLQGLL-----GCGRVAIGGQSDEGERYIA 317
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARkaSPDLARIVNDRHFDRLKGLLddavaKGAKVEFGGQFDAAQRYIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 318 PTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTL 397
Cdd:cd07134 321 PTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLN 400
|
410 420 430
....*....|....*....|....*....|..
gi 1958646404 398 SSLPFGGVGTSGMGRYHGKFSFDTFSNQRACL 429
Cdd:cd07134 401 PNLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
5-427 |
1.03e-175 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 499.70 E-value: 1.03e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 5 EDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDL-HKSAFESEVSEIAISQAEVDLALRNLRSWMK 83
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 84 DEKVSKNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCF 163
Cdd:cd07133 81 PSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 164 AVVLGGPQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQT 243
Cdd:cd07133 161 AVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 244 CVAPDYVLCSQEMQERLVPALQNAITRFYGDnPQTSPNLGRIINQKHFERLQGLL------GCGRVAIG--GQSDEGERY 315
Cdd:cd07133 241 CVAPDYVLVPEDKLEEFVAAAKAAVAKMYPT-LADNPDYTSIINERHYARLQGLLedarakGARVIELNpaGEDFAATRK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 316 IAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHM 395
Cdd:cd07133 320 LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHV 399
|
410 420 430
....*....|....*....|....*....|..
gi 1958646404 396 TLSSLPFGGVGTSGMGRYHGKFSFDTFSNQRA 427
Cdd:cd07133 400 AQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-454 |
4.86e-164 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 471.90 E-value: 4.86e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 1 MDSFEDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAISQAEVDLALRNLRS 80
Cdd:PLN02203 5 GETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 81 WMKDEKVSKNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQ 160
Cdd:PLN02203 85 WMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 161 SCFAVVLGGPQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVD---DNCDPQTVANRVAWFRY 237
Cdd:PLN02203 165 KAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 238 FN-AGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCGRVAI----GGQSDEG 312
Cdd:PLN02203 245 GScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAAsivhGGSIDEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 313 ERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGF 392
Cdd:PLN02203 325 KLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958646404 393 MHMTLSSLPFGGVGTSGMGRYHGKFSFDTFSNQRACLLRSPGMEKinDLRYPPYTSRNLRVL 454
Cdd:PLN02203 405 IQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEF--EFRYPPWNDFKLGFL 464
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
12-430 |
7.90e-134 |
|
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: 393.11 E-value: 7.90e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVsEIAISQAEVDLALRNLRSWMKDEKVSKNL 91
Cdd:cd07078 8 RAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGEVIPSPDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 92 ATQldsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGP 170
Cdd:cd07078 87 GEL---AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNVVTGDG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 171 QETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD 248
Cdd:cd07078 164 DEVGAaLASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 249 YVLCSQEMQERLVPALQNAITRFYGDNP-QTSPNLGRIINQKHFERLQGLL-----GCGRVAIGGQSDEGE--RYIAPTV 320
Cdd:cd07078 244 RLLVHESIYDEFVERLVERVKALKVGNPlDPDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKRLEGGkgYFVPPTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 321 LVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTlSSL 400
Cdd:cd07078 324 LTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGAE-PSA 402
|
410 420 430
....*....|....*....|....*....|
gi 1958646404 401 PFGGVGTSGMGRYHGKFSFDTFSNQRACLL 430
Cdd:cd07078 403 PFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
10-454 |
2.25e-130 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 385.94 E-value: 2.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 10 QLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAISQAEVDLALRNLRSWMKDEKVSK 89
Cdd:PLN02174 18 ELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 90 NLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFAVVLGG 169
Cdd:PLN02174 98 SLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 170 PQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRY-FNAGQTCVAPD 248
Cdd:PLN02174 178 VTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 249 YVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLG----CGRVAIGGQSDEGERYIAPTVLVDV 324
Cdd:PLN02174 258 YILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILLDV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 325 QETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTLSSLPFGG 404
Cdd:PLN02174 338 PLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGG 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958646404 405 VGTSGMGRYHGKFSFDTFSNQRACLLRSpgMEKINDLRYPPYTSRNLRVL 454
Cdd:PLN02174 418 VGESGMGAYHGKFSFDAFSHKKAVLYRS--LFGDSAVRYPPYSRGKLRLL 465
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
12-430 |
5.40e-107 |
|
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: 321.87 E-value: 5.40e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESeVSEIAISQAEVDLALRNLRSWMKDEKVSKNL 91
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 92 ATQldsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGP 170
Cdd:cd06534 83 GGE---AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 171 QETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD 248
Cdd:cd06534 160 DEVGAaLLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 249 YVLCSQEMQERLVpalqnaitrfygdnpqtspnlgriinqkhfERLQgllgcgrvaiggqsdegeryiapTVLVDVQETE 328
Cdd:cd06534 240 RLLVHESIYDEFV------------------------------EKLV-----------------------TVLVDVDPDM 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 329 PVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTLsSLPFGGVGTS 408
Cdd:cd06534 267 PIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP-EAPFGGVKNS 345
|
410 420
....*....|....*....|..
gi 1958646404 409 GMGRYHGKFSFDTFSNQRACLL 430
Cdd:cd06534 346 GIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
12-427 |
2.88e-104 |
|
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: 318.99 E-value: 2.88e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSafesevseIAISQAEVDLALRNLRSW------MKDE 85
Cdd:COG1012 53 RAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKP--------LAEARGEVDRAADFLRYYagearrLYGE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 86 KVSKNLATQLdsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPRYLdq 160
Cdd:COG1012 125 TIPSDAPGTR--AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELleeagLPAGV-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 161 scFAVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYF 238
Cdd:COG1012 201 --LNVVTGDGSEVGAaLVAHpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 239 NAGQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQSDEG 312
Cdd:COG1012 279 NAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIEDAvaegaELLTGGRRPDG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 313 ER--YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGND 390
Cdd:COG1012 359 EGgyFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWIND 438
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958646404 391 GFMHMTLsSLPFGGVGTSGMGRYHGKFSFDTFSNQRA 427
Cdd:COG1012 439 GTTGAVP-QAPFGGVKQSGIGREGGREGLEEYTETKT 474
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
12-427 |
5.40e-90 |
|
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: 281.34 E-value: 5.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSafesevseIAISQAEVDLALRNLRSWMKdekvsknL 91
Cdd:pfam00171 39 RAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP--------LAEARGEVDRAIDVLRYYAG-------L 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 92 ATQLD----------SAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPR 156
Cdd:pfam00171 104 ARRLDgetlpsdpgrLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELfeeagLPA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 157 YLdqscFAVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAW 234
Cdd:pfam00171 184 GV----LNVVTGSGAEVGEaLVEHpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 235 FRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLL-----GCGRVAIGGQ 308
Cdd:pfam00171 260 GAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 309 SDEGE-RYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFC 387
Cdd:pfam00171 340 AGLDNgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVW 419
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1958646404 388 GNDGFMHmTLSSLPFGGVGTSGMGRYHGKFSFDTFSNQRA 427
Cdd:pfam00171 420 INDYTTG-DADGLPFGGFKQSGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
8-427 |
3.96e-88 |
|
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: 276.41 E-value: 3.96e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 8 LQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAfesevseiAISQAEVDLALRNLRSW------ 81
Cdd:cd07099 24 VARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPR--------ADAGLEVLLALEAIDWAarnapr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 82 -MKDEKVSKNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKAT----EKILAEVLPr 156
Cdd:cd07099 96 vLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVgellAEAWAAAGP- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 157 ylDQSCFAVVLGGpQETGQ-LLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWF 235
Cdd:cd07099 175 --PQGVLQVVTGD-GATGAaLIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 236 RYFNAGQTCVAPDYVLCSQEMQERLVPAL--------QNAITRFYGD-NPQTSPNLGRIInQKHFErlQGLLGCGRVAIG 306
Cdd:cd07099 252 AMVNAGQTCISVERVYVHESVYDEFVARLvakaralrPGADDIGDADiGPMTTARQLDIV-RRHVD--DAVAKGAKALTG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 307 G-QSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGG 385
Cdd:cd07099 329 GaRSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGA 408
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958646404 386 FCGNDGFMHMTLSSLPFGGVGTSGMGRYHGKFSFDTFSNQRA 427
Cdd:cd07099 409 VSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKA 450
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
12-427 |
1.44e-66 |
|
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: 220.63 E-value: 1.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAISQAEVDLALRNLRSWMKDEKVSKNL 91
Cdd:cd07098 28 RAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESRPGGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 92 ATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEI----SKATEKILAEVL-----PRYLDQS- 161
Cdd:cd07098 108 LMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQvawsSGFFLSIIRECLaacghDPDLVQLv 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 162 -CFAvvlggpqETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANrvAWFR-- 236
Cdd:cd07098 188 tCLP-------ETAEaLTSHpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIAS--IIMRgt 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 237 YFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNP-QTSPNLGRIINQKHFERLQGLLG----------CGRVAI 305
Cdd:cd07098 259 FQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPlDGDVDVGAMISPARFDRLEELVAdavekgarllAGGKRY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 306 GGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGG 385
Cdd:cd07098 339 PHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGM 418
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1958646404 386 FCGND-GFMHMtLSSLPFGGVGTSGMGRYHGKFSFDTFSNQRA 427
Cdd:cd07098 419 VAINDfGVNYY-VQQLPFGGVKGSGFGRFAGEEGLRGLCNPKS 460
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
12-427 |
4.14e-66 |
|
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: 219.42 E-value: 4.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAG-RTRSAEFRAAQLQGLSHFLRDNKQQLQE----------ALAQDLHKSAFESEVSEIAisqaevDLALRNLRS 80
Cdd:cd07089 29 RRAFDTGdWSTDAEERARCLRQLHEALEARKEELRAllvaevgapvMTARAMQVDGPIGHLRYFA------DLADSFPWE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 81 wmkDEKVSKNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LP 155
Cdd:cd07089 103 ---FDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIiaetdLP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 156 RyldqSCFAVVLGGPQETGQLL--EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVA 233
Cdd:cd07089 180 A----GVVNVVTGSDNAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 234 WFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGD--NPQTspNLGRIINQKHFERLQGLLGCGR------VA 304
Cdd:cd07089 256 GVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGDpaDPGT--VMGPLISAAQRDRVEGYIARGRdegarlVT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 305 IGGQSDEGER--YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTS 382
Cdd:cd07089 334 GGGRPAGLDKgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIR 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958646404 383 SGGFCGNdGFMHMTLSSlPFGGVGTSGMGRYHGKFSFDTFSNQRA 427
Cdd:cd07089 414 TGSVGIN-GGGGYGPDA-PFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
12-423 |
4.31e-65 |
|
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: 216.72 E-value: 4.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAF--NAGRTRSAEfRAAQLQGLSHFLRDNKQQLQEALAQDLHKSafesevseIAISQAEVDLALRNLRSW--MKDeKV 87
Cdd:cd07109 29 RRAFesGWLRLSPAE-RGRLLLRIARLIREHADELARLESLDTGKP--------LTQARADVEAAARYFEYYggAAD-KL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 88 SKNLATQLDS--AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFA 164
Cdd:cd07109 99 HGETIPLGPGyfVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 165 VVLGGPQETGQ-LLEHR-FDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 242
Cdd:cd07109 179 VVTGLGAEAGAaLVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 243 TCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLL-----GCGRVAIGGQSDEGER--- 314
Cdd:cd07109 259 TCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVararaRGARIVAGGRIAEGAPagg 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 315 -YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFM 393
Cdd:cd07109 339 yFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGA 418
|
410 420 430
....*....|....*....|....*....|
gi 1958646404 394 HMTLsSLPFGGVGTSGMGRYHGKFSFDTFS 423
Cdd:cd07109 419 GGGI-ELPFGGVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
97-423 |
2.21e-64 |
|
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: 214.50 E-value: 2.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 97 SAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFAVVLGGPQETGQL 176
Cdd:cd07092 111 TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 177 L--EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 254
Cdd:cd07092 191 LvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 255 EMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLL----GCGRVAIGGQSDEGERY-IAPTVLVDVQETE 328
Cdd:cd07092 271 SVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGRRAEGPGYfYEPTVVAGVAQDD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 329 PVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDgfmHMTLSS-LPFGGVGT 407
Cdd:cd07092 351 EIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPLAAeMPHGGFKQ 427
|
330
....*....|....*.
gi 1958646404 408 SGMGRYHGKFSFDTFS 423
Cdd:cd07092 428 SGYGKDLSIYALEDYT 443
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
13-422 |
6.18e-64 |
|
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: 213.45 E-value: 6.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 13 EAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSafesevseIAISQAEVDLALRNLRsWMKDEKV----- 87
Cdd:cd07103 30 AAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKP--------LAEARGEVDYAASFLE-WFAEEARriygr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 88 ---SKNLATQLdsaFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCF 163
Cdd:cd07103 101 tipSPAPGKRI---LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPAGVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 164 AVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 241
Cdd:cd07103 178 NVVTGSPAEIGEaLCASpRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 242 QTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGL----LGCG-RVAIGGQ-SDEGER 314
Cdd:cd07103 258 QTCVCANRIYVHESIYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALvedaVAKGaKVLTGGKrLGLGGY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 315 YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSG--GFcgNDGF 392
Cdd:cd07103 338 FYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGmvGI--NTGL 415
|
410 420 430
....*....|....*....|....*....|
gi 1958646404 393 mhMTLSSLPFGGVGTSGMGRYHGKFSFDTF 422
Cdd:cd07103 416 --ISDAEAPFGGVKESGLGREGGKEGLEEY 443
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
12-416 |
1.29e-63 |
|
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: 212.39 E-value: 1.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSafesevseIAISQAEVDLALrnlrSWMK-------- 83
Cdd:cd07106 29 KAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKP--------LAEAQFEVGGAV----AWLRytasldlp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 84 DEKVSKNlATQldSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISK-ATEK---ILAEVLPRYLD 159
Cdd:cd07106 97 DEVIEDD-DTR--RVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPlCTLKlgeLAQEVLPPGVL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 160 QscfavVLGGPQETGQLL-EH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRY 237
Cdd:cd07106 174 N-----VVSGGDELGPALtSHpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 238 FNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFY-GDNPQTSPNLGRIINQKHFERLQGLL-----GCGRVAIGGQSDE 311
Cdd:cd07106 249 INSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVedakaKGAKVLAGGEPLD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 312 GERY-IAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNd 390
Cdd:cd07106 329 GPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN- 407
|
410 420
....*....|....*....|....*..
gi 1958646404 391 gfMHMTLS-SLPFGGVGTSGMGRYHGK 416
Cdd:cd07106 408 --THGALDpDAPFGGHKQSGIGVEFGI 432
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
12-430 |
1.78e-62 |
|
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: 209.50 E-value: 1.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTR--SAEFRAAQLQGLSHFLRDNkqqlQEALAQdlhksaFESEVSEIAISQA--EVDLALRNLRswmkdekV 87
Cdd:cd07118 29 RKAFDKGPWPrmSGAERAAVLLKVADLIRAR----RERLAL------IETLESGKPISQArgEIEGAADLWR-------Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 88 SKNLATQL--DS---------AFIRKEPFGLVLIIVPWNYPLnLTL---VPLvgAIAAGNCVVLKPSEISKATEKILAEV 153
Cdd:cd07118 92 AASLARTLhgDSynnlgddmlGLVLREPIGVVGIITPWNFPF-LILsqkLPF--ALAAGCTVVVKPSEFTSGTTLMLAEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 154 LPRY-LDQSCFAVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVAN 230
Cdd:cd07118 169 LIEAgLPAGVVNIVTGYGATVGQaMTEHpDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 231 RVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQnAITRF--YGD--NPQTspNLGRIINQKHFERLQGLLGCGR---- 302
Cdd:cd07118 249 AVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVV-ARSRKvrVGDplDPET--KVGAIINEAQLAKITDYVDAGRaega 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 303 -VAIGGQSDEGE--RYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLA 379
Cdd:cd07118 326 tLLLGGERLASAagLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVAR 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958646404 380 RTSSGGFCGN---DGFMHMtlsslPFGGVGTSGMGRYHGKFSFDTFSNQRACLL 430
Cdd:cd07118 406 RIRAGTVWVNtflDGSPEL-----PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
12-422 |
9.24e-62 |
|
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: 207.97 E-value: 9.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESE--VSEIA------ISQAEVDLALRNLRSWMK 83
Cdd:cd07110 29 RRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdVDDVAgcfeyyADLAEQLDAKAERAVPLP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 84 DEKVSknlatqldsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPRyl 158
Cdd:cd07110 109 SEDFK---------ARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIaaeagLPP-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 159 dqSCFAVVLGGPQETGQ-LLEHR-FDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFR 236
Cdd:cd07110 178 --GVLNVVTGTGDEAGApLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGC 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 237 YFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSP-NLGRIINQKHFERLQGLLGCG-----RVAIGGQSD 310
Cdd:cd07110 256 FWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGvRLGPLVSQAQYEKVLSFIARGkeegaRLLCGGRRP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 311 EGER---YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGF- 386
Cdd:cd07110 336 AHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVw 415
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958646404 387 --CGNDGFMHmtlssLPFGGVGTSGMGRYHGKFSFDTF 422
Cdd:cd07110 416 inCSQPCFPQ-----APWGGYKRSGIGRELGEWGLDNY 448
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-422 |
9.90e-61 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 205.43 E-value: 9.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNA-GRTRSAEfRAAQLQGLSHFLRDNKQQLQEALAQdlhksafesEV-SEIAISQ-AEVDLALRNLRSWMKdekVS 88
Cdd:cd07138 46 RRAFPAwSATSVEE-RAALLERIAEAYEARADELAQAITL---------EMgAPITLARaAQVGLGIGHLRAAAD---AL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 89 KNLA--TQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPRyldqS 161
Cdd:cd07138 113 KDFEfeERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEIldeagLPA----G 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 162 CFAVVLGGPQETGQLL-EH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCD-----PQTVANrvaw 234
Cdd:cd07138 189 VFNLVNGDGPVVGEALsAHpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADlekavPRGVAA---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 235 fRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGG- 307
Cdd:cd07138 265 -CFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIQKGieegaRLVAGGp 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 308 QSDEG-ER--YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSG 384
Cdd:cd07138 344 GRPEGlERgyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAG 423
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958646404 385 GFCGNDGFMHMtlsSLPFGGVGTSGMGRYHGKFSFDTF 422
Cdd:cd07138 424 QVHINGAAFNP---GAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
12-426 |
1.96e-60 |
|
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: 203.53 E-value: 1.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQD----LHKSAFESEVSEIAISQAeVDLALRnlrswMKDEKV 87
Cdd:cd07104 10 AAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIREsgstRPKAAFEVGAAIAILREA-AGLPRR-----PEGEIL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 88 SKNLATQLdsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSE---ISKATekILAEV-----LPRYLd 159
Cdd:cd07104 84 PSDVPGKE--SMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSrtpVTGGL--LIAEIfeeagLPKGV- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 160 qscFAVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRY 237
Cdd:cd07104 159 ---LNVVPGGGSEIGDaLVEHpRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 238 FNAGQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGD--NPQTSpnLGRIINQKHFERLQGLL------GcGRVAIGGQ 308
Cdd:cd07104 236 LHQGQICMAAGRILVHESVYDEFVEKLVAKAKALpVGDprDPDTV--IGPLINERQVDRVHAIVedavaaG-ARLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 309 SDegERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCG 388
Cdd:cd07104 313 YE--GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHI 390
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958646404 389 NDGFMHmTLSSLPFGGVGTSGMGRYHGKFSFDTFSNQR 426
Cdd:cd07104 391 NDQTVN-DEPHVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
5-426 |
2.92e-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: 203.08 E-value: 2.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 5 EDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSafesevseIAISQAEVDLALRNLR----- 79
Cdd:cd07100 2 EAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKP--------IAEARAEVEKCAWICRyyaen 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 80 --SWMKDEKVSknlaTQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEI----SKATEKILAEV 153
Cdd:cd07100 74 aeAFLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNvpgcALAIEELFREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 154 -LPryldQSCFAVVLGGPQETGQLLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANR 231
Cdd:cd07100 150 gFP----EGVFQNLLIDSDQVEAIIADpRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 232 VAWFRYFNAGQTCVAP------DYVLcsQEMQERLVPALQNAITrfyGD--NPQTspNLGRIINQKHFERLQGLL----- 298
Cdd:cd07100 226 AVKGRLQNAGQSCIAAkrfivhEDVY--DEFLEKFVEAMAALKV---GDpmDEDT--DLGPLARKDLRDELHEQVeeava 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 299 -GCgRVAIGGQSDEGER-YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQ 376
Cdd:cd07100 299 aGA-TLLLGGKRPDGPGaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAER 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1958646404 377 VLARTSSGGFCGNDgfmhMTLSS--LPFGGVGTSGMGRYHGKFSFDTFSNQR 426
Cdd:cd07100 378 VARRLEAGMVFING----MVKSDprLPFGGVKRSGYGRELGRFGIREFVNIK 425
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
100-412 |
1.40e-59 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 202.45 E-value: 1.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 100 IRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFAVVLGGPQETGQ-LLE 178
Cdd:PRK13473 134 IRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDaLVG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 179 HR-FDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQ 257
Cdd:PRK13473 214 HPkVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 258 ERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGL------LGCGRVAIGGQSDEGE-RYIAPTVLVDVQETEP 329
Cdd:PRK13473 294 DDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFverakaLGHIRVVTGGEAPDGKgYYYEPTLLAGARQDDE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 330 VMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFmhMTLSSLPFGGVGTSG 409
Cdd:PRK13473 374 IVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHF--MLVSEMPHGGQKQSG 451
|
...
gi 1958646404 410 MGR 412
Cdd:PRK13473 452 YGK 454
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
100-427 |
2.07e-59 |
|
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: 201.40 E-value: 2.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 100 IRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGPQETGQLL- 177
Cdd:cd07150 115 SVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELv 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 178 -EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEM 256
Cdd:cd07150 195 dDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 257 QERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLL------GcGRVAIGGQSDeGERYiAPTVLVDVQETEP 329
Cdd:cd07150 275 YDEFVKKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKRQVedavakG-AKLLTGGKYD-GNFY-QPTVLTDVTPDMR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 330 VMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQvLARTSSGGFCG-NDGFMHMTlSSLPFGGVGTS 408
Cdd:cd07150 352 IFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFK-LAERLESGMVHiNDPTILDE-AHVPFGGVKAS 429
|
330
....*....|....*....
gi 1958646404 409 GMGRYHGKFSFDTFSNQRA 427
Cdd:cd07150 430 GFGREGGEWSMEEFTELKW 448
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
7-423 |
1.68e-58 |
|
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: 199.01 E-value: 1.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 7 KLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSafesevseIAISQAEVDLALRNLRsWMKD-- 84
Cdd:cd07102 23 ALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP--------IAQAGGEIRGMLERAR-YMISia 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 85 EKVSKNLATQLDSAF---IRKEPFGLVLIIVPWNYPLnLTLV-PLVGAIAAGNCVVLKPSEISKATEKILAEV-----LP 155
Cdd:cd07102 94 EEALADIRVPEKDGFeryIRREPLGVVLIIAPWNYPY-LTAVnAVIPALLAGNAVILKHSPQTPLCGERFAAAfaeagLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 156 RYLdqscFAVVLGGPQETGQLL-EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAW 234
Cdd:cd07102 173 EGV----FQVLHLSHETSAALIaDPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 235 FRYFNAGQTCVAPDYVLCSQEMQERLVPALQnAITRFY--GDNPQTSPNLGRIINQKHFERLQGLL------GcGRVAIG 306
Cdd:cd07102 249 GAFFNSGQSCCSIERIYVHESIYDAFVEAFV-AVVKGYklGDPLDPSTTLGPVVSARAADFVRAQIadaiakG-ARALID 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 307 GQ----SDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTS 382
Cdd:cd07102 327 GAlfpeDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLE 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958646404 383 SGGFcgndgFMHMT--LS-SLPFGGVGTSGMGRYHGKFSFDTFS 423
Cdd:cd07102 407 TGTV-----FMNRCdyLDpALAWTGVKDSGRGVTLSRLGYDQLT 445
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
12-423 |
3.27e-57 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 196.38 E-value: 3.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAG--RTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEvseiaISQAEVDLALR---NLRSWMKDEK 86
Cdd:cd07119 45 RRAFDSGewPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESE-----IDIDDVANCFRyyaGLATKETGEV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 87 VSKNLATQldsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATE----KILAEV-LPRyldqS 161
Cdd:cd07119 120 YDVPPHVI---SRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTialfELIEEAgLPA----G 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 162 CFAVVLGGPQETGQLL--EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 239
Cdd:cd07119 193 VVNLVTGSGATVGAELaeSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFN 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 240 AGQTCVAPDYVLCSQEMQERLVPAL---QNAITRFYGDNPQTspNLGRIINQKHFERLQGLLGCG-----RVAIGGQSDE 311
Cdd:cd07119 273 AGQVCSAGSRLLVEESIHDKFVAALaerAKKIKLGNGLDADT--EMGPLVSAEHREKVLSYIQLGkeegaRLVCGGKRPT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 312 GER-----YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGF 386
Cdd:cd07119 351 GDElakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTV 430
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958646404 387 CGNDgfMHMTLSSLPFGGVGTSGMGRYHGKFSFDTFS 423
Cdd:cd07119 431 WIND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
12-427 |
4.22e-57 |
|
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: 195.48 E-value: 4.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKsafesevseiAISQA---EVDLALRNLRSWMKDEKVS 88
Cdd:cd07093 29 KEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGK----------PITLArtrDIPRAAANFRFFADYILQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 89 KNLATQLDSAFI---RKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPRyldq 160
Cdd:cd07093 99 DGESYPQDGGALnyvLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELaneagLPP---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 161 SCFAVVLG-GPqETGQLL-EH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRY 237
Cdd:cd07093 175 GVVNVVHGfGP-EAGAALvAHpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 238 FNAGQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCGR-----VAIGGQSDE 311
Cdd:cd07093 254 SNNGEVCLAGSRILVQRSIYDEFLERFVERAKALkVGDPLDPDTEVGPLISKEHLEKVLGYVELARaegatILTGGGRPE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 312 GER-----YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFS---KRSQvikQVLARTSS 383
Cdd:cd07093 334 LPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTrdlGRAH---RVARRLEA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958646404 384 GGFCGNDGFM-HMTlssLPFGGVGTSGMGRYHGKFSFDTFSNQRA 427
Cdd:cd07093 411 GTVWVNCWLVrDLR---TPFGGVKASGIGREGGDYSLEFYTELKN 452
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
12-423 |
5.63e-57 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 195.51 E-value: 5.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGR--TRSAEFRAAQLQGLSHFLRDNKQQLQ--EALaqDLHKsafesevsEIAISQA-EVDLALRNLRsWMKD-- 84
Cdd:cd07112 34 RRAFESGVwsRLSPAERKAVLLRLADLIEAHRDELAllETL--DMGK--------PISDALAvDVPSAANTFR-WYAEai 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 85 EKVSKNLA-TQLDS-AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPRy 157
Cdd:cd07112 103 DKVYGEVApTGPDAlALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLPA- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 158 ldqSCFAVVLGGPQETGQLL-EHR-FDYIFFTGNTYVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNC-DPQTVANRVA 233
Cdd:cd07112 182 ---GVLNVVPGFGHTAGEALgLHMdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 234 WFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFY-GD--NPQTSpnLGRIINQKHFERLQGLLGCG-----RVAI 305
Cdd:cd07112 259 AGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKpGDplDPATR--MGALVSEAHFDKVLGYIESGkaegaRLVA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 306 GGQS---DEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLA--LYA--FSKRSQVIKQVL 378
Cdd:cd07112 337 GGKRvltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAasVWTsdLSRAHRVARRLR 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958646404 379 ARTSSGGfCGNDGFMhmtlsSLPFGGVGTSGMGRYHGKFSFDTFS 423
Cdd:cd07112 417 AGTVWVN-CFDEGDI-----TTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
96-423 |
6.12e-57 |
|
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: 194.33 E-value: 6.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 96 DSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPryldQSCFAVVLGGP 170
Cdd:cd07105 90 TLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVfheagLP----KGVLNVVTHSP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 171 QE----TGQLLEH---RFdyIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQT 243
Cdd:cd07105 166 EDapevVEALIAHpavRK--VNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 244 CVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQtspnLGRIINQKHFERLQGL----LGCG-RVAIGGQSDEGER--YI 316
Cdd:cd07105 244 CMSTERIIVHESIADEFVEKLKAAAEKLFAGPVV----LGSLVSAAAADRVKELvddaLSKGaKLVVGGLADESPSgtSM 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 317 APTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGfcgndgfMH-- 394
Cdd:cd07105 320 PPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA-------VHin 392
|
330 340 350
....*....|....*....|....*....|...
gi 1958646404 395 -MTL---SSLPFGGVGTSGMGRYHGKFSFDTFS 423
Cdd:cd07105 393 gMTVhdePTLPHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
12-412 |
1.68e-56 |
|
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: 194.10 E-value: 1.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSafesevseIAISQAEVDLALRNLRSWMKDEKVSKNL 91
Cdd:cd07145 31 EKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKP--------IKQSRVEVERTIRLFKLAAEEAKVLRGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 92 ATQLDS--------AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSC 162
Cdd:cd07145 103 TIPVDAyeynerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 163 FAVVLGGPQETG-QLLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 240
Cdd:cd07145 183 INVVTGYGSEVGdEIVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 241 GQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLL------GcGRVAIGGQSDEGE 313
Cdd:cd07145 263 GQVCNAVKRILVEEEVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVndavekG-GKILYGGKRDEGS 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 314 rYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGfM 393
Cdd:cd07145 342 -FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDS-T 419
|
410
....*....|....*....
gi 1958646404 394 HMTLSSLPFGGVGTSGMGR 412
Cdd:cd07145 420 RFRWDNLPFGGFKKSGIGR 438
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
98-420 |
2.26e-55 |
|
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: 191.03 E-value: 2.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 98 AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFAVVLGGPQETGQ-L 176
Cdd:cd07108 111 TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGYGEECGAaL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 177 LEHR-FDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYV--DDNCDpQTVANRVAWFRYFNAGQTCVAPDYVLCS 253
Cdd:cd07108 191 VDHPdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVfpDADLD-DAVDGAIAGMRFTRQGQSCTAGSRLFVH 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 254 QEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCG------RVAIGGQSDEGER-----YIAPTVL 321
Cdd:cd07108 270 EDIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDLGlstsgaTVLRGGPLPGEGPladgfFVQPTIF 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 322 VDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMtlSSLP 401
Cdd:cd07108 350 SGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQ--PGQS 427
|
330
....*....|....*....
gi 1958646404 402 FGGVGTSGMGRyhgKFSFD 420
Cdd:cd07108 428 YGGFKQSGLGR---EASLE 443
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
2-426 |
3.25e-55 |
|
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: 190.34 E-value: 3.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 2 DSFEDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSafesevseiaISQA--EVDLALRNLR 79
Cdd:cd07094 21 ADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKP----------IKDArvEVDRAIDTLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 80 ------SWMKDEKVSKNLATQLDS--AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILA 151
Cdd:cd07094 91 laaeeaERIRGEEIPLDATQGSDNrlAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 152 EVL-PRYLDQSCFAVVLGGPQETGQLL--EHRFDYIFFTGNTYVGKIVMAAAAKhlTPITLELGGKNPCYVDDNCDPQTV 228
Cdd:cd07094 171 KILvEAGVPEGVLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 229 ANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNP-QTSPNLGRIINQKHFERLQ-----GLLGCGR 302
Cdd:cd07094 249 IEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPlDEDTDVGPLISEEAAERVErwveeAVEAGAR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 303 VAIGGQSDegERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTS 382
Cdd:cd07094 329 LLCGGERD--GALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLE 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958646404 383 SGGFCGNDGfMHMTLSSLPFGGVGTSGMGRYHGKFSFDTFSNQR 426
Cdd:cd07094 407 VGGVMVNDS-SAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEK 449
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
12-369 |
3.34e-55 |
|
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: 190.94 E-value: 3.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVsEIAISQAEVDLALRNLRSW----MKDEKV 87
Cdd:cd07088 45 EAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARRIegeiIPSDRP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 88 SKNLatqldsaFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPRYLdqsc 162
Cdd:cd07088 124 NENI-------FIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELvdeagLPAGV---- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 163 FAVVLGGPQETGQLL-EH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 240
Cdd:cd07088 193 LNIVTGRGSVVGDALvAHpKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINC 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 241 GQTCVAPD--YVLCS--QEMQERLVPALQNAItrfYGDNPQTSPNLGRIINQKHFERLQGLL------GcGRVAIGGQSD 310
Cdd:cd07088 273 GQVCTCAErvYVHEDiyDEFMEKLVEKMKAVK---VGDPFDAATDMGPLVNEAALDKVEEMVeraveaG-ATLLTGGKRP 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958646404 311 EGER--YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSK 369
Cdd:cd07088 349 EGEKgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTE 409
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
99-427 |
8.09e-55 |
|
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: 189.57 E-value: 8.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 99 FIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGPQETGQ-L 176
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAaL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 177 LEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQE 255
Cdd:cd07115 192 VEHpDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 256 MQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQSDeGER--YIAPTVLVDVQET 327
Cdd:cd07115 272 IYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGreegaRLLTGGKRP-GARgfFVEPTIFAAVPPE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 328 EPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDgfMHMTLSSLPFGGVGT 407
Cdd:cd07115 351 MRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINT--YNRFDPGSPFGGYKQ 428
|
330 340
....*....|....*....|
gi 1958646404 408 SGMGRYHGKFSFDTFSNQRA 427
Cdd:cd07115 429 SGFGREMGREALDEYTEVKS 448
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
12-423 |
2.60e-54 |
|
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: 188.48 E-value: 2.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAiSQAEVDLALRNLRSWMKDEKVSKNL 91
Cdd:TIGR01804 45 RRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLETLDTGKTLQETIVADMD-SGADVFEFFAGLAPALNGEIIPLGG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 92 ATQldsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGP 170
Cdd:TIGR01804 124 PSF---AYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 171 QETGQLL-EHR-FDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD 248
Cdd:TIGR01804 201 AEVGPLLvNHPdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGT 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 249 YVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQSDEGER-----YIA 317
Cdd:TIGR01804 281 RVFVHKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIEKGkaegaTLATGGGRPENVGlqngfFVE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 318 PTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDgfMHMTL 397
Cdd:TIGR01804 361 PTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYP 438
|
410 420
....*....|....*....|....*.
gi 1958646404 398 SSLPFGGVGTSGMGRYHGKFSFDTFS 423
Cdd:TIGR01804 439 AEAPFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
98-427 |
2.00e-53 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 186.46 E-value: 2.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 98 AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGPQETGQ- 175
Cdd:cd07144 138 AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSa 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 176 LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 254
Cdd:cd07144 218 LAEHpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 255 EMQERLVPALQNAITRFY--GDNPQTSPNLGRIINQKHFERLQGLLGCGR------VAIGGQSDEGER---YIAPTVLVD 323
Cdd:cd07144 298 SIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKkegaklVYGGEKAPEGLGkgyFIPPTIFTD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 324 VQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGF---CGNDGFMHMtlssl 400
Cdd:cd07144 378 VPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVwinSSNDSDVGV----- 452
|
330 340
....*....|....*....|....*..
gi 1958646404 401 PFGGVGTSGMGRYHGKFSFDTFSNQRA 427
Cdd:cd07144 453 PFGGFKMSGIGRELGEYGLETYTQTKA 479
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
8-412 |
3.20e-53 |
|
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: 185.11 E-value: 3.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 8 LQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSafesevseIAISQAEVDLALRNLRsWMKDEkv 87
Cdd:cd07149 27 IAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKP--------IKDARKEVDRAIETLR-LSAEE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 88 SKNLATQ---LDS--------AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPR 156
Cdd:cd07149 96 AKRLAGEtipFDAspggegriGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 157 -YLDQSCFAVVLGGPQETG-QLLEH-RFDYIFFTGNTYVGKIVMAAAAkhLTPITLELGGKNPCYVDDNCDPQTVANRVA 233
Cdd:cd07149 176 aGLPKGALNVVTGSGETVGdALVTDpRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 234 WFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGD--NPQTspNLGRIINQKHFERLQGLL-----GCGRVAI 305
Cdd:cd07149 254 SGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLvVGDplDEDT--DVGPMISEAEAERIEEWVeeaveGGARLLT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 306 GGQSDegERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGG 385
Cdd:cd07149 332 GGKRD--GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGG 409
|
410 420 430
....*....|....*....|....*....|.
gi 1958646404 386 FCGNDG----FMHMtlsslPFGGVGTSGMGR 412
Cdd:cd07149 410 VMINDSstfrVDHM-----PYGGVKESGTGR 435
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
12-416 |
1.01e-52 |
|
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: 183.66 E-value: 1.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHK---SAFEsEVSEIAISQAEVdlaLRNLRSWMKDEKVS 88
Cdd:cd07101 28 RAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarrHAFE-EVLDVAIVARYY---ARRAERLLKPRRRR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 89 KNLATqLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPRYLdqscF 163
Cdd:cd07101 104 GAIPV-LTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELlieagLPRDL----W 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 164 AVVLGGPQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVAnRVAWFRYF-NAGQ 242
Cdd:cd07101 179 QVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAA-AGAVRACFsNAGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 243 TCVAPD--YVLCS--QEMQERLVPALQNAITrfyGDNPQTSPNLGRIINQKHFERLQGLLGCGR-----VAIGGQS--DE 311
Cdd:cd07101 258 LCVSIEriYVHESvyDEFVRRFVARTRALRL---GAALDYGPDMGSLISQAQLDRVTAHVDDAVakgatVLAGGRArpDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 312 GERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDG 391
Cdd:cd07101 335 GPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEG 414
|
410 420
....*....|....*....|....*..
gi 1958646404 392 FMhMTLSSL--PFGGVGTSGMGRYHGK 416
Cdd:cd07101 415 YA-AAWASIdaPMGGMKDSGLGRRHGA 440
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-412 |
4.39e-52 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 182.93 E-value: 4.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 8 LQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESevseiaiSQAEVDLALRNLRSWMKDEKV 87
Cdd:cd07559 44 VDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRET-------LAADIPLAIDHFRYFAGVIRA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 88 SKNLATQLDS---AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFA 164
Cdd:cd07559 117 QEGSLSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 165 VVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNP-------CYVDDNCDPQTVANRVAWF 235
Cdd:cd07559 197 VVTGFGSEAGKpLASHpRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPniffddaMDADDDFDDKAEEGQLGFA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 236 ryFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQ-TSPNLGRIINQKHFERLQGLLGCGR-----VAIGGQ- 308
Cdd:cd07559 277 --FNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLdPETMMGAQVSKDQLEKILSYVDIGKeegaeVLTGGEr 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 309 ----SDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSG 384
Cdd:cd07559 355 ltlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTG 434
|
410 420
....*....|....*....|....*...
gi 1958646404 385 GFCGNDgfMHMTLSSLPFGGVGTSGMGR 412
Cdd:cd07559 435 RVWVNC--YHQYPAHAPFGGYKKSGIGR 460
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
98-427 |
5.69e-52 |
|
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: 181.98 E-value: 5.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 98 AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPRYLdqscFAVVLGGPQE 172
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPPGV----VNVVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 173 TGQLL-EH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYV 250
Cdd:cd07114 189 TGEALvEHpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 251 LCSQEMQERLVPALQnAITRF--YGD--NPQTspNLGRIINQKHFERLQGLLGC-----GRVAIGGQSDEGER-----YI 316
Cdd:cd07114 269 LVQRSIYDEFVERLV-ARARAirVGDplDPET--QMGPLATERQLEKVERYVARareegARVLTGGERPSGADlgagyFF 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 317 APTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDgfmHMT 396
Cdd:cd07114 346 EPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT---YRA 422
|
330 340 350
....*....|....*....|....*....|..
gi 1958646404 397 LS-SLPFGGVGTSGMGRYHGKFSFDTFSNQRA 427
Cdd:cd07114 423 LSpSSPFGGFKDSGIGRENGIEAIREYTQTKS 454
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
12-422 |
9.12e-52 |
|
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: 181.62 E-value: 9.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAG---RTRSAEfRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAISQAEVDLALRNLRSW-MKDEKV 87
Cdd:cd07139 46 RRAFDNGpwpRLSPAE-RAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFpFEERRP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 88 SKNLATQLdsafIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPryldQSC 162
Cdd:cd07139 125 GSGGGHVL----VRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAaeeagLP----PGV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 163 FAVVLGGPQETGQLLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 241
Cdd:cd07139 197 VNVVPADREVGEYLVRHpGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 242 QTCVAPDYVLCSQEMQERLVPALQNAITRF-YGD--NPQTSpnLGRIINQKHFERLQGLLGCG-----RVAIGGQSDEG- 312
Cdd:cd07139 277 QVCVALTRILVPRSRYDEVVEALAAAVAALkVGDplDPATQ--IGPLASARQRERVEGYIAKGraegaRLVTGGGRPAGl 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 313 ER--YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGND 390
Cdd:cd07139 355 DRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNG 434
|
410 420 430
....*....|....*....|....*....|..
gi 1958646404 391 GFMHMtlsSLPFGGVGTSGMGRYHGKFSFDTF 422
Cdd:cd07139 435 FRLDF---GAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
98-411 |
9.74e-52 |
|
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: 181.02 E-value: 9.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 98 AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGPQETGQL 176
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 177 LEH--RFDYIFFTGNTYVGKIVMAAAAkhLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 254
Cdd:cd07146 194 LIThpDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 255 EMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQK---HFE-RLQGLLGCG-RVAIGGQSDeGERYiAPTVLVDVQETE 328
Cdd:cd07146 272 SVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDEEaaiQIEnRVEEAIAQGaRVLLGNQRQ-GALY-APTVLDHVPPDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 329 PVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGfMHMTLSSLPFGGVGTS 408
Cdd:cd07146 350 ELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEV-PGFRSELSPFGGVKDS 428
|
...
gi 1958646404 409 GMG 411
Cdd:cd07146 429 GLG 431
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
2-427 |
2.09e-51 |
|
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: 181.01 E-value: 2.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 2 DSFEDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFES--EVSEiAISQAevDLALRNLR 79
Cdd:cd07131 37 SDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGrgDVQE-AIDMA--QYAAGEGR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 80 SwMKDEKVSKNLATQLdsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-L 158
Cdd:cd07131 114 R-LFGETVPSELPNKD--AMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 159 DQSCFAVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFR 236
Cdd:cd07131 191 PPGVVNVVHGRGEEVGEaLVEHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 237 YFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNL-GRIINQKHFERLQG-----------LLGCGRVA 304
Cdd:cd07131 271 FGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDmGPLINEAQLEKVLNyneigkeegatLLLGGERL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 305 IGGQSDEGeRYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPL--ALYA--FSKRSQVIKQVLAr 380
Cdd:cd07131 351 TGGGYEKG-YFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLssAIYTedVNKAFRARRDLEA- 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958646404 381 tssggfcgndGFMHMTLSS------LPFGGVGTSGMG-RYHGKFSFDTFSNQRA 427
Cdd:cd07131 429 ----------GITYVNAPTigaevhLPFGGVKKSGNGhREAGTTALDAFTEWKA 472
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
98-412 |
1.03e-50 |
|
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: 178.94 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 98 AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPryldQSCFA-----VVLG-GPQ 171
Cdd:cd07091 135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIK----EAGFPpgvvnIVPGfGPT 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 172 ETGQLLEH-RFDYIFFTGNTYVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANrVAWFR-YFNAGQTCVAPD 248
Cdd:cd07091 211 AGAAISSHmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVE-WAAFGiFFNQGQCCCAGS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 249 YVLCSQEMQERLVPAL-QNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQ--SDEGeRYIAPTV 320
Cdd:cd07091 290 RIFVQESIYDEFVEKFkARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESGkkegaTLLTGGErhGSKG-YFIQPTV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 321 LVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGfmHMTLSSL 400
Cdd:cd07091 369 FTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTY--NVFDAAV 446
|
330
....*....|..
gi 1958646404 401 PFGGVGTSGMGR 412
Cdd:cd07091 447 PFGGFKQSGFGR 458
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
9-415 |
1.03e-49 |
|
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: 175.56 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 9 QQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQD----LHKSAFESEVSEIAISQAevdlalrnlrswmkd 84
Cdd:cd07152 20 ARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVREsgsiRPKAGFEVGAAIGELHEA--------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 85 ekvsKNLATQ-----LDSA-----FIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEK-ILAEV 153
Cdd:cd07152 85 ----AGLPTQpqgeiLPSApgrlsLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGvVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 154 -----LPRYLDQscfavVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQ 226
Cdd:cd07152 161 feeagLPAGVLH-----VLPGGADAGEaLVEDpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 227 TVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSP-NLGRIINQKHFERLQGL------LG 299
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIvddsvaAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 300 cGRVAIGGQSDegERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLA 379
Cdd:cd07152 316 -ARLEAGGTYD--GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958646404 380 RTSSGGFCGNDGfmhmTLSS---LPFGGVGTSGMGRYHG 415
Cdd:cd07152 393 RLRTGMLHINDQ----TVNDephNPFGGMGASGNGSRFG 427
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
5-431 |
1.14e-49 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 176.34 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 5 EDKLQQLREAFNAGRTRSAEF-------RAAQLQGLSHFLRDNKQQLQEALAQDLHK---SAFESEVSEIAISQAEVDLA 74
Cdd:TIGR03374 34 EASAEQVDAAVRAADAAFAEWgqttpkaRAECLLKLADVIEENAQVFAELESRNCGKplhSVFNDEIPAIVDVFRFFAGA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 75 LRNLRSWMKDEKVSKNlatqldSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVL 154
Cdd:TIGR03374 114 ARCLSGLAAGEYLEGH------TSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 155 PRYLDQSCFAVVLGGPQETGQLL--EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRV 232
Cdd:TIGR03374 188 KDIFPAGVVNILFGRGKTVGDPLtgHEKVRMVSLTGSIATGEHILSHTAPSIKRTHMELGGKAPVIVFDDADIDAVVEGV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 233 AWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGL------LGCGRVAI 305
Cdd:TIGR03374 268 RTFGFYNAGQDCTAACRIYAQRGIYDTLVEKLGAAVATLkSGAPDDESTELGPLSSLAHLERVMKAveeakaLGHIKVIT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 306 GGQSDEGE-RYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSG 384
Cdd:TIGR03374 348 GGEKRKGNgYYFAPTLLAGAKQDDAIVQKEVFGPVVSITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYG 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958646404 385 GFCGNDGFmhMTLSSLPFGGVGTSGMGRYHGKFSFDTFSNQRACLLR 431
Cdd:TIGR03374 428 CTWVNTHF--MLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHIMVK 472
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
5-422 |
1.94e-49 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 176.03 E-value: 1.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 5 EDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESeVSEIAISQAEVDlalrnlrsWMKD 84
Cdd:PLN02278 65 NDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEA-IGEVAYGASFLE--------YFAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 85 E--KVSKNL--ATQLDS-AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-L 158
Cdd:PLN02278 136 EakRVYGDIipSPFPDRrLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 159 DQSCFAVVLGGPQETGQLL--EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFR 236
Cdd:PLN02278 216 PPGVLNVVMGDAPEIGDALlaSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 237 YFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQG------------LLGCGRV 303
Cdd:PLN02278 296 FRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVEShvqdavskgakvLLGGKRH 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 304 AIGGQsdegerYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSS 383
Cdd:PLN02278 376 SLGGT------FYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEY 449
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958646404 384 GGFCGNDGFMHMTlsSLPFGGVGTSGMGRYHGKFSFDTF 422
Cdd:PLN02278 450 GIVGVNEGLISTE--VAPFGGVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
5-431 |
2.55e-49 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 175.32 E-value: 2.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 5 EDKLQQLREAF-NAGRTRSAEFRAAQLQGLShflrDNKQQLQEALAQdlhksaFESEVS--EIAISQA-EVDLALRNLR- 79
Cdd:cd07113 40 DAAVASAWRAFvSAWAKTTPAERGRILLRLA----DLIEQHGEELAQ------LETLCSgkSIHLSRAfEVGQSANFLRy 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 80 --SWMKdeKVS-KNLATQLDS-------AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKI 149
Cdd:cd07113 110 faGWAT--KINgETLAPSIPSmqgerytAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 150 LAEV-----LPryldQSCFAVVLGGPQETGQLLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNC 223
Cdd:cd07113 188 VAELakeagIP----DGVLNVVNGKGAVGAQLISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 224 DPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFY-GDNPQTSPNLGRIINQKHFERLQGLLGCGR 302
Cdd:cd07113 264 DIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLDDAR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 303 -----VAIGGQSDEGERY-IAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINrrEKPLALYAfSKRSQVIKQ 376
Cdd:cd07113 344 aegdeIVRGGEALAGEGYfVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLIN--DTPFGLTA-SVWTNNLSK 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958646404 377 VL---ARTSSGGFCGNdgfMHMTLS-SLPFGGVGTSGMGRYHGKFSFDTFSNQRACLLR 431
Cdd:cd07113 421 ALryiPRIEAGTVWVN---MHTFLDpAVPFGGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
12-423 |
1.72e-48 |
|
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: 172.82 E-value: 1.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEvseiaisqAEVDLALRNLR-------SWMKD 84
Cdd:cd07097 47 AAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEAR--------GEVTRAGQIFRyyagealRLSGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 85 EKVSKNLATQLdsaFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCF 163
Cdd:cd07097 119 TLPSTRPGVEV---ETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 164 AVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 241
Cdd:cd07097 196 NLVMGSGSEVGQaLVEHpDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 242 QTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERL-----QGLLGCGRVAIGGQSDEGER- 314
Cdd:cd07097 276 QRCTASSRLIVTEGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDlryieIARSEGAKLVYGGERLKRPDe 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 315 --YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLAL--------YA--FSKRSQ--VIKqVLAR 380
Cdd:cd07097 356 gyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAgivttslkHAthFKRRVEagVVM-VNLP 434
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958646404 381 TSsggfcGNDgfMHmtlssLPFGGVGTSGMG-RYHGKFSFDTFS 423
Cdd:cd07097 435 TA-----GVD--YH-----VPFGGRKGSSYGpREQGEAALEFYT 466
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
12-415 |
1.23e-47 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 171.60 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEaLAQ----DLHKSAFEsEVSEIAISqaevdlAL---RNLRSWMKD 84
Cdd:PRK09407 64 RAAQRAWAATPVRERAAVLLRFHDLVLENREELLD-LVQletgKARRHAFE-EVLDVALT------ARyyaRRAPKLLAP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 85 EKVSKNLATqLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPRYLd 159
Cdd:PRK09407 136 RRRAGALPV-LTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELlyeagLPRDL- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 160 qscFAVVLGGPQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 239
Cdd:PRK09407 214 ---WQVVTGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSN 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 240 AGQTCVAPDYVLCSQEMQERLVPALQNAITRF-----YGDNPQtspnLGRIINQKHFERLQGLLGCGR-----VAIGGQS 309
Cdd:PRK09407 291 AGQLCISIERIYVHESIYDEFVRAFVAAVRAMrlgagYDYSAD----MGSLISEAQLETVSAHVDDAVakgatVLAGGKA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 310 --DEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINrrEKPLALYA--FSKRSQVIKQVLARTSSGG 385
Cdd:PRK09407 367 rpDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAN--DTPYGLNAsvWTGDTARGRAIAARIRAGT 444
|
410 420 430
....*....|....*....|....*....|..
gi 1958646404 386 FCGNDGFMhMTLSSL--PFGGVGTSGMGRYHG 415
Cdd:PRK09407 445 VNVNEGYA-AAWGSVdaPMGGMKDSGLGRRHG 475
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
12-423 |
3.17e-47 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 169.56 E-value: 3.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESevseiaiSQAEVDLALRNLRSWMKDEKVSKNL 91
Cdd:cd07117 48 QEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRET-------RAVDIPLAADHFRYFAGVIRAEEGS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 92 ATQLDSAF---IRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKAT----EKILAEVLPRyldqSCFA 164
Cdd:cd07117 121 ANMIDEDTlsiVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSllelAKIIQDVLPK----GVVN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 165 VVLGGPQETGQ-LLEHR-FDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 242
Cdd:cd07117 197 IVTGKGSKSGEyLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 243 TCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQT-SPNLGRIINQKHFERLQGLLGCG-----RVAIGGQS------D 310
Cdd:cd07117 277 VCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDpDTQMGAQVNKDQLDKILSYVDIAkeegaKILTGGHRltenglD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 311 EGErYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGND 390
Cdd:cd07117 357 KGF-FIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNT 435
|
410 420 430
....*....|....*....|....*....|...
gi 1958646404 391 gfMHMTLSSLPFGGVGTSGMGRYHGKFSFDTFS 423
Cdd:cd07117 436 --YNQIPAGAPFGGYKKSGIGRETHKSMLDAYT 466
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-422 |
7.82e-47 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 169.14 E-value: 7.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAF--NAGRTRSA---EFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESE-----VS---EIAISQAEvdlALrnl 78
Cdd:PLN02467 55 RKAFkrNKGKDWARttgAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAwdmddVAgcfEYYADLAE---AL--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 79 rswmkDEKVSKNLATQLDS--AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV--- 153
Cdd:PLN02467 129 -----DAKQKAPVSLPMETfkGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADIcre 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 154 --LPRyldqSCFAVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDpqtVA 229
Cdd:PLN02467 204 vgLPP----GVLNVVTGLGTEAGApLASHpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVD---LD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 230 NRVAW--FRYF-NAGQTCVAPDYVLCSQ----EMQERLVPALQNaITrfYGDNPQTSPNLGRIINQKHFERLQGLLGCGR 302
Cdd:PLN02467 277 KAVEWamFGCFwTNGQICSATSRLLVHEriasEFLEKLVKWAKN-IK--ISDPLEEGCRLGPVVSEGQYEKVLKFISTAK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 303 -----VAIGGQSDEGER---YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVI 374
Cdd:PLN02467 354 segatILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERC 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958646404 375 KQVLARTSSGGF---CGNDGFmhmtlSSLPFGGVGTSGMGRYHGKFSFDTF 422
Cdd:PLN02467 434 ERVSEAFQAGIVwinCSQPCF-----CQAPWGGIKRSGFGRELGEWGLENY 479
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
14-412 |
2.97e-46 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 166.98 E-value: 2.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 14 AFNAGR----TRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESevseiaisQAEVD----------LALRNL- 78
Cdd:cd07082 47 AYDAGRgwwpTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDA--------LKEVDrtidyirdtiEELKRLd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 79 RSWMKDEKVSKNLATQldsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPseiskATE-KILAEVLPRY 157
Cdd:cd07082 119 GDSLPGDWFPGTKGKI---AQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKP-----ATQgVLLGIPLAEA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 158 LDQSCF-----AVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKhlTPITLELGGKNPCYVDDNCDPQTVAN 230
Cdd:cd07082 191 FHDAGFpkgvvNVVTGRGREIGDpLVTHgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 231 RVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNP-QTSPNLGRIINQKHFERLQGLL------GcGRV 303
Cdd:cd07082 269 EIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPwDNGVDITPLIDPKSADFVEGLIddavakG-ATV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 304 AIGGQSdEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSS 383
Cdd:cd07082 348 LNGGGR-EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEV 426
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958646404 384 G-----GFC--GNDGFmhmtlsslPFGGVGTSGMGR 412
Cdd:cd07082 427 GtvninSKCqrGPDHF--------PFLGRKDSGIGT 454
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
98-427 |
3.10e-46 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 166.94 E-value: 3.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 98 AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGPQETGQL 176
Cdd:cd07143 138 TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 177 LE-H-RFDYIFFTGNTYVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCS 253
Cdd:cd07143 218 ISsHmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 254 QEMQERLVPALQNAITRFYGDNPqTSPNL--GRIINQKHFERLQGLLGCGR-----VAIGGQSDEGERY-IAPTVLVDVQ 325
Cdd:cd07143 298 EGIYDKFVKRFKEKAKKLKVGDP-FAEDTfqGPQVSQIQYERIMSYIESGKaegatVETGGKRHGNEGYfIEPTIFTDVT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 326 ETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKR-SQVIKQVLARTSSGGFCGNDGFMHmtlSSLPFGG 404
Cdd:cd07143 377 EDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNiNNAIRVANALKAGTVWVNCYNLLH---HQVPFGG 453
|
330 340
....*....|....*....|...
gi 1958646404 405 VGTSGMGRYHGKFSFDTFSNQRA 427
Cdd:cd07143 454 YKQSGIGRELGEYALENYTQIKA 476
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
98-423 |
4.06e-46 |
|
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: 166.33 E-value: 4.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 98 AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGpQETGQL 176
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 177 LEHRFDY--IFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVL--- 251
Cdd:cd07090 189 LCEHPDVakVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFvqr 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 252 -CSQEMQERLVPALQNAITrfyGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQSD------EGERYIAPT 319
Cdd:cd07090 269 sIKDEFTERLVERTKKIRI---GDPLDEDTQMGALISEEHLEKVLGYIESAkqegaKVLCGGERVvpedglENGFYVSPC 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 320 VLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDgfMHMTLSS 399
Cdd:cd07090 346 VLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVE 423
|
330 340
....*....|....*....|....
gi 1958646404 400 LPFGGVGTSGMGRYHGKFSFDTFS 423
Cdd:cd07090 424 VPFGGYKQSGFGRENGTAALEHYT 447
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
12-423 |
2.26e-45 |
|
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: 164.05 E-value: 2.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGR-TRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVsEIAISQAEVD----LAlRNLRSWMKDEK 86
Cdd:cd07120 29 RRAFDETDwAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF-EISGAISELRyyagLA-RTEAGRMIEPE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 87 vSKNLATQLdsafirKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKP----SEISKATEKILAEVlpRYLDQSC 162
Cdd:cd07120 107 -PGSFSLVL------REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPagqtAQINAAIIRILAEI--PSLPAGV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 163 FAVVLGGPQETGQLL--EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 240
Cdd:cd07120 178 VNLFTESGSEGAAHLvaSPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 241 GQTCVAPDYVLC----SQEMQERLVPALQNAITrfyGDNPQTSPNLGRIINQKHFERLQGLLG-----CGRVAI-GGQSD 310
Cdd:cd07120 258 GQFCMAGSRVLVqrsiADEVRDRLAARLAAVKV---GPGLDPASDMGPLIDRANVDRVDRMVEraiaaGAEVVLrGGPVT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 311 EGER---YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFC 387
Cdd:cd07120 335 EGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVW 414
|
410 420 430
....*....|....*....|....*....|....*..
gi 1958646404 388 GNDgfmHMTL-SSLPFGGVGTSGMGRYHGKFSFDTFS 423
Cdd:cd07120 415 IND---WNKLfAEAEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
12-415 |
5.44e-45 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 162.93 E-value: 5.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDlhkSAFesEVSEIAisqAEVDLALRNLRSWmkdekvsKNL 91
Cdd:cd07107 29 RAAFPEWRATTPLERARMLRELATRLREHAEELALIDALD---CGN--PVSAML---GDVMVAAALLDYF-------AGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 92 ATQLDSA----------FIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQS 161
Cdd:cd07107 94 VTELKGEtipvggrnlhYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 162 CFAVVLGGPQETGQ-LLEHR-FDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANR-VAWFRYF 238
Cdd:cd07107 174 VFNILPGDGATAGAaLVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAaVAGMNFT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 239 NAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPqTSPN--LGRIINQKHFERLQGLLGCG-----RVAIGGQSDE 311
Cdd:cd07107 254 WCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDP-TDPAttMGPLVSRQQYDRVMHYIDSAkregaRLVTGGGRPE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 312 GER-----YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREkpLALYAfSKRSQVIKQVL--ARTSSG 384
Cdd:cd07107 333 GPAleggfYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVE--YGLTA-AIWTNDISQAHrtARRVEA 409
|
410 420 430
....*....|....*....|....*....|..
gi 1958646404 385 GFCG-NDGFMHMTlsSLPFGGVGTSGMGRYHG 415
Cdd:cd07107 410 GYVWiNGSSRHFL--GAPFGGVKNSGIGREEC 439
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
4-356 |
8.91e-45 |
|
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: 163.55 E-value: 8.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 4 FEDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFES--EVSEiAISQAE--VDLALRNLR 79
Cdd:cd07124 71 AEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEAdaDVAE-AIDFLEyyAREMLRLRG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 80 SWMKDEKVSKNlatqldsaFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-L 158
Cdd:cd07124 150 FPVEMVPGEDN--------RYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 159 DQSCFAVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAK------HLTPITLELGGKNPCYVDDNCDPQTVAN 230
Cdd:cd07124 222 PPGVVNFLPGPGEEVGDyLVEHpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 231 RV--AWFRYfnAGQTCVApdyvlCS---------QEMQERLVpALQNAITrfYGDNPQTSPNLGRIINQKHFERLQGLL- 298
Cdd:cd07124 302 GIvrSAFGF--QGQKCSA-----CSrvivhesvyDEFLERLV-ERTKALK--VGDPEDPEVYMGPVIDKGARDRIRRYIe 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958646404 299 ---GCGRVAIGGQSDEGER---YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFIN 356
Cdd:cd07124 372 igkSEGRLLLGGEVLELAAegyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIAN 435
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
100-426 |
1.22e-44 |
|
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: 162.47 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 100 IRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSE---ISKATekILAEVLPRY-LDQSCFAVVLGGPQETG- 174
Cdd:cd07151 126 VYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASdtpITGGL--LLAKIFEEAgLPKGVLNVVVGAGSEIGd 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 175 QLLEHRF-DYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCS 253
Cdd:cd07151 204 AFVEHPVpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVH 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 254 QEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLL------GcGRVAIGGQSdEGeRYIAPTVLVDVQE 326
Cdd:cd07151 284 EDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIeqaveeG-ATLLVGGEA-EG-NVLEPTVLSDVTN 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 327 TEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHmTLSSLPFGGVG 406
Cdd:cd07151 361 DMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVN-DEPHVPFGGEK 439
|
330 340
....*....|....*....|
gi 1958646404 407 TSGMGRYHGKFSFDTFSNQR 426
Cdd:cd07151 440 NSGLGRFNGEWALEEFTTDK 459
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
67-427 |
4.90e-44 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 161.12 E-value: 4.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 67 SQAEVDLALRNLR---SWMKDEKVSKNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEIS 143
Cdd:cd07142 101 RYAEVPLAARLFRyyaGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQT 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 144 KATE----KILAEV-LPryldQSCFAVVLG-GPQETGQLLEHR-FDYIFFTGNTYVGKIVMAAAAK-HLTPITLELGGKN 215
Cdd:cd07142 181 PLSAllaaKLAAEAgLP----DGVLNIVTGfGPTAGAAIASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 216 PCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVP-ALQNAITRFYGDNPQTSPNLGRIINQKHFERL 294
Cdd:cd07142 257 PFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEkAKARALKRVVGDPFRKGVEQGPQVDKEQFEKI 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 295 QGLLGCG-----RVAIGGQS--DEGeRYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAF 367
Cdd:cd07142 337 LSYIEHGkeegaTLITGGDRigSKG-YYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVF 415
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958646404 368 SKRSQVIKQVLARTSSGGFCGN--DGFMhmtlSSLPFGGVGTSGMGRYHGKFSFDTFSNQRA 427
Cdd:cd07142 416 SKNIDTANTLSRALKAGTVWVNcyDVFD----ASIPFGGYKMSGIGREKGIYALNNYLQVKA 473
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
99-359 |
6.44e-44 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 159.13 E-value: 6.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 99 FIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGPQETGQLL 177
Cdd:PRK10090 66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 178 --EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQE 255
Cdd:PRK10090 146 agNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 256 MQERLVPALQNAITRFYGDNP--QTSPNLGRIINQKHFERLQGLLG-----CGRVAIGGQSDEGERYI-APTVLVDVQET 327
Cdd:PRK10090 226 IYDQFVNRLGEAMQAVQFGNPaeRNDIAMGPLINAAALERVEQKVAraveeGARVALGGKAVEGKGYYyPPTLLLDVRQE 305
|
250 260 270
....*....|....*....|....*....|..
gi 1958646404 328 EPVMQEEIFGPILPLVTVTNLDEAIEFINRRE 359
Cdd:PRK10090 306 MSIMHEETFGPVLPVVAFDTLEEAIAMANDSD 337
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
5-415 |
1.57e-43 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 160.42 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 5 EDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSeiaISQAeVDLALRNLRSWMKD 84
Cdd:TIGR01237 72 EHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAE---VAEA-IDFMEYYARQMIEL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 85 EKVSKNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCF 163
Cdd:TIGR01237 148 AKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAgLPKGVV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 164 AVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAK------HLTPITLELGGKNPCYVDDNCDPQTVANRVAWF 235
Cdd:TIGR01237 228 QFVPGSGSEVGDyLVDHpKTSLITFTGSREVGTRIFERAAKvqpgqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 236 RYFNAGQTCVAPDYVLCSQ----EMQERLVPALQNAITrfyGDNPQTSPNLGRIINQKHFERLQGLLGCG----RVAIGG 307
Cdd:TIGR01237 308 AFGFAGQKCSAGSRAVVHEkvydEVVERFVEITESLKV---GPPDSADVYVGPVIDQKSFNKIMEYIEIGkaegRLVSGG 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 308 QSDEGERY-IAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGF 386
Cdd:TIGR01237 385 CGDDSKGYfIGPTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNL 464
|
410 420
....*....|....*....|....*....
gi 1958646404 387 CGNDGFMHMTLSSLPFGGVGTSGMGRYHG 415
Cdd:TIGR01237 465 YFNRNITGAIVGYQPFGGFKMSGTDSKAG 493
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
4-428 |
1.69e-43 |
|
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: 159.65 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 4 FEDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFES--EVSE-IAISQAEVDLALRNLRS 80
Cdd:cd07086 37 VEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGlgEVQEmIDICDYAVGLSRMLYGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 81 WMKDEKVSKNLATQLdsafirkEPFGLVLIIVPWNYPL-----NLTLvplvgAIAAGNCVVLKPSE----ISKATEKILA 151
Cdd:cd07086 117 TIPSERPGHRLMEQW-------NPLGVVGVITAFNFPVavpgwNAAI-----ALVCGNTVVWKPSEttplTAIAVTKILA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 152 EVLPRY-LDQSCFAVVLGGpQETGQLLEH--RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTV 228
Cdd:cd07086 185 EVLEKNgLPPGVVNLVTGG-GDGGELLVHdpRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 229 ANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNL-GRIINQKHFERLQGLL------GcG 301
Cdd:cd07086 264 VRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLvGPLINQAAVEKYLNAIeiaksqG-G 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 302 RVAIGG---QSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVL 378
Cdd:cd07086 343 TVLTGGkriDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWL 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958646404 379 ARTSSGgfCG----NDGfmhmtlSS-----LPFGGVGTSGMGRYHGKFSFDTFSNQRAC 428
Cdd:cd07086 423 GPKGSD--CGivnvNIP------TSgaeigGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
12-423 |
5.19e-43 |
|
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: 158.28 E-value: 5.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAG---RTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESevseiaiSQAEVDLALRNLR---SWmKDE 85
Cdd:cd07141 54 RAAFKLGspwRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFSKS-------YLVDLPGAIKVLRyyaGW-ADK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 86 KVSKNLATQLDS-AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAE------------ 152
Cdd:cd07141 126 IHGKTIPMDGDFfTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASlikeagfppgvv 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 153 -VLPRYldqscfavvlgGPQETGQLLEH-RFDYIFFTGNTYVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVA 229
Cdd:cd07141 206 nVVPGY-----------GPTAGAAISSHpDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 230 NRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVP-ALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RV 303
Cdd:cd07141 275 EQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKrSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGkkegaKL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 304 AIGGqSDEGER--YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRsqvIKQVLArT 381
Cdd:cd07141 355 ECGG-KRHGDKgyFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD---IDKAIT-F 429
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1958646404 382 SSGGFCGN---DGFMHMTLSSlPFGGVGTSGMGRYHGKFSFDTFS 423
Cdd:cd07141 430 SNALRAGTvwvNCYNVVSPQA-PFGGYKMSGNGRELGEYGLQEYT 473
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
12-359 |
1.16e-41 |
|
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: 154.60 E-value: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFES--------EVSEIAISQAEVdlalrnlrswMK 83
Cdd:cd07085 48 KAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADArgdvlrglEVVEFACSIPHL----------LK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 84 DEkVSKNLATQLDSAFIRkEPFGLVLIIVPWNYPLnltLVPL---VGAIAAGNCVVLKPSEISKATEKILAEV-----LP 155
Cdd:cd07085 118 GE-YLENVARGIDTYSYR-QPLGVVAGITPFNFPA---MIPLwmfPMAIACGNTFVLKPSERVPGAAMRLAELlqeagLP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 156 RyldqSCFAVVLGGPQETGQLLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAW 234
Cdd:cd07085 193 D----GVLNVVHGGKEAVNALLDHpDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 235 FRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRF---YGDNPQTspNLGRIINQKHFERLQGLLGCG-----RVAIG 306
Cdd:cd07085 269 AAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLkvgAGDDPGA--DMGPVISPAAKERIEGLIESGveegaKLVLD 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958646404 307 G---QSDEGER--YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRRE 359
Cdd:cd07085 347 GrgvKVPGYENgnFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANP 404
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
13-412 |
1.42e-41 |
|
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: 153.56 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 13 EAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHK--SAFESEVSE-IAISQAEVDLALRNLRSWMKDEKVSK 89
Cdd:cd07147 32 KAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKpiKDARGEVARaIDTFRIAAEEATRIYGEVLPLDISAR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 90 NLATQldsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLG 168
Cdd:cd07147 112 GEGRQ---GLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETgLPKGAFSVLPC 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 169 GPQETGQLLEH-RFDYIFFTGNTYVG-KIVMAAAAKHltpITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA 246
Cdd:cd07147 189 SRDDADLLVTDeRIKLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCIS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 247 PDYVLCSQ----EMQERLVPALQNAITrfyGDNPQTSPNLGRIINQKHFERLQGLL-----GCGRVAIGGQSDEGerYIA 317
Cdd:cd07147 266 VQRVLVHRsvydEFKSRLVARVKALKT---GDPKDDATDVGPMISESEAERVEGWVneavdAGAKLLTGGKRDGA--LLE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 318 PTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGND--GFmhm 395
Cdd:cd07147 341 PTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDvpTF--- 417
|
410
....*....|....*..
gi 1958646404 396 TLSSLPFGGVGTSGMGR 412
Cdd:cd07147 418 RVDHMPYGGVKDSGIGR 434
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
102-422 |
7.07e-41 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 152.67 E-value: 7.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 102 KEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLG-GPQETGQLLEH 179
Cdd:PLN02766 156 KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGfGPTAGAAIASH 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 180 R-FDYIFFTGNTYVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQ 257
Cdd:PLN02766 236 MdVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIY 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 258 ERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCGR-----VAIGGQS--DEGeRYIAPTVLVDVQETEP 329
Cdd:PLN02766 316 DEFVKKLVEKAKDWvVGDPFDPRARQGPQVDKQQFEKILSYIEHGKregatLLTGGKPcgDKG-YYIEPTIFTDVTEDMK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 330 VMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVlARTSSGGFCGNDGFMHMTlSSLPFGGVGTSG 409
Cdd:PLN02766 395 IAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTV-SRSIRAGTIWVNCYFAFD-PDCPFGGYKMSG 472
|
330
....*....|...
gi 1958646404 410 MGRYHGKFSFDTF 422
Cdd:PLN02766 473 FGRDQGMDALDKY 485
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
14-411 |
9.65e-41 |
|
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: 152.35 E-value: 9.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 14 AFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAfeseVSEIAISQAEVDLALRNLRS---WMKDEKVSKN 90
Cdd:cd07083 67 AFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNW----VEAIDDVAEAIDFIRYYARAalrLRYPAVEVVP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 91 LATQLDSAFIRkePFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSE----ISKATEKILAEV-LPRYLDQSCFAV 165
Cdd:cd07083 143 YPGEDNESFYV--GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEdavvVGYKVFEIFHEAgFPPGVVQFLPGV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 166 vlgGPQETGQLLEH-RFDYIFFTGNTYVGKIVMAAAAKHLT------PITLELGGKNPCYVDDNCDPQTVANRVAWFRYF 238
Cdd:cd07083 221 ---GEEVGAYLTEHeRIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 239 NAGQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCGR----VAIGGQSDEGE 313
Cdd:cd07083 298 FQGQKCSAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKnegqLVLGGKRLEGE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 314 RY-IAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLD--EAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGND 390
Cdd:cd07083 378 GYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINR 457
|
410 420
....*....|....*....|.
gi 1958646404 391 GFMHMTLSSLPFGGVGTSGMG 411
Cdd:cd07083 458 KITGALVGVQPFGGFKLSGTN 478
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
92-416 |
5.17e-40 |
|
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: 149.85 E-value: 5.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 92 ATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGP 170
Cdd:cd07111 135 AQLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 171 QETGQLLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 249
Cdd:cd07111 215 SFGSALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 250 VLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERLQGLLGCGRvAIGGQ--------SDEGERYiAPTV 320
Cdd:cd07111 295 LLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADvfqpgadlPSKGPFY-PPTL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 321 LVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDgfMHMTLSSL 400
Cdd:cd07111 373 FTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING--HNLFDAAA 450
|
330
....*....|....*.
gi 1958646404 401 PFGGVGTSGMGRYHGK 416
Cdd:cd07111 451 GFGGYRESGFGREGGK 466
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
103-409 |
9.13e-40 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 150.09 E-value: 9.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 103 EPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGPQETGQ-LLEH- 179
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDyLVDHp 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 180 RFDYIFFTGNTYVGKIVMAAAAK------HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVApdyvlCS 253
Cdd:PRK03137 250 KTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSA-----CS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 254 Q---------EMQERLVpALQNAITrfYGdNPQTSPNLGRIINQKHFERLQGLL----GCGRVAIGGQSDEGERY-IAPT 319
Cdd:PRK03137 325 RaivhedvydEVLEKVV-ELTKELT--VG-NPEDNAYMGPVINQASFDKIMSYIeigkEEGRLVLGGEGDDSKGYfIQPT 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 320 VLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTLSS 399
Cdd:PRK03137 401 IFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGY 480
|
330
....*....|
gi 1958646404 400 LPFGGVGTSG 409
Cdd:PRK03137 481 HPFGGFNMSG 490
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
12-412 |
1.35e-39 |
|
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: 147.80 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEvSEIAISQAEVDLALRNLrswmkDEKVS-KN 90
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQ-TEVAAMAGKIDISIKAY-----HERTGeRA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 91 LATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVL-PRYLDQSCFAVVLGG 169
Cdd:cd07095 84 TPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPGVLNLVQGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 170 PQETGQLLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPI-TLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAP 247
Cdd:cd07095 164 RETGEALAAHeGIDGLLFTGSAATGLLLHRQFAGRPGKIlALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 248 DYVLCSQEMQ-ERLVPALQNAITRFYGDNPQTSPN-LGRIINQKHFERL----QGLLGCGRVAIGGQS--DEGERYIAPT 319
Cdd:cd07095 244 RRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPfMGPLIIAAAAARYllaqQDLLALGGEPLLAMErlVAGTAFLSPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 320 vLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGN---DGfmhmT 396
Cdd:cd07095 324 -IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNrptTG----A 398
|
410
....*....|....*.
gi 1958646404 397 LSSLPFGGVGTSGMGR 412
Cdd:cd07095 399 SSTAPFGGVGLSGNHR 414
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
98-423 |
7.48e-39 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 146.96 E-value: 7.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 98 AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGPQETGQL 176
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 177 L--EHRFDYIFFTGNTYVGKIVMA-AAAKHLTPITLELGGKNPCYVDDNC-DPQTVANRVAWFRYFNAGQTCVAPDYVLC 252
Cdd:PRK09847 231 LsrHNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 253 SQEMQERLVPALQNAITRFY-GD--NPQTSpnLGRIINQKHFER----LQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQ 325
Cdd:PRK09847 311 EESIADEFLALLKQQAQNWQpGHplDPATT--MGTLIDCAHADSvhsfIREGESKGQLLLDGRNAGLAAAIGPTIFVDVD 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 326 ETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALyAFSKRSQVIKQVLARTSSGG--FCG--NDGFMhmtlsSLP 401
Cdd:PRK09847 389 PNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGA-AVWTRDLSRAHRMSRRLKAGsvFVNnyNDGDM-----TVP 462
|
330 340
....*....|....*....|..
gi 1958646404 402 FGGVGTSGMGRYHGKFSFDTFS 423
Cdd:PRK09847 463 FGGYKQSGNGRDKSLHALEKFT 484
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
102-422 |
1.21e-37 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 143.51 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 102 KEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGPQETGQLLEHR 180
Cdd:PRK11241 144 KQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVGGELTSN 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 181 --FDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQE 258
Cdd:PRK11241 224 plVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYD 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 259 RLVPALQNAITRFY-GDNPQTSPNLGRIINQKHFERLQ-----GLLGCGRVAIGGQSDE-GERYIAPTVLVDVQETEPVM 331
Cdd:PRK11241 304 RFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPANAKVA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 332 QEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKR-SQVIKqvLARTSSGGFCG-NDGFMHMTLSslPFGGVGTSG 409
Cdd:PRK11241 384 KEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDlSRVFR--VGEALEYGIVGiNTGIISNEVA--PFGGIKASG 459
|
330
....*....|...
gi 1958646404 410 MGRYHGKFSFDTF 422
Cdd:PRK11241 460 LGREGSKYGIEDY 472
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
8-432 |
2.09e-37 |
|
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: 142.59 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 8 LQQLREAFNA-GRTRSAEfRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESevseiaiSQAEVDLALRNLRSWMKDEK 86
Cdd:cd07116 44 LDAAHAAKEAwGKTSVAE-RANILNKIADRMEANLEMLAVAETWDNGKPVRET-------LAADIPLAIDHFRYFAGCIR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 87 VSKNLATQLDS---AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCF 163
Cdd:cd07116 116 AQEGSISEIDEntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 164 AVVLGGPQETGQLL--EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNP-CYVDD--NCDPQTVANRVAWFRYF 238
Cdd:cd07116 196 NVVNGFGLEAGKPLasSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPnIFFADvmDADDAFFDKALEGFVMF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 239 --NAGQTCVAPDYVLCSQEMQERLvpaLQNAITRF----YGDNPQTSPNLGRIINQKHFERLQGLLGCGR-----VAIGG 307
Cdd:cd07116 276 alNQGEVCTCPSRALIQESIYDRF---MERALERVkaikQGNPLDTETMIGAQASLEQLEKILSYIDIGKeegaeVLTGG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 308 Q-----SDEGERYIAPTVLVDVQETEpVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTS 382
Cdd:cd07116 353 ErnelgGLLGGGYYVPTTFKGGNKMR-IFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQ 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958646404 383 SGGFCGNdgFMHMTLSSLPFGGVGTSGMGRYHGKFSFDTFsNQRACLLRS 432
Cdd:cd07116 432 AGRVWTN--CYHLYPAHAAFGGYKQSGIGRENHKMMLDHY-QQTKNLLVS 478
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
103-427 |
8.35e-37 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 141.87 E-value: 8.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 103 EPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLG-GPQETGQLLEHR 180
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGfGPTAGAALASHM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 181 -FDYIFFTGNTYVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQE 258
Cdd:PLN02466 274 dVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 259 RLV-PALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCG-----RVAIGGQ--SDEGeRYIAPTVLVDVQETEPV 330
Cdd:PLN02466 354 EFVeKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGvesgaTLECGGDrfGSKG-YYIQPTVFSNVQDDMLI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 331 MQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIkQVLARTSSGGFCGNDGFmHMTLSSLPFGGVGTSGM 410
Cdd:PLN02466 433 AQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTA-NTLSRALRVGTVWVNCF-DVFDAAIPFGGYKMSGI 510
|
330
....*....|....*..
gi 1958646404 411 GRYHGKFSFDTFSNQRA 427
Cdd:PLN02466 511 GREKGIYSLNNYLQVKA 527
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
96-423 |
2.22e-36 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 140.02 E-value: 2.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 96 DSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPRYLdqscFAVVlGGP 170
Cdd:PRK13252 134 SFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIyteagLPDGV----FNVV-QGD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 171 QETGQLL-EH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQT------VANrvawfrYFNAGQ 242
Cdd:PRK13252 209 GRVGAWLtEHpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRaadiamLAN------FYSSGQ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 243 TCVAPDYVLCSQEMQERLVPALQNAITRFY-GD--NPQTspNLGRIINQKHFERLQGLLGCG-----RVAIGGQ------ 308
Cdd:PRK13252 283 VCTNGTRVFVQKSIKAAFEARLLERVERIRiGDpmDPAT--NFGPLVSFAHRDKVLGYIEKGkaegaRLLCGGErltegg 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 309 SDEGErYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSK---RS-QVIKQVLArtssg 384
Cdd:PRK13252 361 FANGA-FVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTAdlsRAhRVIHQLEA----- 434
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958646404 385 GFC-----GNdgfmhmTLSSLPFGGVGTSGMGRYHGKFSFDTFS 423
Cdd:PRK13252 435 GICwintwGE------SPAEMPVGGYKQSGIGRENGIATLEHYT 472
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
99-412 |
4.27e-32 |
|
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: 128.00 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 99 FIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQSCFAVVLGGPQETGQLL 177
Cdd:cd07140 142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAgFPKGVINILPGSGSLVGQRL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 178 EHRFDY--IFFTGNTYVGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQ 254
Cdd:cd07140 222 SDHPDVrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 255 EMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERL-----QGLLGCGRVAIGG-QSDEGERYIAPTVLVDVQET 327
Cdd:cd07140 302 SIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLveyceRGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDH 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 328 EPVMQEEIFGPILPLVTVTN--LDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDgfMHMTLSSLPFGGV 405
Cdd:cd07140 382 MFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNT--YNKTDVAAPFGGF 459
|
....*..
gi 1958646404 406 GTSGMGR 412
Cdd:cd07140 460 KQSGFGK 466
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
2-411 |
7.41e-32 |
|
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: 127.70 E-value: 7.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 2 DSFEDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFE--SEVSEiAISQAE--VDLALRN 77
Cdd:cd07125 69 EDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADadAEVRE-AIDFCRyyAAQAREL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 78 LRSWMKDEKVSKNlatqldsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEIS-----KATEKILAE 152
Cdd:cd07125 148 FSDPELPGPTGEL-------NGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTpliaaRAVELLHEA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 153 VLPRYLDQscfaVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAAAKHLTPITL---ELGGKNPCYVDDNCDP-Q 226
Cdd:cd07125 221 GVPRDVLQ----LVPGDGEEIGEaLVAHpRIDGVIFTGSTETAKLINRALAERDGPILPliaETGGKNAMIVDSTALPeQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 227 TVANRVA-WFRyfNAGQTCVAPDyVLCSQE-MQERLVPALQNAITRFYGDNPQT-SPNLGRIINQKHFERLQGLL----G 299
Cdd:cd07125 297 AVKDVVQsAFG--SAGQRCSALR-LLYLQEeIAERFIEMLKGAMASLKVGDPWDlSTDVGPLIDKPAGKLLRAHTelmrG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 300 CGRVAIGGQSDEGE-RYIAPTVLVDVqeTEPVMQEEIFGPILPLVT--VTNLDEAIEFINRREKPLALYAFSKRSQVIKQ 376
Cdd:cd07125 374 EAWLIAPAPLDDGNgYFVAPGIIEIV--GIFDLTTEVFGPILHVIRfkAEDLDEAIEDINATGYGLTLGIHSRDEREIEY 451
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958646404 377 VLARTSSGGFCGNDGfmhMT---LSSLPFGGVGTSGMG 411
Cdd:cd07125 452 WRERVEAGNLYINRN---ITgaiVGRQPFGGWGLSGTG 486
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
2-424 |
1.27e-29 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 120.74 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 2 DSFEDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEvSEIAISQAEVDLALRNLRSW 81
Cdd:PRK13968 29 DDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVAKSANLCDWYAEHGPAM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 82 MKDEKVsknlATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRY-LDQ 160
Cdd:PRK13968 108 LKAEPT----LVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAgIPQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 161 SCFAVVLGGPQETGQLL-EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 239
Cdd:PRK13968 184 GVYGWLNADNDGVSQMInDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 240 AGQTCVAPDYVLC----SQEMQERLVPALQnAITrfYGDNPQTSPNLGRI----INQKHFERLQGLLGCG-RVAIGGQSD 310
Cdd:PRK13968 264 TGQVCAAAKRFIIeegiASAFTERFVAAAA-ALK--MGDPRDEENALGPMarfdLRDELHHQVEATLAEGaRLLLGGEKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 311 EGE-RYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSG----- 384
Cdd:PRK13968 341 AGAgNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGgvfin 420
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1958646404 385 GFCGNDgfmhmtlSSLPFGGVGTSGMGRYHGKFSFDTFSN 424
Cdd:PRK13968 421 GYCASD-------ARVAFGGVKKSGFGRELSHFGLHEFCN 453
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
12-409 |
1.51e-28 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 117.75 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 12 REAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEvSEIAISQAEVDLALR--NLRSWmkdEKVSK 89
Cdd:PRK09457 47 RAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAA-TEVTAMINKIAISIQayHERTG---EKRSE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 90 NLATQldsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV-----LPryldQSCFA 164
Cdd:PRK09457 123 MADGA---AVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLwqqagLP----AGVLN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 165 VVLGGPqETGQ-LLEHR-FDYIFFTGNTYVGKIVMAAAAKHLTPI-TLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 241
Cdd:PRK09457 196 LVQGGR-ETGKaLAAHPdIDGLLFTGSANTGYLLHRQFAGQPEKIlALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 242 QTCVAPDYVLCSQEMQ-ERLVPALQNAITRFYGDNP--QTSPNLGRIINQKHFERL----QGLLGCGRVAI--GGQSDEG 312
Cdd:PRK09457 275 QRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWdaEPQPFMGAVISEQAAQGLvaaqAQLLALGGKSLleMTQLQAG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 313 ERYIAPTvLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGN--- 389
Cdd:PRK09457 355 TGLLTPG-IIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNkpl 433
|
410 420
....*....|....*....|
gi 1958646404 390 DGfmhmTLSSLPFGGVGTSG 409
Cdd:PRK09457 434 TG----ASSAAPFGGVGASG 449
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
104-356 |
1.94e-26 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 111.53 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 104 PFGLVLIIVPWNYPL-----NLTLvplvgAIAAGNCVVLKPSE----ISKATEKILAEVLPRY-LDQSCFAVVLGGpQET 173
Cdd:cd07130 132 PLGVVGVITAFNFPVavwgwNAAI-----ALVCGNVVVWKPSPttplTAIAVTKIVARVLEKNgLPGAIASLVCGG-ADV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 174 GQLLEH--RFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVL 251
Cdd:cd07130 206 GEALVKdpRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 252 CSQEMQERLVPALQNAITRFYGDNPQTSPNL-GRIINQKHFERLQGLL------GcGRVAIGGQSDEGE-RYIAPTVlVD 323
Cdd:cd07130 286 VHESIYDEVLERLKKAYKQVRIGDPLDDGTLvGPLHTKAAVDNYLAAIeeaksqG-GTVLFGGKVIDGPgNYVEPTI-VE 363
|
250 260 270
....*....|....*....|....*....|...
gi 1958646404 324 VQETEPVMQEEIFGPILPLVTVTNLDEAIEFIN 356
Cdd:cd07130 364 GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
2-412 |
2.28e-26 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 110.98 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 2 DSFEDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSafesevseIAISQAEVDLALRNLRSW 81
Cdd:PRK09406 23 DEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT--------LASAKAEALKCAKGFRYY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 82 -------MKDE--KVSKNLATQldsAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAE 152
Cdd:PRK09406 95 aehaealLADEpaDAAAVGASR---AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 153 VLPRY-LDQSCFAVVL-GGPQETGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVAN 230
Cdd:PRK09406 172 LFRRAgFPDGCFQTLLvGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 231 RVAWFRYFNAGQTCVAPDYVLCS----QEMQERLVPALQnAITrfYGDNPQTSPNLGRIINQKHFERLQGLL-----GCG 301
Cdd:PRK09406 252 TAVTARVQNNGQSCIAAKRFIVHadvyDAFAEKFVARMA-ALR--VGDPTDPDTDVGPLATEQGRDEVEKQVddavaAGA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 302 RVAIGGQSDEGER-YIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSkRSQVIKQVLAR 380
Cdd:PRK09406 329 TILCGGKRPDGPGwFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWT-RDEAEQERFID 407
|
410 420 430
....*....|....*....|....*....|....
gi 1958646404 381 TSSGGFCGNDGfmhMTLS--SLPFGGVGTSGMGR 412
Cdd:PRK09406 408 DLEAGQVFING---MTVSypELPFGGVKRSGYGR 438
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
98-411 |
7.84e-26 |
|
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: 109.43 E-value: 7.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 98 AFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEIS----KATEKILAEV-LPrylDQSCFAVVLGGPQE 172
Cdd:cd07148 118 AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATplscLAFVDLLHEAgLP---EGWCQAVPCENAVA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 173 TGQLLEHRFDYIFFTGNTYVGKIVMAAAAKHlTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLC 252
Cdd:cd07148 195 EKLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 253 SQEMQERLVPALQNAITRF-YGDNPQTSPNLGRIINQKHFERL-----QGLLGCGRVAIGGQSdEGERYIAPTVLVDVQE 326
Cdd:cd07148 274 PAEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVeewvnEAVAAGARLLCGGKR-LSDTTYAPTVLLDPPR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 327 TEPVMQEEIFGPILPLVTVTNLDEAIEFINrrEKPLALYA--FSKRSQVIKQVLARTSSGGFCGNDgfmHMTLSS--LPF 402
Cdd:cd07148 353 DAKVSTQEIFGPVVCVYSYDDLDEAIAQAN--SLPVAFQAavFTKDLDVALKAVRRLDATAVMVND---HTAFRVdwMPF 427
|
....*....
gi 1958646404 403 GGVGTSGMG 411
Cdd:cd07148 428 AGRRQSGYG 436
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
103-411 |
9.33e-24 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 103.84 E-value: 9.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 103 EPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSE-----ISKATEKILAEVLPryldQSCFAVVLGGPQETGQLL 177
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEqtsliAYRAVELMQEAGFP----AGTIQLLPGRGADVGAAL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 178 --EHRFDYIFFTGNTYVGKIVMAAAAKHL---TPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDyVLC 252
Cdd:TIGR01238 235 tsDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALR-VLC 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 253 SQE-MQERLVPALQNAITRFYGDNP-QTSPNLGRIINQK-------HFERLQGLLGCGRVAIGGQSDEGER--YIAPTV- 320
Cdd:TIGR01238 314 VQEdVADRVLTMIQGAMQELKVGVPhLLTTDVGPVIDAEakqnllaHIEHMSQTQKKIAQLTLDDSRACQHgtFVAPTLf 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 321 -LVDVQEtepvMQEEIFGPILPLV--TVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTL 397
Cdd:TIGR01238 394 eLDDIAE----LSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVV 469
|
330
....*....|....
gi 1958646404 398 SSLPFGGVGTSGMG 411
Cdd:TIGR01238 470 GVQPFGGQGLSGTG 483
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
3-428 |
4.40e-23 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 101.83 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 3 SFEDKLQQLREAFNAGRT---RSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFES--EVSEIaisqaeVDlalrn 77
Cdd:PLN02315 54 SLEDYEEGLRACEEAAKIwmqVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGigEVQEI------ID----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 78 lrswMKDEKVSknLATQLDSAFIRKE-----------PFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLK--PSE--I 142
Cdd:PLN02315 123 ----MCDFAVG--LSRQLNGSIIPSErpnhmmmevwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKgaPTTplI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 143 SKATEKILAEVLPRY-LDQSCFAVVLGGpQETGQLL--EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYV 219
Cdd:PLN02315 197 TIAMTKLVAEVLEKNnLPGAIFTSFCGG-AEIGEAIakDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 220 DDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRF-YGDNPQTSPNLGRI---INQKHFE--- 292
Cdd:PLN02315 276 MDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVkIGDPLEKGTLLGPLhtpESKKNFEkgi 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 293 ---RLQGllgcGRVAIGGQSDEGE-RYIAPTVlVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFS 368
Cdd:PLN02315 356 eiiKSQG----GKILTGGSAIESEgNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFT 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958646404 369 KRSQVIKQVLARTSSGgfCGndgfmhMTLSSLP---------FGGVGTSGMGRYHGKFSFDTFSNQRAC 428
Cdd:PLN02315 431 RNPETIFKWIGPLGSD--CG------IVNVNIPtngaeiggaFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
26-356 |
6.59e-23 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 101.37 E-value: 6.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 26 RAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESeVSEIAISQAEVDLA----LRNL--------RSWMKDEKVSKNLAT 93
Cdd:PLN00412 77 RAELLHKAAAILKEHKAPIAECLVKEIAKPAKDA-VTEVVRSGDLISYTaeegVRILgegkflvsDSFPGNERNKYCLTS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 94 qldsafirKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSeiskaTEkilAEVLPRYLDQsCF---------- 163
Cdd:PLN00412 156 --------KIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPP-----TQ---GAVAALHMVH-CFhlagfpkgli 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 164 AVVLGGPQETGQLL-EHR-FDYIFFTGntyvGKIVMAAAAK-HLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 240
Cdd:PLN00412 219 SCVTGKGSEIGDFLtMHPgVNCISFTG----GDTGIAISKKaGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYS 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 241 GQTCVAPDYVLCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCGRVAIGGQSDEGER---YIA 317
Cdd:PLN00412 295 GQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKRegnLIW 374
|
330 340 350
....*....|....*....|....*....|....*....
gi 1958646404 318 PTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFIN 356
Cdd:PLN00412 375 PLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCN 413
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
104-411 |
3.57e-19 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 90.80 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 104 PFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSE----ISKATEKILAEVlpryldqscfavvlGGPQETGQLL-- 177
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEqtplIAAQAVRILLEA--------------GVPAGVVQLLpg 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 178 -----------EHRFDYIFFTGNTYVGKIVMAAAAKHL------TPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 240
Cdd:PRK11809 834 rgetvgaalvaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSA 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 241 GQTCVAPDyVLCSQE-MQERLVPALQNAITRFYGDNP-QTSPNLGRIIN-------QKHFERLQgllGCGRV---AIGGQ 308
Cdd:PRK11809 914 GQRCSALR-VLCLQDdVADRTLKMLRGAMAECRMGNPdRLSTDIGPVIDaeakaniERHIQAMR---AKGRPvfqAAREN 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 309 SDEGER--YIAPTV--LVDVQEtepvMQEEIFGPILPLV--TVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTS 382
Cdd:PRK11809 990 SEDWQSgtFVPPTLieLDSFDE----LKREVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAH 1065
|
330 340
....*....|....*....|....*....
gi 1958646404 383 SGGFCGNDGFMHMTLSSLPFGGVGTSGMG 411
Cdd:PRK11809 1066 VGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
11-415 |
5.74e-19 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 88.83 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 11 LREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAISQAEVDLALRNLRS------WMKD 84
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAfviysyRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 85 EKV-SKNLATQLDSAFIRKePFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLpRY---LDQ 160
Cdd:cd07084 81 EPGnHLGQGLKQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLL-HYaglLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 161 SCFAVVLGGPQETGQLLEH-RFDYIFFTGNTYVGKIVMAAAakHLTPITLELGGKNPCYVDDNCDP-QTVANRVAWFRYF 238
Cdd:cd07084 159 EDVTLINGDGKTMQALLLHpNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 239 NAGQTCVAPDYVLCSQEMQ-ERLVPALQNAITRfygDNPQTSpNLGRIINQKHFERLQGLLG-CGRVAIGGQSDEGERYI 316
Cdd:cd07084 237 CSGQKCTAQSMLFVPENWSkTPLVEKLKALLAR---RKLEDL-LLGPVQTFTTLAMIAHMENlLGSVLLFSGKELKNHSI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 317 --------APTVLVDVQE---TEPVMQEEIFGPILPLVTVTNLDEA--IEFINRREKPLALYAFSKRSQVIKQVLARTSS 383
Cdd:cd07084 313 psiygacvASALFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWV 392
|
410 420 430
....*....|....*....|....*....|..
gi 1958646404 384 GGfcgndgfmhMTLSSLPfgGVGTSGMGRYHG 415
Cdd:cd07084 393 AG---------RTYAILR--GRTGVAPNQNHG 413
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
2-423 |
1.16e-18 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 88.65 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 2 DSFEDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQL-------QEALAQDLHKSAFES-EVSEIAISQAEVDL 73
Cdd:PLN02419 151 EEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLamnitteQGKTLKDSHGDIFRGlEVVEHACGMATLQM 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 74 AlrnlrswmkdeKVSKNLATQLDSAFIRkEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEV 153
Cdd:PLN02419 231 G-----------EYLPNVSNGVDTYSIR-EPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAEL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 154 -LPRYLDQSCFAVVLGGPQETGQLLEHR-FDYIFFTGNTYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANR 231
Cdd:PLN02419 299 aMEAGLPDGVLNIVHGTNDTVNAICDDEdIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 232 VAWFRYFNAGQTCVAPDYVLC---SQEMQERLVPALQnAITRFYGDNPQTspNLGRIINQKHFERLQGLLGCG-----RV 303
Cdd:PLN02419 379 LLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVERAK-ALKVTCGSEPDA--DLGPVISKQAKERICRLIQSGvddgaKL 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 304 AIGGQS-----DEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVL 378
Cdd:PLN02419 456 LLDGRDivvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQ 535
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958646404 379 ARTSSGGFcGNDGFMHMTLSSLPFGGVGTSGMG--RYHGKFSFDTFS 423
Cdd:PLN02419 536 MDIEAGQI-GINVPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFT 581
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
103-411 |
3.04e-17 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 84.92 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 103 EPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEiskATEKILAEvlpryldqscfAVVL----GGPQETGQLL- 177
Cdd:PRK11905 675 KPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAE---QTPLIAAR-----------AVRLlheaGVPKDALQLLp 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 178 ------------EHRFDYIFFTGNTYVGKIVMAAAAKHLTPITL---ELGGKNPCYVDDNCDP-QTVANRVA-WFRyfNA 240
Cdd:PRK11905 741 gdgrtvgaalvaDPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPliaETGGQNAMIVDSSALPeQVVADVIAsAFD--SA 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 241 GQTCVAPDyVLCSQE-MQERLVPALQNAITRFYGDNP-QTSPNLGRIINQK-------HFERLQGLlGCG--RVAIGGQS 309
Cdd:PRK11905 819 GQRCSALR-VLCLQEdVADRVLTMLKGAMDELRIGDPwRLSTDVGPVIDAEaqanieaHIEAMRAA-GRLvhQLPLPAET 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 310 DEGeRYIAPTVLvdvqETE--PVMQEEIFGPILPLVTV--TNLDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSGG 385
Cdd:PRK11905 897 EKG-TFVAPTLI----EIDsiSDLEREVFGPVLHVVRFkaDELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGN 971
|
330 340
....*....|....*....|....*.
gi 1958646404 386 FCGNDGFMHMTLSSLPFGGVGTSGMG 411
Cdd:PRK11905 972 IYVNRNIIGAVVGVQPFGGEGLSGTG 997
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
2-411 |
3.49e-15 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 78.32 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 2 DSFEDKLQQLREAFNAGRTRSAEFRAAQLQGLSHFLRDNKQQLQeALaqdLHKSAFESevseIAISQAEVDLALRNLRSW 81
Cdd:PRK11904 585 EQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELI-AL---CVREAGKT----LQDAIAEVREAVDFCRYY 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 82 mkdekvsKNLATQLDSA------------FIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSE----ISKA 145
Cdd:PRK11904 657 -------AAQARRLFGApeklpgptgesnELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEqtplIAAE 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 146 TEKIL------AEVLpryldqscfAVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIV-MAAAAKHLTPITL--ELGGK 214
Cdd:PRK11904 730 AVKLLheagipKDVL---------QLLPGDGATVGAaLTADpRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQ 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 215 NPCYVDDNCDPQTVANRV---AwFRyfNAGQTCVAPDyVLCSQE-MQERLVPALQNA-----ItrfyGDNPQTSPNLGRI 285
Cdd:PRK11904 801 NAMIVDSTALPEQVVDDVvtsA-FR--SAGQRCSALR-VLFVQEdIADRVIEMLKGAmaelkV----GDPRLLSTDVGPV 872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 286 INQ-------KHFERLQ--GLLGCgRVAIGGQSDEGErYIAPTvLVDVQETEpVMQEEIFGPILPLVT--VTNLDEAIEF 354
Cdd:PRK11904 873 IDAeakanldAHIERMKreARLLA-QLPLPAGTENGH-FVAPT-AFEIDSIS-QLEREVFGPILHVIRykASDLDKVIDA 948
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958646404 355 INRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTLSSLPFGGVGTSGMG 411
Cdd:PRK11904 949 INATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
128-359 |
5.90e-15 |
|
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: 76.81 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 128 AIAAGNCVVLKPSEISKATEKILAEVLPRYLDQS-----CFAVVLGGPQETGQ-LLEH-RFDYIFFTGNTYVGKIVMAAA 200
Cdd:cd07129 131 ALAAGCPVVVKAHPAHPGTSELVARAIRAALRATglpagVFSLLQGGGREVGVaLVKHpAIKAVGFTGSRRGGRALFDAA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 201 AKHLTPIT--LELGGKNPCYVDdncdPQTVANR--------VAWFRyFNAGQTCVAPDYVLCSQ-EMQERLVPALQNAIT 269
Cdd:cd07129 211 AARPEPIPfyAELGSVNPVFIL----PGALAERgeaiaqgfVGSLT-LGAGQFCTNPGLVLVPAgPAGDAFIAALAEALA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 270 RFygdNPQT--SPNLgriinQKHF----ERLQGLLGcGRVAIGGQSDEGERYIAPTVL-VDVQE--TEPVMQEEIFGPIL 340
Cdd:cd07129 286 AA---PAQTmlTPGI-----AEAYrqgvEALAAAPG-VRVLAGGAAAEGGNQAAPTLFkVDAAAflADPALQEEVFGPAS 356
|
250
....*....|....*....
gi 1958646404 341 PLVTVTNLDEAIEFINRRE 359
Cdd:cd07129 357 LVVRYDDAAELLAVAEALE 375
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
106-409 |
2.65e-14 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 74.93 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 106 GLVLIIVPWNYP---LNLTLVPlvgAIAaGNCVVLKPSEI----SKATEKILAEV-LPRYLDQscFavVLGGPQETGQ-L 176
Cdd:cd07123 172 GFVYAVSPFNFTaigGNLAGAP---ALM-GNVVLWKPSDTavlsNYLVYKILEEAgLPPGVIN--F--VPGDGPVVGDtV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 177 LEHR-FDYIFFTGNTYVGKIVMAAAAKHLT-----P-ITLELGGKNPCYVDDNCDPQTVAN---RVAwFRYfnAGQTCVA 246
Cdd:cd07123 244 LASPhLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTatvRGA-FEY--QGQKCSA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 247 PD--YVLCS--QEMQERLVPALQnAITrfYGDNPQTSPNLGRIINQKHFERLQGLLGCGR------VAIGGQSDEGERY- 315
Cdd:cd07123 321 ASraYVPESlwPEVKERLLEELK-EIK--MGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKsdpeaeIIAGGKCDDSVGYf 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 316 IAPTVLVDVQETEPVMQEEIFGPILplvTV-----TNLDEAIEFINRREkPLALYA--FSKRSQVIKQVLA--RTSSGGF 386
Cdd:cd07123 398 VEPTVIETTDPKHKLMTEEIFGPVL---TVyvypdSDFEETLELVDTTS-PYALTGaiFAQDRKAIREATDalRNAAGNF 473
|
330 340
....*....|....*....|...
gi 1958646404 387 CGNDGFMHMTLSSLPFGGVGTSG 409
Cdd:cd07123 474 YINDKPTGAVVGQQPFGGARASG 496
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
90-356 |
1.08e-11 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 67.27 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 90 NLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSE----ISKATEKILAEV-LPRyldqSCFA 164
Cdd:COG4230 666 AQARRLFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEqtplIAARAVRLLHEAgVPA----DVLQ 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 165 VVLGGPQETGQLL--EHRFDYIFFTGNTYVGKIV-MAAAAKHLTPITL--ELGGKNPCYVDDNCDP-QTVANRVA-WFRy 237
Cdd:COG4230 742 LLPGDGETVGAALvaDPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIVDSSALPeQVVDDVLAsAFD- 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 238 fNAGQTCVAPDyVLCSQE-----MQERLVPALQN-AItrfyGDNPQTSPNLGRIIN-------QKHFERLQ--GLLgCGR 302
Cdd:COG4230 821 -SAGQRCSALR-VLCVQEdiadrVLEMLKGAMAElRV----GDPADLSTDVGPVIDaearanlEAHIERMRaeGRL-VHQ 893
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958646404 303 VAIGGQSDEGeRYIAPTV--LVDVQEtepvMQEEIFGPILPLVTV--TNLDEAIEFIN 356
Cdd:COG4230 894 LPLPEECANG-TFVAPTLieIDSISD----LEREVFGPVLHVVRYkaDELDKVIDAIN 946
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
104-377 |
8.02e-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: 64.04 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 104 PFGLVLII----VP-WN-YPlnltlvPLVGAIAAGNCVVLKPSEIS----KATEKILAEVLPRY-LDQSCFAVVLGGPQE 172
Cdd:cd07127 193 PRGVALVIgcstFPtWNgYP------GLFASLATGNPVIVKPHPAAilplAITVQVAREVLAEAgFDPNLVTLAADTPEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 173 --TGQLLEH-RFDYIFFTGNTYVGKIVMAAAAKHLtpITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 249
Cdd:cd07127 267 piAQTLATRpEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQN 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 250 VLCS----QEMQERLVP-----ALQNAITRFYGDNPQTSPNLGRIINQKHFERLQGLLGCGRVAIGGQSDE-----GERY 315
Cdd:cd07127 345 IYVPrdgiQTDDGRKSFdevaaDLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLGEVLLASEAVAhpefpDARV 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958646404 316 IAPTVLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIEFINR--REK-PLALYAFSKRSQVIKQV 377
Cdd:cd07127 425 RTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgAMTVGVYSTDPEVVERV 489
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
16-232 |
7.22e-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: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 16 NAGR---TRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDL---HKSAFESEVSEIAISQAEV-DLALRNLRSWMKDEKVS 88
Cdd:cd07077 5 NAQRtlaVNHDEQRDLIINAIANALYDTRQRLASEAVSERgayIRSLIANWIAMMGCSESKLyKNIDTERGITASVGHIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 89 KNLATQLDSAFIRKEPFGLVLIIVPWNYPLNLTLVPLVGaIAAGNCVVLKPSEISKATEKILAEVLPRyldqscfAVVLG 168
Cdd:cd07077 85 DVLLPDNGETYVRAFPIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALALLFQA-------ADAAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 169 GPQETGQLLEHR-------------FDYIFFTGntyvGKIVMAAAAKHLTPITLeLG---GKNPCYVDDNCDPQTVANRV 232
Cdd:cd07077 157 GPKILVLYVPHPsdelaeellshpkIDLIVATG----GRDAVDAAVKHSPHIPV-IGfgaGNSPVVVDETADEERASGSV 231
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
103-353 |
6.46e-06 |
|
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: 48.42 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 103 EPFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLpryLDQscfAVVLGGPQ----------- 171
Cdd:cd07081 94 EPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLL---LQA---AVAAGAPEnligwidnpsi 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 172 ETGQLLEHR--FDYIFFTGntyvGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGqtcvapdy 249
Cdd:cd07081 168 ELAQRLMKFpgIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNG-------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 250 VLCSQEMQERLVPALQNAITRFYGDNPqtspnlGRIINQKHFERLQGLL---GCGRVAIGGQS-------------DEGE 313
Cdd:cd07081 236 VICASEQSVIVVDSVYDEVMRLFEGQG------AYKLTAEELQQVQPVIlknGDVNRDIVGQDaykiaaaaglkvpQETR 309
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958646404 314 RYIAPTVLVDvqETEPVMQEEIfGPILPLVTVTNLDEAIE 353
Cdd:cd07081 310 ILIGEVTSLA--EHEPFAHEKL-SPVLAMYRAANFADADA 346
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
104-384 |
9.32e-06 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 47.88 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 104 PFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLK-PSEISkatekILAEVLPRYL------DQSCFAVVLGGPQETGQL 176
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKvDSKVS-----VVMEQFLRLLhlcgmpATDVDLIHSDGPTMNKIL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 177 LEHRFDYIFFTGNTYV---------GKIVMAAAA---KHLTPITLELGgknpcYVDDNCDPQTvanrvawfrYFNAGQTC 244
Cdd:cd07126 217 LEANPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQDA---------YACSGQKC 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 245 VAPDyVLCSQE--MQERLVPALQNAITRFYGDNPQTSPNLG----RIINqkHFERLQGLLGcGRVAIGGQSDEGERYIA- 317
Cdd:cd07126 283 SAQS-ILFAHEnwVQAGILDKLKALAEQRKLEDLTIGPVLTwtteRILD--HVDKLLAIPG-AKVLFGGKPLTNHSIPSi 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 318 -----PT-VLVDVQ-----ETEPVMQEEIFGPILPLVTVTN--LDEAIEFINRREKPLALYAFSKRSQVIKQVLARTSSG 384
Cdd:cd07126 359 ygayePTaVFVPLEeiaieENFELVTTEVFGPFQVVTEYKDeqLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNG 438
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
16-370 |
6.73e-05 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 45.12 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 16 NAGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFESEVSEIAIsqaevdlalrnLRSWMKDekvsknlatql 95
Cdd:pfam05893 22 DPNYSKRHIETLAQITGYSEAMLNYLKSLMAFCRRRNLQNVLESELGQPFI-----------LDEWLPT----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 96 DSAFIRKEPFGLVLIIVPWNYPLnLTLVPLVGAIAAGNCVVLKPSeiskATEKILAEVLPRYL---DQSC-----FAVVL 167
Cdd:pfam05893 80 KPSYEKAFPPGLVFHVLSGNVPL-LPVMSILMGLLVKNVNLLKVS----SSDPFTAAALLASFadlDPTHpladsLSVVY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 168 --GGPQETGQLLEHRFDYIFFTGNTYVGKIVM--AAAAKHLtpitLELGGK-NPCYVDDNCDPQTVANRVAWFRYFNAGQ 242
Cdd:pfam05893 155 wdGGSTQLEDLIVANADVVIAWGGEDAINAIRecLKPGKQW----IDFGAKiSFAVVDREAALDKAAERAADDICVFDQQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 243 TCVAPDYVLCS-------QEMQERLVPALQNAITRFygdnPQTSPNLG---RIINQKHFERLQGLLGCGRvaiGGQSDEG 312
Cdd:pfam05893 231 ACLSPQTVFVEsddkitpDEFAERLAAALAKRARIL----PKAVLDIDeaaKISSDRAECKLDYAFAGER---GVWSDFH 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958646404 313 ERYiapTVLVDVQetepvmQEEIFGPI---LPLVTVTNLDEAIEFINRREKPL---ALYAFSKR 370
Cdd:pfam05893 304 QRW---TVIWSDG------QEELNSPLnrtVNVVPVPSLSDVVRYVSENRTYLqtcGLAPYSGR 358
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
128-378 |
7.08e-05 |
|
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: 45.34 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 128 AIAAGNCVVLKPseiskATEK-ILAEVLPRYLDQS------CFAVVLGGpqeTGQLLEH--RFDYIFFTGNTYVGKI--V 196
Cdd:cd07128 168 ALLAGVPVIVKP-----ATATaYLTEAVVKDIVESgllpegALQLICGS---VGDLLDHlgEQDVVAFTGSAATAAKlrA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 197 MAAAAKHLTPITLELGGKNPCYVDDNCDPQT-----VANRVAWFRYFNAGQTCVAPDYVLCSQEMQERLVPALQNAITRF 271
Cdd:cd07128 240 HPNIVARSIRFNAEADSLNAAILGPDATPGTpefdlFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 272 -YGDNPQTSPNLGRIINQKHFERLQG----LLGCGRVAIGGQSD--------EGERYIAPTVLV--DVQETEPVMQEEIF 336
Cdd:cd07128 320 vVGDPRLEGVRMGPLVSREQREDVRAavatLLAEAEVVFGGPDRfevvgadaEKGAFFPPTLLLcdDPDAATAVHDVEAF 399
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958646404 337 GPILPLVTVTNLDEAIEFINRREKPLALYAFSKRSQVIKQVL 378
Cdd:cd07128 400 GPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
104-353 |
8.18e-05 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 44.92 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 104 PFGLVLIIVPWNYPLNLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSC----FAVVLGGP--QETGQLL 177
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGgpdnLVVTVEEPtiETTNELM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 178 EHR-FDYIFFTGNTYVGKIVMAAAAKhltpiTLELGGKNP-CYVDDNCDPQTVANRVAWFRYFNAGQTC----------- 244
Cdd:cd07121 177 AHPdINLLVVTGGPAVVKAALSSGKK-----AIGAGAGNPpVVVDETADIEKAARDIVQGASFDNNLPCiaekeviavds 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958646404 245 VAPD----------YVLCSQEMQERLVPALQNaitrfygdnpqtspNLGRIINQKHFER-LQGLLGcgrvAIGGQSDEGE 313
Cdd:cd07121 252 VADYliaamqrngaYVLNDEQAEQLLEVVLLT--------------NKGATPNKKWVGKdASKILK----AAGIEVPADI 313
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1958646404 314 RYIaptvLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIE 353
Cdd:cd07121 314 RLI----IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
304-353 |
2.89e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 39.89 E-value: 2.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958646404 304 AIGGQSDEGERYIaptvLVDVQETEPVMQEEIFGPILPLVTVTNLDEAIE 353
Cdd:PRK15398 334 AAGINVPKDTRLL----IVETDANHPFVVTELMMPVLPVVRVKDVDEAIA 379
|
|
| |
