|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
6-447 |
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: 868.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 6 DTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDE 85
Cdd:cd07132 2 EAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 RVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAV 165
Cdd:cd07132 82 PVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 166 VLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCV 245
Cdd:cd07132 162 VLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 246 APDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSDESDRYIAPTVLVDVQ 325
Cdd:cd07132 242 APDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 326 EMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGV 405
Cdd:cd07132 322 PSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGV 401
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1169285 406 GASGMGRYHGKFSFDTFSHHRACLLRSPGMEKLNALRYPPQS 447
Cdd:cd07132 402 GNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
6-429 |
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: 700.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 6 DTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDE 85
Cdd:cd07087 2 ELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 RVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAV 165
Cdd:cd07087 82 RVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 166 VLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCV 245
Cdd:cd07087 162 VEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 246 APDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSDESDRYIAPTVLVDVQ 325
Cdd:cd07087 242 APDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 326 EMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGV 405
Cdd:cd07087 322 PDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGV 401
|
410 420
....*....|....*....|....
gi 1169285 406 GASGMGRYHGKFSFDTFSHHRACL 429
Cdd:cd07087 402 GNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
6-454 |
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: 623.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 6 DTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDE 85
Cdd:cd07136 2 SLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 RVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAV 165
Cdd:cd07136 82 RVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 166 VLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCV 245
Cdd:cd07136 162 VEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 246 APDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSDESDRYIAPTVLVDVQ 325
Cdd:cd07136 242 APDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNVT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 326 EMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGV 405
Cdd:cd07136 322 WDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGV 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1169285 406 GASGMGRYHGKFSFDTFSHHRACLLRSPGMEklNALRYPPQSPRRLRML 454
Cdd:cd07136 402 GNSGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPPYKGKKKKLK 448
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
2-459 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 612.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 2 DPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAW 81
Cdd:PTZ00381 7 EIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 82 MKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQS 161
Cdd:PTZ00381 87 LKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 162 CFAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 241
Cdd:PTZ00381 167 YVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 242 QTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGC--GRVAIGGQSDESDRYIAPT 319
Cdd:PTZ00381 247 QTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDhgGKVVYGGEVDIENKYVAPT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 320 VLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLAS 399
Cdd:PTZ00381 327 IIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPN 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 400 LPFGGVGASGMGRYHGKFSFDTFSHHRACLLRSPGMEKLNALRYPPQSPRRLRMLLVAME 459
Cdd:PTZ00381 407 LPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSWVLSFLLK 466
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
10-427 |
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: 578.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 10 RLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDERVPK 89
Cdd:cd07135 13 RLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAKDEKVKD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 90 NLATQ-LDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLG 168
Cdd:cd07135 93 GPLAFmFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQVVQG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 169 GPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD 248
Cdd:cd07135 173 GVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 249 YVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGC--GRVAIGGQSDESDRYIAPTVLVDVQE 326
Cdd:cd07135 253 YVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTtkGKVVIGGEMDEATRFIPPTIVSDVSW 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 327 MEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVG 406
Cdd:cd07135 333 DDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGVG 412
|
410 420
....*....|....*....|.
gi 1169285 407 ASGMGRYHGKFSFDTFSHHRA 427
Cdd:cd07135 413 DSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
7-429 |
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: 517.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 7 TLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDER 86
Cdd:cd07137 4 LVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 87 VPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVV 166
Cdd:cd07137 84 VKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 167 LGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRY-FNAGQTCV 245
Cdd:cd07137 164 EGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 246 APDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAI----GGQSDESDRYIAPTVL 321
Cdd:cd07137 244 APDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDDPSVADkivhGGERDEKNLYIEPTIL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 322 VDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLP 401
Cdd:cd07137 324 LDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLP 403
|
410 420
....*....|....*....|....*...
gi 1169285 402 FGGVGASGMGRYHGKFSFDTFSHHRACL 429
Cdd:cd07137 404 FGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
10-429 |
1.56e-179 |
|
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: 509.08 E-value: 1.56e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 10 RLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDERVPK 89
Cdd:cd07134 6 AQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 90 NLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGG 169
Cdd:cd07134 86 PLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 170 PQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 249
Cdd:cd07134 166 AEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 250 VLCSPEMQERLLPALQSTITRFYGDDP--QSSPNLGRIINQKQFQRLRALL-----GCGRVAIGGQSDESDRYIAPTVLV 322
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIEKFYGKDAarKASPDLARIVNDRHFDRLKGLLddavaKGAKVEFGGQFDAAQRYIAPTVLT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 323 DVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPF 402
Cdd:cd07134 326 NVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPF 405
|
410 420
....*....|....*....|....*..
gi 1169285 403 GGVGASGMGRYHGKFSFDTFSHHRACL 429
Cdd:cd07134 406 GGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
6-427 |
3.95e-168 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 480.44 E-value: 3.95e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 6 DTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDL-HKSAFESEVSEVAISQGEVTLALRNLRAWMKD 84
Cdd:cd07133 2 ALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 85 ERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFA 164
Cdd:cd07133 82 SRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 165 VVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 244
Cdd:cd07133 162 VVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 245 VAPDYVLCSPEMQERLLPALQSTITRFYGDDPqSSPNLGRIINQKQFQRLRALL------GCGRVAIG--GQSDESDRYI 316
Cdd:cd07133 242 VAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLA-DNPDYTSIINERHYARLQGLLedarakGARVIELNpaGEDFAATRKL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 317 APTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMT 396
Cdd:cd07133 321 PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVA 400
|
410 420 430
....*....|....*....|....*....|.
gi 1169285 397 LASLPFGGVGASGMGRYHGKFSFDTFSHHRA 427
Cdd:cd07133 401 QDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-454 |
6.33e-165 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 474.21 E-value: 6.33e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 1 MDPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRA 80
Cdd:PLN02203 5 GETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 81 WMKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQ 160
Cdd:PLN02203 85 WMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 161 SCFAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVD---DNCDPQTVANRVAWFRY 237
Cdd:PLN02203 165 KAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 238 FN-AGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAI----GGQSDES 312
Cdd:PLN02203 245 GScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAAsivhGGSIDEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 313 DRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGF 392
Cdd:PLN02203 325 KLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1169285 393 MHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRACLLRSPGMEKLnaLRYPPQSPRRLRML 454
Cdd:PLN02203 405 IQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEFE--FRYPPWNDFKLGFL 464
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
7-430 |
7.62e-136 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 398.12 E-value: 7.62e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 7 TLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVsEVAISQGEVTLALRNLRAWMKDER 86
Cdd:cd07078 3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 87 VPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQY-VDQSCFAV 165
Cdd:cd07078 82 PSPDPGEL---AIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 166 VLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQT 243
Cdd:cd07078 159 VTGDGDEVGAaLASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 244 CVAPDYVLCSPEMQERLLPALQSTITRFY-GDDPQSSPNLGRIINQKQFQRLRALL-----GCGRVAIGGQSDESD--RY 315
Cdd:cd07078 239 CTAASRLLVHESIYDEFVERLVERVKALKvGNPLDPDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKRLEGGkgYF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 316 IAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHM 395
Cdd:cd07078 319 VPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGA 398
|
410 420 430
....*....|....*....|....*....|....*
gi 1169285 396 TlASLPFGGVGASGMGRYHGKFSFDTFSHHRACLL 430
Cdd:cd07078 399 E-PSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
11-454 |
2.61e-125 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 373.23 E-value: 2.61e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 11 LREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDERVPKN 90
Cdd:PLN02174 19 LRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 91 LATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGP 170
Cdd:PLN02174 99 LTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 171 QETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRY-FNAGQTCVAPDY 249
Cdd:PLN02174 179 TETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 250 VLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLG----CGRVAIGGQSDESDRYIAPTVLVDVQ 325
Cdd:PLN02174 259 ILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILLDVP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 326 EMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGV 405
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGV 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1169285 406 GASGMGRYHGKFSFDTFSHHRACLLRSpgMEKLNALRYPPQSPRRLRML 454
Cdd:PLN02174 419 GESGMGAYHGKFSFDAFSHKKAVLYRS--LFGDSAVRYPPYSRGKLRLL 465
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
12-430 |
6.50e-109 |
|
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: 326.88 E-value: 6.50e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESeVSEVAISQGEVTLALRNLRAWMKDERVPKNL 91
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEA-LGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 92 ATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQY-VDQSCFAVVLGGP 170
Cdd:cd06534 83 GGE---AYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 171 QETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD 248
Cdd:cd06534 160 DEVGAaLLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 249 YVLCSPEMQERLLPALQstitrfygddpqsspnlgriinqkqfqrlrallgcgrvaiggqsdesdryiapTVLVDVQEME 328
Cdd:cd06534 240 RLLVHESIYDEFVEKLV-----------------------------------------------------TVLVDVDPDM 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 329 PVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTlASLPFGGVGAS 408
Cdd:cd06534 267 PIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVG-PEAPFGGVKNS 345
|
410 420
....*....|....*....|..
gi 1169285 409 GMGRYHGKFSFDTFSHHRACLL 430
Cdd:cd06534 346 GIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
12-424 |
7.55e-105 |
|
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: 320.53 E-value: 7.55e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESevsevaisQGEVTLALRNLRAW------MKDE 85
Cdd:COG1012 53 RAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEA--------RGEVDRAADFLRYYagearrLYGE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 RVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS-----KNVEkILAEV-LPQYVd 159
Cdd:COG1012 125 TIPSDAPGTR--AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTplsalLLAE-LLEEAgLPAGV- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 160 qscFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRY 237
Cdd:COG1012 201 ---LNVVTGDGSEVGAaLVAHpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAF 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 238 FNAGQTCVAPDYVLC----SPEMQERLLPALQSTItrfYGDDPQSSPNLGRIINQKQFQRLRALLGCG-----RVAIGGQ 308
Cdd:COG1012 278 GNAGQRCTAASRLLVhesiYDEFVERLVAAAKALK---VGDPLDPGTDMGPLISEAQLERVLAYIEDAvaegaELLTGGR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 309 --SDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF 386
Cdd:COG1012 355 rpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMV 434
|
410 420 430
....*....|....*....|....*....|....*...
gi 1169285 387 CGNDGFMHMtLASLPFGGVGASGMGRYHGKFSFDTFSH 424
Cdd:COG1012 435 WINDGTTGA-VPQAPFGGVKQSGIGREGGREGLEEYTE 471
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
12-423 |
4.00e-92 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 287.12 E-value: 4.00e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEvsevaisqGEVTLALRNLRAW------MKDE 85
Cdd:pfam00171 39 RAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR--------GEVDRAIDVLRYYaglarrLDGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 RVPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdq 160
Cdd:pfam00171 111 TLPSDPGRL---AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELfeeagLPAGV-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 161 scFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYF 238
Cdd:pfam00171 186 --LNVVTGSGAEVGEaLVEHpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 239 NAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLRALL-----GCGRVAIGGQSDES 312
Cdd:pfam00171 264 NAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 313 D-RYIAPTVLVDV-QEMePVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGND 390
Cdd:pfam00171 344 NgYFVEPTVLANVtPDM-RIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWIND 422
|
410 420 430
....*....|....*....|....*....|...
gi 1169285 391 GFMHmTLASLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:pfam00171 423 YTTG-DADGLPFGGFKQSGFGREGGPYGLEEYT 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
6-427 |
5.28e-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: 276.02 E-value: 5.28e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 6 DTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAfesevsevAISQGEVTLALRNLRAW---- 81
Cdd:cd07099 22 AAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPR--------ADAGLEVLLALEAIDWAarna 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 82 ---MKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNV----EKILAEVL 154
Cdd:cd07099 94 prvLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVgellAEAWAAAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 155 PqyvDQSCFAVVLGGpQETGQ-LLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVA 233
Cdd:cd07099 174 P---PQGVLQVVTGD-GATGAaLIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 234 WFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLR-----ALLGCGRVAIGG 307
Cdd:cd07099 250 WGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRrhvddAVAKGAKALTGG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 308 -QSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF 386
Cdd:cd07099 330 aRSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAV 409
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1169285 387 CGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRA 427
Cdd:cd07099 410 SINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKA 450
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
9-424 |
4.59e-69 |
|
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: 226.26 E-value: 4.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 9 RRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQD----LHKSAFESEVSeVAISQGEVTLALRnlrawMKD 84
Cdd:cd07104 7 AAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIREsgstRPKAAFEVGAA-IAILREAAGLPRR-----PEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 85 ERVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE---ISKNVekILAEV-----LPQ 156
Cdd:cd07104 81 EILPSDVPGKE--SMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSrtpVTGGL--LIAEIfeeagLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 157 YVdqscFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAW 234
Cdd:cd07104 157 GV----LNVVPGGGSEIGDaLVEHpRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 235 FRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGD--DPQSSpnLGRIINQKQFQRLRALL------GcGRVAI 305
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALpVGDprDPDTV--IGPLINERQVDRVHAIVedavaaG-ARLLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 306 GGQSDesDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGG 385
Cdd:cd07104 310 GGTYE--GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGM 387
|
410 420 430
....*....|....*....|....*....|....*....
gi 1169285 386 FCGNDGFMHmTLASLPFGGVGASGMGRYHGKFSFDTFSH 424
Cdd:cd07104 388 VHINDQTVN-DEPHVPFGGVKASGGGRFGGPASLEEFTE 425
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
12-416 |
3.18e-68 |
|
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: 224.33 E-value: 3.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSafesevseVAISQGEVTLALrnlrAWMK-------- 83
Cdd:cd07106 29 KAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKP--------LAEAQFEVGGAV----AWLRytasldlp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 84 DERVPKNlATQldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS-----KNVEkILAEVLPQYV 158
Cdd:cd07106 97 DEVIEDD-DTR--RVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTplctlKLGE-LAQEVLPPGV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 159 DQscfavVLGGPQETGQLL-EH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFR 236
Cdd:cd07106 173 LN-----VVSGGDELGPALtSHpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 237 YFNAGQTCVAPD--YVlcsPEMQ-ERLLPALQSTITRFY-GDDPQSSPNLGRIINQKQFQRLRALL-----GCGRVAIGG 307
Cdd:cd07106 248 FINSGQVCAAIKrlYV---HESIyDEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVedakaKGAKVLAGG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 308 QSDESDRY-IAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF 386
Cdd:cd07106 325 EPLDGPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTV 404
|
410 420 430
....*....|....*....|....*....|.
gi 1169285 387 CGNdgfMHMTLA-SLPFGGVGASGMGRYHGK 416
Cdd:cd07106 405 WIN---THGALDpDAPFGGHKQSGIGVEFGI 432
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
30-416 |
2.78e-67 |
|
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: 222.56 E-value: 2.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 30 LQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDERVPKNLATQLDSAFIRKEPFGLVL 109
Cdd:cd07098 46 LRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPLGVVG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 110 IIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS--------KNVEKILAEV-----LPQYVdqSCFAvvlggpqETGQ- 175
Cdd:cd07098 126 AIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVawssgfflSIIRECLAACghdpdLVQLV--TCLP-------ETAEa 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 176 LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANrvAWFR--YFNAGQTCVAPDYVLC 252
Cdd:cd07098 197 LTSHpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIAS--IIMRgtFQSSGQNCIGIERVIV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 253 SPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLRALLG----------CGRVAIGGQSDESDRYIAPTVL 321
Cdd:cd07098 275 HEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVAdavekgarllAGGKRYPHPEYPQGHYFPPTLL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 322 VDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGND-GFMHMtLASL 400
Cdd:cd07098 355 VDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDfGVNYY-VQQL 433
|
410
....*....|....*.
gi 1169285 401 PFGGVGASGMGRYHGK 416
Cdd:cd07098 434 PFGGVKGSGFGRFAGE 449
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
12-427 |
7.18e-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: 218.65 E-value: 7.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAG-RTRPAEFRAAQLQGLGRFLQENKQLLhdalaqdlhksaFESEVSEVAISQG-----EVTLALRNLRAW---- 81
Cdd:cd07089 29 RRAFDTGdWSTDAEERARCLRQLHEALEARKEEL------------RALLVAEVGAPVMtaramQVDGPIGHLRYFadla 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 82 ----MKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV---- 153
Cdd:cd07089 97 dsfpWEFDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIiaet 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 154 -LPQYVdqscFAVVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVAN 230
Cdd:cd07089 177 dLPAGV----VNVVTGSDNAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 231 RVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGD--DPqsSPNLGRIINQKQFQRLRALLGCGR----- 302
Cdd:cd07089 253 AAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGDpaDP--GTVMGPLISAAQRDRVEGYIARGRdegar 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 303 -VAIGGQSDESDR--YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLT 379
Cdd:cd07089 331 lVTGGGRPAGLDKgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVAR 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1169285 380 QTSSGGFCGNdGFMHMtLASLPFGGVGASGMGRYHGKFSFDTFSHHRA 427
Cdd:cd07089 411 RIRTGSVGIN-GGGGY-GPDAPFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
13-422 |
6.89e-65 |
|
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: 215.76 E-value: 6.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 13 EAFHAGRTRPAEFRAAQLQGLGRFLQENKqllhDALAQDLH----KSafeseVSEvaiSQGEVTLALRNLRaWMKDE--R 86
Cdd:cd07103 30 AAFKTWRKTTARERAAILRRWADLIRERA----EDLARLLTleqgKP-----LAE---ARGEVDYAASFLE-WFAEEarR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 87 V------PKNLATQLdsaFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEisknvE---------KILA 151
Cdd:cd07103 97 IygrtipSPAPGKRI---LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAE-----EtplsalalaELAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 152 EV-LPQYVdqscFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTV 228
Cdd:cd07103 169 EAgLPAGV----LNVVTGSPAEIGEaLCASpRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 229 ANRVAWFRYFNAGQTCVAPD--YVLCS--PEMQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLRAL----LGC 300
Cdd:cd07103 245 VDGAIASKFRNAGQTCVCANriYVHESiyDEFVEKLVERVKKLKV---GNGLDEGTDMGPLINERAVEKVEALvedaVAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 301 G-RVAIGGQSDESD-RYIAPTVLVDV-QEMEpVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRV 377
Cdd:cd07103 322 GaKVLTGGKRLGLGgYFYEPTVLTDVtDDML-IMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1169285 378 LTQTSSG--GFcgNDGFmhMTLASLPFGGVGASGMGRYHGKFSFDTF 422
Cdd:cd07103 401 AEALEAGmvGI--NTGL--ISDAEAPFGGVKESGLGREGGKEGLEEY 443
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
69-423 |
4.55e-63 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 211.03 E-value: 4.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 69 GEVTLALRNLRAWMKDERVPKNLATQLDSA----FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK 144
Cdd:cd07150 80 FETTFTPELLRAAAGECRRVRGETLPSDSPgtvsMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 145 NVEKILAEV-----LPQYVdqscFAVVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPC 217
Cdd:cd07150 160 VIGLKIAEImeeagLPKGV----FNVVTGGGAEVGDELvdDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 218 YVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLR- 295
Cdd:cd07150 236 IVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKr 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 296 ----ALLGCGRVAIGGQSDesDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLalyafsnSS 371
Cdd:cd07150 316 qvedAVAKGAKLLTGGKYD--GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGL-------SA 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1169285 372 QVVKRVLTQTSSGGFCGNDGFMHMTLASL------PFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07150 387 AILTNDLQRAFKLAERLESGMVHINDPTIldeahvPFGGVKASGFGREGGEWSMEEFT 444
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
7-425 |
6.30e-63 |
|
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: 210.95 E-value: 6.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 7 TLRRLREAFHAGRTRPAEFRAAQLQglgRFLqenkqllhDALAQdlHKSAFESEVSE-----VAISQGEVTLALRnlRAW 81
Cdd:cd07102 23 ALERARAAQKGWRAVPLEERKAIVT---RAV--------ELLAA--NTDEIAEELTWqmgrpIAQAGGEIRGMLE--RAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 82 MKDERVPKNLATQLDSA------FIRKEPFGLVLIIAPWNYPLnLTLV-PLVGALAAGNCVVLKPSE----ISKNVEKIL 150
Cdd:cd07102 88 YMISIAEEALADIRVPEkdgferYIRREPLGVVLIIAPWNYPY-LTAVnAVIPALLAGNAVILKHSPqtplCGERFAAAF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 151 AEV-LPQYVdqscFAVVLGGPQETGQLL-EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTV 228
Cdd:cd07102 167 AEAgLPEGV----FQVLHLSHETSAALIaDPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 229 ANRVAWFRYFNAGQTCvapdyvlCSPE-------MQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLR----- 295
Cdd:cd07102 243 AESLVDGAFFNSGQSC-------CSIEriyvhesIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRaqiad 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 296 ALLGCGRVAIGGQ----SDESDRYIAPTVLVDV-QEMEpVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNS 370
Cdd:cd07102 316 AIAKGARALIDGAlfpeDKAGGAYLAPTVLTNVdHSMR-VMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169285 371 SQVVKRVLTQTSSGGFCGN-----DgfmhmtlASLPFGGVGASGMGRYHGKFSFDTF----SHH 425
Cdd:cd07102 395 IARAEALGEQLETGTVFMNrcdylD-------PALAWTGVKDSGRGVTLSRLGYDQLtrpkSYH 451
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
97-423 |
9.11e-63 |
|
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: 210.26 E-value: 9.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 97 SAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEI----SKNVEKILAEVLPQYVdqscFAVVLGGPQE 172
Cdd:cd07092 111 TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETtpltTLLLAELAAEVLPPGV----VNVVCGGGAS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 173 TGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYV 250
Cdd:cd07092 187 AGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 251 LCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLRALL----GCGRVAIGGQSDESDRY-IAPTVLVDV 324
Cdd:cd07092 267 YVHESVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGRRAEGPGYfYEPTVVAGV 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 325 QEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfmHMTLAS-LPFG 403
Cdd:cd07092 347 AQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPLAAeMPHG 423
|
330 340
....*....|....*....|
gi 1169285 404 GVGASGMGRYHGKFSFDTFS 423
Cdd:cd07092 424 GFKQSGYGKDLSIYALEDYT 443
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
12-424 |
2.87e-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: 209.13 E-value: 2.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESE--VSEVA------ISQGEVTLALRNLRAWMK 83
Cdd:cd07110 29 RRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwdVDDVAgcfeyyADLAEQLDAKAERAVPLP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 84 DERVpknlatqldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYV 158
Cdd:cd07110 109 SEDF---------KARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIaaeagLPPGV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 159 dqscFAVVLGGPQETGQ-LLEHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFR 236
Cdd:cd07110 180 ----LNVVTGTGDEAGApLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGC 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 237 YFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSP-NLGRIINQKQFQRLRALLGCG-----RVAIGGQSD 310
Cdd:cd07110 256 FWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGvRLGPLVSQAQYEKVLSFIARGkeegaRLLCGGRRP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 311 ESDR---YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF- 386
Cdd:cd07110 336 AHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVw 415
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1169285 387 --CGNDGFMHmtlasLPFGGVGASGMGRYHGKFSFDTFSH 424
Cdd:cd07110 416 inCSQPCFPQ-----APWGGYKRSGIGRELGEWGLDNYLE 450
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
12-422 |
2.42e-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: 206.97 E-value: 2.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHA-GRTRPAEfRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDERVPKN 90
Cdd:cd07138 46 RRAFPAwSATSVEE-RAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEERRGNS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 91 LatqldsafIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqscFAV 165
Cdd:cd07138 125 L--------VVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEIldeagLPAGV----FNL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 166 VLGGPQETGQLL-EH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCD-----PQTVANrvawfRYF 238
Cdd:cd07138 193 VNGDGPVVGEALsAHpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADlekavPRGVAA-----CFA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 239 NAGQTCVAPDYVL----CSPEMQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLRALLGCG-----RVAIGG-- 307
Cdd:cd07138 268 NSGQSCNAPTRMLvprsRYAEAEEIAAAAAEAYVV---GDPRDPATTLGPLASAAQFDRVQGYIQKGieegaRLVAGGpg 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 308 --QSDESDRYIAPTVLVDV-QEMEpVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 384
Cdd:cd07138 345 rpEGLERGYFVKPTVFADVtPDMT-IAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAG 423
|
410 420 430
....*....|....*....|....*....|....*...
gi 1169285 385 GFCGNDGFMHMtlaSLPFGGVGASGMGRYHGKFSFDTF 422
Cdd:cd07138 424 QVHINGAAFNP---GAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
12-423 |
3.71e-61 |
|
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: 206.32 E-value: 3.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFH--AGRTRPAEfRAAQLQGLGRFLQENKQLLHDALAQDLHKSafesevseVAISQGEVTLALRNLR--AWMKDERV 87
Cdd:cd07109 29 RRAFEsgWLRLSPAE-RGRLLLRIARLIREHADELARLESLDTGKP--------LTQARADVEAAARYFEyyGGAADKLH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 88 PKNLATQLD-SAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQY-VDQSCFAV 165
Cdd:cd07109 100 GETIPLGPGyFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 166 VLGGPQETGQ-LLEHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQT 243
Cdd:cd07109 180 VTGLGAEAGAaLVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 244 CVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALL-----GCGRVAIGGQ----SDESDR 314
Cdd:cd07109 260 CSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVararaRGARIVAGGRiaegAPAGGY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 315 YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMH 394
Cdd:cd07109 340 FVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNYGAG 419
|
410 420
....*....|....*....|....*....
gi 1169285 395 MTLaSLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07109 420 GGI-ELPFGGVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
12-420 |
1.81e-58 |
|
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: 199.12 E-value: 1.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISqGEVTLALRNLRAWMKDERVPKNl 91
Cdd:cd07108 29 KAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVL-ADLFRYFGGLAGELKGETLPFG- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 92 ATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----NVEKILAEVLPQYVdqscFAVVL 167
Cdd:cd07108 107 PDVL--TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPlavlLLAEILAQVLPAGV----LNVIT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 168 GGPQETGQ-LLEHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYV--DDNCDpQTVANRVAWFRYFNAGQT 243
Cdd:cd07108 181 GYGEECGAaLVDHPdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVfpDADLD-DAVDGAIAGMRFTRQGQS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 244 CVAPDYVLCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALLGCG------RVAIGGQSDESDR-- 314
Cdd:cd07108 260 CTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPlDEATDIGAIISEKQFAKVCGYIDLGlstsgaTVLRGGPLPGEGPla 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 315 ---YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDG 391
Cdd:cd07108 340 dgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQG 419
|
410 420
....*....|....*....|....*....
gi 1169285 392 FMHMtlASLPFGGVGASGMGRyhgKFSFD 420
Cdd:cd07108 420 GGQQ--PGQSYGGFKQSGLGR---EASLE 443
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
13-423 |
3.72e-58 |
|
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: 197.80 E-value: 3.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 13 EAFHA-GRTRPAE-----FRAAQLqglgrfLQENKQLLHDALAQDLHKSAFESEVS-EVAISQGEVTLALRNLRawmKDE 85
Cdd:cd07105 11 AAFPAwSKTPPSErrdilLKAADL------LESRRDEFIEAMMEETGATAAWAGFNvDLAAGMLREAASLITQI---IGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 RVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVDQ 160
Cdd:cd07105 82 SIPSDKPGTL--AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVfheagLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 161 SCFAVVLGGPQETGQLLEH---RFdyIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRY 237
Cdd:cd07105 160 VVTHSPEDAPEVVEALIAHpavRK--VNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 238 FNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQsspnLGRIINQKQFQRLRAL----LGCG-RVAIGGQSDES 312
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVV----LGSLVSAAAADRVKELvddaLSKGaKLVVGGLADES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 313 DR--YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGfcgnd 390
Cdd:cd07105 314 PSgtSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA----- 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 1169285 391 gfMH---MTL---ASLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07105 389 --VHingMTVhdePTLPHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
12-423 |
1.19e-57 |
|
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: 196.79 E-value: 1.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTR--PAEFRAAQLQGLGRFLQENKqllhDALAQdlhksaFESEVSEVAISQ--GEVTLALRnlrAWmkdeRV 87
Cdd:cd07118 29 RKAFDKGPWPrmSGAERAAVLLKVADLIRARR----ERLAL------IETLESGKPISQarGEIEGAAD---LW----RY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 88 PKNLATQL--DS---------AFIRKEPFGLVLIIAPWNYPLnLTL---VPLvgALAAGNCVVLKPSEISKNVEKILAEV 153
Cdd:cd07118 92 AASLARTLhgDSynnlgddmlGLVLREPIGVVGIITPWNFPF-LILsqkLPF--ALAAGCTVVVKPSEFTSGTTLMLAEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 154 -----LPQYVdqscFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQ 226
Cdd:cd07118 169 lieagLPAGV----VNIVTGYGATVGQaMTEHpDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 227 TVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPAL--QSTITRFyGD--DPQSspNLGRIINQKQFQRLRALLGCGR 302
Cdd:cd07118 245 AAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVvaRSRKVRV-GDplDPET--KVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 303 -----VAIGGQSDESD--RYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVK 375
Cdd:cd07118 322 aegatLLLGGERLASAagLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1169285 376 RVLTQTSSGGFCGN---DGFmhmtlASLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07118 402 TVARRIRAGTVWVNtflDGS-----PELPFGGFKQSGIGRELGRYGVEEYT 447
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
12-377 |
7.74e-57 |
|
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: 195.18 E-value: 7.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSafesevseVAISQGEVTLA---LRNLRAW---MKDE 85
Cdd:cd07088 45 EAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKT--------LSLARVEVEFTadyIDYMAEWarrIEGE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 RVPKNLATQldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdq 160
Cdd:cd07088 117 IIPSDRPNE--NIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELvdeagLPAGV-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 161 scFAVVLGGPQETGQLL-EH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYF 238
Cdd:cd07088 193 --LNIVTGRGSVVGDALvAHpKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRII 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 239 NAGQTCVAPD--YVLCS--PEMQERLLPALQSTItrfYGDDPQSSPNLGRIINQKQFQRL-----RALLGCGRVAIGGQS 309
Cdd:cd07088 271 NCGQVCTCAErvYVHEDiyDEFMEKLVEKMKAVK---VGDPFDAATDMGPLVNEAALDKVeemveRAVEAGATLLTGGKR 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169285 310 DESDR--YIAPTVLVDV-QEMEpVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRV 377
Cdd:cd07088 348 PEGEKgyFYEPTVLTNVrQDME-IVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRA 417
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
5-426 |
1.81e-56 |
|
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: 193.66 E-value: 1.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 5 GDTLRRLREAFHAGR---TRPAEFRAAQLQGLGRFLQENKQLLHDALAQD----LHKSAFESEVSEVAISQGeVTLALRN 77
Cdd:cd07152 13 ADVDRAAARAAAAQRawaATPPRERAAVLRRAADLLEEHADEIADWIVREsgsiRPKAGFEVGAAIGELHEA-AGLPTQP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 78 LRAWMKDERVPKNLAtqldsafiRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKP---SEISKNVekILAEV- 153
Cdd:cd07152 92 QGEILPSAPGRLSLA--------RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPdprTPVSGGV--VIARLf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 154 ----LPQYVDQscfavVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQT 227
Cdd:cd07152 162 eeagLPAGVLH-----VLPGGADAGEaLVEDpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 228 VANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSP-NLGRIINQKQFQRLRAL------LGc 300
Cdd:cd07152 237 AASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIvddsvaAG- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 301 GRVAIGGQSDesDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQ 380
Cdd:cd07152 316 ARLEAGGTYD--GLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADR 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1169285 381 TSSGGFCGNDGfmhmTLAS---LPFGGVGASGMG-RYHGKFSFDTFSHHR 426
Cdd:cd07152 394 LRTGMLHINDQ----TVNDephNPFGGMGASGNGsRFGGPANWEEFTQWQ 439
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
103-423 |
4.52e-56 |
|
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: 192.78 E-value: 4.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqscFAVVLG-GPqETGQL 176
Cdd:cd07093 116 QPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELaneagLPPGV----VNVVHGfGP-EAGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 177 L-EH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCvapdyvLCSp 254
Cdd:cd07093 191 LvAHpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVC------LAG- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 255 emqERLLpaLQSTI-----TRF--------YGDDPQSSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQSDESDR-- 314
Cdd:cd07093 264 ---SRIL--VQRSIydeflERFverakalkVGDPLDPDTEVGPLISKEHLEKVLGYVELARaegatILTGGGRPELPDle 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 315 ---YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDG 391
Cdd:cd07093 339 ggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCW 418
|
330 340 350
....*....|....*....|....*....|...
gi 1169285 392 FM-HMTlasLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07093 419 LVrDLR---TPFGGVKASGIGREGGDYSLEFYT 448
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
99-427 |
9.34e-56 |
|
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: 191.88 E-value: 9.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 99 FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----NVEKILAEV-LPQYVdqscFAVVLGGPQET 173
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPlsalRIAELMAEAgFPAGV----LNVVTGFGEVA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 174 GQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVL 251
Cdd:cd07115 188 GAaLVEHpDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 252 CSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALLGCGR------VAIGGQSDESDRYIAPTVLVDV 324
Cdd:cd07115 268 VHESIYDEFLERFTSLARSLRPGDPlDPKTQMGPLVSQAQFDRVLDYVDVGReegarlLTGGKRPGARGFFVEPTIFAAV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 325 QEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPFGG 404
Cdd:cd07115 348 PPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWINT--YNRFDPGSPFGG 425
|
330 340
....*....|....*....|...
gi 1169285 405 VGASGMGRYHGKFSFDTFSHHRA 427
Cdd:cd07115 426 YKQSGFGREMGREALDEYTEVKS 448
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
100-412 |
1.39e-55 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 192.05 E-value: 1.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 100 IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEI----SKNVEKILAEVLPQYVdqscFAVVLGGPQETGQ 175
Cdd:PRK13473 134 IRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEItpltALKLAELAADILPPGV----LNVVTGRGATVGD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 176 -LLEHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCS 253
Cdd:PRK13473 210 aLVGHPkVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 254 PEMQERL---LPALQSTITrfYGDDPQSSPNLGRIINQKQFQRL-----RAL-LGCGRVAIGGQ-SDESDRYIAPTVLVD 323
Cdd:PRK13473 290 RGIYDDLvakLAAAVATLK--VGDPDDEDTELGPLISAAHRDRVagfveRAKaLGHIRVVTGGEaPDGKGYYYEPTLLAG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 324 VQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMhmtLAS-LPF 402
Cdd:PRK13473 368 ARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM---LVSeMPH 444
|
330
....*....|
gi 1169285 403 GGVGASGMGR 412
Cdd:PRK13473 445 GGQKQSGYGK 454
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
6-422 |
1.45e-55 |
|
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: 190.75 E-value: 1.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 6 DTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSafesevseVAISQGEVTLALRNLR------ 79
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKP--------IAEARAEVEKCAWICRyyaena 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 80 -AWMKDERVPknlaTQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEI----SKNVEKILAEV- 153
Cdd:cd07100 75 eAFLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNvpgcALAIEELFREAg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 154 LPQYVdqscFAVVLGGPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRV 232
Cdd:cd07100 151 FPEGV----FQNLLIDSDQVEAIIADpRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 233 AWFRYFNAGQTCVAP----------DyvlcspEMQERLLPALQSTITrfyGDD--------PQSSPNLGRIInQKQFQrl 294
Cdd:cd07100 227 VKGRLQNAGQSCIAAkrfivhedvyD------EFLEKFVEAMAALKV---GDPmdedtdlgPLARKDLRDEL-HEQVE-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 295 RALLGCGRVAIGGQSDESDR-YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQV 373
Cdd:cd07100 295 EAVAAGATLLLGGKRPDGPGaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLER 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1169285 374 VKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGRYHGKFSFDTF 422
Cdd:cd07100 375 AERVARRLEAGMVFING--MVKSDPRLPFGGVKRSGYGRELGRFGIREF 421
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
12-423 |
7.03e-55 |
|
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: 190.21 E-value: 7.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAG--RTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEvsevaISQGEVTLALR---NLRAWMKDER 86
Cdd:cd07119 45 RRAFDSGewPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESE-----IDIDDVANCFRyyaGLATKETGEV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 87 VPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----NVEKILAEV-LPQYVdqs 161
Cdd:cd07119 120 YDVPPHVI---SRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPlttiALFELIEEAgLPAGV--- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 162 cFAVVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 239
Cdd:cd07119 194 -VNLVTGSGATVGAELaeSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFN 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 240 AGQTCVAPDYVLCSPEMQERLLPALQSTITRF---YGDDPqsSPNLGRIINQKQFQRLRALLGCG-----RVAIGGQSDE 311
Cdd:cd07119 273 AGQVCSAGSRLLVEESIHDKFVAALAERAKKIklgNGLDA--DTEMGPLVSAEHREKVLSYIQLGkeegaRLVCGGKRPT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 312 SDR-----YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF 386
Cdd:cd07119 351 GDElakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTV 430
|
410 420 430
....*....|....*....|....*....|....*..
gi 1169285 387 CGNDgfMHMTLASLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07119 431 WIND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
96-423 |
5.72e-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: 187.71 E-value: 5.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 96 DSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----NVEKILAEV-LPQYVdqscFAVVLGGP 170
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPltalKVAEIMEEAgLPKGV----FNVVQGDG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 171 QETGQLL-EHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD 248
Cdd:TIGR01804 201 AEVGPLLvNHPdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGT 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 249 YVLCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALLGCG-----RVAIGGQSDESDR-----YIA 317
Cdd:TIGR01804 281 RVFVHKKIKERFLARLVERTERIKLGDPfDEATEMGPLISAAHRDKVLSYIEKGkaegaTLATGGGRPENVGlqngfFVE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 318 PTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTL 397
Cdd:TIGR01804 361 PTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYP 438
|
330 340
....*....|....*....|....*.
gi 1169285 398 ASLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:TIGR01804 439 AEAPFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
98-423 |
1.44e-53 |
|
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: 186.27 E-value: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqscFAVVLGGPQE 172
Cdd:cd07112 118 ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLPAGV----LNVVPGFGHT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 173 TGQLL-EHR-FDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNC-DPQTVANRVAWFRYFNAGQTCVAPD 248
Cdd:cd07112 194 AGEALgLHMdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 249 YVLCSPEMQERLLPALQSTITRFY-GD--DPQSSpnLGRIINQKQFQRLRALLGCG-----RVAIGGQSDESDR---YIA 317
Cdd:cd07112 274 RLLVHESIKDEFLEKVVAAAREWKpGDplDPATR--MGALVSEAHFDKVLGYIESGkaegaRLVAGGKRVLTETggfFVE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 318 PTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF---CGNDGFMh 394
Cdd:cd07112 352 PTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVwvnCFDEGDI- 430
|
330 340
....*....|....*....|....*....
gi 1169285 395 mtlaSLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07112 431 ----TTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
12-412 |
3.40e-53 |
|
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: 185.49 E-value: 3.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAG--RTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESevsevaiSQGEVTLALRNLR--AWMKDE-- 85
Cdd:cd07091 51 RAAFETGwwRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEES-------AKGDVALSIKCLRyyAGWADKiq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 -RVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----NVEKILAEV-LPQYVd 159
Cdd:cd07091 124 gKTIPIDGNFL--AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPlsalYLAELIKEAgFPPGV- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 160 qscFAVVLG-GPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANrVAWFR 236
Cdd:cd07091 201 ---VNIVPGfGPTAGAAISSHmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVE-WAAFG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 237 -YFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFY-GDDPQSSPNLGRIINQKQFQRL----------RALLGCGrva 304
Cdd:cd07091 277 iFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKIlsyiesgkkeGATLLTG--- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 305 iGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 384
Cdd:cd07091 354 -GERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAG 432
|
410 420
....*....|....*....|....*...
gi 1169285 385 GFCGNDGfmHMTLASLPFGGVGASGMGR 412
Cdd:cd07091 433 TVWVNTY--NVFDAAVPFGGFKQSGFGR 458
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-427 |
3.69e-53 |
|
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: 185.63 E-value: 3.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKqllhDALAQDLHKsafesEV-SEVAISQGEVTLAL----------RNlra 80
Cdd:cd07131 47 REAFPEWRKVPAPRRAEYLFRAAELLKKRK----EELARLVTR-----EMgKPLAEGRGDVQEAIdmaqyaagegRR--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 81 wMKDERVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVL-----P 155
Cdd:cd07131 115 -LFGETVPSELPNKD--AMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFaeaglP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 156 QYVdqscFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVA 233
Cdd:cd07131 192 PGV----VNVVHGRGEEVGEaLVEHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGAL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 234 WFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNL-GRIINQKQFQRL-----------RALLGCG 301
Cdd:cd07131 268 WSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDmGPLINEAQLEKVlnyneigkeegATLLLGG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 302 RVAIGGQSDESdRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQT 381
Cdd:cd07131 348 ERLTGGGYEKG-YFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDL 426
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1169285 382 SSGGFCGNDGfmhmTL---ASLPFGGVGASGMG-RYHGKFSFDTFSHHRA 427
Cdd:cd07131 427 EAGITYVNAP----TIgaeVHLPFGGVKKSGNGhREAGTTALDAFTEWKA 472
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
8-412 |
5.55e-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: 184.34 E-value: 5.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 8 LRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSafesevseVAISQGEVTLALRNLR------AW 81
Cdd:cd07149 27 IAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKP--------IKDARKEVDRAIETLRlsaeeaKR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 82 MKDERVPknlatqLDS--------AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV 153
Cdd:cd07149 99 LAGETIP------FDAspggegriGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 154 LPQ-YVDQSCFAVVLGGPQETG-QLLEH-RFDYIFFTGSPRVGKIVMTAAAkhLTPVTLELGGKNPCYVDDNCDPQTVAN 230
Cdd:cd07149 173 LLEaGLPKGALNVVTGSGETVGdALVTDpRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 231 RVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRL-----RALLGCGRVA 304
Cdd:cd07149 251 RCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLvVGDPLDEDTDVGPMISEAEAERIeewveEAVEGGARLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 305 IGGQSDEsdRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 384
Cdd:cd07149 331 TGGKRDG--AILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVG 408
|
410 420 430
....*....|....*....|....*....|..
gi 1169285 385 GFCGNDG----FMHMtlaslPFGGVGASGMGR 412
Cdd:cd07149 409 GVMINDSstfrVDHM-----PYGGVKESGTGR 435
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
12-423 |
6.43e-53 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 184.17 E-value: 6.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVsEVAISQGEVTLALRNLRAwMKDERVPKNL 91
Cdd:cd07094 31 RAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV-EVDRAIDTLRLAAEEAER-IRGEEIPLDA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 92 ATQLDS--AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVL-PQYVDQSCFAVVLG 168
Cdd:cd07094 109 TQGSDNrlAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEGVLQVVTG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 169 GPQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKhlTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA 246
Cdd:cd07094 189 EREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCIS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 247 PDYVLCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRL-----RALLGCGRVAIGGQSDesDRYIAPTV 320
Cdd:cd07094 267 VQRIYVHEELYDEFIEAFVAAVKKLKVGDPlDEDTDVGPLISEEAAERVerwveEAVEAGARLLCGGERD--GALFKPTV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 321 LVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfMHMTLASL 400
Cdd:cd07094 345 LEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDS-SAFRTDWM 423
|
410 420
....*....|....*....|...
gi 1169285 401 PFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07094 424 PFGGVKESGVGREGVPYAMEEMT 446
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
9-416 |
9.57e-53 |
|
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: 184.05 E-value: 9.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 9 RRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHK---SAFEsEVSEVAISqgeVTLALRNLRAWMKDE 85
Cdd:cd07101 25 ARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarrHAFE-EVLDVAIV---ARYYARRAERLLKPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 RVPKNLATqLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS-----KNVEKILAEVLPQYVdq 160
Cdd:cd07101 101 RRRGAIPV-LTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTaltalWAVELLIEAGLPRDL-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 161 scFAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVAnRVAWFRYF-N 239
Cdd:cd07101 178 --WQVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAA-AGAVRACFsN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 240 AGQTCVAPD--YVLCS--PEMQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQS- 309
Cdd:cd07101 255 AGQLCVSIEriYVHESvyDEFVRRFVARTRALRL---GAALDYGPDMGSLISQAQLDRVTAHVDDAVakgatVLAGGRAr 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 310 -DESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCG 388
Cdd:cd07101 332 pDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNV 411
|
410 420 430
....*....|....*....|....*....|
gi 1169285 389 NDGFMhMTLASL--PFGGVGASGMGRYHGK 416
Cdd:cd07101 412 NEGYA-AAWASIdaPMGGMKDSGLGRRHGA 440
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
12-422 |
2.95e-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: 183.16 E-value: 2.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAG---RTRPAEfRAAQLQGLGRFLQENKQLLHDALAQDLH--KSAFESEVSEVAISQGEVTLALRNLRAWmKDER 86
Cdd:cd07139 46 RRAFDNGpwpRLSPAE-RAAVLRRLADALEARADELARLWTAENGmpISWSRRAQGPGPAALLRYYAALARDFPF-EERR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 87 VPKNLATQLdsafIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqs 161
Cdd:cd07139 124 PGSGGGHVL----VRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAaeeagLPPGV--- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 162 cFAVVLGGPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 240
Cdd:cd07139 197 -VNVVPADREVGEYLVRHpGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 241 GQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGD--DPqsSPNLGRIINQKQFQRLRALLGCGR------VAIGGQSDE 311
Cdd:cd07139 276 GQVCVALTRILVPRSRYDEVVEALAAAVAALkVGDplDP--ATQIGPLASARQRERVEGYIAKGRaegarlVTGGGRPAG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 312 SDR--YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGN 389
Cdd:cd07139 354 LDRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN 433
|
410 420 430
....*....|....*....|....*....|...
gi 1169285 390 DGFMHMtlaSLPFGGVGASGMGRYHGKFSFDTF 422
Cdd:cd07139 434 GFRLDF---GAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
7-423 |
4.11e-51 |
|
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: 179.81 E-value: 4.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 7 TLRRLREAFHAGR--------TRPAEfRAAQLQGLGRFLQENKQLLHDALAQDLH----KSAFESEVSeVAISQGEVTLA 74
Cdd:cd07151 30 SKEDVDEAYRAAAaaqkewaaTLPQE-RAEILEKAAQILEERRDEIVEWLIRESGstriKANIEWGAA-MAITREAATFP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 75 LRnlrawMKDERVPKNLATQldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE---ISKNVekILA 151
Cdd:cd07151 108 LR-----MEGRILPSDVPGK--ENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASdtpITGGL--LLA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 152 EV-----LPQYVdqscFAVVLGGPQETG-QLLEHRF-DYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCD 224
Cdd:cd07151 179 KIfeeagLPKGV----LNVVVGAGSEIGdAFVEHPVpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDAD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 225 PQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRL-----RALL 298
Cdd:cd07151 255 IDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLldkieQAVE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 299 GCGRVAIGGQSDesDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVL 378
Cdd:cd07151 335 EGATLLVGGEAE--GNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFA 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1169285 379 TQTSSGGFCGNDGFMHmTLASLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07151 413 RRIDAGMTHINDQPVN-DEPHVPFGGEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
12-423 |
4.86e-51 |
|
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: 179.28 E-value: 4.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAG--RTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKsafesevsevAISqgEVTLALRNLRAW-------- 81
Cdd:cd07114 29 RAAFEGGawRKLTPTERGKLLRRLADLIEANAEELAELETRDNGK----------LIR--ETRAQVRYLAEWyryyagla 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 82 --MKDERVPKNLATQLdsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----L 154
Cdd:cd07114 97 dkIEGAVIPVDKGDYL--NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 155 PQYVdqscFAVVLGGPQETGQLL-EH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRV 232
Cdd:cd07114 175 PPGV----VNVVTGFGPETGEALvEHpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 233 AWFRYFNAGQTCVAPDYVLCSPEMQERLLPALqSTITRF--YGDDPQSSPNLGRIINQKQFQRLRALLGC-----GRVAI 305
Cdd:cd07114 251 VAGIFAAAGQTCVAGSRLLVQRSIYDEFVERL-VARARAirVGDPLDPETQMGPLATERQLEKVERYVARareegARVLT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 306 GGQ---SDESDR--YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQ 380
Cdd:cd07114 330 GGErpsGADLGAgyFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARA 409
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1169285 381 TSSGGFCGNDgfMHMTLASLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07114 410 IEAGTVWVNT--YRALSPSSPFGGFKDSGIGRENGIEAIREYT 450
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
12-412 |
7.26e-51 |
|
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: 179.08 E-value: 7.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVsevaisqgEVTLALRNLRAWMKDERVPKNL 91
Cdd:cd07145 31 EKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV--------EVERTIRLFKLAAEEAKVLRGE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 92 ATQLDS--------AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQY-VDQSC 162
Cdd:cd07145 103 TIPVDAyeynerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 163 FAVVLGGPQETG-QLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA 240
Cdd:cd07145 183 INVVTGYGSEVGdEIVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 241 GQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRL-----RALLGCGRVAIGGQSDESDr 314
Cdd:cd07145 263 GQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPlDESTDLGPLISPEAVERMenlvnDAVEKGGKILYGGKRDEGS- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 315 YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfMH 394
Cdd:cd07145 342 FFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDS-TR 420
|
410
....*....|....*...
gi 1169285 395 MTLASLPFGGVGASGMGR 412
Cdd:cd07145 421 FRWDNLPFGGFKKSGIGR 438
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
98-427 |
1.03e-50 |
|
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: 179.14 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----NVEKILAEV-LPQYVdqscFAVVLGGPQE 172
Cdd:cd07144 138 AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPlsllYFANLVKEAgFPPGV----VNIIPGYGAV 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 173 TGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYV 250
Cdd:cd07144 214 AGSaLAEHpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRI 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 251 LCSPEMQERLLPALQSTITRFY--GDDPQSSPNLGRIINQKQFQRLRALLGCGR------VAIG---GQSDESDRYIAPT 319
Cdd:cd07144 294 YVQESIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKkegaklVYGGekaPEGLGKGYFIPPT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 320 VLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF---CGNDGFMHMt 396
Cdd:cd07144 374 IFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVwinSSNDSDVGV- 452
|
330 340 350
....*....|....*....|....*....|.
gi 1169285 397 laslPFGGVGASGMGRYHGKFSFDTFSHHRA 427
Cdd:cd07144 453 ----PFGGFKMSGIGRELGEYGLETYTQTKA 479
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
12-424 |
1.05e-50 |
|
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: 179.08 E-value: 1.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHA-GRTRPAEfRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESevsevaiSQGEVTLALRNLRAWMKDERVPKN 90
Cdd:cd07559 48 HEAFKTwGKTSVAE-RANILNKIADRIEENLELLAVAETLDNGKPIRET-------LAADIPLAIDHFRYFAGVIRAQEG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 91 LATQLDS---AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----NVEKILAEVLPQYVdqscF 163
Cdd:cd07559 120 SLSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPlsilVLMELIGDLLPKGV----V 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 164 AVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNP-------CYVDDNCDPQTVANRVAW 234
Cdd:cd07559 196 NVVTGFGSEAGKpLASHpRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPniffddaMDADDDFDDKAEEGQLGF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 235 FryFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQ-SSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQ 308
Cdd:cd07559 276 A--FNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLdPETMMGAQVSKDQLEKILSYVDIGKeegaeVLTGGE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 309 SDESDR-----YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSS 383
Cdd:cd07559 354 RLTLGGldkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQT 433
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1169285 384 GGFCGNDgfMHMTLASLPFGGVGASGMGRYHGKFSFDTFSH 424
Cdd:cd07559 434 GRVWVNC--YHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQ 472
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
12-423 |
4.21e-50 |
|
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: 177.44 E-value: 4.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEvsevaisqGEVTLALRNLR-----AW-MKDE 85
Cdd:cd07097 47 AAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEAR--------GEVTRAGQIFRyyageALrLSGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 RVP---KNLatqldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQY 157
Cdd:cd07097 119 TLPstrPGV-----EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEIleeagLPAG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 158 VdqscFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWF 235
Cdd:cd07097 194 V----FNLVMGSGSEVGQaLVEHpDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 236 RYFNAGQTCVAPDYVLCSPEMQERLLPAL-QSTITRFYGDDPQSSPNLGRIINQKQFQR-LRAL-LG---CGRVAIGGQ- 308
Cdd:cd07097 270 AFFSTGQRCTASSRLIVTEGIHDRFVEALvERTKALKVGDALDEGVDIGPVVSERQLEKdLRYIeIArseGAKLVYGGEr 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 309 --SDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREkplalyaFSNSSQVVKRVL-------- 378
Cdd:cd07097 350 lkRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTE-------FGLSAGIVTTSLkhathfkr 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1169285 379 -TQTssggfcgndGFMHMTLAS------LPFGGVGASGMG-RYHGKFSFDTFS 423
Cdd:cd07097 423 rVEA---------GVVMVNLPTagvdyhVPFGGRKGSSYGpREQGEAALEFYT 466
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
99-422 |
7.23e-49 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 174.49 E-value: 7.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 99 FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQY-VDQSCFAVVLGGPQETGQLL 177
Cdd:PLN02278 155 LVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIGDAL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 178 --EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPE 255
Cdd:PLN02278 235 laSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 256 MQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLRA------------LLGCGRVAIGGQsdesdrYIAPTVLV 322
Cdd:PLN02278 315 IYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVEShvqdavskgakvLLGGKRHSLGGT------FYEPTVLG 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 323 DVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLAslPF 402
Cdd:PLN02278 389 DVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PF 466
|
330 340
....*....|....*....|
gi 1169285 403 GGVGASGMGRYHGKFSFDTF 422
Cdd:PLN02278 467 GGVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
98-411 |
2.51e-47 |
|
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: 169.46 E-value: 2.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqscFAVVLGGPQE 172
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLlyeagLPPDM----LSVVTGEPGE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 173 TGQLLEH--RFDYIFFTGSPRVGK-IVMTAAAKHLtpvTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 249
Cdd:cd07146 190 IGDELIThpDVDLVTFTGGVAVGKaIAATAGYKRQ---LLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKR 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 250 VLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQK---QFQR--LRALLGCGRVAIGGQSDESdrYIAPTVLVD 323
Cdd:cd07146 267 ILVHESVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDEEaaiQIENrvEEAIAQGARVLLGNQRQGA--LYAPTVLDH 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 324 VQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGfMHMTLASLPFG 403
Cdd:cd07146 345 VPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEV-PGFRSELSPFG 423
|
....*...
gi 1169285 404 GVGASGMG 411
Cdd:cd07146 424 GVKDSGLG 431
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
12-423 |
2.77e-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: 169.94 E-value: 2.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGR-TRPAEfRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAisqgevtLALRNLRAWMKDERVPKN 90
Cdd:cd07117 48 QEAFKTWRkTTVAE-RANILNKIADIIDENKELLAMVETLDNGKPIRETRAVDIP-------LAADHFRYFAGVIRAEEG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 91 LATQLDSAF---IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----NVEKILAEVLPQYVdqscF 163
Cdd:cd07117 120 SANMIDEDTlsiVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSlsllELAKIIQDVLPKGV----V 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 164 AVVLGGPQETGQ-LLEHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 241
Cdd:cd07117 196 NIVTGKGSKSGEyLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 242 QTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQS-SPNLGRIINQKQFQRLRALLGCG-----RVAIGGQ---SDES 312
Cdd:cd07117 276 QVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDpDTQMGAQVNKDQLDKILSYVDIAkeegaKILTGGHrltENGL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 313 DR--YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGND 390
Cdd:cd07117 356 DKgfFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNT 435
|
410 420 430
....*....|....*....|....*....|...
gi 1169285 391 gfMHMTLASLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07117 436 --YNQIPAGAPFGGYKKSGIGRETHKSMLDAYT 466
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
9-415 |
6.59e-47 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 169.67 E-value: 6.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 9 RRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDaLAQ----DLHKSAFEsEVSEVAIsqgeVTL-ALRNLRAWMK 83
Cdd:PRK09407 61 ARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLD-LVQletgKARRHAFE-EVLDVAL----TARyYARRAPKLLA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 84 DERVPKNLATqLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQY-VDQSC 162
Cdd:PRK09407 135 PRRRAGALPV-LTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 163 FAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 242
Cdd:PRK09407 214 WQVVTGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 243 TCVAPD--YVLCS--PEMQERLLPALQS-TITRFYGDDPQsspnLGRIINQKQFQRLRALLGCGR-----VAIGGQS--D 310
Cdd:PRK09407 294 LCISIEriYVHESiyDEFVRAFVAAVRAmRLGAGYDYSAD----MGSLISEAQLETVSAHVDDAVakgatVLAGGKArpD 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 311 ESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINrrEKPLALYA--FSNSSQVVKRVLTQTSSGGFCG 388
Cdd:PRK09407 370 LGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERAN--DTPYGLNAsvWTGDTARGRAIAARIRAGTVNV 447
|
410 420
....*....|....*....|....*....
gi 1169285 389 NDGFMhMTLASL--PFGGVGASGMGRYHG 415
Cdd:PRK09407 448 NEGYA-AAWGSVdaPMGGMKDSGLGRRHG 475
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
98-424 |
4.64e-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: 165.94 E-value: 4.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQY-VDQSCFAVVLGGpQETGQL 176
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 177 LEHRFDY--IFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSP 254
Cdd:cd07090 189 LCEHPDVakVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 255 EMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALLGCG-----RVAIGGQSDESDR------YIAPTVLV 322
Cdd:cd07090 269 SIKDEFTERLVERTKKIRIGDPlDEDTQMGALISEEHLEKVLGYIESAkqegaKVLCGGERVVPEDglengfYVSPCVLT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 323 DVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLPF 402
Cdd:cd07090 349 DCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVEVPF 426
|
330 340
....*....|....*....|..
gi 1169285 403 GGVGASGMGRYHGKFSFDTFSH 424
Cdd:cd07090 427 GGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
97-431 |
6.00e-46 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 166.08 E-value: 6.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 97 SAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqscFAVVLGGPQ 171
Cdd:cd07113 135 TAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELakeagIPDGV----LNVVNGKGA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 172 ETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYV 250
Cdd:cd07113 211 VGAQLISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 251 LCSPEMQERLLPALQSTITRFYGDDPQS-SPNLGRIINQKQFQRLRALLGCGR------VAIGGQSDESDRYIAPTVLVD 323
Cdd:cd07113 291 YVHRSKFDELVTKLKQALSSFQVGSPMDeSVMFGPLANQPHFDKVCSYLDDARaegdeiVRGGEALAGEGYFVQPTLVLA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 324 VQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNdgfMHMTL-ASLPF 402
Cdd:cd07113 371 RSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLdPAVPF 447
|
330 340
....*....|....*....|....*....
gi 1169285 403 GGVGASGMGRYHGKFSFDTFSHHRACLLR 431
Cdd:cd07113 448 GGMKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
12-411 |
6.23e-46 |
|
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: 166.63 E-value: 6.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFES--EVSEvAISQGE--VTLALRNLRAWMKDERV 87
Cdd:cd07124 79 RAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEAdaDVAE-AIDFLEyyAREMLRLRGFPVEMVPG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 88 PKNlatqldsaFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqsc 162
Cdd:cd07124 158 EDN--------RYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEIleeagLPPGV---- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 163 FAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAK------HLTPVTLELGGKNPCYVDDNCDPQTVANRV-- 232
Cdd:cd07124 226 VNFLPGPGEEVGDyLVEHpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIvr 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 233 AWFRYfnAGQTCVApdyvlCS---------PEMQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLR----ALLG 299
Cdd:cd07124 306 SAFGF--QGQKCSA-----CSrvivhesvyDEFLERLVERTKALKV---GDPEDPEVYMGPVIDKGARDRIRryieIGKS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 300 CGRVAIGGQSDESDR---YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKR 376
Cdd:cd07124 376 EGRLLLGGEVLELAAegyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLER 455
|
410 420 430
....*....|....*....|....*....|....*
gi 1169285 377 VLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMG 411
Cdd:cd07124 456 ARREFEVGNLYANRKITGALVGRQPFGGFKMSGTG 490
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-424 |
9.30e-46 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 166.06 E-value: 9.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTR-----PAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESE--VSEVA------ISQGEvTLALRNl 78
Cdd:PLN02467 55 RKAFKRNKGKdwartTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAwdMDDVAgcfeyyADLAE-ALDAKQ- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 79 rawmkdeRVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV----- 153
Cdd:PLN02467 133 -------KAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADIcrevg 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 154 LPQYVdqscFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDpqtVANR 231
Cdd:PLN02467 206 LPPGV----LNVVTGLGTEAGApLASHpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVD---LDKA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 232 VAW--FRYF-NAGQTCVAPDYVLC----SPEMQERLLPALQStITrfYGDDPQSSPNLGRIINQKQFQRLRALLGCGR-- 302
Cdd:PLN02467 279 VEWamFGCFwTNGQICSATSRLLVheriASEFLEKLVKWAKN-IK--ISDPLEEGCRLGPVVSEGQYEKVLKFISTAKse 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 303 ---VAIGGQSDESDR---YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKR 376
Cdd:PLN02467 356 gatILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCER 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1169285 377 VLTQTSSGGF---CGNDGFmhmtlASLPFGGVGASGMGRYHGKFSFDTFSH 424
Cdd:PLN02467 436 VSEAFQAGIVwinCSQPCF-----CQAPWGGIKRSGFGRELGEWGLENYLS 481
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
98-427 |
9.33e-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: 165.78 E-value: 9.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKnvekILAEVLPQYVDQSCFA-----VVLGGPQE 172
Cdd:cd07143 138 TYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTP----LSALYMTKLIPEAGFPpgvinVVSGYGRT 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 173 TGQLLE-H-RFDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 249
Cdd:cd07143 214 CGNAISsHmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSR 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 250 VLCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQSDESDRY-IAPTVLV 322
Cdd:cd07143 294 IYVQEGIYDKFVKRFKEKAKKLKVGDPfAEDTFQGPQVSQIQYERIMSYIESGKaegatVETGGKRHGNEGYfIEPTIFT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 323 DVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF---CGNdgfmhMTLAS 399
Cdd:cd07143 374 DVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVwvnCYN-----LLHHQ 448
|
330 340
....*....|....*....|....*...
gi 1169285 400 LPFGGVGASGMGRYHGKFSFDTFSHHRA 427
Cdd:cd07143 449 VPFGGYKQSGIGRELGEYALENYTQIKA 476
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
12-412 |
1.04e-45 |
|
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: 164.37 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEvSEVAISQGEVTLALRNLrawmkDERV-PKN 90
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQ-TEVAAMAGKIDISIKAY-----HERTgERA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 91 LATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqscFAV 165
Cdd:cd07095 84 TPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELweeagLPPGV----LNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 166 VLGGPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHltP---VTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 241
Cdd:cd07095 160 VQGGRETGEALAAHeGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 242 QTCVAPDYVLCSPEMQ-ERLLPALQSTITRFYGDDPQSSPN--LGRIINQKQFQRLRA---LLGCGRVAIGGQS--DESD 313
Cdd:cd07095 238 QRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPfmGPLIIAAAAARYLLAqqdLLALGGEPLLAMErlVAGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 314 RYIAPTvLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNdgfM 393
Cdd:cd07095 318 AFLSPG-IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWN---R 393
|
410 420
....*....|....*....|.
gi 1169285 394 HMTLAS--LPFGGVGASGMGR 412
Cdd:cd07095 394 PTTGASstAPFGGVGLSGNHR 414
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
7-428 |
2.10e-45 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 164.66 E-value: 2.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 7 TLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFES--EVSE-VAISQGEVTLALRNLRAWMK 83
Cdd:cd07086 40 AVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGlgEVQEmIDICDYAVGLSRMLYGLTIP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 84 DERVPKNLATQLdsafirkEPFGLVLIIAPWNYPL-----NLTLvplvgALAAGNCVVLKPSE----ISKNVEKILAEVL 154
Cdd:cd07086 120 SERPGHRLMEQW-------NPLGVVGVITAFNFPVavpgwNAAI-----ALVCGNTVVWKPSEttplTAIAVTKILAEVL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 155 PQY-VDQSCFAVVLGGpQETGQLLEH--RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANR 231
Cdd:cd07086 188 EKNgLPPGVVNLVTGG-GDGGELLVHdpRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 232 VAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNL-GRIINQKQFQR-LRAL-----LGcGRVA 304
Cdd:cd07086 267 VLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLvGPLINQAAVEKyLNAIeiaksQG-GTVL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 305 IGG---QSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQT 381
Cdd:cd07086 346 TGGkriDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPK 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1169285 382 SSGgfCG----NDGfmhmTL---ASLPFGGVGASGMGRYHGKFSFDTFSHHRAC 428
Cdd:cd07086 426 GSD--CGivnvNIP----TSgaeIGGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
12-415 |
5.49e-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: 5.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDlhkSAFEseVSEVAisqGEVTLALRNLRAW------MKDE 85
Cdd:cd07107 29 RAAFPEWRATTPLERARMLRELATRLREHAEELALIDALD---CGNP--VSAML---GDVMVAAALLDYFaglvteLKGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 RVPknlATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----NVEKILAEVLPQYVdqs 161
Cdd:cd07107 101 TIP---VGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPlsalRLAELAREVLPPGV--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 162 cFAVVLGGPQETGQ-LLEHR-FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANR-VAWFRYF 238
Cdd:cd07107 175 -FNILPGDGATAGAaLVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAaVAGMNFT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 239 NAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPqSSPN--LGRIINQKQFQRLRALLGCGR------VAIGGQSD 310
Cdd:cd07107 254 WCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDP-TDPAttMGPLVSRQQYDRVMHYIDSAKregarlVTGGGRPE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 311 ----ESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF 386
Cdd:cd07107 333 gpalEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYV 412
|
410 420
....*....|....*....|....*....
gi 1169285 387 CGNDGFMHMTlaSLPFGGVGASGMGRYHG 415
Cdd:cd07107 413 WINGSSRHFL--GAPFGGVKNSGIGREEC 439
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
12-423 |
1.34e-44 |
|
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: 162.13 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGR-TRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVsEVAISQGEV----TLAlRNLRAWMKDER 86
Cdd:cd07120 29 RRAFDETDwAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF-EISGAISELryyaGLA-RTEAGRMIEPE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 87 vPKNLATQLdsafirKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKP----SEISKNVEKILAEV--LPQYVDQ 160
Cdd:cd07120 107 -PGSFSLVL------REPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPagqtAQINAAIIRILAEIpsLPAGVVN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 161 ScfaVVLGGPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 239
Cdd:cd07120 180 L---FTESGSEGAAHLVASpDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 240 AGQTCVAPDYVLC----SPEMQERLLPALQStITRFYGDDPQSspNLGRIINQKQFQRL-----RALLGCGRVAI-GGQS 309
Cdd:cd07120 257 AGQFCMAGSRVLVqrsiADEVRDRLAARLAA-VKVGPGLDPAS--DMGPLIDRANVDRVdrmveRAIAAGAEVVLrGGPV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 310 DESDR---YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGF 386
Cdd:cd07120 334 TEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTV 413
|
410 420 430
....*....|....*....|....*....|....*...
gi 1169285 387 CGNDgfmHMTL-ASLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07120 414 WIND---WNKLfAEAEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
14-431 |
1.87e-44 |
|
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: 162.09 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 14 AF-HAGRTRPaEFRAAQLQGLGRFLQENKQLLHDALAQDLHK---SAFESEVSEVAISQGEVTLALRNLRAWMKDERVPK 89
Cdd:TIGR03374 50 AFaEWGQTTP-KARAECLLKLADVIEENAQVFAELESRNCGKplhSVFNDEIPAIVDVFRFFAGAARCLSGLAAGEYLEG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 90 NlatqldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGG 169
Cdd:TIGR03374 129 H------TSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 170 PQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAP 247
Cdd:TIGR03374 203 GKTVGDPLtgHEKVRMVSLTGSIATGEHILSHTAPSIKRTHMELGGKAPVIVFDDADIDAVVEGVRTFGFYNAGQDCTAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 248 DYVLCSPEMQERLLPALQSTITRFYGDDPQ-SSPNLGRIINQKQFQRLRAL------LGCGRVAIGGQSDESD-RYIAPT 319
Cdd:TIGR03374 283 CRIYAQRGIYDTLVEKLGAAVATLKSGAPDdESTELGPLSSLAHLERVMKAveeakaLGHIKVITGGEKRKGNgYYFAPT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 320 VLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFmhMTLAS 399
Cdd:TIGR03374 363 LLAGAKQDDAIVQKEVFGPVVSITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHF--MLVSE 440
|
410 420 430
....*....|....*....|....*....|..
gi 1169285 400 LPFGGVGASGMGRYHGKFSFDTFSHHRACLLR 431
Cdd:TIGR03374 441 MPHGGQKLSGYGKDMSLYGLEDYTVVRHIMVK 472
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
67-427 |
1.98e-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: 161.89 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 67 SQGEVTLALRNLR---AWMKD---ERVPknlATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPS 140
Cdd:cd07142 101 RYAEVPLAARLFRyyaGWADKihgMTLP---ADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 141 EISK----NVEKILAEV-LPQYVdqscFAVVLG-GPQETGQLLEHR-FDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELG 212
Cdd:cd07142 178 EQTPlsalLAAKLAAEAgLPDGV----LNIVTGfGPTAGAAIASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 213 GKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLP-ALQSTITRFYGDDPQSSPNLGRIINQKQF 291
Cdd:cd07142 254 GKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEkAKARALKRVVGDPFRKGVEQGPQVDKEQF 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 292 QRL----------RALLGCGRVAIGGQSdesdRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKP 361
Cdd:cd07142 334 EKIlsyiehgkeeGATLITGGDRIGSKG----YYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYG 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1169285 362 LALYAFSNSSQVVKRVLTQTSSGGFCGN--DGFMhmtlASLPFGGVGASGMGRYHGKFSFDTFSHHRA 427
Cdd:cd07142 410 LAAGVFSKNIDTANTLSRALKAGTVWVNcyDVFD----ASIPFGGYKMSGIGREKGIYALNNYLQVKA 473
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
99-384 |
8.24e-44 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 158.75 E-value: 8.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 99 FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqscFAVVLGGPQET 173
Cdd:PRK10090 66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIvdeigLPKGV----FNLVLGRGETV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 174 GQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPD--Y 249
Cdd:PRK10090 142 GQELagNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAErvY 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 250 VLCS--PEMQERLLPALQSTItrfYGDDPQ-SSPNLGRIINQKQFQRL-----RALLGCGRVAIGGQSDESDRYI-APTV 320
Cdd:PRK10090 222 VQKGiyDQFVNRLGEAMQAVQ---FGNPAErNDIAMGPLINAAALERVeqkvaRAVEEGARVALGGKAVEGKGYYyPPTL 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1169285 321 LVDV-QEMEpVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 384
Cdd:PRK10090 299 LLDVrQEMS-IMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFG 362
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
14-412 |
3.77e-43 |
|
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: 158.50 E-value: 3.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 14 AFHAGR----TRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESevsevaisQGEVT----------LALRNL- 78
Cdd:cd07082 47 AYDAGRgwwpTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDA--------LKEVDrtidyirdtiEELKRLd 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 79 RAWMKDERVPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSeiSKNVekILAEVLPQYV 158
Cdd:cd07082 119 GDSLPGDWFPGTKGKI---AQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA--TQGV--LLGIPLAEAF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 159 DQSCF-----AVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKhlTPVTLELGGKNPCYVDDNCDPQTVANR 231
Cdd:cd07082 192 HDAGFpkgvvNVVTGRGREIGDpLVTHgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 232 VAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALL------GcGRVA 304
Cdd:cd07082 270 IVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPwDNGVDITPLIDPKSADFVEGLIddavakG-ATVL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 305 IGGQSdESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 384
Cdd:cd07082 349 NGGGR-EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVG 427
|
410 420 430
....*....|....*....|....*....|....*
gi 1169285 385 -----GFC--GNDGFmhmtlaslPFGGVGASGMGR 412
Cdd:cd07082 428 tvninSKCqrGPDHF--------PFLGRKDSGIGT 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
14-411 |
1.11e-42 |
|
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: 157.74 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 14 AFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFEsEVSEVAISQGEVTLALRNLRAWMKDERVPKNLAT 93
Cdd:cd07083 67 AFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVE-AIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 94 QLDSAFIRkePFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKNVEKILAEV-LPQYVDQSCFAVvlg 168
Cdd:cd07083 146 EDNESFYV--GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEdavvVGYKVFEIFHEAgFPPGVVQFLPGV--- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 169 GPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLT------PVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 241
Cdd:cd07083 221 GEEVGAYLTEHeRIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 242 QTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQS-SPNLGRIINQKQFQRLRALLGCGR----VAIGGQSDESDRY- 315
Cdd:cd07083 301 QKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEEnGTDLGPVIDAEQEAKVLSYIEHGKnegqLVLGGKRLEGEGYf 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 316 IAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLD--EAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFM 393
Cdd:cd07083 381 VAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKIT 460
|
410
....*....|....*...
gi 1169285 394 HMTLASLPFGGVGASGMG 411
Cdd:cd07083 461 GALVGVQPFGGFKLSGTN 478
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
98-423 |
1.58e-42 |
|
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: 156.74 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISknveKILAEVLPQYVDQSCFA-----VVLG-GPQ 171
Cdd:cd07141 139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQT----PLTALYLASLIKEAGFPpgvvnVVPGyGPT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 172 ETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDY 249
Cdd:cd07141 215 AGAAISSHpDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 250 VLC-SPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGR------VAIGGQSDESDRYIAPTVLV 322
Cdd:cd07141 295 TFVqESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKkegaklECGGKRHGDKGYFIQPTVFS 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 323 DVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSsqvVKRVLTQTSS--GGFCGNDGFMHMTlASL 400
Cdd:cd07141 375 DVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD---IDKAITFSNAlrAGTVWVNCYNVVS-PQA 450
|
330 340
....*....|....*....|...
gi 1169285 401 PFGGVGASGMGRYHGKFSFDTFS 423
Cdd:cd07141 451 PFGGYKMSGNGRELGEYGLQEYT 473
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
103-409 |
1.86e-42 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 157.40 E-value: 1.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVDQscfaVVLGGPQETGQ-L 176
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVleeagLPAGVVN----FVPGSGSEVGDyL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 177 LEH-RFDYIFFTGSPRVGKIVMTAAAK------HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVApdy 249
Cdd:PRK03137 246 VDHpKTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSA--- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 250 vlCS---------PEMQERLLpALQSTITrfYGDdPQSSPNLGRIINQKQFQRLRALL----GCGRVAIGGQSDESDRY- 315
Cdd:PRK03137 323 --CSraivhedvyDEVLEKVV-ELTKELT--VGN-PEDNAYMGPVINQASFDKIMSYIeigkEEGRLVLGGEGDDSKGYf 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 316 IAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHM 395
Cdd:PRK03137 397 IQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGA 476
|
330
....*....|....
gi 1169285 396 TLASLPFGGVGASG 409
Cdd:PRK03137 477 IVGYHPFGGFNMSG 490
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
38-422 |
3.85e-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: 153.06 E-value: 3.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 38 QENKQLLHDALAqDLHKSAfesEVSEVAISqgevtlaLRNLrawMKDERVPkNLATQLDSAFIRkEPFGLVLIIAPWNYP 117
Cdd:cd07085 86 LEHGKTLADARG-DVLRGL---EVVEFACS-------IPHL---LKGEYLE-NVARGIDTYSYR-QPLGVVAGITPFNFP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 118 LnltLVPL---VGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqscFAVVLGGPQETGQLLEH-RFDYIFFTG 188
Cdd:cd07085 150 A---MIPLwmfPMAIACGNTFVLKPSERVPGAAMRLAELlqeagLPDGV----LNVVHGGKEAVNALLDHpDIKAVSFVG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 189 SPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTI 268
Cdd:cd07085 223 STPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 269 TRF---YGDDPqsSPNLGRIINQKQFQRLRALLGCG-----RVAIGGQSDESDRY-----IAPTVLVDVQEMEPVMQEEI 335
Cdd:cd07085 303 KKLkvgAGDDP--GADMGPVISPAAKERIEGLIESGveegaKLVLDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEI 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 336 FGPILPIVNVQSLDEAIEFINRREkplalYA-----FSNSSQVVKRVLTQTsSGGFCG-NDGfMHMTLASLPFGGVGASG 409
Cdd:cd07085 381 FGPVLSIVRVDTLDEAIAIINANP-----YGngaaiFTRSGAAARKFQREV-DAGMVGiNVP-IPVPLAFFSFGGWKGSF 453
|
410
....*....|....*
gi 1169285 410 MGRYH--GKFSFDTF 422
Cdd:cd07085 454 FGDLHfyGKDGVRFY 468
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
12-416 |
4.57e-41 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 152.94 E-value: 4.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEvsevaisQGEVTLALRNLR---AWmkdervp 88
Cdd:cd07111 69 RTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESR-------DCDIPLVARHFYhhaGW------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 89 knlATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqscF 163
Cdd:cd07111 135 ---AQLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEIcaeagLPPGV----L 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 164 AVVLGGPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 242
Cdd:cd07111 208 NIVTGNGSFGSALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 243 TCVAPDYVLCSPEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLRALLGCGRvAIGGQSDESDR------- 314
Cdd:cd07111 288 VCCAGSRLLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADVFQPGAdlpskgp 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 315 YIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMH 394
Cdd:cd07111 367 FYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING--HN 444
|
410 420
....*....|....*....|..
gi 1169285 395 MTLASLPFGGVGASGMGRYHGK 416
Cdd:cd07111 445 LFDAAAGFGGYRESGFGREGGK 466
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
104-415 |
8.27e-41 |
|
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: 152.71 E-value: 8.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 104 PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQY-VDQSCFAVVLGGPQETGQ-LLEH-R 180
Cdd:TIGR01237 167 PTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAgLPKGVVQFVPGSGSEVGDyLVDHpK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 181 FDYIFFTGSPRVGKIVMTAAAK------HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA-PDYVLCS 253
Cdd:TIGR01237 247 TSLITFTGSREVGTRIFERAAKvqpgqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAgSRAVVHE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 254 P---EMQERLLPALQSTITRfYGDDPqsSPNLGRIINQKQFQRLRALLGCG----RVAIGGQSDESDRY-IAPTVLVDVQ 325
Cdd:TIGR01237 327 KvydEVVERFVEITESLKVG-PPDSA--DVYVGPVIDQKSFNKIMEYIEIGkaegRLVSGGCGDDSKGYfIGPTIFADVD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 326 EMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGV 405
Cdd:TIGR01237 404 RKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGF 483
|
330
....*....|
gi 1169285 406 GASGMGRYHG 415
Cdd:TIGR01237 484 KMSGTDSKAG 493
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
13-412 |
1.36e-40 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 150.86 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 13 EAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEvSEVA-------ISQGEVTlalRNLRAWMKDE 85
Cdd:cd07147 32 KAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDAR-GEVAraidtfrIAAEEAT---RIYGEVLPLD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 RVPKNLATQldsAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVL-PQYVDQSCFA 164
Cdd:cd07147 108 ISARGEGRQ---GLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaETGLPKGAFS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 165 VVLGGPQETGQLLEH-RFDYIFFTGSPRVG-KIVMTAAAKHltpVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQ 242
Cdd:cd07147 185 VLPCSRDDADLLVTDeRIKLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 243 TCVAPDYVLCS----PEMQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLR-----ALLGCGRVAIGGQSDESd 313
Cdd:cd07147 262 SCISVQRVLVHrsvyDEFKSRLVARVKALKT---GDPKDDATDVGPMISESEAERVEgwvneAVDAGAKLLTGGKRDGA- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 314 rYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGND--G 391
Cdd:cd07147 338 -LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDvpT 416
|
410 420
....*....|....*....|...
gi 1169285 392 FM--HMtlaslPFGGVGASGMGR 412
Cdd:cd07147 417 FRvdHM-----PYGGVKDSGIGR 434
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
102-424 |
1.37e-39 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 149.20 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 102 KEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQY-VDQSCFAVVLG-GPQETGQLLEH 179
Cdd:PLN02766 156 KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGfGPTAGAAIASH 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 180 R-FDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQ 257
Cdd:PLN02766 236 MdVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIY 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 258 ERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQS-DESDRYIAPTVLVDVQEMEPV 330
Cdd:PLN02766 316 DEFVKKLVEKAKDWVVGDPfDPRARQGPQVDKQQFEKILSYIEHGKregatLLTGGKPcGDKGYYIEPTIFTDVTEDMKI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 331 MQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTlaSLPFGGVGASGM 410
Cdd:PLN02766 396 AQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDP--DCPFGGYKMSGF 473
|
330
....*....|....
gi 1169285 411 GRYHGKFSFDTFSH 424
Cdd:PLN02766 474 GRDQGMDALDKYLQ 487
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
18-432 |
3.57e-38 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 144.90 E-value: 3.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 18 GRTRPAEfRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESevsevaiSQGEVTLALRNLRAWMKDERVPKNLATQLDS 97
Cdd:cd07116 55 GKTSVAE-RANILNKIADRMEANLEMLAVAETWDNGKPVRET-------LAADIPLAIDHFRYFAGCIRAQEGSISEIDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 98 ---AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGPQETG 174
Cdd:cd07116 127 ntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 175 QLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNP-CYVDD--NCDPQTVANRVAWFRYF--NAGQTCVAP 247
Cdd:cd07116 207 KPLasSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPnIFFADvmDADDAFFDKALEGFVMFalNQGEVCTCP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 248 DYVLCSPEMQERLLP-ALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGR-----VAIGGQ-----SDESDRYI 316
Cdd:cd07116 287 SRALIQESIYDRFMErALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKeegaeVLTGGErnelgGLLGGGYY 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 317 APTVLVDVQEMEpVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNdgFMHMT 396
Cdd:cd07116 367 VPTTFKGGNKMR-IFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLY 443
|
410 420 430
....*....|....*....|....*....|....*.
gi 1169285 397 LASLPFGGVGASGMGRYHGKFSFDTFSHHRaCLLRS 432
Cdd:cd07116 444 PAHAAFGGYKQSGIGRENHKMMLDHYQQTK-NLLVS 478
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
103-427 |
9.48e-38 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 144.57 E-value: 9.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISK----NVEKILAEV-LPQYVdqscFAVVLG-GPQETGQL 176
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPlsalYAAKLLHEAgLPPGV----LNVVSGfGPTAGAAL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 177 LEHR-FDYIFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSP 254
Cdd:PLN02466 270 ASHMdVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 255 EM-QERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQR-LR---------ALLGCGrvaiGGQSDESDRYIAPTVLVD 323
Cdd:PLN02466 350 RVyDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKiLRyiksgvesgATLECG----GDRFGSKGYYIQPTVFSN 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 324 VQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGN--DGFMhmtlASLP 401
Cdd:PLN02466 426 VQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFD----AAIP 501
|
330 340
....*....|....*....|....*.
gi 1169285 402 FGGVGASGMGRYHGKFSFDTFSHHRA 427
Cdd:PLN02466 502 FGGYKMSGIGREKGIYSLNNYLQVKA 527
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
98-423 |
1.59e-37 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 143.50 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 98 AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqscFAVVLGGPQE 172
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLakeagLPDGV----LNVVTGFGHE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 173 TGQLL--EHRFDYIFFTGSPRVGKIVMT-AAAKHLTPVTLELGGKNPCYVDDNC-DPQTVANRVAWFRYFNAGQTCVAPD 248
Cdd:PRK09847 227 AGQALsrHNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGT 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 249 YVLCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRLRALL----GCGRVAIGGQSDESDRYIAPTVLVD 323
Cdd:PRK09847 307 RLLLEESIADEFLALLKQQAQNWQPGHPlDPATTMGTLIDCAHADSVHSFIregeSKGQLLLDGRNAGLAAAIGPTIFVD 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 324 VQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGG-FCG--NDGFMhmtlaSL 400
Cdd:PRK09847 387 VDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSvFVNnyNDGDM-----TV 461
|
330 340
....*....|....*....|...
gi 1169285 401 PFGGVGASGMGRYHGKFSFDTFS 423
Cdd:PRK09847 462 PFGGYKQSGNGRDKSLHALEKFT 484
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
13-422 |
2.55e-37 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 142.74 E-value: 2.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 13 EAFHAGRTRPAEFRAAQLQGLGRFLQENKQllhdalaqDLHKSAFESEVSEVAISQGEVTLALRNLRaWMKDE--RVPKN 90
Cdd:PRK11241 59 RALPAWRALTAKERANILRRWFNLMMEHQD--------DLARLMTLEQGKPLAEAKGEISYAASFIE-WFAEEgkRIYGD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 91 L--ATQLDSAFIR-KEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQY-VDQSCFAVV 166
Cdd:PRK11241 130 TipGHQADKRLIViKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 167 LGGPQETGQLLEHR--FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTC 244
Cdd:PRK11241 210 TGSAGAVGGELTSNplVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTC 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 245 VAPDYVLCSPEMQERLLPALQSTITRFY-GDDPQSSPNLGRIINQKQFQRLR-----ALLGCGRVAIGGQSDE-SDRYIA 317
Cdd:PRK11241 290 VCANRLYVQDGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 318 PTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTL 397
Cdd:PRK11241 370 PTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV 449
|
410 420
....*....|....*....|....*
gi 1169285 398 AslPFGGVGASGMGRYHGKFSFDTF 422
Cdd:PRK11241 450 A--PFGGIKASGLGREGSKYGIEDY 472
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
96-423 |
6.05e-36 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 138.86 E-value: 6.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 96 DSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVdqscFAVVlGGP 170
Cdd:PRK13252 134 SFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIyteagLPDGV----FNVV-QGD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 171 QETGQLL-EH-RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQT------VANrvawfrYFNAGQ 242
Cdd:PRK13252 209 GRVGAWLtEHpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRaadiamLAN------FYSSGQ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 243 TCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQS-SPNLGRIINQKQFQRLR----------ALLGCGRVAIGGQSDE 311
Cdd:PRK13252 283 VCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDpATNFGPLVSFAHRDKVLgyiekgkaegARLLCGGERLTEGGFA 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 312 SDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSgGFC---- 387
Cdd:PRK13252 363 NGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEA-GICwint 441
|
330 340 350
....*....|....*....|....*....|....*..
gi 1169285 388 -GNdgfmhmTLASLPFGGVGASGMGRYHGKFSFDTFS 423
Cdd:PRK13252 442 wGE------SPAEMPVGGYKQSGIGRENGIATLEHYT 472
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
12-409 |
1.38e-32 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 129.31 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEvSEVAISQGEVTLALR--NLRAWMKDERVPK 89
Cdd:PRK09457 47 RAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAA-TEVTAMINKIAISIQayHERTGEKRSEMAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 90 NlatqldSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEV-----LPQYVDQscfa 164
Cdd:PRK09457 126 G------AAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLwqqagLPAGVLN---- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 165 VVLGGPqETGQ-LLEHR-FDYIFFTGSPRVGKIVMTAAAKHltP---VTLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 239
Cdd:PRK09457 196 LVQGGR-ETGKaLAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFIS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 240 AGQTCVAPDYVLCSPEMQ-ERLLPALQSTITRF----YGDDPQssPNLGRIINQKQFQRL----RALLGCGRVAI--GGQ 308
Cdd:PRK09457 273 AGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLtvgrWDAEPQ--PFMGAVISEQAAQGLvaaqAQLLALGGKSLleMTQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 309 SDESDRYIAPTvLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCG 388
Cdd:PRK09457 351 LQAGTGLLTPG-IIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNW 429
|
410 420
....*....|....*....|...
gi 1169285 389 NDgfmHMTLAS--LPFGGVGASG 409
Cdd:PRK09457 430 NK---PLTGASsaAPFGGVGASG 449
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
99-412 |
4.03e-29 |
|
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: 119.52 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 99 FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS-----KNVEKILAEVLPQYVdqscFAVVLGGPQET 173
Cdd:cd07140 142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTpltalKFAELTVKAGFPKGV----INILPGSGSLV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 174 GQLLEHRFDY--IFFTGSPRVGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYV 250
Cdd:cd07140 218 GQRLSDHPDVrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 251 LCSPEMQERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRL-----RALLGCGRVAIGG-QSDESDRYIAPTVLVD 323
Cdd:cd07140 298 FVEESIHDEFVRRVVEEVKKMKIGDPlDRSTDHGPQNHKAHLDKLveyceRGVKEGATLVYGGkQVDRPGFFFEPTVFTD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 324 VQEMEPVMQEEIFGPILPIVNVQS--LDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDgfMHMTLASLP 401
Cdd:cd07140 378 VEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNT--YNKTDVAAP 455
|
330
....*....|.
gi 1169285 402 FGGVGASGMGR 412
Cdd:cd07140 456 FGGFKQSGFGK 466
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
22-411 |
2.18e-28 |
|
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: 116.75 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 22 PAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVsEVAISQGEVTLALRNLRAwMKDERVPKNLaTQLDS---A 98
Cdd:cd07148 42 PAHERIAILERLADLMEERADELALLIAREGGKPLVDAKV-EVTRAIDGVELAADELGQ-LGGREIPMGL-TPASAgriA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 99 FIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEIS----KNVEKILAEV-LPQyvdQSCFAVVLGGPQET 173
Cdd:cd07148 119 FTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATplscLAFVDLLHEAgLPE---GWCQAVPCENAVAE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 174 GQLLEHRFDYIFFTGSPRVGKIVMTAAAKHlTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCS 253
Cdd:cd07148 196 KLVTDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 254 PEMQERLLPALQSTITRF-YGDDPQSSPNLGRIINQKQFQRLR-----ALLGCGRVAIGGQSdESDRYIAPTVLVDVQEM 327
Cdd:cd07148 275 AEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVEewvneAVAAGARLLCGGKR-LSDTTYAPTVLLDPPRD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 328 EPVMQEEIFGPILPIVNVQSLDEAIEFINrrEKPLALYA--FSNSSQVVKRVLTQTSSGGFCGNDgfmHMTLAS--LPFG 403
Cdd:cd07148 354 AKVSTQEIFGPVVCVYSYDDLDEAIAQAN--SLPVAFQAavFTKDLDVALKAVRRLDATAVMVND---HTAFRVdwMPFA 428
|
....*...
gi 1169285 404 GVGASGMG 411
Cdd:cd07148 429 GRRQSGYG 436
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
8-411 |
3.40e-28 |
|
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: 116.91 E-value: 3.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 8 LRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFE--SEVSEvAISqgevtlALR----NLRAW 81
Cdd:cd07125 75 LAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADadAEVRE-AID------FCRyyaaQAREL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 82 MKDERVPKNLAtQLDsaFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKNVEKILAEV-LPQ 156
Cdd:cd07125 148 FSDPELPGPTG-ELN--GLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEqtplIAARAVELLHEAgVPR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 157 YVDQscfaVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKH---LTPVTLELGGKNPCYVDDNCDP-QTVAN 230
Cdd:cd07125 225 DVLQ----LVPGDGEEIGEaLVAHpRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPeQAVKD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 231 RVA-WFRyfNAGQTCVAPDyVLC-----SPEMQERLLPALQSTITrfygDDPQ-SSPNLGRIINQKQFQRLRALL----G 299
Cdd:cd07125 301 VVQsAFG--SAGQRCSALR-LLYlqeeiAERFIEMLKGAMASLKV----GDPWdLSTDVGPLIDKPAGKLLRAHTelmrG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 300 CGRVAIGGQSDESD-RYIAPTVLVDVQemEPVMQEEIFGPILPIV--NVQSLDEAIEFINRREKPLALYAFSNSSQVVKR 376
Cdd:cd07125 374 EAWLIAPAPLDDGNgYFVAPGIIEIVG--IFDLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEY 451
|
410 420 430
....*....|....*....|....*....|....*...
gi 1169285 377 VLTQTSSGGFCGNDGfmhMTLA---SLPFGGVGASGMG 411
Cdd:cd07125 452 WRERVEAGNLYINRN---ITGAivgRQPFGGWGLSGTG 486
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
2-422 |
3.96e-26 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 110.34 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 2 DPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEvSEVAISQgevtlalrNLRAW 81
Cdd:PRK13968 29 DDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVAKSA--------NLCDW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 82 MKdERVPKNLATQL-----DSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQ 156
Cdd:PRK13968 100 YA-EHGPAMLKAEPtlvenQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 157 Y-VDQSCFAVVLGGPQETGQLL-EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAW 234
Cdd:PRK13968 179 AgIPQGVYGWLNADNDGVSQMInDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 235 FRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPN-LGRI----INQKQFQRLRALLGCG-RVAIGGQ 308
Cdd:PRK13968 259 GRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENaLGPMarfdLRDELHHQVEATLAEGaRLLLGGE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 309 SDESD-RYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG--- 384
Cdd:PRK13968 339 KIAGAgNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGgvf 418
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1169285 385 --GFCGNDgfmhmtlASLPFGGVGASGMGRYHGKFSFDTF 422
Cdd:PRK13968 419 inGYCASD-------ARVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
6-356 |
1.91e-25 |
|
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: 108.45 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 6 DTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFES--EVSE-VAISQGEVTLAlRNLR-AW 81
Cdd:cd07130 38 STIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGlgEVQEmIDICDFAVGLS-RQLYgLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 82 MKDERVPKNLATQLDsafirkePFGLVLIIAPWNYPL-----NLTLvplvgALAAGNCVVLKPSE----ISKNVEKILAE 152
Cdd:cd07130 117 IPSERPGHRMMEQWN-------PLGVVGVITAFNFPVavwgwNAAI-----ALVCGNVVVWKPSPttplTAIAVTKIVAR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 153 VLPQY-VDQSCFAVVLGGpQETGQLLEH--RFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVA 229
Cdd:cd07130 185 VLEKNgLPGAIASLVCGG-ADVGEALVKdpRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 230 NRVAWFRYFNAGQTCVAPDYVLcspeMQERLLPALQSTITRFYGD----DPQSSPNL-GRIINQKQFQRLRALL------ 298
Cdd:cd07130 264 RAVLFAAVGTAGQRCTTTRRLI----VHESIYDEVLERLKKAYKQvrigDPLDDGTLvGPLHTKAAVDNYLAAIeeaksq 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1169285 299 GcGRVAIGGQS-DESDRYIAPTVlVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFIN 356
Cdd:cd07130 340 G-GTVLFGGKViDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDTLEEAIAWNN 396
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
2-412 |
1.26e-23 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 102.89 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 2 DPLGD-----TLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSafesevseVAISQGEVTLALR 76
Cdd:PRK09406 18 TALTDdevdaAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT--------LASAKAEALKCAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 77 NLRAWMkdERVPKNLATQLDS--------AFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEiskNVEK 148
Cdd:PRK09406 90 GFRYYA--EHAEALLADEPADaaavgasrAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS---NVPQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 149 I---LAEVLPQY-VDQSCFAVVL-GGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNC 223
Cdd:PRK09406 165 TalyLADLFRRAgFPDGCFQTLLvGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 224 DPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQE---RLLPALQSTITrfYGD--DPQS-----SPNLGRIINQKQFQr 293
Cdd:PRK09406 245 DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDafaEKFVARMAALR--VGDptDPDTdvgplATEQGRDEVEKQVD- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 294 lRALLGCGRVAIGGQS-DESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQ 372
Cdd:PRK09406 322 -DAVAAGATILCGGKRpDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1169285 373 VVKRVLTQTSSGGFCGNDgfMHMTLASLPFGGVGASGMGR 412
Cdd:PRK09406 401 EQERFIDDLEAGQVFING--MTVSYPELPFGGVKRSGYGR 438
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
103-411 |
9.87e-23 |
|
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: 100.76 E-value: 9.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 103 EPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQY-VDQSCFAVVLGGPQETGQLL--EH 179
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRGADVGAALtsDP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 180 RFDYIFFTGSPRVGKIVMTAAAKHL---TPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEM 256
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 257 QERLLPALQSTITRFYGDDP-QSSPNLGRIINQKQFQRL----RALLGCGR-----VAIGGQSDESDRYIAPTV--LVDV 324
Cdd:TIGR01238 319 ADRVLTMIQGAMQELKVGVPhLLTTDVGPVIDAEAKQNLlahiEHMSQTQKkiaqlTLDDSRACQHGTFVAPTLfeLDDI 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 325 QEmepvMQEEIFGPILPIV--NVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPF 402
Cdd:TIGR01238 399 AE----LSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPF 474
|
....*....
gi 1169285 403 GGVGASGMG 411
Cdd:TIGR01238 475 GGQGLSGTG 483
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
91-428 |
5.37e-22 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 98.75 E-value: 5.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 91 LATQLDSAFIRKE-----------PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLK--PSE--ISKNVEKILAEVLP 155
Cdd:PLN02315 130 LSRQLNGSIIPSErpnhmmmevwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKgaPTTplITIAMTKLVAEVLE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 156 QY-VDQSCFAVVLGGpQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRV 232
Cdd:PLN02315 210 KNnLPGAIFTSFCGG-AEIGEAIakDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSV 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 233 AWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDP-------------QSSPNLGRIINQKQFQrlrallg 299
Cdd:PLN02315 289 LFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPlekgtllgplhtpESKKNFEKGIEIIKSQ------- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 300 CGRVAIGGQSDESD-RYIAPTVlVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVL 378
Cdd:PLN02315 362 GGKILTGGSAIESEgNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWI 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1169285 379 TQTSSGgfCGndgfmhMTLASLP---------FGGVGASGMGRYHGKFSFDTFSHHRAC 428
Cdd:PLN02315 441 GPLGSD--CG------IVNVNIPtngaeiggaFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
26-411 |
2.61e-20 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 93.28 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 26 RAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESeVSEVAISQGEVTLA----LRNLR--AWMKDERVPKNLATQLdsAF 99
Cdd:PLN00412 77 RAELLHKAAAILKEHKAPIAECLVKEIAKPAKDA-VTEVVRSGDLISYTaeegVRILGegKFLVSDSFPGNERNKY--CL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 100 IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPseisknveKILAEVLPQYVDQsCF----------AVVLGG 169
Cdd:PLN00412 154 TSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKP--------PTQGAVAALHMVH-CFhlagfpkgliSCVTGK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 170 PQETGQLL-EHR-FDYIFFTGsprvGKIVMTAAAK-HLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVA 246
Cdd:PLN00412 225 GSEIGDFLtMHPgVNCISFTG----GDTGIAISKKaGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 247 PDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSDESDR---YIAPTVLVD 323
Cdd:PLN00412 301 VKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKRegnLIWPLLLDN 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 324 VQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNS-------SQVVKRVLTQTSSGGFCGNDGFmhmt 396
Cdd:PLN00412 381 VRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDinkailiSDAMETGTVQINSAPARGPDHF---- 456
|
410
....*....|....*
gi 1169285 397 laslPFGGVGASGMG 411
Cdd:PLN00412 457 ----PFQGLKDSGIG 467
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
11-415 |
4.56e-20 |
|
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: 92.30 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 11 LREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFES---EVSEVAISQGEVTLALRNLRAW---MKD 84
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTgkgWMFAENICGDQVQLRARAFVIYsyrIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 85 ERV-PKNLATQLDSAFIRKePFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQ--YVDQS 161
Cdd:cd07084 81 EPGnHLGQGLKQQSHGYRW-PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 162 CFAVVLGGPQETGQLLEH-RFDYIFFTGSPRVGKIVMTAAakHLTPVTLELGGKNPCYVDDNCDP-QTVANRVAWFRYFN 239
Cdd:cd07084 160 DVTLINGDGKTMQALLLHpNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMTAC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 240 AGQTCVAPD--YVLCSPEMQeRLLPALQSTITRfygddpqSSPN---LGRIIN---QKQFQRLRALLgcGRVAIGGQSDE 311
Cdd:cd07084 238 SGQKCTAQSmlFVPENWSKT-PLVEKLKALLAR-------RKLEdllLGPVQTfttLAMIAHMENLL--GSVLLFSGKEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 312 SDRYI--------APTVLVDVQE---MEPVMQEEIFGPILPIVNVQSLDEA--IEFINRREKPLALYAFSNSSQVVKRVL 378
Cdd:cd07084 308 KNHSIpsiygacvASALFVPIDEilkTYELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELI 387
|
410 420 430
....*....|....*....|....*....|....*..
gi 1169285 379 TQTSSGGfcgndgfmhMTLASLPFGGVGASGMgrYHG 415
Cdd:cd07084 388 GNLWVAG---------RTYAILRGRTGVAPNQ--NHG 413
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
12-424 |
1.29e-18 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 88.65 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 12 REAFHAGRTRPAEFRAAQLQGLGRFLQENKQLL-------HDALAQDLHKSAFES-EVSEVAIsqGEVTLALrnlrawmk 83
Cdd:PLN02419 161 KQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLamnitteQGKTLKDSHGDIFRGlEVVEHAC--GMATLQM-------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 84 DERVPkNLATQLDSAFIRkEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCF 163
Cdd:PLN02419 231 GEYLP-NVSNGVDTYSIR-EPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGV 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 164 AVVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAG 241
Cdd:PLN02419 309 LNIVHGTNDTVNAIcdDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAG 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 242 QTCVAPDYVLC---SPEMQERLL---PALQSTItrfyGDDPQSspNLGRIINQKQFQRLRALLGCG-----RVAIGGQS- 309
Cdd:PLN02419 389 QRCMALSTVVFvgdAKSWEDKLVeraKALKVTC----GSEPDA--DLGPVISKQAKERICRLIQSGvddgaKLLLDGRDi 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 310 ----DESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGG 385
Cdd:PLN02419 463 vvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQ 542
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1169285 386 FcGNDGFMHMTLASLPFGGVGASGMG--RYHGKFSFDTFSH 424
Cdd:PLN02419 543 I-GINVPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQ 582
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
104-411 |
2.36e-17 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 85.41 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 104 PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKNVEKILAEV-LPQYVDQscfavVLGGPQET-GQLL 177
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEqtplIAAQAVRILLEAgVPAGVVQ-----LLPGRGETvGAAL 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 178 --EHRFDYIFFTGSPRVGKIVMTAAAKHL------TPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDy 249
Cdd:PRK11809 843 vaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALR- 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 250 VLCSPE-MQERLLPALQSTITRF-YGDDPQSSPNLGRIIN-------QKQFQRLRAllgCGRV---AIGGQSDESDR--Y 315
Cdd:PRK11809 922 VLCLQDdVADRTLKMLRGAMAECrMGNPDRLSTDIGPVIDaeakaniERHIQAMRA---KGRPvfqAARENSEDWQSgtF 998
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 316 IAPTV--LVDVQEmepvMQEEIFGPILPIV--NVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDG 391
Cdd:PRK11809 999 VPPTLieLDSFDE----LKREVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRN 1074
|
330 340
....*....|....*....|
gi 1169285 392 FMHMTLASLPFGGVGASGMG 411
Cdd:PRK11809 1075 MVGAVVGVQPFGGEGLSGTG 1094
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
106-409 |
6.56e-17 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 83.02 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 106 GLVLIIAPWNYP---LNLTLVPlvgALAaGNCVVLKPSE--ISKN--VEKILAEV-LPQYVDQscFavVLGGPQETGQ-L 176
Cdd:cd07123 172 GFVYAVSPFNFTaigGNLAGAP---ALM-GNVVLWKPSDtaVLSNylVYKILEEAgLPPGVIN--F--VPGDGPVVGDtV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 177 LEHR-FDYIFFTGSPRVGKIVMTAAAKHLT-----P-VTLELGGKNPCYVDDNCDPQTVAN---RVAwFRYfnAGQTCVA 246
Cdd:cd07123 244 LASPhLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTatvRGA-FEY--QGQKCSA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 247 PD--YVLCS--PEMQERLLPALqSTITrfYGDDPQSSPNLGRIINQKQFQRLRALLGCGR------VAIGGQSDESDRY- 315
Cdd:cd07123 321 ASraYVPESlwPEVKERLLEEL-KEIK--MGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKsdpeaeIIAGGKCDDSVGYf 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 316 IAPTVLVDVQEMEPVMQEEIFGPILpivNVQSLDEAiEFinrrEKPLAL------YA-----FSNSSQVVKRVLT--QTS 382
Cdd:cd07123 398 VEPTVIETTDPKHKLMTEEIFGPVL---TVYVYPDS-DF----EETLELvdttspYAltgaiFAQDRKAIREATDalRNA 469
|
330 340
....*....|....*....|....*..
gi 1169285 383 SGGFCGNDGFMHMTLASLPFGGVGASG 409
Cdd:cd07123 470 AGNFYINDKPTGAVVGQQPFGGARASG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
8-357 |
9.71e-16 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 80.24 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 8 LRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENK------------QLLHDALAqdlhksafesEVSEvAI-------SQ 68
Cdd:PRK11904 591 LAAARAAFPAWSRTPVEERAAILERAADLLEANRaelialcvreagKTLQDAIA----------EVRE-AVdfcryyaAQ 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 69 GEVTLAlrnlrawmKDERVP-----KNlatqldsaFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE-- 141
Cdd:PRK11904 660 ARRLFG--------APEKLPgptgeSN--------ELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEqt 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 142 --ISKNVEKILAEV-LPQYVdqscFAVVLGGPQETGQ-LLEH-RFDYIFFTGSPRVGKIV-MTAAAKHLTPVTL--ELGG 213
Cdd:PRK11904 724 plIAAEAVKLLHEAgIPKDV----LQLLPGDGATVGAaLTADpRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGG 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 214 KNPCYVDDNCDPQTVANRV---AwFRyfNAGQTCVAPDyVLCSPE-MQERLLPALQSTITRFYGDDPQS-SPNLGRIINQ 288
Cdd:PRK11904 800 QNAMIVDSTALPEQVVDDVvtsA-FR--SAGQRCSALR-VLFVQEdIADRVIEMLKGAMAELKVGDPRLlSTDVGPVIDA 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 289 KQFQRLRA----------LLgcGRVAIGGQSDESDrYIAPTvLVDVQEMEpVMQEEIFGPILPIV--NVQSLDEAIEFIN 356
Cdd:PRK11904 876 EAKANLDAhiermkrearLL--AQLPLPAGTENGH-FVAPT-AFEIDSIS-QLEREVFGPILHVIryKASDLDKVIDAIN 950
|
.
gi 1169285 357 R 357
Cdd:PRK11904 951 A 951
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
8-356 |
6.66e-14 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 74.52 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 8 LRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFEsevsevAIsqGEVTLALRNLR--AwmkdE 85
Cdd:PRK11905 596 LAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLAN------AI--AEVREAVDFLRyyA----A 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 86 RVPKNLATQldsafiRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKNVEKILAEV-LPQYVDQ 160
Cdd:PRK11905 664 QARRLLNGP------GHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEqtplIAARAVRLLHEAgVPKDALQ 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 161 scfaVVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIVMTAAAKHLT-PVTL--ELGGKNPCYVDDNCDP-QTVANRVA- 233
Cdd:PRK11905 738 ----LLPGDGRTVGAALvaDPRIAGVMFTGSTEVARLIQRTLAKRSGpPVPLiaETGGQNAMIVDSSALPeQVVADVIAs 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 234 WFRyfNAGQTCVAPDyVLC-----SPEMQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQRLRA------LLGCG- 301
Cdd:PRK11905 814 AFD--SAGQRCSALR-VLClqedvADRVLTMLKGAMDELRI---GDPWRLSTDVGPVIDAEAQANIEAhieamrAAGRLv 887
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 302 -RVAIGGQSDESdRYIAPTVLvdvqEME--PVMQEEIFGPILPIVNVQS--LDEAIEFIN 356
Cdd:PRK11905 888 hQLPLPAETEKG-TFVAPTLI----EIDsiSDLEREVFGPVLHVVRFKAdeLDRVIDDIN 942
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
104-359 |
7.15e-13 |
|
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: 70.26 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 104 PFGLVLIIAPWNYPLNLTLVplvG-----ALAAGNCVVLKP-------SEI-SKNVEKILAEV-LPQYVdqscFAVVLGG 169
Cdd:cd07129 105 PLGPVAVFGASNFPLAFSVA---GgdtasALAAGCPVVVKAhpahpgtSELvARAIRAALRATgLPAGV----FSLLQGG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 170 PQETGQ-LLEH-RFDYIFFTGSPRVGKIVMTAAAKHLT--PVTLELGGKNPCYVDdncdPQTVANR--------VAWFRy 237
Cdd:cd07129 178 GREVGVaLVKHpAIKAVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFIL----PGALAERgeaiaqgfVGSLT- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 238 FNAGQTCVAPDYVLC--SPEmQERLLPALQSTITRFygdDPQS--SPNLGRIInQKQFQRLRALLGcGRVAIGGQSDESD 313
Cdd:cd07129 253 LGAGQFCTNPGLVLVpaGPA-GDAFIAALAEALAAA---PAQTmlTPGIAEAY-RQGVEALAAAPG-VRVLAGGAAAEGG 326
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1169285 314 RYIAPTVL-VDVQEM--EPVMQEEIFGPILPIVNVQSLDEAIEFINRRE 359
Cdd:cd07129 327 NQAAPTLFkVDAAAFlaDPALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
80-377 |
1.11e-12 |
|
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: 69.81 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 80 AWMKDERVP----------KNLATQLDSAFiRKEPFGLVLIIA-----PWN-YPlnltlvPLVGALAAGNCVVLKPSEIS 143
Cdd:cd07127 160 AWREMSRIPptaewekpqgKHDPLAMEKTF-TVVPRGVALVIGcstfpTWNgYP------GLFASLATGNPVIVKPHPAA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 144 ----KNVEKILAEVLPQY-VDQSCFAVVLGGPQE--TGQLLEH-RFDYIFFTGSPRVGKIVMTAAAKHLtpVTLELGGKN 215
Cdd:cd07127 233 ilplAITVQVAREVLAEAgFDPNLVTLAADTPEEpiAQTLATRpEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVN 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 216 PCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPE----MQERLLP-----ALQSTITRFYGDDPQSSPNLGRII 286
Cdd:cd07127 311 TVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgiqtDDGRKSFdevaaDLAAAIDGLLADPARAAALLGAIQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 287 NQKQFQRLRALLGCGRVAIGGQSDESDRYI-----APTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINR--RE 359
Cdd:cd07127 391 SPDTLARIAEARQLGEVLLASEAVAHPEFPdarvrTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvRE 470
|
330
....*....|....*....
gi 1169285 360 K-PLALYAFSNSSQVVKRV 377
Cdd:cd07127 471 HgAMTVGVYSTDPEVVERV 489
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
90-356 |
3.51e-11 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 65.73 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 90 NLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSE----ISKNVEKILAEV-LPQYVDQscfa 164
Cdd:COG4230 666 AQARRLFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEqtplIAARAVRLLHEAgVPADVLQ---- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 165 VVLGGPQETGQLL--EHRFDYIFFTGSPRVGKIV-MTAAAKHLTPVTL--ELGGKNPCYVDDNCDPQTVANRV---AwFR 236
Cdd:COG4230 742 LLPGDGETVGAALvaDPRIAGVAFTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIVDSSALPEQVVDDVlasA-FD 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 237 yfNAGQTCVAPDyVLCSPE-------------MQERLL--PALQSTitrfygDdpqsspnLGRIINQKQFQRLRA----L 297
Cdd:COG4230 821 --SAGQRCSALR-VLCVQEdiadrvlemlkgaMAELRVgdPADLST------D-------VGPVIDAEARANLEAhierM 884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1169285 298 LGCGR-VAIGGQSDESDR--YIAPTvLVDVQEMEpVMQEEIFGPILPIV--NVQSLDEAIEFIN 356
Cdd:COG4230 885 RAEGRlVHQLPLPEECANgtFVAPT-LIEIDSIS-DLEREVFGPVLHVVryKADELDKVIDAIN 946
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
5-383 |
3.43e-08 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 55.74 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 5 GDTLRRLreAFHAgrtrpaefRAAQLQGLGRFLQENKQLLHDaLAqdLHKSAFESEvSEVAISQGEVTLAL-----RNLr 79
Cdd:cd07128 50 GPALRAL--TFHE--------RAAMLKALAKYLMERKEDLYA-LS--AATGATRRD-SWIDIDGGIGTLFAyaslgRRE- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 80 awMKDERV-PKNLATQL--DSAFIRKEPF----GLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKP----SEISKNVEK 148
Cdd:cd07128 115 --LPNAHFlVEGDVEPLskDGTFVGQHILtprrGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPatatAYLTEAVVK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 149 ILAE--VLPQyvdqSCFAVVLGGpqeTGQLLEH--RFDYIFFTGSPRVGKIVMT--AAAKHLTPVTLELGGKNPCYVDDN 222
Cdd:cd07128 193 DIVEsgLLPE----GALQLICGS---VGDLLDHlgEQDVVAFTGSAATAAKLRAhpNIVARSIRFNAEADSLNAAILGPD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 223 CDPQT-----VANRVAWFRYFNAGQTCVAPDYVLCsPE-----MQERLLPALQSTITrfyGDDPQSSPNLGRIINQKQFQ 292
Cdd:cd07128 266 ATPGTpefdlFVKEVAREMTVKAGQKCTAIRRAFV-PEarvdaVIEALKARLAKVVV---GDPRLEGVRMGPLVSREQRE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 293 RLRA----LLGCGRVAIGGQSDESDR--------YIAPTVLVDVQEMEP--VMQEEIFGPILPIVNVQSLDEAIEFINRR 358
Cdd:cd07128 342 DVRAavatLLAEAEVVFGGPDRFEVVgadaekgaFFPPTLLLCDDPDAAtaVHDVEAFGPVATLMPYDSLAEAIELAARG 421
|
410 420
....*....|....*....|....*
gi 1169285 359 EKPLALYAFSNSSQVVKRVLTQTSS 383
Cdd:cd07128 422 RGSLVASVVTNDPAFARELVLGAAP 446
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
69-384 |
4.16e-08 |
|
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: 55.58 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 69 GEVTLALRNLRAWMKDE--------RVPKNLATQLDSAFirKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLK-P 139
Cdd:cd07126 101 GEVVVTRKFLENFAGDQvrflarsfNVPGDHQGQQSSGY--RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKvD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 140 SEISKNVEK-----ILAEVLPQYVDqscfAVVLGGPQETGQLLEHRFDYIFFTGSPRV---------GKIVMTAAA---K 202
Cdd:cd07126 179 SKVSVVMEQflrllHLCGMPATDVD----LIHSDGPTMNKILLEANPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 203 HLTPVTLELGgknpcYVDDNCDPQTvanrvawfrYFNAGQTCVAPDyVLCSPE--MQERLLPALQSTITRFYGDDPQSSP 280
Cdd:cd07126 255 ILGPDVSDVD-----YVAWQCDQDA---------YACSGQKCSAQS-ILFAHEnwVQAGILDKLKALAEQRKLEDLTIGP 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 281 NLG----RIINqkQFQRLRALLGcGRVAIGGQS----DESDRY--IAPT-VLVDVQEME-----PVMQEEIFGP--ILPI 342
Cdd:cd07126 320 VLTwtteRILD--HVDKLLAIPG-AKVLFGGKPltnhSIPSIYgaYEPTaVFVPLEEIAieenfELVTTEVFGPfqVVTE 396
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1169285 343 VNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSG 384
Cdd:cd07126 397 YKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNG 438
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
26-394 |
2.68e-07 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 52.65 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 26 RAAQlQGLGRFLQENKQLLHDALAQDLHKSAFEseVSEVAISQ---GEVT-------LALRNLRAWMKDERVPKNLATql 95
Cdd:cd07081 9 KVAQ-QGLSCKSQEMVDLIFRAAAEAAEDARID--LAKLAVSEtgmGRVEdkviknhFAAEYIYNVYKDEKTCGVLTG-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 96 DSAF---IRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYvdqscfAVVLGGPQ- 171
Cdd:cd07081 84 DENGgtlIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQA------AVAAGAPEn 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 172 ----------ETGQLLEHR--FDYIFFTGSPRVGKivmtAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFN 239
Cdd:cd07081 158 ligwidnpsiELAQRLMKFpgIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 240 AGqtcvapdyVLCSPEMQERLLPALQSTITRFYGDDPqsspnlGRIINQKQFQRLRALL---GCGRVAIGGQSDESdryI 316
Cdd:cd07081 234 NG--------VICASEQSVIVVDSVYDEVMRLFEGQG------AYKLTAEELQQVQPVIlknGDVNRDIVGQDAYK---I 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1169285 317 APTVLVDVQEMEPVMqeeifgpilpIVNVQSLDEAIEFINRREKP-LALYAFSNSSQVVKRVLTQTSSGGfCGNDGFMH 394
Cdd:cd07081 297 AAAAGLKVPQETRIL----------IGEVTSLAEHEPFAHEKLSPvLAMYRAANFADADAKALALKLEGG-CGHTSAMY 364
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
104-353 |
2.20e-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: 46.46 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 104 PFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSC----FAVVLGGP--QETGQLL 177
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAGgpdnLVVTVEEPtiETTNELM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 178 EHR-FDYIFFTGSPRVGKIVMTAAAKhltpvTLELGGKNP-CYVDDNCDPQTVANRVAWFRYFNAGQTC----------- 244
Cdd:cd07121 177 AHPdINLLVVTGGPAVVKAALSSGKK-----AIGAGAGNPpVVVDETADIEKAARDIVQGASFDNNLPCiaekeviavds 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 245 VAPD----------YVLCSPEMQERLLPALQstitrfygDDPQSSPNlgriinqKQF--QRLRALLGcgrvAIGGQSDES 312
Cdd:cd07121 252 VADYliaamqrngaYVLNDEQAEQLLEVVLL--------TNKGATPN-------KKWvgKDASKILK----AAGIEVPAD 312
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1169285 313 DRYIaptvLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIE 353
Cdd:cd07121 313 IRLI----IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
23-232 |
6.50e-05 |
|
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: 44.91 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 23 AEFRAAQlQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWM-------------------K 83
Cdd:cd07077 1 ESAKNAQ-RTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMgcsesklyknidtergitaS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 84 DERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGaLAAGNCVVLKPSEISKNVEKILAEVLPQyvdqscf 163
Cdd:cd07077 80 VGHIQDVLLPDNGETYVRAFPIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALALLFQA------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169285 164 AVVLGGPQETGQLLEHR-------------FDYIFFTGSPRVGKivmtAAAKH--LTPVTLELGGKNPCYVDDNCDPQTV 228
Cdd:cd07077 152 ADAAHGPKILVLYVPHPsdelaeellshpkIDLIVATGGRDAVD----AAVKHspHIPVIGFGAGNSPVVVDETADEERA 227
|
....
gi 1169285 229 ANRV 232
Cdd:cd07077 228 SGSV 231
|
|
| |
