|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
5-444 |
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: 796.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 5 VLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPA 84
Cdd:cd07132 4 VRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 85 KKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVN 164
Cdd:cd07132 84 KKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 165 GGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAP 244
Cdd:cd07132 164 GGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 245 DYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLKGQKIAFGGEMDEATRYLAPTILTDVDPN 324
Cdd:cd07132 244 DYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 325 SKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGA 404
Cdd:cd07132 324 DPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGN 403
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 568971250 405 SGMGAYHGKYSFDTFSHQRPCLLKGLKGESVNKLRYPPNS 444
Cdd:cd07132 404 SGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
5-426 |
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: 695.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 5 VLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPA 84
Cdd:cd07087 4 VARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 85 KKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVN 164
Cdd:cd07087 84 SVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 165 GGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAP 244
Cdd:cd07087 164 GGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 245 DYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLKGQKIAFGGEMDEATRYLAPTILTDVDPN 324
Cdd:cd07087 244 DYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSPD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 325 SKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGA 404
Cdd:cd07087 324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGN 403
|
410 420
....*....|....*....|..
gi 568971250 405 SGMGAYHGKYSFDTFSHQRPCL 426
Cdd:cd07087 404 SGMGAYHGKAGFDTFSHLKSVL 425
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
5-469 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 637.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 5 VLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPA 84
Cdd:PTZ00381 13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 85 KKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVN 164
Cdd:PTZ00381 93 DTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 165 GGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAP 244
Cdd:PTZ00381 173 GGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 245 DYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLK--GQKIAFGGEMDEATRYLAPTILTDVD 322
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDIENKYVAPTIIVNPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 323 PNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGV 402
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568971250 403 GASGMGAYHGKYSFDTFSHQRPCLLKGLKGESVNKLRYPPNSESKVSWAKFFL-LKQFNKGRLGMLLF 469
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSWVLSFLLkLSIPVQSEVLKSRL 480
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
2-447 |
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: 628.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASA 81
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 82 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYA 161
Cdd:cd07136 81 KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 162 IVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTC 241
Cdd:cd07136 161 VVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 242 IAPDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLKGQKIAFGGEMDEATRYLAPTILTDV 321
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 322 DPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGG 401
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 568971250 402 VGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESvnKLRYPPNSESK 447
Cdd:cd07136 401 VGNSGMGSYHGKYSFDTFSHKKSILKKSTWFDL--PLRYPPYKGKK 444
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
7-424 |
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: 586.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 7 RLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPAKK 86
Cdd:cd07135 13 RLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAKDEKVKD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 87 NLLT-MMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVNG 165
Cdd:cd07135 93 GPLAfMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQVVQG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 166 GIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPD 245
Cdd:cd07135 173 GVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 246 YILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLK--GQKIAFGGEMDEATRYLAPTILTDVDP 323
Cdd:cd07135 253 YVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDttKGKVVIGGEMDEATRFIPPTIVSDVSW 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 324 NSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVG 403
Cdd:cd07135 333 DDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGVG 412
|
410 420
....*....|....*....|.
gi 568971250 404 ASGMGAYHGKYSFDTFSHQRP 424
Cdd:cd07135 413 DSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
23-426 |
0e+00 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 514.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 23 RLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPAKKNLLTMMDEAYVQPEPL 102
Cdd:cd07134 22 RIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPLLLFGTKSKIRYEPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 103 GVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVNGGIPETTELLKQRFDHIL 182
Cdd:cd07134 102 GVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAEVAQALLELPFDHIF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 183 YTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIK 262
Cdd:cd07134 182 FTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 263 ETVKDFYGEN--IKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATRYLAPTILTDVDPNSKVMQEEIFGP 335
Cdd:cd07134 262 AEIEKFYGKDaaRKASPDLARIVNDRHFDRLKGLLddavaKGAKVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 336 ILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMGAYHGKYS 415
Cdd:cd07134 342 VLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGSYHGVYG 421
|
410
....*....|.
gi 568971250 416 FDTFSHQRPCL 426
Cdd:cd07134 422 FKAFSHERAVL 432
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
2-426 |
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: 514.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASA 81
Cdd:cd07137 2 PRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 82 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYA 161
Cdd:cd07137 82 EKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 162 IVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNC-GQT 240
Cdd:cd07137 162 VIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 241 CIAPDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLK----GQKIAFGGEMDEATRYLAPT 316
Cdd:cd07137 242 CIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDdpsvADKIVHGGERDEKNLYIEPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 317 ILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNS 396
Cdd:cd07137 322 ILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDT 401
|
410 420 430
....*....|....*....|....*....|
gi 568971250 397 LPFGGVGASGMGAYHGKYSFDTFSHQRPCL 426
Cdd:cd07137 402 LPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
7-424 |
2.10e-178 |
|
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: 507.02 E-value: 2.10e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 7 RLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADlskselnaYSH---------EVITILGEIDFMLGNLPE 77
Cdd:cd07133 6 RQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISAD--------FGHrsrhetllaEILPSIAGIKHARKHLKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 78 LASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQ 157
Cdd:cd07133 78 WMKPSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 158 DLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNC 237
Cdd:cd07133 158 DEVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 238 GQTCIAPDYILCEASLQNQIVQKIKETVKDFYGeNIKASPDYERIINLRHFKRLQSLL-----KGQKI---AFGGEMDEA 309
Cdd:cd07133 238 GQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLedaraKGARVielNPAGEDFAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 310 TRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVI 389
Cdd:cd07133 317 TRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTL 396
|
410 420 430
....*....|....*....|....*....|....*
gi 568971250 390 MHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRP 424
Cdd:cd07133 397 LHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-468 |
2.30e-154 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 447.64 E-value: 2.30e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 1 MERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELAS 80
Cdd:PLN02203 8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 81 ARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLY 160
Cdd:PLN02203 88 PKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 161 AIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYID---RDCDLDVACRRIAWGKYMNC 237
Cdd:PLN02203 168 KVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 238 -GQTCIAPDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLKGQKIA----FGGEMDEATRY 312
Cdd:PLN02203 248 aGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAasivHGGSIDEKKLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 313 LAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHF 392
Cdd:PLN02203 328 IEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQY 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568971250 393 TVNSLPFGGVGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESvnKLRYPPNSESKVSwakfFLLKQFNKGRLGMLL 468
Cdd:PLN02203 408 ACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEF--EFRYPPWNDFKLG----FLRLVYRFDYFGLLL 477
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
2-427 |
1.73e-131 |
|
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: 387.33 E-value: 1.73e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAyshevitiLGEIDFMLGNL---PEL 78
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEA--------LGEVARAADTFryyAGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 79 ASARPAKKNLLTMMD-EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LD 156
Cdd:cd07078 73 ARRLHGEVIPSPDPGeLAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 157 QDLYAIVNGGIPET-TELLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKY 234
Cdd:cd07078 153 PGVLNVVTGDGDEVgAALASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 235 MNCGQTCIAPDYILCEASLQNQIVQKIKETVKDFYGEN-IKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDE 308
Cdd:cd07078 233 GNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIedakaEGAKLLCGGKRLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 309 AT--RYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGN 386
Cdd:cd07078 313 GGkgYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 568971250 387 DVIMHFTVNsLPFGGVGASGMGAYHGKYSFDTFSHQRPCLL 427
Cdd:cd07078 393 DYSVGAEPS-APFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
5-452 |
1.74e-128 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 381.70 E-value: 1.74e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 5 VLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPA 84
Cdd:PLN02174 16 VTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 85 KKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVN 164
Cdd:PLN02174 96 KTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 165 GGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKY-MNCGQTCIA 243
Cdd:PLN02174 176 GAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACIS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 244 PDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLK----GQKIAFGGEMDEATRYLAPTILT 319
Cdd:PLN02174 256 PDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 320 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPF 399
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPF 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 568971250 400 GGVGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESVnkLRYPPNSESKVSWAK 452
Cdd:PLN02174 416 GGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSA--VRYPPYSRGKLRLLK 466
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
9-427 |
9.52e-107 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 321.87 E-value: 9.52e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYShEVITILGEIDFmlgnLPELASARPAKKNL 88
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRY----AAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 89 LTMMD-EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGG 166
Cdd:cd06534 79 SPDPGgEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 167 IPET-TELLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAP 244
Cdd:cd06534 159 GDEVgAALLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 245 DYILCEASLQNQIVQKIKetvkdfygenikaspdyeriinlrhfkrlqsllkgqkiafggemdeatrylapTILTDVDPN 324
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV-----------------------------------------------------TVLVDVDPD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 325 SKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNsLPFGGVGA 404
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-APFGGVKN 344
|
410 420
....*....|....*....|...
gi 568971250 405 SGMGAYHGKYSFDTFSHQRPCLL 427
Cdd:cd06534 345 SGIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
9-423 |
6.03e-98 |
|
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: 303.20 E-value: 6.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAyshevitiLGEIDFMLGNL---PELASARPAK 85
Cdd:COG1012 53 RAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEA--------RGEVDRAADFLryyAGEARRLYGE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 86 KNLLTMMD-EAYVQPEPLGVVLIIGAWNYPFVLTMQP------------LvgaiaagnaaivKPSELSENTAKILAELLP 152
Cdd:COG1012 125 TIPSDAPGtRAYVRREPLGVVGAITPWNFPLALAAWKlapalaagntvvL------------KPAEQTPLSALLLAELLE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 153 QY-LDQDLYAIVNGGIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRI 229
Cdd:COG1012 193 EAgLPAGVLNVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 230 AWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFG 303
Cdd:COG1012 273 VRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIedavaEGAELLTG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 304 GE--MDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSG 381
Cdd:COG1012 353 GRrpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAG 432
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 568971250 382 GVTGNDVIMHFTVNsLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:COG1012 433 MVWINDGTTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETK 473
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
3-423 |
1.03e-89 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 281.03 E-value: 1.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 3 RQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSElNAYSHEVITILGEIDFMLGNLPELASAR 82
Cdd:cd07099 22 AAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPR-ADAGLEVLLALEAIDWAARNAPRVLAPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 83 PAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYA 161
Cdd:cd07099 101 KVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAgPPQGVLQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 162 IVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTC 241
Cdd:cd07099 181 VVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 242 IAPDYILCEASLQNQIVQKIKETVKDF---YGENIKA------SPDYERIINlRHFKrlQSLLKGQKIAFGGE-MDEATR 311
Cdd:cd07099 261 ISVERVYVHESVYDEFVARLVAKARALrpgADDIGDAdigpmtTARQLDIVR-RHVD--DAVAKGAKALTGGArSNGGGP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 312 YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMH 391
Cdd:cd07099 338 FYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLT 417
|
410 420 430
....*....|....*....|....*....|..
gi 568971250 392 FTVNSLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07099 418 AGIPALPFGGVKDSGGGRRHGAEGLREFCRPK 449
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
9-423 |
7.12e-86 |
|
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: 271.33 E-value: 7.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYsHEVITILGEIDFMLGNLPELA-SARPAKKN 87
Cdd:pfam00171 39 RAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR-GEVDRAIDVLRYYAGLARRLDgETLPSDPG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 88 LLtmmdeAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGG 166
Cdd:pfam00171 118 RL-----AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLNVVTGS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 167 IPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAP 244
Cdd:pfam00171 193 GAEVGEALVEhpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTAT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 245 DYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEAT-RYLAPTI 317
Cdd:pfam00171 273 SRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLDNgYFVEPTV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 318 LTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMhFTVNSL 397
Cdd:pfam00171 353 LANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTT-GDADGL 431
|
410 420
....*....|....*....|....*.
gi 568971250 398 PFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:pfam00171 432 PFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
2-413 |
3.57e-76 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 246.44 E-value: 3.57e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASA 81
Cdd:cd07098 21 DEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 82 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL-----D 156
Cdd:cd07098 101 ESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLaacghD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 157 QDLYAIVNGgIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKY 234
Cdd:cd07098 181 PDLVQLVTC-LPETAEALTShpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 235 MNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEM-- 306
Cdd:cd07098 260 QSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVadaveKGARLLAGGKRyp 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 307 ---DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGV 383
Cdd:cd07098 340 hpeYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMV 419
|
410 420 430
....*....|....*....|....*....|
gi 568971250 384 TGNDVIMHFTVNSLPFGGVGASGMGAYHGK 413
Cdd:cd07098 420 AINDFGVNYYVQQLPFGGVKGSGFGRFAGE 449
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
9-377 |
7.61e-64 |
|
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: 214.05 E-value: 7.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPE-----LASARP 83
Cdd:cd07088 45 EAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARRiegeiIPSDRP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 84 AKKnlltmmdeAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAI 162
Cdd:cd07088 124 NEN--------IFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 163 VNGGIPETTELL--KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQT 240
Cdd:cd07088 196 VTGRGSVVGDALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 241 CIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGGEMDEATR--Y 312
Cdd:cd07088 276 CTCAERVYVHEDIYDEFMEKLVEKMKAVkVGDPFDAATDMGPLVNEAALDKVEEMVEraveaGATLLTGGKRPEGEKgyF 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568971250 313 LAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDE 377
Cdd:cd07088 356 YEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNE 420
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
2-423 |
8.09e-64 |
|
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: 212.78 E-value: 8.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEIL-------------AAIAADLSKSELNAYSHEVITILGEI 68
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIAdwliresgstrpkAAFEVGAAIAILREAAGLPRRPEGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 69 dfmlgnlpeLASARPAKKNlltmmdeaYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENT----- 143
Cdd:cd07104 83 ---------LPSDVPGKES--------MVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgglli 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 144 AKILAEL-LPQyldqDLYAIVNGGIPETTELL--KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDC 220
Cdd:cd07104 146 AEIFEEAgLPK----GVLNVVPGGGSEIGDALveHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 221 DLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGEniKASPDYE--RIINLRHFKRLQSLL-- 295
Cdd:cd07104 222 DLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALpVGD--PRDPDTVigPLINERQVDRVHAIVed 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 296 ---KGQKIAFGGEMDEatRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIK 372
Cdd:cd07104 300 avaAGARLLTGGTYEG--LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAM 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 568971250 373 RVIDETSSGGVTGNDVimhfTVNS---LPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07104 378 AFAERLETGMVHINDQ----TVNDephVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
9-423 |
1.75e-60 |
|
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: 204.72 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFmlgnLPELASARPAkkNL 88
Cdd:cd07093 29 KEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIPRAAANFRF----FADYILQLDG--ES 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 89 LTMMDEA--YVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyLDQDL----YAI 162
Cdd:cd07093 103 YPQDGGAlnYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELA---NEAGLppgvVNV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 163 VNGGIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQT 240
Cdd:cd07093 180 VHGFGPEAGAALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 241 CIAPDYILCEASLQNQIVQKIKETVKdfygeNIKA----SPDYE--RIINLRHFKRLQSLLK-----GQKIAFGGEMDEA 309
Cdd:cd07093 260 CLAGSRILVQRSIYDEFLERFVERAK-----ALKVgdplDPDTEvgPLISKEHLEKVLGYVElaraeGATILTGGGRPEL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 310 TR-----YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVT 384
Cdd:cd07093 335 PDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVW 414
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 568971250 385 GNDvimhFTVNSL--PFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07093 415 VNC----WLVRDLrtPFGGVKASGIGREGGDYSLEFYTELK 451
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
10-419 |
1.46e-58 |
|
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: 199.58 E-value: 1.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 10 QAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADL------SKSELNA-------YSHEVITILGEIdfmlgnLP 76
Cdd:cd07103 30 AAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQgkplaeARGEVDYaasflewFAEEARRIYGRT------IP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 77 elaSARPAKKNLltmmdeayVQPEPLGVVLIIGAWNYPFVL-------------TMqplvgaiaagnaaIVKPSELSENT 143
Cdd:cd07103 104 ---SPAPGKRIL--------VIKQPVGVVAAITPWNFPAAMitrkiapalaagcTV-------------VLKPAEETPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 144 AKILAELLPQY-LDQDLYAIVNGGIPETTELLKQRFD--HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDC 220
Cdd:cd07103 160 ALALAELAEEAgLPAGVLNVVTGSPAEIGEALCASPRvrKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 221 DLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL---- 295
Cdd:cd07103 240 DLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALVedav 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 296 -KGQKIAFGGEMDEAT-RYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKR 373
Cdd:cd07103 320 aKGAKVLTGGKRLGLGgYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWR 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 568971250 374 VIDETSSGGVTGNDVIMhfTVNSLPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07103 400 VAEALEAGMVGINTGLI--SDAEAPFGGVKESGLGREGGKEGLEEY 443
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
7-421 |
4.28e-58 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 198.62 E-value: 4.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 7 RLRQAFRSGRSRPLRFRLqqlEALRRMVqerekEILAAIAADLSKS-------ELNAYSHEVITILGEIDFMLGNLPE-L 78
Cdd:cd07102 26 RARAAQKGWRAVPLEERK---AIVTRAV-----ELLAANTDEIAEEltwqmgrPIAQAGGEIRGMLERARYMISIAEEaL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 79 ASARPAKKNLLtmmdEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELS----ENTAKILAE-LLPQ 153
Cdd:cd07102 98 ADIRVPEKDGF----ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTplcgERFAAAFAEaGLPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 154 yldqDLYAIVNGGIPETTELLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWG 232
Cdd:cd07102 174 ----GVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 233 KYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRH--FKRLQ---SLLKGQKIAFGGEM 306
Cdd:cd07102 250 AFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAadFVRAQiadAIAKGARALIDGAL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 307 ----DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGG 382
Cdd:cd07102 330 fpedKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGT 409
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 568971250 383 VTGN--DvimhFTVNSLPFGGVGASGMGAYHGKYSFDTFSH 421
Cdd:cd07102 410 VFMNrcD----YLDPALAWTGVKDSGRGVTLSRLGYDQLTR 446
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
10-423 |
7.17e-58 |
|
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: 197.94 E-value: 7.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 10 QAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYshevitilGEIDFMLGNLPELASA--RPAKKn 87
Cdd:cd07150 32 DAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW--------FETTFTPELLRAAAGEcrRVRGE- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 88 llTMMDEA-----YVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYA 161
Cdd:cd07150 103 --TLPSDSpgtvsMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 162 IVNGGIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQ 239
Cdd:cd07150 181 VVTGGGAEVGDELVDdpRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 240 TCIAPDYILCEASLQNQIVQKIKE-----TVKDFYGENIKASPdyerIINLRHFKRLQSLL-----KGQKIAFGGEMDea 309
Cdd:cd07150 261 ICMSASRIIVEEPVYDEFVKKFVArasklKVGDPRDPDTVIGP----LISPRQVERIKRQVedavaKGAKLLTGGKYD-- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 310 TRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVI 389
Cdd:cd07150 335 GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPT 414
|
410 420 430
....*....|....*....|....*....|....
gi 568971250 390 MHFTVNsLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07150 415 ILDEAH-VPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
100-423 |
1.24e-56 |
|
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: 194.48 E-value: 1.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 100 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELL--KQ 176
Cdd:cd07118 118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMteHP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 177 RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQ 256
Cdd:cd07118 198 DVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 257 IVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGGEMDE--ATRYLAPTILTDVDPNSKVM 328
Cdd:cd07118 278 FVAAVVARSRKVrVGDPLDPETKVGAIINEAQLAKITDYVDagraeGATLLLGGERLAsaAGLFYQPTIFTDVTPDMAIA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 329 QEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTvnSLPFGGVGASGMG 408
Cdd:cd07118 358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIG 435
|
330
....*....|....*
gi 568971250 409 AYHGKYSFDTFSHQR 423
Cdd:cd07118 436 RELGRYGVEEYTELK 450
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
9-419 |
6.07e-56 |
|
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: 193.39 E-value: 6.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSR-PLRFRLQQLEALRRMVqEREKEILAAI-AADLSKS-ELNAYSH--EVITIL----GEIDFMLGnlpELA 79
Cdd:cd07144 55 RKAFESWWSKvTGEERGELLDKLADLV-EKNRDLLAAIeALDSGKPyHSNALGDldEIIAVIryyaGWADKIQG---KTI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 80 SARPAKknlltmmdEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQD 158
Cdd:cd07144 131 PTSPNK--------LAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 159 LYAIVNGGIPETTELLKQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMN 236
Cdd:cd07144 203 VVNIIPGYGAVAGSALAEHpdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 237 CGQTCIAPDYILCEASLQNQIVQKIKETVK------DFYGENIKASP-----DYERIINLRHfkrlQSLLKGQKIAFGGE 305
Cdd:cd07144 283 SGQNCTATSRIYVQESIYDKFVEKFVEHVKqnykvgSPFDDDTVVGPqvsktQYDRVLSYIE----KGKKEGAKLVYGGE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 306 ----MDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSG 381
Cdd:cd07144 359 kapeGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAG 438
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 568971250 382 GV---TGNDviMHFTVnslPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07144 439 MVwinSSND--SDVGV---PFGGFKMSGIGRELGEYGLETY 474
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
9-420 |
3.39e-55 |
|
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: 190.62 E-value: 3.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGnlpelaSAR----PA 84
Cdd:cd07092 29 HAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFRFFAG------AARtlegPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 85 KKNLLTMMdEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVN 164
Cdd:cd07092 103 AGEYLPGH-TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 165 GGIPETTELL--KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCI 242
Cdd:cd07092 182 GGGASAGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 243 APDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL----KGQKIAFGGEMDEATRY-LAPT 316
Cdd:cd07092 262 AACRVYVHESVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVerapAHARVLTGGRRAEGPGYfYEPT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 317 ILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDvimHFT-VN 395
Cdd:cd07092 342 VVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIPlAA 418
|
410 420
....*....|....*....|....*
gi 568971250 396 SLPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07092 419 EMPHGGFKQSGYGKDLSIYALEDYT 443
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
100-420 |
4.12e-55 |
|
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: 190.10 E-value: 4.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 100 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyLDQDLYAivnGGI----------PE 169
Cdd:cd07105 97 EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVF---HEAGLPK---GVLnvvthspedaPE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 170 TTELLkqrFDH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAP 244
Cdd:cd07105 171 VVEAL---IAHpavrkVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMST 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 245 DYILCEASLQNQIVQKIKETVkdfygENIKASPDYERI-INLRHFKRLQSLL-----KGQKIAFGG--EMDEATRYLAPT 316
Cdd:cd07105 248 ERIIVHESIADEFVEKLKAAA-----EKLFAGPVVLGSlVSAAAADRVKELVddalsKGAKLVVGGlaDESPSGTSMPPT 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 317 ILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHfTVNS 396
Cdd:cd07105 323 ILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVH-DEPT 401
|
330 340
....*....|....*....|....
gi 568971250 397 LPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07105 402 LPHGGVKSSGYGRFNGKWGIDEFT 425
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
95-420 |
1.23e-54 |
|
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: 189.37 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 95 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTEL 173
Cdd:cd07109 111 VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGLGAEAGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 174 LKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEA 251
Cdd:cd07109 191 LVAhpGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 252 SLQNQIVQKIKETVKDF---YGEnikASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATR----YLAPTILT 319
Cdd:cd07109 271 SIYDEVLERLVERFRALrvgPGL---EDPDLGPLISAKQLDRVEGFVararaRGARIVAGGRIAEGAPaggyFVAPTLLD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 320 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDvimHFTVN--SL 397
Cdd:cd07109 348 DVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNN---YGAGGgiEL 424
|
330 340
....*....|....*....|...
gi 568971250 398 PFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07109 425 PFGGVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
9-414 |
1.97e-53 |
|
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: 185.81 E-value: 1.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYshevitilGEIDFMLGNLPELASarpakknl 88
Cdd:cd07106 29 KAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ--------FEVGGAVAWLRYTAS-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 89 LTMMDEAYVQPE---------PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDL 159
Cdd:cd07106 93 LDLPDEVIEDDDtrrvelrrkPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 160 YAIVNGGiPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNC 237
Cdd:cd07106 173 LNVVSGG-DELGPALTShpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 238 GQTCIAPDYILCEASLQNQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATR 311
Cdd:cd07106 252 GQVCAAIKRLYVHESIYDEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVedakaKGAKVLAGGEPLDGPG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 312 Y-LAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNdviM 390
Cdd:cd07106 332 YfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN---T 408
|
410 420
....*....|....*....|....*
gi 568971250 391 HFTVN-SLPFGGVGASGMGAYHGKY 414
Cdd:cd07106 409 HGALDpDAPFGGHKQSGIGVEFGIE 433
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
1-423 |
2.07e-53 |
|
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: 186.29 E-value: 2.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 1 MERQVLRLRQAF-RSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELA 79
Cdd:cd07089 21 VDAAIAAARRAFdTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSFP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 80 --SARPAKkNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyLDQ 157
Cdd:cd07089 101 weFDLPVP-ALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEII---AET 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 158 DLYA----IVNGGIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAW 231
Cdd:cd07089 177 DLPAgvvnVVTGSDNAVGEALTTdpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 232 GKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVkdfygENIK----ASPD--YERIINLRHFKRLQSLLK-----GQKI 300
Cdd:cd07089 257 VCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAF-----EALPvgdpADPGtvMGPLISAAQRDRVEGYIArgrdeGARL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 301 AFGGEMDEATR---YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDE 377
Cdd:cd07089 332 VTGGGRPAGLDkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARR 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 568971250 378 TSSGGVTGNDViMHFTVNSlPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07089 412 IRTGSVGINGG-GGYGPDA-PFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
95-417 |
3.10e-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: 186.26 E-value: 3.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 95 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQD-LYAIVNGGIPETTEL 173
Cdd:cd07091 135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPgVVNIVPGFGPTAGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 174 LKQ--RFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07091 215 ISShmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQ 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 251 ASLQNQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGGE-MDEATRYLAPTILTDVDP 323
Cdd:cd07091 295 ESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIEsgkkeGATLLTGGErHGSKGYFIQPTVFTDVKD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 324 NSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGN--DVIMHftvnSLPFGG 401
Cdd:cd07091 375 DMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtyNVFDA----AVPFGG 450
|
330
....*....|....*.
gi 568971250 402 VGASGMGAYHGKYSFD 417
Cdd:cd07091 451 FKQSGFGRELGEEGLE 466
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
1-419 |
5.20e-53 |
|
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: 185.40 E-value: 5.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 1 MERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELAS 80
Cdd:cd07138 38 VDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 81 ARPAKKNLLTMmdeayvqpEPLGVVLIIGAWNYPF-----------------VLtmqplvgaiaagnaaivKPSELSENT 143
Cdd:cd07138 118 EERRGNSLVVR--------EPIGVCGLITPWNWPLnqivlkvapalaagctvVL-----------------KPSEVAPLS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 144 AKILAELLpqyLDQDLYA----IVNGGIPETTELLK--QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYID 217
Cdd:cd07138 173 AIILAEIL---DEAGLPAgvfnLVNGDGPVVGEALSahPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIIL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 218 RDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVkdfygENIKA-SPDYER-----IINLRHFKRL 291
Cdd:cd07138 250 DDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAA-----EAYVVgDPRDPAttlgpLASAAQFDRV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 292 QSLLK-----GQKIAFGG----EMDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALY 362
Cdd:cd07138 325 QGYIQkgieeGARLVAGGpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGY 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 568971250 363 VFSRNNKLIKRVIDETSSGGVTGNDVIMHFtvnSLPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07138 405 VWSADPERARAVARRLRAGQVHINGAAFNP---GAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
3-408 |
8.31e-53 |
|
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: 184.49 E-value: 8.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 3 RQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPEL-ASA 81
Cdd:cd07108 23 RAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVLADLFRYFGGLAGELkGET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 82 RPAKKNLLTmmdeaYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYA 161
Cdd:cd07108 103 LPFGPDVLT-----YTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 162 IVNGGIPETTELLKQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRR-IAWGKYMNCG 238
Cdd:cd07108 178 VITGYGEECGAALVDHpdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGaIAGMRFTRQG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 239 QTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL------KGQKIAFGGEMDEATR 311
Cdd:cd07108 258 QSCTAGSRLFVHEDIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIdlglstSGATVLRGGPLPGEGP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 312 -----YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGN 386
Cdd:cd07108 338 ladgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVN 417
|
410 420
....*....|....*....|..
gi 568971250 387 DviMHFTVNSLPFGGVGASGMG 408
Cdd:cd07108 418 Q--GGGQQPGQSYGGFKQSGLG 437
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
95-423 |
1.03e-52 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 184.29 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 95 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL-----LPQyldqDLYAIVNGGIPE 169
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPP----GVVNVVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 170 TTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYI 247
Cdd:cd07114 189 TGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 248 LCEASLQNQIVQKIKETVKdfygeNIK-ASPDYER-----IINLRHFKRLQSLLK-----GQKIAFGGE-MDEATR---- 311
Cdd:cd07114 269 LVQRSIYDEFVERLVARAR-----AIRvGDPLDPEtqmgpLATERQLEKVERYVArareeGARVLTGGErPSGADLgagy 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 312 YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDviMH 391
Cdd:cd07114 344 FFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YR 421
|
330 340 350
....*....|....*....|....*....|..
gi 568971250 392 FTVNSLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07114 422 ALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
1-408 |
2.06e-52 |
|
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: 183.18 E-value: 2.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 1 MERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSelnaysheVITILGEIDFMLGNLpELaS 80
Cdd:cd07149 23 VEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKP--------IKDARKEVDRAIETL-RL-S 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 81 ARPAKKNLLTM--MDE--------AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL 150
Cdd:cd07149 93 AEEAKRLAGETipFDAspggegriGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 151 LPQ-YLDQDLYAIVNGGIPET-TELLK-QRFDHILYTGNTAVGKIVMEAAAkhLTPVTLELGGKSPCYIDRDCDLDVACR 227
Cdd:cd07149 173 LLEaGLPKGALNVVTGSGETVgDALVTdPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 228 RIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVK-----DFYGENIKASPdyerIINLRHFKRLQSLL-----KG 297
Cdd:cd07149 251 RCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKklvvgDPLDEDTDVGP----MISEAEAERIEEWVeeaveGG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 298 QKIAFGGEMDEAtrYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDE 377
Cdd:cd07149 327 ARLLTGGKRDGA--ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARE 404
|
410 420 430
....*....|....*....|....*....|.
gi 568971250 378 TSSGGVTGNDvIMHFTVNSLPFGGVGASGMG 408
Cdd:cd07149 405 LEVGGVMIND-SSTFRVDHMPYGGVKESGTG 434
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
100-419 |
4.46e-52 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 183.35 E-value: 4.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 100 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELL---- 174
Cdd:PLN02278 159 QPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEIGDALlasp 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 175 KQRfdHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQ 254
Cdd:PLN02278 239 KVR--KITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIY 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 255 NQIVQKIKETVK-----DFYGENIKASPdyerIINLRHFKRLQSLL-----KGQKIAFGGE-MDEATRYLAPTILTDVDP 323
Cdd:PLN02278 317 DKFAEAFSKAVQklvvgDGFEEGVTQGP----LINEAAVQKVESHVqdavsKGAKVLLGGKrHSLGGTFYEPTVLGDVTE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 324 NSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVnsLPFGGVG 403
Cdd:PLN02278 393 DMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEV--APFGGVK 470
|
330
....*....|....*.
gi 568971250 404 ASGMGAYHGKYSFDTF 419
Cdd:PLN02278 471 QSGLGREGSKYGIDEY 486
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
101-423 |
6.64e-52 |
|
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: 181.72 E-value: 6.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 101 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENT-----AKILAEL-LPQYLDQdlyaIVNGGiPETTELL 174
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSggvviARLFEEAgLPAGVLH----VLPGG-ADAGEAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 175 --KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEAS 252
Cdd:cd07152 185 veDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHES 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 253 LQNQIVQKIKE-----TVKDFYGENIKASPdyerIINLRHFKRLQ-----SLLKGQKIAFGGEMDEatRYLAPTILTDVD 322
Cdd:cd07152 265 VADAYTAKLAAkakhlPVGDPATGQVALGP----LINARQLDRVHaivddSVAAGARLEAGGTYDG--LFYRPTVLSGVK 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 323 PNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVimhfTVNS---LPF 399
Cdd:cd07152 339 PGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVNDephNPF 414
|
330 340
....*....|....*....|....*
gi 568971250 400 GGVGASGMGAYHG-KYSFDTFSHQR 423
Cdd:cd07152 415 GGMGASGNGSRFGgPANWEEFTQWQ 439
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
9-423 |
7.21e-52 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 182.17 E-value: 7.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEReKEILAAIAADLSKSELNAYSHEVITILGEIDFMlgnlPELASARPAKKNL 88
Cdd:cd07110 29 RRAFPRWKKTTGAERAKYLRAIAEGVRER-REELAELEARDNGKPLDEAAWDVDDVAGCFEYY----ADLAEQLDAKAER 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 89 -LTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL-----LPQyldqDL 159
Cdd:cd07110 104 aVPLPSEdfkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIaaeagLPP----GV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 160 YAIVNGGIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNC 237
Cdd:cd07110 180 LNVVTGTGDEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 238 GQTCIAPDYILCEASLQNQIVQKIKETVkdfygENIKASPDYER------IINLRHFKRLQSLLK-----GQKIAFGGEM 306
Cdd:cd07110 260 GQICSATSRLLVHESIADAFLERLATAA-----EAIRVGDPLEEgvrlgpLVSQAQYEKVLSFIArgkeeGARLLCGGRR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 307 DEATR---YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGV 383
Cdd:cd07110 335 PAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIV 414
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 568971250 384 TGNDVIMHFTvnSLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07110 415 WINCSQPCFP--QAPWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
23-420 |
3.44e-50 |
|
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: 177.50 E-value: 3.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 23 RLQQLEALRRMVQEREKEILAAIAADLSKSELNAyshevitiLGEIDFMLGNLPELAS--ARPAKKNLLTMMD--EAYVQ 98
Cdd:cd07151 56 RAEILEKAAQILEERRDEIVEWLIRESGSTRIKA--------NIEWGAAMAITREAATfpLRMEGRILPSDVPgkENRVY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 99 PEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENT-----AKILAEL-LPQyldqDLYAIVNGGIPEtte 172
Cdd:cd07151 128 REPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITgglllAKIFEEAgLPK----GVLNVVVGAGSE--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 173 lLKQRF-DH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDY 246
Cdd:cd07151 201 -IGDAFvEHpvprlISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 247 ILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGGEMDEatRYLAPTILTD 320
Cdd:cd07151 280 IIVHEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIEqaveeGATLLVGGEAEG--NVLEPTVLSD 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 321 VDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVimhfTVNS---L 397
Cdd:cd07151 358 VTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQ----PVNDephV 433
|
410 420
....*....|....*....|...
gi 568971250 398 PFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07151 434 PFGGEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
95-421 |
3.04e-49 |
|
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: 174.80 E-value: 3.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 95 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGiPETTEL 173
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 174 LKQRFD--HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEA 251
Cdd:cd07090 189 LCEHPDvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 252 SLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGGE---MD---EATRYLAPTILT 319
Cdd:cd07090 269 SIKDEFTERLVERTKKIrIGDPLDEDTQMGALISEEHLEKVLGYIEsakqeGAKVLCGGErvvPEdglENGFYVSPCVLT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 320 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDvimhFTVNS--L 397
Cdd:cd07090 349 DCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT----YNISPveV 424
|
330 340
....*....|....*....|....
gi 568971250 398 PFGGVGASGMGAYHGKYSFDTFSH 421
Cdd:cd07090 425 PFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
96-420 |
1.08e-48 |
|
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: 173.39 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 96 YVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELL 174
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 175 KQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEAS 252
Cdd:cd07115 192 VEHpdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 253 LQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATR-YLAPTILTDVDPNS 325
Cdd:cd07115 272 IYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDRVLDYVdvgreEGARLLTGGKRPGARGfFVEPTIFAAVPPEM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 326 KVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNdvIMHFTVNSLPFGGVGAS 405
Cdd:cd07115 352 RIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQS 429
|
330
....*....|....*
gi 568971250 406 GMGAYHGKYSFDTFS 420
Cdd:cd07115 430 GFGREMGREALDEYT 444
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
7-413 |
7.14e-48 |
|
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: 171.34 E-value: 7.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 7 RLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPELASARPaKK 86
Cdd:cd07101 26 RARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFE-EVLDVAIVARYYARRAERLLKPRR-RR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 87 NLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNG 165
Cdd:cd07101 104 GAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLPRDLWQVVTG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 166 GIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPD 245
Cdd:cd07101 184 PGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 246 YILCEASLQNQIVQKIKETVkdfygENIKASPDYE------RIINLRHFKRLQSLL-----KGQKIAFGGEM--DEATRY 312
Cdd:cd07101 264 RIYVHESVYDEFVRRFVART-----RALRLGAALDygpdmgSLISQAQLDRVTAHVddavaKGATVLAGGRArpDLGPYF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 313 LAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDvIMHF 392
Cdd:cd07101 339 YEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE-GYAA 417
|
410 420
....*....|....*....|...
gi 568971250 393 TVNSL--PFGGVGASGMGAYHGK 413
Cdd:cd07101 418 AWASIdaPMGGMKDSGLGRRHGA 440
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
79-408 |
7.19e-48 |
|
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: 171.76 E-value: 7.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 79 ASARPAKKNLLTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL 155
Cdd:cd07559 111 AGVIRAQEGSLSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 156 DQDLYAIVNGGIPETTELLK--QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYI-----DRDCDLDVACRR 228
Cdd:cd07559 191 PKGVVNVVTGFGSEAGKPLAshPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 229 IAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVkdfygENIKA-SP-DYERII----NLRHFKRLQSLLK-----G 297
Cdd:cd07559 271 GQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERF-----EAIKVgNPlDPETMMgaqvSKDQLEKILSYVDigkeeG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 298 QKIAFGGEM-----DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIK 372
Cdd:cd07559 346 AEVLTGGERltlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRAL 425
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568971250 373 RVIDETSSGGVTGNdvimhfTVNSLP----FGGVGASGMG 408
Cdd:cd07559 426 RVARGIQTGRVWVN------CYHQYPahapFGGYKKSGIG 459
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
2-421 |
1.10e-47 |
|
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: 171.38 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSK--SELNAyshEVITILGEIDFMLGNLPEL- 78
Cdd:cd07131 40 DAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKplAEGRG---DVQEAIDMAQYAAGEGRRLf 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 79 ----ASARPAKknlltmmdEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY 154
Cdd:cd07131 117 getvPSELPNK--------DAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 155 -LDQDLYAIVNGGIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAW 231
Cdd:cd07131 189 gLPPGVVNVVHGRGEEVGEALVEhpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALW 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 232 GKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQ-----------SLLKGQK 299
Cdd:cd07131 269 SAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLnyneigkeegaTLLLGGE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 300 IAFGGEMDEATrYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETS 379
Cdd:cd07131 349 RLTGGGYEKGY-FVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLE 427
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 568971250 380 SGGVTGNDVIMHFTVNsLPFGGVGASGMGAYHGKYS-FDTFSH 421
Cdd:cd07131 428 AGITYVNAPTIGAEVH-LPFGGVKKSGNGHREAGTTaLDAFTE 469
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
1-419 |
1.40e-46 |
|
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: 168.14 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 1 MERQVLRLRQAFRSG--RSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLgnlpEL 78
Cdd:cd07139 38 VDAAVAAARRAFDNGpwPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGPGPAALLRYYA----AL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 79 ASARPAKKNLLTM-MDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LD 156
Cdd:cd07139 114 ARDFPFEERRPGSgGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 157 QDLYAIVNGGIpETTELLKQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKY 234
Cdd:cd07139 194 PGVVNVVPADR-EVGEYLVRHpgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 235 MNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEM-D 307
Cdd:cd07139 273 MNNGQVCVALTRILVPRSRYDEVVEALAAAVAALkVGDPLDPATQIGPLASARQRERVEGYIakgraEGARLVTGGGRpA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 308 EATR--YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFS----RNNKLIKRVidetSSG 381
Cdd:cd07139 353 GLDRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTadveRGLAVARRI----RTG 428
|
410 420 430
....*....|....*....|....*....|....*...
gi 568971250 382 GVTGNDVIMHFtvnSLPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07139 429 TVGVNGFRLDF---GAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
94-420 |
1.87e-46 |
|
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: 167.87 E-value: 1.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 94 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTE 172
Cdd:cd07119 127 ISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 173 LL--KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07119 207 ELaeSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 251 ASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEM---DEATR--YLAPTILT 319
Cdd:cd07119 287 ESIHDKFVAALAERAKKIkLGNGLDADTEMGPLVSAEHREKVLSYIqlgkeEGARLVCGGKRptgDELAKgyFVEPTIFD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 320 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDviMHFTVNSLPF 399
Cdd:cd07119 367 DVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPW 444
|
330 340
....*....|....*....|.
gi 568971250 400 GGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07119 445 GGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
36-420 |
4.52e-46 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 166.94 E-value: 4.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 36 EREKEILAAIAA-DLSKSELNAYSHEVITILGEIDFMLGnlpelasarPAKKNLLTMMDE-----AYVQPEPLGVVLIIG 109
Cdd:cd07143 82 ERNLDYLASIEAlDNGKTFGTAKRVDVQASADTFRYYGG---------WADKIHGQVIETdikklTYTRHEPIGVCGQII 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 110 AWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELLKQ--RFDHILYTGN 186
Cdd:cd07143 153 PWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISShmDIDKVAFTGS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 187 TAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETV 265
Cdd:cd07143 233 TLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 266 K-----DFYGENIKASP-----DYERIIN-LRHFKRlqsllKGQKIAFGGEMDEATRY-LAPTILTDVDPNSKVMQEEIF 333
Cdd:cd07143 313 KklkvgDPFAEDTFQGPqvsqiQYERIMSyIESGKA-----EGATVETGGKRHGNEGYfIEPTIFTDVTEDMKIVKEEIF 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 334 GPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDV-IMHFTVnslPFGGVGASGMGAYHG 412
Cdd:cd07143 388 GPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYnLLHHQV---PFGGYKQSGIGRELG 464
|
....*...
gi 568971250 413 KYSFDTFS 420
Cdd:cd07143 465 EYALENYT 472
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
93-420 |
1.08e-45 |
|
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: 165.75 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 93 DEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETT 171
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 172 ELLKQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILC 249
Cdd:TIGR01804 205 PLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 250 EASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGG------EMDEATrYLAPTI 317
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIEkgkaeGATLATGGgrpenvGLQNGF-FVEPTV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 318 LTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDviMHFTVNSL 397
Cdd:TIGR01804 364 FADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEA 441
|
330 340
....*....|....*....|...
gi 568971250 398 PFGGVGASGMGAYHGKYSFDTFS 420
Cdd:TIGR01804 442 PFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
2-412 |
1.79e-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: 164.86 E-value: 1.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEiLAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELasa 81
Cdd:cd07107 22 DRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEE-LALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTEL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 82 rpaKKNLLTMMDEA--YVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDL 159
Cdd:cd07107 98 ---KGETIPVGGRNlhYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 160 YAIVNGGIPETTELLKQRFD--HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGkyMN- 236
Cdd:cd07107 175 FNILPGDGATAGAALVRHPDvkRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAG--MNf 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 237 --CGQTCIAPDYILCEASLQNQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGG---- 304
Cdd:cd07107 253 twCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIdsakrEGARLVTGGgrpe 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 305 -EMDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGV 383
Cdd:cd07107 333 gPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYV 412
|
410 420
....*....|....*....|....*....
gi 568971250 384 TGNDVIMHFTvnSLPFGGVGASGMGAYHG 412
Cdd:cd07107 413 WINGSSRHFL--GAPFGGVKNSGIGREEC 439
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
9-408 |
1.86e-45 |
|
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: 164.53 E-value: 1.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAyshevitiLGEIDFMLGNLpELASAR------ 82
Cdd:cd07094 31 RAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA--------RVEVDRAIDTL-RLAAEEaerirg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 83 ---PAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELL-PQYLDQD 158
Cdd:cd07094 102 eeiPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 159 LYAIVNGGIPETTELL--KQRFDHILYTGNTAVGKIVMEAAAKhlTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMN 236
Cdd:cd07094 182 VLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 237 CGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEAT 310
Cdd:cd07094 260 AGQVCISVQRIYVHEELYDEFIEAFVAAVKKLkVGDPLDEDTDVGPLISEEAAERVERWVeeaveAGARLLCGGERDGAL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 311 RYlaPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRN-NKLIKrVIDETSSGGVTGNDVi 389
Cdd:cd07094 340 FK--PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDlNVAFK-AAEKLEVGGVMVNDS- 415
|
410
....*....|....*....
gi 568971250 390 MHFTVNSLPFGGVGASGMG 408
Cdd:cd07094 416 SAFRTDWMPFGGVKESGVG 434
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
95-420 |
2.04e-45 |
|
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: 164.70 E-value: 2.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 95 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL-----LPQyldqDLYAIVNGGIPE 169
Cdd:cd07112 118 ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLPA----GVLNVVPGFGHT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 170 TTELL--KQRFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDC-DLDVACRRIAWGKYMNCGQTCIAPD 245
Cdd:cd07112 194 AGEALglHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 246 YILCEASLQNQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATR---YLAPT 316
Cdd:cd07112 274 RLLVHESIKDEFLEKVVAAAREWKpGDPLDPATRMGALVSEAHFDKVLGYIesgkaEGARLVAGGKRVLTETggfFVEPT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 317 ILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNdvimhfTVN- 395
Cdd:cd07112 354 VFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN------CFDe 427
|
330 340
....*....|....*....|....*...
gi 568971250 396 ---SLPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07112 428 gdiTTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
1-419 |
3.14e-45 |
|
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: 163.40 E-value: 3.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 1 MERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAyshevitiLGEI-------DFMLG 73
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA--------RAEVekcawicRYYAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 74 NLPELASARPAKknllTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQ 153
Cdd:cd07100 73 NAEAFLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 154 Y-LDQDLYAIVNGGIPETTELLK-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAW 231
Cdd:cd07100 149 AgFPEGVFQNLLIDSDQVEAIIAdPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 232 GKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVK-----DFYGENIK----ASPDyeriinLR---HFKRLQSLLKGQK 299
Cdd:cd07100 229 GRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAalkvgDPMDEDTDlgplARKD------LRdelHEQVEEAVAAGAT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 300 IAFGGE-MDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDET 378
Cdd:cd07100 303 LLLGGKrPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRL 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 568971250 379 SSGGVTGNDVimhftVNS---LPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07100 383 EAGMVFINGM-----VKSdprLPFGGVKRSGYGRELGRFGIREF 421
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
95-408 |
4.14e-45 |
|
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: 163.67 E-value: 4.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 95 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPET-TE 172
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVgDE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 173 LLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEA 251
Cdd:cd07145 197 IVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 252 SLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATrYLAPTILTDVDPNS 325
Cdd:cd07145 277 EVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVndaveKGGKILYGGKRDEGS-FFPPTVLENDTPDM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 326 KVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMhFTVNSLPFGGVGAS 405
Cdd:cd07145 356 IVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR-FRWDNLPFGGFKKS 434
|
...
gi 568971250 406 GMG 408
Cdd:cd07145 435 GIG 437
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
2-420 |
5.45e-45 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 163.30 E-value: 5.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRF-RLQQLEALRRMVQEREKEILAAIAADLSKS-------------ELNAYSHEVITILGE 67
Cdd:cd07146 20 EEALREALALAASYRSTLTRYqRSAILNKAAALLEARREEFARLITLESGLClkdtryevgraadVLRFAAAEALRDDGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 68 -IDFmlgnlpELASARPAKKnlltmmdeAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKI 146
Cdd:cd07146 100 sFSC------DLTANGKARK--------IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 147 LAELLPQY-LDQDLYAIVNGGIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAA-KHLTpvtLELGGKSPCYIDRDCDL 222
Cdd:cd07146 166 LADLLYEAgLPPDMLSVVTGEPGEIGDELIThpDVDLVTFTGGVAVGKAIAATAGyKRQL---LELGGNDPLIVMDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 223 DVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIIN---LRHFKR--LQSLLK 296
Cdd:cd07146 243 ERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDeeaAIQIENrvEEAIAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 297 GQKIAFGGEMDEAtrYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVID 376
Cdd:cd07146 323 GARVLLGNQRQGA--LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 568971250 377 ETSSGGVTGNDViMHFTVNSLPFGGVGASGMGAYHG-KYSFDTFS 420
Cdd:cd07146 401 RLDVGTVNVNEV-PGFRSELSPFGGVKDSGLGGKEGvREAMKEMT 444
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
27-381 |
1.31e-44 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 161.44 E-value: 1.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 27 LEALRRMVQEREKEILAAIAADLSKSELNAySHEVITILGEIDFML-------GNLpeLASARPaKKNLLtmmdeayVQP 99
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAewarryeGEI--IQSDRP-GENIL-------LFK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 100 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELL--KQ 176
Cdd:PRK10090 70 RALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELagNP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 177 RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQ 256
Cdd:PRK10090 150 KVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 257 IVQKIKETVKDF-YGENIKAS-PDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATRYL-APTILTDVDPNSKVM 328
Cdd:PRK10090 230 FVNRLGEAMQAVqFGNPAERNdIAMGPLINAAALERVEQKVaraveEGARVALGGKAVEGKGYYyPPTLLLDVRQEMSIM 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 568971250 329 QEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSG 381
Cdd:PRK10090 310 HEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFG 362
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
2-423 |
1.39e-44 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 163.51 E-value: 1.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPE-LAS 80
Cdd:PRK09407 57 EAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFE-EVLDVALTARYYARRAPKlLAP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 81 ARpaKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDL 159
Cdd:PRK09407 136 RR--RAGALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 160 YAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQ 239
Cdd:PRK09407 214 WQVVTGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 240 TCIAPDYILCEASLQNQIVQKIKETVKDFygeNIKASPDYE----RIINLRHFKRLQS-----LLKGQKIAFGGEM--DE 308
Cdd:PRK09407 294 LCISIERIYVHESIYDEFVRAFVAAVRAM---RLGAGYDYSadmgSLISEAQLETVSAhvddaVAKGATVLAGGKArpDL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 309 ATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDV 388
Cdd:PRK09407 371 GPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEG 450
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 568971250 389 IMH-FTVNSLPFGGVGASGMGAYHG-----KYS-FDTFSHQR 423
Cdd:PRK09407 451 YAAaWGSVDAPMGGMKDSGLGRRHGaegllKYTeSQTIATQR 492
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
79-408 |
8.73e-44 |
|
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: 160.70 E-value: 8.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 79 ASARPAKKNLLTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL 155
Cdd:cd07117 111 AGVIRAEEGSANMIDEdtlSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 156 DQDLYAIVNGGIPETTELLKQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGK 233
Cdd:cd07117 191 PKGVVNIVTGKGSKSGEYLLNHpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 234 YMNCGQTCIAPDYILCEASLQNQIVQKIKETVkdfygENIKA----SPDYE--RIINLRHFKRLQSLLK-----GQKIAF 302
Cdd:cd07117 271 LFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKF-----ENVKVgnplDPDTQmgAQVNKDQLDKILSYVDiakeeGAKILT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 303 GGEM-----DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDE 377
Cdd:cd07117 346 GGHRltengLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARA 425
|
330 340 350
....*....|....*....|....*....|....*
gi 568971250 378 TSSGGVTGNdvimhfTVNSLP----FGGVGASGMG 408
Cdd:cd07117 426 VETGRVWVN------TYNQIPagapFGGYKKSGIG 454
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
10-408 |
5.21e-43 |
|
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: 157.79 E-value: 5.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 10 QAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAY-------------SHEVITILGEIdfmlgnLP 76
Cdd:cd07147 32 KAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARgevaraidtfriaAEEATRIYGEV------LP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 77 ELASARPAKKnlltmmdEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELL-PQYL 155
Cdd:cd07147 106 LDISARGEGR-------QGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaETGL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 156 DQDLYAIVNGGIPETTELLK-QRFDHILYTGNTAVG-KIVMEAAAKHltpVTLELGGKSPCYIDRDCDLDVACRRIAWGK 233
Cdd:cd07147 179 PKGAFSVLPCSRDDADLLVTdERIKLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 234 YMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK-----GQKIAFGGEMD 307
Cdd:cd07147 256 FYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALkTGDPKDDATDVGPMISESEAERVEGWVNeavdaGAKLLTGGKRD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 308 EATryLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGND 387
Cdd:cd07147 336 GAL--LEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIND 413
|
410 420
....*....|....*....|.
gi 568971250 388 ViMHFTVNSLPFGGVGASGMG 408
Cdd:cd07147 414 V-PTFRVDHMPYGGVKDSGIG 433
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
95-419 |
5.53e-42 |
|
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: 155.73 E-value: 5.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 95 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTEL 173
Cdd:cd07142 135 VYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 174 LKQRF--DHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07142 215 IASHMdvDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVH 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 251 ASLQNQIVQKIKE-----TVKDFYGENIKASPDyeriINLRHFKRLQSLLK-----GQKIAFGGE-MDEATRYLAPTILT 319
Cdd:cd07142 295 ESIYDEFVEKAKAralkrVVGDPFRKGVEQGPQ----VDKEQFEKILSYIEhgkeeGATLITGGDrIGSKGYYIQPTIFS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 320 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGN--DVimhFTVnSL 397
Cdd:cd07142 371 DVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDV---FDA-SI 446
|
330 340
....*....|....*....|..
gi 568971250 398 PFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07142 447 PFGGYKMSGIGREKGIYALNNY 468
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
9-423 |
7.62e-42 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 155.66 E-value: 7.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSR-----PLRFRLQQLEALRRMVQEREKEILAAIAADLSKSeLNAYSHEVITILGEIDFMLGnLPELASARp 83
Cdd:PLN02467 55 RKAFKRNKGKdwartTGAVRAKYLRAIAAKITERKSELAKLETLDCGKP-LDEAAWDMDDVAGCFEYYAD-LAEALDAK- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 84 AKKNLLTMMDE--AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAE------LLPQYL 155
Cdd:PLN02467 132 QKAPVSLPMETfkGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADicrevgLPPGVL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 156 DqdlyaIVNGGIPETTELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGK 233
Cdd:PLN02467 212 N-----VVTGLGTEAGAPLAShpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGC 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 234 YMNCGQTCIAPDYILCEASLQNQIVQKIKETVKdfygeNIKASPDYER------IINLRHFKRLQSLL-----KGQKIAF 302
Cdd:PLN02467 287 FWTNGQICSATSRLLVHERIASEFLEKLVKWAK-----NIKISDPLEEgcrlgpVVSEGQYEKVLKFIstaksEGATILC 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 303 GGEMDEATR---YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETS 379
Cdd:PLN02467 362 GGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQ 441
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 568971250 380 SGGVTGNDVIMHFTvnSLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:PLN02467 442 AGIVWINCSQPCFC--QAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
94-409 |
7.95e-42 |
|
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: 155.10 E-value: 7.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 94 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQyldqdlyaivnGGIPETT-- 171
Cdd:cd07097 128 EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEE-----------AGLPAGVfn 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 172 -----------ELLK-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQ 239
Cdd:cd07097 197 lvmgsgsevgqALVEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 240 TCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGE-MDEATR- 311
Cdd:cd07097 277 RCTASSRLIVTEGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIeiarsEGAKLVYGGErLKRPDEg 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 312 -YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGN--DV 388
Cdd:cd07097 357 yYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlpTA 436
|
330 340
....*....|....*....|.
gi 568971250 389 IMHFTVnslPFGGVGASGMGA 409
Cdd:cd07097 437 GVDYHV---PFGGRKGSSYGP 454
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
95-408 |
4.42e-41 |
|
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: 153.37 E-value: 4.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 95 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGgipeTTEL 173
Cdd:cd07113 136 AFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNG----KGAV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 174 LKQRFDH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYIL 248
Cdd:cd07113 212 GAQLISHpdvakVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 249 CEASLQNQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGE-MDEATRYLAPTILTDV 321
Cdd:cd07113 292 VHRSKFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEaLAGEGYFVQPTLVLAR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 322 DPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNdviMHFTVN-SLPFG 400
Cdd:cd07113 372 SADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDpAVPFG 448
|
....*...
gi 568971250 401 GVGASGMG 408
Cdd:cd07113 449 GMKQSGIG 456
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
96-417 |
1.19e-40 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 151.99 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 96 YVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVNGGIPETTELL- 174
Cdd:PRK13473 133 MIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALv 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 175 -KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASL 253
Cdd:PRK13473 213 gHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGI 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 254 QNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSL------LKGQKIAFGGEM-DEATRYLAPTILTDVDPNS 325
Cdd:PRK13473 293 YDDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFverakaLGHIRVVTGGEApDGKGYYYEPTLLAGARQDD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 326 KVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMhfTVNSLPFGGVGAS 405
Cdd:PRK13473 373 EIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQS 450
|
330
....*....|....*.
gi 568971250 406 GmgayHGK----YSFD 417
Cdd:PRK13473 451 G----YGKdmslYGLE 462
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
9-409 |
1.24e-40 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 152.76 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKS--ELNAYSHEVItilgeiDF-------MLGNLPELA 79
Cdd:cd07124 79 RAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNwaEADADVAEAI------DFleyyareMLRLRGFPV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 80 SARPAKKNLLTMmdeayvqpEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyldqdl 159
Cdd:cd07124 153 EMVPGEDNRYVY--------RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEIL-------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 160 yaiVNGGIP---------ETTELLKQRFDH-----ILYTGNTAVGKIVMEAAAK------HLTPVTLELGGKSPCYIDRD 219
Cdd:cd07124 217 ---EEAGLPpgvvnflpgPGEEVGDYLVEHpdvrfIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 220 CDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLL--- 295
Cdd:cd07124 294 ADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALkVGDPEDPEVYMGPVIDKGARDRIRRYIeig 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 296 -KGQKIAFGGE-MDEATR--YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLI 371
Cdd:cd07124 374 kSEGRLLLGGEvLELAAEgyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHL 453
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 568971250 372 KRVIDETSSG------GVTGNDVIMHftvnslPFGGVGASGMGA 409
Cdd:cd07124 454 ERARREFEVGnlyanrKITGALVGRQ------PFGGFKMSGTGS 491
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
1-408 |
2.09e-39 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 148.80 E-value: 2.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 1 MERQVLRLRQAFRSG-------RSR-PLRFRLQQLealrrmvQEREKEILAAIAADLSKS--ELNAYSHEVITI------ 64
Cdd:cd07140 45 VDRAVAAAKEAFENGewgkmnaRDRgRLMYRLADL-------MEEHQEELATIESLDSGAvyTLALKTHVGMSIqtfryf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 65 LGEIDFMLGNLPELASARPaKKNLltmmdeAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTA 144
Cdd:cd07140 118 AGWCDKIQGKTIPINQARP-NRNL------TLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 145 KILAELlpqyldqdlyaIVNGGIPE--------TTELLKQRF-DH-----ILYTGNTAVGKIVMEAAAK-HLTPVTLELG 209
Cdd:cd07140 191 LKFAEL-----------TVKAGFPKgvinilpgSGSLVGQRLsDHpdvrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 210 GKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHF 288
Cdd:cd07140 260 GKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 289 KRL-----QSLLKGQKIAFGG-EMDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKN--VDEAINFINDREKPLA 360
Cdd:cd07140 340 DKLveyceRGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLA 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 568971250 361 LYVFSRNNKLIKRVIDETSSGGVTGNdvIMHFTVNSLPFGGVGASGMG 408
Cdd:cd07140 420 SGVFTKDINKALYVSDKLEAGTVFVN--TYNKTDVAAPFGGFKQSGFG 465
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
2-408 |
6.99e-39 |
|
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: 146.94 E-value: 6.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRS--RPLRFrlqqlEALRRMVQE-REKeiLAAIAADLSKselnayshEVITIL----GEI------ 68
Cdd:cd07086 38 EAAVAAAREAFKEWRKvpAPRRG-----EIVRQIGEAlRKK--KEALGRLVSL--------EMGKILpeglGEVqemidi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 69 -DFMLG-----NLPELASARPAKKnlltMMDeayvQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSE---- 138
Cdd:cd07086 103 cDYAVGlsrmlYGLTIPSERPGHR----LME----QWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSEttpl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 139 LSENTAKILAELLPQY-LDQDLYAIVNGGiPETTELLK--QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCY 215
Cdd:cd07086 175 TAIAVTKILAEVLEKNgLPPGVVNLVTGG-GDGGELLVhdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAII 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 216 IDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSL 294
Cdd:cd07086 254 VMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 295 LK-----GQKIAFGGEM---DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSR 366
Cdd:cd07086 334 IEiaksqGGTVLTGGKRidgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTE 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 568971250 367 NNKLIKRVIDETSS--------GGVTGNDVimhftvnSLPFGGVGASGMG 408
Cdd:cd07086 414 DLREAFRWLGPKGSdcgivnvnIPTSGAEI-------GGAFGGEKETGGG 456
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
95-420 |
1.31e-38 |
|
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: 146.34 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 95 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL-------------LPQYLDQDLYA 161
Cdd:cd07141 139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLikeagfppgvvnvVPGYGPTAGAA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 162 IVNggipettellKQRFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQT 240
Cdd:cd07141 219 ISS----------HPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQC 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 241 CIAPDYILCEASLQNQIVQKI-----KETVKDFYGENIKASPDyeriINLRHFKRLQSLLK-----GQKIAFGGE-MDEA 309
Cdd:cd07141 289 CCAGSRTFVQESIYDEFVKRSverakKRVVGNPFDPKTEQGPQ----IDEEQFKKILELIEsgkkeGAKLECGGKrHGDK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 310 TRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNnklIKRVIdeTSSGGVTGNDVI 389
Cdd:cd07141 365 GYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD---IDKAI--TFSNALRAGTVW 439
|
330 340 350
....*....|....*....|....*....|....*
gi 568971250 390 M----HFTVNSlPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07141 440 VncynVVSPQA-PFGGYKMSGNGRELGEYGLQEYT 473
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
94-420 |
1.95e-38 |
|
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: 145.79 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 94 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTE 172
Cdd:cd07082 134 IAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGD 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 173 LL--KQRFDHILYTGNTAVGKIVMEAAAKhlTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07082 214 PLvtHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVH 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 251 ASLQNQIVQKIKE-----TVKDFYGENI-------KASPDYeriinlrhfkrLQSLL-----KGQKIAFGGEMDEATrYL 313
Cdd:cd07082 292 ESVADELVELLKEevaklKVGMPWDNGVditplidPKSADF-----------VEGLIddavaKGATVLNGGGREGGN-LI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 314 APTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHfT 393
Cdd:cd07082 360 YPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQR-G 438
|
330 340
....*....|....*....|....*..
gi 568971250 394 VNSLPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07082 439 PDHFPFLGRKDSGIGTQGIGDALRSMT 465
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
9-420 |
4.05e-38 |
|
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: 144.41 E-value: 4.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSG---RSRPLRFRlqqleALRRMVQ--EREKEILAAIAA--------------DLSKSELNAYSHEVITILGeid 69
Cdd:cd07120 29 RRAFDETdwaHDPRLRAR-----VLLELADafEANAERLARLLAlengkilgearfeiSGAISELRYYAGLARTEAG--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 70 fmlgnlpelASARPAKKNLLTMMDEayvqpePLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAE 149
Cdd:cd07120 101 ---------RMIEPEPGSFSLVLRE------PMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 150 LLPQ--YLDQDLYAIVNGGIPETTELL--KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVA 225
Cdd:cd07120 166 ILAEipSLPAGVVNLFTESGSEGAAHLvaSPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 226 CRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKEtvkdfYGENIKASPDYER------IINLRHFKRLQSLLK--- 296
Cdd:cd07120 246 LPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAA-----RLAAVKVGPGLDPasdmgpLIDRANVDRVDRMVErai 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 297 ---GQKIAFGGEMDEATR---YLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKL 370
Cdd:cd07120 321 aagAEVVLRGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLAR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 568971250 371 IKRVIDETSSGGVTGNDVIMHFtvNSLPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07120 401 AMRVARAIRAGTVWINDWNKLF--AEAEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
94-421 |
1.03e-37 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 144.19 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 94 EAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTE 172
Cdd:PLN02766 151 QGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGFGPTAGA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 173 LLKQRFD--HILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILC 249
Cdd:PLN02766 231 AIASHMDvdKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 250 EASLQNQIVQKIKETVKDF-----YGENIKASP-----DYERIIN-LRHFKRL-QSLLKGQKIAFggemdEATRYLAPTI 317
Cdd:PLN02766 311 QEGIYDEFVKKLVEKAKDWvvgdpFDPRARQGPqvdkqQFEKILSyIEHGKREgATLLTGGKPCG-----DKGYYIEPTI 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 318 LTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNdviMHFTV-NS 396
Cdd:PLN02766 386 FTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYFAFdPD 462
|
330 340
....*....|....*....|....*
gi 568971250 397 LPFGGVGASGMGAYHGKYSFDTFSH 421
Cdd:PLN02766 463 CPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
100-406 |
4.90e-37 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 142.38 E-value: 4.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 100 EPLGVVLIIGAWNYPFVL----TMQPLVGAIAAGNaaivKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELL 174
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAImagmTLAAIVAGNTVLL----KPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 175 ----KQRFdhILYTGNTAVGKIVMEAAAK------HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAP 244
Cdd:PRK03137 246 vdhpKTRF--ITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSAC 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 245 DYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKR-LQSLLKGQ---KIAFGGEMDEATRY-LAPTILT 319
Cdd:PRK03137 324 SRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKiMSYIEIGKeegRLVLGGEGDDSKGYfIQPTIFA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 320 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSG------GVTGNDVIMHft 393
Cdd:PRK03137 404 DVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGnlyfnrGCTGAIVGYH-- 481
|
330
....*....|...
gi 568971250 394 vnslPFGGVGASG 406
Cdd:PRK03137 482 ----PFGGFNMSG 490
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
97-419 |
5.45e-37 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 141.97 E-value: 5.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 97 VQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPET-TELL 174
Cdd:PRK11241 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVgGELT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 175 KQRFDHIL-YTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASL 253
Cdd:PRK11241 222 SNPLVRKLsFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 254 QNQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQ-----SLLKGQKIAFGGEMDE-ATRYLAPTILTDVDPNSK 326
Cdd:PRK11241 302 YDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPANAK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 327 VMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVnsLPFGGVGASG 406
Cdd:PRK11241 382 VAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV--APFGGIKASG 459
|
330
....*....|...
gi 568971250 407 MGAYHGKYSFDTF 419
Cdd:PRK11241 460 LGREGSKYGIEDY 472
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
95-420 |
8.82e-35 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 135.79 E-value: 8.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 95 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTEL 173
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 174 LKQR--FDHILYTGNTAVGKIVM-EAAAKHLTPVTLELGGKSPCYIDRDC-DLDVACRRIAWGKYMNCGQTCIAPDYILC 249
Cdd:PRK09847 231 LSRHndIDAIAFTGSTRTGKQLLkDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 250 EASLQNQIVQKIKETVKDFY-GENIKASPDYERIINLRHFKRLQSLL-----KGQKIAFGGEMDEATrYLAPTILTDVDP 323
Cdd:PRK09847 311 EESIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIregesKGQLLLDGRNAGLAA-AIGPTIFVDVDP 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 324 NSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGV---TGNDVIMhftvnSLPFG 400
Cdd:PRK09847 390 NASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVfvnNYNDGDM-----TVPFG 464
|
330 340
....*....|....*....|
gi 568971250 401 GVGASGMGAYHGKYSFDTFS 420
Cdd:PRK09847 465 GYKQSGNGRDKSLHALEKFT 484
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
100-419 |
3.54e-34 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 134.94 E-value: 3.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 100 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELLKQRF 178
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASHM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 179 --DHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQN 255
Cdd:PLN02466 274 dvDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 256 QIVQK-----IKETVKDFYGENIKASPDyeriINLRHFKRLQSLLK-----GQKIAFGGE-MDEATRYLAPTILTDVDPN 324
Cdd:PLN02466 354 EFVEKakaraLKRVVGDPFKKGVEQGPQ----IDSEQFEKILRYIKsgvesGATLECGGDrFGSKGYYIQPTVFSNVQDD 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 325 SKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGN--DVimhFTVnSLPFGGV 402
Cdd:PLN02466 430 MLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDV---FDA-AIPFGGY 505
|
330
....*....|....*..
gi 568971250 403 GASGMGAYHGKYSFDTF 419
Cdd:PLN02466 506 KMSGIGREKGIYSLNNY 522
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
9-419 |
6.19e-34 |
|
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: 133.41 E-value: 6.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYShEVITILGEIDFMLGnLPELASARPAKkNL 88
Cdd:cd07085 48 KAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARG-DVLRGLEVVEFACS-IPHLLKGEYLE-NV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 89 LTMMDeAYVQPEPLGVVLIIGAWNYP-----------------FVLtmqplvgaiaagnaaivKPSELSENTAKILAELL 151
Cdd:cd07085 125 ARGID-TYSYRQPLGVVAGITPFNFPamiplwmfpmaiacgntFVL-----------------KPSERVPGAAMRLAELL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 152 PQY-LDQDLYAIVNGGIPETTELLkqrfDH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVA 225
Cdd:cd07085 187 QEAgLPDGVLNVVHGGKEAVNALL----DHpdikaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 226 CRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLkGQKIAFGG 304
Cdd:cd07085 263 ANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLkVGAGDDPGADMGPVISPAAKERIEGLI-ESGVEEGA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 305 EM--D---------EATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKR 373
Cdd:cd07085 342 KLvlDgrgvkvpgyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARK 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 568971250 374 VIDETSSGGVTGNDVI-----MHftvnslPFGGVGASGMGAYH--GKYSFDTF 419
Cdd:cd07085 422 FQREVDAGMVGINVPIpvplaFF------SFGGWKGSFFGDLHfyGKDGVRFY 468
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
9-406 |
2.06e-32 |
|
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: 128.16 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPElasaRPAKKNL 88
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQT-EVAAMAGKIDISIKAYHE----RTGERAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 89 LTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELL-PQYLDQDLYAIVNGGI 167
Cdd:cd07095 85 PMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPGVLNLVQGGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 168 PETTELLKQ-RFDHILYTGNTAVGKIVMEAAAKHltP---VTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTC-- 241
Cdd:cd07095 165 ETGEALAAHeGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCtc 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 242 ----IAPDYILCEASLQnQIVQKIKETVKD-------FYGENI--KASPDYERIINLRHFKRLQSLLKGQKiafggeMDE 308
Cdd:cd07095 243 arrlIVPDGAVGDAFLE-RLVEAAKRLRIGapdaeppFMGPLIiaAAAARYLLAQQDLLALGGEPLLAMER------LVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 309 ATRYLAPTILtDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDV 388
Cdd:cd07095 316 GTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRP 394
|
410
....*....|....*...
gi 568971250 389 IMhFTVNSLPFGGVGASG 406
Cdd:cd07095 395 TT-GASSTAPFGGVGLSG 411
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
9-413 |
2.87e-32 |
|
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: 128.67 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSelnayshevITILGEIDFMLGNLPELASARPAKKnl 88
Cdd:cd07111 69 RTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKP---------IRESRDCDIPLVARHFYHHAGWAQL-- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 89 ltmMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGI 167
Cdd:cd07111 138 ---LDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 168 PETTELLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDY 246
Cdd:cd07111 215 SFGSALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 247 ILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLK------GQKIAFGGEMDEATRYLAPTILT 319
Cdd:cd07111 295 LLVQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEegraegADVFQPGADLPSKGPFYPPTLFT 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 320 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMhFTVNSlPF 399
Cdd:cd07111 375 NVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNL-FDAAA-GF 452
|
410
....*....|....
gi 568971250 400 GGVGASGMGAYHGK 413
Cdd:cd07111 453 GGYRESGFGREGGK 466
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
11-412 |
5.72e-31 |
|
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: 125.00 E-value: 5.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 11 AFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAySHEVITILGEIDFMLGNLPELASARPAKKNLLT 90
Cdd:cd07083 67 AFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA-IDDVAEAIDFIRYYARAALRLRYPAVEVVPYPG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 91 MMDEAYVQPepLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNGGIPE 169
Cdd:cd07083 146 EDNESFYVG--LGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVVQFLPGVGEE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 170 TTELL--KQRFDHILYTGNTAVGKIVMEAAAKHLT------PVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTC 241
Cdd:cd07083 224 VGAYLteHERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKC 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 242 IAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLKGQK----IAFGGEMDEATRY-LAP 315
Cdd:cd07083 304 SAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKnegqLVLGGKRLEGEGYfVAP 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 316 TILTDVDPNSKVMQEEIFGPILPIVSVKNVD--EAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFT 393
Cdd:cd07083 384 TVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGAL 463
|
410
....*....|....*....
gi 568971250 394 VNSLPFGGVGASGMGAYHG 412
Cdd:cd07083 464 VGVQPFGGFKLSGTNAKTG 482
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
1-408 |
7.55e-31 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 124.20 E-value: 7.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 1 MERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPELAS 80
Cdd:PRK13968 31 IENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-EVAKSANLCDWYAEHGPAMLK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 81 ARPAkknlLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELlpqYLDQDLY 160
Cdd:PRK13968 110 AEPT----LVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQV---FKDAGIP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 161 AIVNGGIPETTELLKQ-----RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYM 235
Cdd:PRK13968 183 QGVYGWLNADNDGVSQmindsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 236 NCGQTCIAPDYILCEASLQNQIVQKIKETVKDFygeNIKASPDYERII------NLR---HFKRLQSLLKGQKIAFGGE- 305
Cdd:PRK13968 263 NTGQVCAAAKRFIIEEGIASAFTERFVAAAAAL---KMGDPRDEENALgpmarfDLRdelHHQVEATLAEGARLLLGGEk 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 306 MDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVtg 385
Cdd:PRK13968 340 IAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGV-- 417
|
410 420
....*....|....*....|....*
gi 568971250 386 ndVIMHFTVNS--LPFGGVGASGMG 408
Cdd:PRK13968 418 --FINGYCASDarVAFGGVKKSGFG 440
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
93-408 |
2.19e-30 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 123.45 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 93 DEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVNG-GipET 170
Cdd:PRK13252 134 SFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVVQGdG--RV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 171 TELLKQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYIL 248
Cdd:PRK13252 212 GAWLTEhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVF 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 249 CEASLQNQIVQKIKETVK-----DFYGENIKASPdyerIINLRHFKRLQS-----------LLKGQKIAFGGEMDEATrY 312
Cdd:PRK13252 292 VQKSIKAAFEARLLERVEririgDPMDPATNFGP----LVSFAHRDKVLGyiekgkaegarLLCGGERLTEGGFANGA-F 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 313 LAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVtgndvimhf 392
Cdd:PRK13252 367 VAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGIC--------- 437
|
330 340
....*....|....*....|...
gi 568971250 393 TVNS-------LPFGGVGASGMG 408
Cdd:PRK13252 438 WINTwgespaeMPVGGYKQSGIG 460
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
79-408 |
6.76e-29 |
|
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: 118.71 E-value: 6.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 79 ASARPAKKNLLTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL 155
Cdd:cd07116 111 AGCIRAQEGSISEIDEntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 156 DQDLYAIVNGGIPETTELL--KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSP-CYIDRDCDLDVA-CRRIAW 231
Cdd:cd07116 191 PPGVVNVVNGFGLEAGKPLasSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPnIFFADVMDADDAfFDKALE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 232 GKYM---NCGQTCIAPDYILCEASLQNQIVQKIKETVKDFygenIKASP-DYERII----NLRHFKRLQSLLK-----GQ 298
Cdd:cd07116 271 GFVMfalNQGEVCTCPSRALIQESIYDRFMERALERVKAI----KQGNPlDTETMIgaqaSLEQLEKILSYIDigkeeGA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 299 KIAFGGEMDEATR------YLAPTILTdvDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIK 372
Cdd:cd07116 347 EVLTGGERNELGGllgggyYVPTTFKG--GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAY 424
|
330 340 350
....*....|....*....|....*....|....*.
gi 568971250 373 RVIDETSSGGVTGNdvIMHFTVNSLPFGGVGASGMG 408
Cdd:cd07116 425 RMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIG 458
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
2-416 |
3.69e-26 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 110.60 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSeLNAYSHEVITILGEIDFMLGNLPELASA 81
Cdd:PRK09406 26 DAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LASAKAEALKCAKGFRYYAEHAEALLAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 82 RPAKKNLLTMmDEAYVQPEPLGVVLIIGAWNYPFVLTMQplvgaiaagnaaIVKPSELSENTAkIL--AELLPQ---YLd 156
Cdd:PRK09406 105 EPADAAAVGA-SRAYVRYQPLGVVLAVMPWNFPLWQVVR------------FAAPALMAGNVG-LLkhASNVPQtalYL- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 157 QDLYAivNGGIPE---TTELL----------KQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLD 223
Cdd:PRK09406 170 ADLFR--RAGFPDgcfQTLLVgsgaveailrDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 224 VACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKE-----TVKDFYGENIKASP--------DYERIINlrhfkr 290
Cdd:PRK09406 248 RAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVArmaalRVGDPTDPDTDVGPlateqgrdEVEKQVD------ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 291 lQSLLKGQKIAFGGE-MDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNK 369
Cdd:PRK09406 322 -DAVAAGATILCGGKrPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 568971250 370 LIKRVIDETSSGGVTGNDviMHFTVNSLPFGGVGASGMG---AYHGKYSF 416
Cdd:PRK09406 401 EQERFIDDLEAGQVFING--MTVSYPELPFGGVKRSGYGrelSAHGIREF 448
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
95-408 |
4.80e-24 |
|
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: 104.42 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 95 AYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQyldqdlyaivnGGIPE----- 169
Cdd:cd07148 118 AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHE-----------AGLPEgwcqa 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 170 ------TTELL--KQRFDHILYTGNTAVGKIVMEAAAKHlTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTC 241
Cdd:cd07148 187 vpcenaVAEKLvtDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVC 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 242 IAPDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRL-----QSLLKGQKIAFGGEMDEATRYlAP 315
Cdd:cd07148 266 VSVQRVFVPAEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVeewvnEAVAAGARLLCGGKRLSDTTY-AP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 316 TILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDvimH--FT 393
Cdd:cd07148 345 TVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND---HtaFR 421
|
330
....*....|....*
gi 568971250 394 VNSLPFGGVGASGMG 408
Cdd:cd07148 422 VDWMPFAGRRQSGYG 436
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
1-411 |
1.81e-23 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 103.04 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 1 MERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSH-----EVITILGEID-FMLGN 74
Cdd:TIGR01722 40 VDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDvarglEVVEHACGVNsLLKGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 75 LPElasarpakkNLLTMMDeAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY 154
Cdd:TIGR01722 120 TST---------QVATRVD-VYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 155 -LDQDLYAIVNGGIPETTELLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWG 232
Cdd:TIGR01722 190 gAPDGVLNVVHGDKEAVDRLLEHpDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 233 KYMNCGQTCIAPDYILCEASLQnQIVQKIKETVKDF-YGENIKASPDYERIINLRHFKRLQSLLkGQKIAFGGEM----- 306
Cdd:TIGR01722 270 AYGAAGQRCMAISAAVLVGAAD-EWVPEIRERAEKIrIGPGDDPGAEMGPLITPQAKDRVASLI-AGGAAEGAEVlldgr 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 307 ------DEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSS 380
Cdd:TIGR01722 348 gykvdgYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEV 427
|
410 420 430
....*....|....*....|....*....|.
gi 568971250 381 GGVtGNDVIMHFTVNSLPFGGVGASGMGAYH 411
Cdd:TIGR01722 428 GQV-GVNVPIPVPLPYFSFTGWKDSFFGDHH 457
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
2-367 |
3.28e-23 |
|
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: 101.90 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRFR---LQQL-EALRRmvqerEKEILAAIAadlskselnaySHEVITI----LGEI----- 68
Cdd:cd07130 37 ESTIKAAQEAFKEWRDVPAPKRgeiVRQIgDALRK-----KKEALGKLV-----------SLEMGKIlpegLGEVqemid 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 69 --DFMLG-----NLPELASARPAKKnlltMMDeayvQPEPLGVVLIIGAWNYP-------FVLTMqplvgaiAAGNAAIV 134
Cdd:cd07130 101 icDFAVGlsrqlYGLTIPSERPGHR----MME----QWNPLGVVGVITAFNFPvavwgwnAAIAL-------VCGNVVVW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 135 KPSELSENTA----KILAELLPQY-LDQDLYAIVNGGIPETTELLK-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLEL 208
Cdd:cd07130 166 KPSPTTPLTAiavtKIVARVLEKNgLPGAIASLVCGGADVGEALVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 209 GGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILceasLQNQIVQKIKETVKDFY-----GENIKASPDYERII 283
Cdd:cd07130 246 GGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLI----VHESIYDEVLERLKKAYkqvriGDPLDDGTLVGPLH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 284 NLRHFKRLQSLLK-----GQKIAFGGE-MDEATRYLAPTILTdVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREK 357
Cdd:cd07130 322 TKAAVDNYLAAIEeaksqGGTVLFGGKvIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQ 400
|
410
....*....|
gi 568971250 358 PLALYVFSRN 367
Cdd:cd07130 401 GLSSSIFTTD 410
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
19-409 |
2.10e-18 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 87.50 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 19 PLRFRLQQLEALRRMVQEREKEILAAIAADLSKS------------ELNAYS-HEVITILGEIDFMLGNlpelaSARPAK 85
Cdd:PLN00412 73 PLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPakdavtevvrsgDLISYTaEEGVRILGEGKFLVSD-----SFPGNE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 86 KNLLTMMDEAyvqpePLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYAIVN 164
Cdd:PLN00412 148 RNKYCLTSKI-----PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAgFPKGLISCVT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 165 GGIPETTELLKQR--FDHILYTGNTAVGKIVMEAAakhLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCI 242
Cdd:PLN00412 223 GKGSEIGDFLTMHpgVNCISFTGGDTGIAISKKAG---MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCT 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 243 APDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLL---KGQKIAFGGEMDEATRYLAPTILT 319
Cdd:PLN00412 300 AVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVmdaKEKGATFCQEWKREGNLIWPLLLD 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 320 DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRN-NKLIkRVIDETSSGGVTGNDVIM----HFtv 394
Cdd:PLN00412 380 NVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDiNKAI-LISDAMETGTVQINSAPArgpdHF-- 456
|
410
....*....|....*
gi 568971250 395 nslPFGGVGASGMGA 409
Cdd:PLN00412 457 ---PFQGLKDSGIGS 468
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
2-409 |
2.32e-18 |
|
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: 87.64 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYShEVitilGE-IDF-------MLG 73
Cdd:cd07125 72 DAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADA-EV----REaIDFcryyaaqARE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 74 NLPELASARP-AKKNLLTMmdeayvqpEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELL- 151
Cdd:cd07125 147 LFSDPELPGPtGELNGLEL--------HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLh 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 152 ----PQYLdqdLYAIVNGGIPETTELLKQ-RFDHILYTGNTAVGKIVMEAAAKH---LTPVTLELGGKSPCYIDRDCDLD 223
Cdd:cd07125 219 eagvPRDV---LQLVPGDGEEIGEALVAHpRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 224 VACRRI---AWGkymNCGQTCIAPDyILCeasLQNQIVQKIKETVKDFY-----GENIKASPDYERIINLRHFKRLQS-- 293
Cdd:cd07125 296 QAVKDVvqsAFG---SAGQRCSALR-LLY---LQEEIAERFIEMLKGAMaslkvGDPWDLSTDVGPLIDKPAGKLLRAht 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 294 -LLKGQ-KIAFGGEMDEAT-RYLAPTILTDVdpNSKVMQEEIFGPILPIVSVK--NVDEAINFINDREKPLALYVFSRNN 368
Cdd:cd07125 369 eLMRGEaWLIAPAPLDDGNgYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDE 446
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 568971250 369 KLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMGA 409
Cdd:cd07125 447 REIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGP 487
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
2-406 |
4.77e-18 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 86.55 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 2 ERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPElasa 81
Cdd:PRK09457 40 DAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAAT-EVTAMINKIAISIQAYHE---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 82 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLY 160
Cdd:PRK09457 115 RTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 161 AIVNGGiPETTELL--KQRFDHILYTGNTAVGKIVMEAAAKHltP---VTLELGGKSPCYIDRDCDLDVACRRIAWGKYM 235
Cdd:PRK09457 195 NLVQGG-RETGKALaaHPDIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 236 NCGQTCIAPDYILCEASLQNQ-IVQKIKETVKdfygeNIKA-SPDYE------RIINLRHFKRLqslLKGQK--IAFGG- 304
Cdd:PRK09457 272 SAGQRCTCARRLLVPQGAQGDaFLARLVAVAK-----RLTVgRWDAEpqpfmgAVISEQAAQGL---VAAQAqlLALGGk 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 305 ---EM---DEATRYLAPTILtDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDET 378
Cdd:PRK09457 344 sllEMtqlQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEI 422
|
410 420
....*....|....*....|....*...
gi 568971250 379 SSGGVTGNDVIMHFTvNSLPFGGVGASG 406
Cdd:PRK09457 423 RAGIVNWNKPLTGAS-SAAPFGGVGASG 449
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
101-409 |
1.48e-15 |
|
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: 78.43 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 101 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQ--YLDQDLYAIVNGGIPETTELLKQ-R 177
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGKTMQALLLHpN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 178 FDHILYTGNTAVGKIVmeAAAKHLTPVTLELGGKSPCYIDRDCD-LDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNq 256
Cdd:cd07084 180 PKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWSK- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 257 ivQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSL--LKGQKIAFGGEMDEATRY-------LAPTILTDVDPN--- 324
Cdd:cd07084 257 --TPLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMenLLGSVLLFSGKELKNHSIpsiygacVASALFVPIDEIlkt 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 325 SKVMQEEIFGPILPIVSVKNVDEA--INFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTV--NSLPFG 400
Cdd:cd07084 335 YELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVapNQNHGG 414
|
....*....
gi 568971250 401 GVGASGMGA 409
Cdd:cd07084 415 GPAADPRGA 423
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
9-421 |
5.33e-15 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 77.48 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 9 RQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYShEVITILGEIDFMLGNLP-ELASARPAKKN 87
Cdd:PLN02419 161 KQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG-DIFRGLEVVEHACGMATlQMGEYLPNVSN 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 88 LLtmmdEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAEL-LPQYLDQDLYAIVNGG 166
Cdd:PLN02419 240 GV----DTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELaMEAGLPDGVLNIVHGT 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 167 IPETTELLK-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPD 245
Cdd:PLN02419 316 NDTVNAICDdEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALS 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 246 YILC---EASLQNQIVQKIKeTVKDFYGENIKAS--PDYERIINLRHFKRLQS--------LLKGQKIAFGGEmdEATRY 312
Cdd:PLN02419 396 TVVFvgdAKSWEDKLVERAK-ALKVTCGSEPDADlgPVISKQAKERICRLIQSgvddgaklLLDGRDIVVPGY--EKGNF 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 313 LAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVtGNDVIMHF 392
Cdd:PLN02419 473 IGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQI-GINVPIPV 551
|
410 420 430
....*....|....*....|....*....|.
gi 568971250 393 TVNSLPFGGVGASGMG--AYHGKYSFDTFSH 421
Cdd:PLN02419 552 PLPFFSFTGNKASFAGdlNFYGKAGVDFFTQ 582
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
60-425 |
1.32e-14 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 76.03 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 60 EVITILGEIDFMLG-----NLPELASARPAKknlltMMDEAYvqpEPLGVVLIIGAWNYP-FVLTMQP-LVGAIAAGNAA 132
Cdd:PLN02315 116 EVQEIIDMCDFAVGlsrqlNGSIIPSERPNH-----MMMEVW---NPLGIVGVITAFNFPcAVLGWNAcIALVCGNCVVW 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 133 IVKPSE--LSENTAKILAELLPQY-LDQDLYAIVNGGIPETTELLKQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLEL 208
Cdd:PLN02315 188 KGAPTTplITIAMTKLVAEVLEKNnLPGAIFTSFCGGAEIGEAIAKDtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLEL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 209 GGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILceasLQNQIVQKIKETVKDFYGENIKASP-DYERIINLRH 287
Cdd:PLN02315 268 SGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLL----LHESIYDDVLEQLLTVYKQVKIGDPlEKGTLLGPLH 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 288 -------FKRLQSLLKGQ--KIAFGGEMDEAT-RYLAPTILtDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREK 357
Cdd:PLN02315 344 tpeskknFEKGIEIIKSQggKILTGGSAIESEgNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQ 422
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568971250 358 PLALYVFSRNNKLIKRVIdetssgGVTGND---VIMHFTVNSL----PFGGVGASGMGAYHGKYSFDTFSHQRPC 425
Cdd:PLN02315 423 GLSSSIFTRNPETIFKWI------GPLGSDcgiVNVNIPTNGAeiggAFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
100-412 |
1.51e-13 |
|
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: 72.64 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 100 EPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQyldqdlyaivnGGIPETT-ELL---- 174
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQE-----------AGFPAGTiQLLpgrg 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 175 ---------KQRFDHILYTGNTAVGKIVMEAAAKHL---TPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCI 242
Cdd:TIGR01238 228 advgaaltsDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCS 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 243 APDYILCEASLQNQIVQKIKETVKDF-YGENIKASPDYERIIN-------LRHFKRLQSllKGQKIA-FGGEMDEATRY- 312
Cdd:TIGR01238 308 ALRVLCVQEDVADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDaeakqnlLAHIEHMSQ--TQKKIAqLTLDDSRACQHg 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 313 -LAPTILTDVDpNSKVMQEEIFGPILPIVSVK--NVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVI 389
Cdd:TIGR01238 386 tFVAPTLFELD-DIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQ 464
|
330 340
....*....|....*....|...
gi 568971250 390 MHFTVNSLPFGGVGASGMGAYHG 412
Cdd:TIGR01238 465 VGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
207-406 |
3.55e-11 |
|
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: 65.30 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 207 ELGGKSPCYIDRDCDLD---VACRRIAWGkYmnCGQTCIAPDYILCEASLQNQIVQKIKETVKDfygenIKASPDYE--- 280
Cdd:cd07123 284 ETGGKNFHLVHPSADVDslvTATVRGAFE-Y--QGQKCSAASRAYVPESLWPEVKERLLEELKE-----IKMGDPDDfsn 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 281 ---RIINLRHFKRLQSLLK------GQKIAFGGEMDEATRY-LAPTILTDVDPNSKVMQEEIFGPILpIVSV---KNVDE 347
Cdd:cd07123 356 fmgAVIDEKAFDRIKGYIDhaksdpEAEIIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFGPVL-TVYVypdSDFEE 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568971250 348 AINFINDREkPLALY--VFSRNNKLIKRV------------IDETSSGGVTGNDvimhftvnslPFGGVGASG 406
Cdd:cd07123 435 TLELVDTTS-PYALTgaIFAQDRKAIREAtdalrnaagnfyINDKPTGAVVGQQ----------PFGGARASG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
285-408 |
3.90e-08 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 55.98 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 285 LRHFKRLQsllKGQKIAFGGEMDEATR---YLAPTI--LTDVDpnskVMQEEIFGPILPIVSVK--NVDEAINFINDREK 357
Cdd:PRK11904 882 DAHIERMK---REARLLAQLPLPAGTEnghFVAPTAfeIDSIS----QLEREVFGPILHVIRYKasDLDKVIDAINATGY 954
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568971250 358 PLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMG 408
Cdd:PRK11904 955 GLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
101-408 |
1.17e-07 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 54.59 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 101 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTA----KILAE---------LLPqyldqdlyaivngGI 167
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAaqavRILLEagvpagvvqLLP-------------GR 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 168 PET--TELLK-QRFDHILYTGNTAVGKIVMEAAAKHL------TPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCG 238
Cdd:PRK11809 835 GETvgAALVAdARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAG 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 239 QTCIAPDyILCeasLQNQIVQKIKETVKDFYGENIKASPDY-----------ERIINL-RHFKRLQSllKGQKIaFGGEM 306
Cdd:PRK11809 915 QRCSALR-VLC---LQDDVADRTLKMLRGAMAECRMGNPDRlstdigpvidaEAKANIeRHIQAMRA--KGRPV-FQAAR 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 307 DEATR-----YLAPTI--LTDVDPnskvMQEEIFGPILPIVSVK--NVDEAINFINDREKPLALYVFSRNNKLIKRVIDE 377
Cdd:PRK11809 988 ENSEDwqsgtFVPPTLieLDSFDE----LKREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGS 1063
|
330 340 350
....*....|....*....|....*....|.
gi 568971250 378 TSSGGVTGNDVIMHFTVNSLPFGGVGASGMG 408
Cdd:PRK11809 1064 AHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
285-408 |
2.25e-05 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 47.24 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 285 LRHFKRLQSllKGQKIaFGGEMDEATR---YLAPTI--LTDVDpnskVMQEEIFGPILPIVSVK--NVDEAINFINDREK 357
Cdd:COG4230 878 EAHIERMRA--EGRLV-HQLPLPEECAngtFVAPTLieIDSIS----DLEREVFGPVLHVVRYKadELDKVIDAINATGY 950
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 358 PLALYVFSRNNKLIKRVIDETSsggvTGNdvimhFTVN---------SLPFGGVGASGMG 408
Cdd:COG4230 951 GLTLGVHSRIDETIDRVAARAR----VGN-----VYVNrniigavvgVQPFGGEGLSGTG 1001
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
167-349 |
1.17e-04 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 44.40 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 167 IPETTELLKQR-FDHILYTGNTAVGKivmeAAAKHLTPVtleLG---GKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCi 242
Cdd:cd07122 167 IELTQELMKHPdVDLILATGGPGMVK----AAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTIC- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 243 apdyilceASLQNQIVQK-IKETVKdfygENIKASPDYerIINLRHFKRLQSLL--------------KGQKIA--FGGE 305
Cdd:cd07122 239 --------ASEQSVIVDDeIYDEVR----AELKRRGAY--FLNEEEKEKLEKALfddggtlnpdivgkSAQKIAelAGIE 304
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568971250 306 MDEATRYLAPTIlTDVDPNSKVMQEEIFgPILPIVSVKNVDEAI 349
Cdd:cd07122 305 VPEDTKVLVAEE-TGVGPEEPLSREKLS-PVLAFYRAEDFEEAL 346
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
299-408 |
1.20e-04 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 44.86 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 299 KIAFGGEMDEATrYLAPTILtDVDpNSKVMQEEIFGPILPIVSVK--NVDEAINFINDREKPLALYVFSRNNKLIKRVID 376
Cdd:PRK11905 889 QLPLPAETEKGT-FVAPTLI-EID-SISDLEREVFGPVLHVVRFKadELDRVIDDINATGYGLTFGLHSRIDETIAHVTS 965
|
90 100 110
....*....|....*....|....*....|..
gi 568971250 377 ETSSGGVTGNDVIMHFTVNSLPFGGVGASGMG 408
Cdd:PRK11905 966 RIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTG 997
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
301-429 |
7.31e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 41.81 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 301 AFGGEMDEATRylapTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINfindrekpLALYV----------FSRN-NK 369
Cdd:PRK15398 334 AAGINVPKDTR----LLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIA--------LAVKLehgnrhtaimHSRNvDN 401
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568971250 370 LIK--RVIDETssggvtgndvImhFTVNSLPFGGVGASGMGAY---------HGKYSFDTFSHQRPCLLKG 429
Cdd:PRK15398 402 LNKmaRAIQTS----------I--FVKNGPSYAGLGLGGEGFTtftiatptgEGVTSARTFTRRRRCVLVD 460
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
101-409 |
1.34e-03 |
|
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: 40.94 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 101 PLGVVLIIGAWNYPFVLTMQPLVGAIAAGnaaiVKPSELSENTAKILAELLPQYL--------DQDLyaiVNGGIPETTE 172
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMG----NKPLLKVDSKVSVVMEQFLRLLhlcgmpatDVDL---IHSDGPTMNK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 173 LLKQ-RFDHILYTGNTAV---------GKIVMEAAA---KHLTPVTLELGgkspcYIDRDCDLDVacrriawgkYMNCGQ 239
Cdd:cd07126 215 ILLEaNPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQDA---------YACSGQ 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 240 TCIAPDYILC-EASLQNQIVQKIKETVKDFYGENIKASP----DYERIINlrHFKRLQSlLKGQKIAFGGEmdEATRYLA 314
Cdd:cd07126 281 KCSAQSILFAhENWVQAGILDKLKALAEQRKLEDLTIGPvltwTTERILD--HVDKLLA-IPGAKVLFGGK--PLTNHSI 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 315 PTILTDVDP--------------NSKVMQEEIFGPILPIVSVKNVDEainfindrekPLALYVFSRnnklikrvIDETSS 380
Cdd:cd07126 356 PSIYGAYEPtavfvpleeiaieeNFELVTTEVFGPFQVVTEYKDEQL----------PLVLEALER--------MHAHLT 417
|
330 340 350
....*....|....*....|....*....|....
gi 568971250 381 GGVTGNDV-----IMHFTVNSLPFGGVGASGMGA 409
Cdd:cd07126 418 AAVVSNDIrflqeVLANTVNGTTYAGIRARTTGA 451
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
317-350 |
2.14e-03 |
|
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: 40.30 E-value: 2.14e-03
10 20 30
....*....|....*....|....*....|....
gi 568971250 317 ILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAIN 350
Cdd:cd07121 316 IIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIE 349
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
289-375 |
6.30e-03 |
|
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: 39.18 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 289 KRLQSLLKGQKIAFGGEMDEATR--------YLAPTILT--DVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKP 358
Cdd:cd07128 345 AAVATLLAEAEVVFGGPDRFEVVgadaekgaFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGS 424
|
90
....*....|....*..
gi 568971250 359 LALYVFSRNNKLIKRVI 375
Cdd:cd07128 425 LVASVVTNDPAFARELV 441
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
82-383 |
8.45e-03 |
|
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: 38.61 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 82 RPAKKNLLTMMDEAYvQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELS----ENTAKILAELLPQY-LD 156
Cdd:cd07127 175 KPQGKHDPLAMEKTF-TVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAilplAITVQVAREVLAEAgFD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 157 QDLYAIV--NGGIPETTEL-LKQRFDHILYTGNTAVGKIvMEAAAKHLTPVTlELGGKSPCYIDRDCDLDVACRRIAWGK 233
Cdd:cd07127 254 PNLVTLAadTPEEPIAQTLaTRPEVRIIDFTGSNAFGDW-LEANARQAQVYT-EKAGVNTVVVDSTDDLKAMLRNLAFSL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 234 YMNCGQTCIAPDYILCEAS-LQN--------QIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQS-------LLKG 297
Cdd:cd07127 332 SLYSGQMCTTPQNIYVPRDgIQTddgrksfdEVAADLAAAIDGLLADPARAAALLGAIQSPDTLARIAEarqlgevLLAS 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 298 QKIAFGGEMDEATRylAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFIND--REK-PLALYVFSRNNKLIKRV 374
Cdd:cd07127 412 EAVAHPEFPDARVR--TPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgAMTVGVYSTDPEVVERV 489
|
....*....
gi 568971250 375 IDETSSGGV 383
Cdd:cd07127 490 QEAALDAGV 498
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
172-383 |
9.32e-03 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 38.19 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 172 ELLKQRFDHIL-YTGNTAVgkivmEAAAKHLTPVT--LELGGK-SPCYIDRDCDLDVACRRIA-----WGKymncgQTCI 242
Cdd:pfam05893 164 DLIVANADVVIaWGGEDAI-----NAIRECLKPGKqwIDFGAKiSFAVVDREAALDKAAERAAddicvFDQ-----QACL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568971250 243 APDYILCEASLQNQivqkIKETVKDFYGENIKASPDYER----------IINLRHFKRLQSLLKGQkiaFGGEMDEATRY 312
Cdd:pfam05893 234 SPQTVFVESDDKIT----PDEFAERLAAALAKRARILPKavldideaakISSDRAECKLDYAFAGE---RGVWSDFHQRW 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568971250 313 LapTILTDvdpnskvMQEEIFGPI---LPIVSVKNVDEAINFIN---DREKPLALYVFSRNnklIKRVIDETSSGGV 383
Cdd:pfam05893 307 T--VIWSD-------GQEELNSPLnrtVNVVPVPSLSDVVRYVSenrTYLQTCGLAPYSGR---LPYLDRKLALAGV 371
|
|
| |
