|
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: 800.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 5 VQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPEWVTPTPA 84
Cdd:cd07132 4 VRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 85 KKNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLYAVIN 164
Cdd:cd07132 84 KKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 165 GGVEETTELLKHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAP 244
Cdd:cd07132 164 GGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 245 DYVLCEASLQNQIVQKIKETVKEFYGENVKESPDYERIINLRHFKRIQSLLEGQKIAFGGETDEATRYIAPTILTDVDPK 324
Cdd:cd07132 244 DYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 325 SRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNALPFGGVGA 404
Cdd:cd07132 324 DPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGN 403
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 514452363 405 SGMGAYHGKYSFDTFSHHRACLLKSLKREGANKLRYPPNS 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: 691.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 5 VQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPEWVTPTPA 84
Cdd:cd07087 4 VARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 85 KKNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLYAVIN 164
Cdd:cd07087 84 SVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 165 GGVEETTELLKHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAP 244
Cdd:cd07087 164 GGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 245 DYVLCEASLQNQIVQKIKETVKEFYGENVKESPDYERIINLRHFKRIQSLLEGQKIAFGGETDEATRYIAPTILTDVDPK 324
Cdd:cd07087 244 DYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSPD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 325 SRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNALPFGGVGA 404
Cdd:cd07087 324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGN 403
|
410 420
....*....|....*....|..
gi 514452363 405 SGMGAYHGKYSFDTFSHHRACL 426
Cdd:cd07087 404 SGMGAYHGKAGFDTFSHLKSVL 425
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
5-479 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 633.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 5 VQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPEWVTPTPA 84
Cdd:PTZ00381 13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 85 KKNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLYAVIN 164
Cdd:PTZ00381 93 DTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 165 GGVEETTELLKHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAP 244
Cdd:PTZ00381 173 GGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 245 DYVLCEASLQNQIVQKIKETVKEFYGENVKESPDYERIINLRHFKRIQSLLE--GQKIAFGGETDEATRYIAPTILTDVD 322
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDIENKYVAPTIIVNPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 323 PKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNALPFGGV 402
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514452363 403 GASGMGAYHGKYSFDTFSHHRACLLKSLKREGANKLRYPPNSQSKVNLAKFLL-LKQFSRGKLGLLMLtFLCAVAAVF 479
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSWVLSFLLkLSIPVQSEVLKSRL-FVSALVFVA 489
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
5-452 |
0e+00 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 622.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 5 VQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPEWVTPTPA 84
Cdd:cd07136 4 VEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKPKRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 85 KKNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLYAVIN 164
Cdd:cd07136 84 KTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 165 GGVEETTELLKHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAP 244
Cdd:cd07136 164 GGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 245 DYVLCEASLQNQIVQKIKETVKEFYGENVKESPDYERIINLRHFKRIQSLLEGQKIAFGGETDEATRYIAPTILTDVDPK 324
Cdd:cd07136 244 DYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNVTWD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 325 SRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNALPFGGVGA 404
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGGVGN 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 514452363 405 SGMGAYHGKYSFDTFSHHRACLLKSLKREgaNKLRYPPNSQSKVNLAK 452
Cdd:cd07136 404 SGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPPYKGKKKKLKK 449
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
2-424 |
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: 583.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPEWVTP 81
Cdd:cd07135 8 DSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAKD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 82 TPAKKNLLT-LLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLY 160
Cdd:cd07135 88 EKVKDGPLAfMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 161 AVINGGVEETTELLKHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQT 240
Cdd:cd07135 168 QVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 241 CIAPDYVLCEASLQNQIVQKIKETVKEFYGENVKESPDYERIINLRHFKRIQSLLE--GQKIAFGGETDEATRYIAPTIL 318
Cdd:cd07135 248 CVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDttKGKVVIGGEMDEATRFIPPTIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 319 TDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNALP 398
Cdd:cd07135 328 SDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAP 407
|
410 420
....*....|....*....|....*.
gi 514452363 399 FGGVGASGMGAYHGKYSFDTFSHHRA 424
Cdd:cd07135 408 FGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| 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: 526.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPEWVTP 81
Cdd:cd07137 2 PRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 82 TPAKKNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLYA 161
Cdd:cd07137 82 EKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 162 VINGGVEETTELLKHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNC-GQT 240
Cdd:cd07137 162 VIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 241 CIAPDYVLCEASLQNQIVQKIKETVKEFYGENVKESPDYERIINLRHFKRIQSLLE----GQKIAFGGETDEATRYIAPT 316
Cdd:cd07137 242 CIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDdpsvADKIVHGGERDEKNLYIEPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 317 ILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNA 396
Cdd:cd07137 322 ILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDT 401
|
410 420 430
....*....|....*....|....*....|
gi 514452363 397 LPFGGVGASGMGAYHGKYSFDTFSHHRACL 426
Cdd:cd07137 402 LPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
23-426 |
9.33e-180 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 510.62 E-value: 9.33e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 23 RLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPEWVTPTPAKKNLLTLLDEVYVQPEPL 102
Cdd:cd07134 22 RIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPLLLFGTKSKIRYEPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 103 GVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLYAVINGGVEETTELLKHRFDHIL 182
Cdd:cd07134 102 GVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAEVAQALLELPFDHIF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 183 YTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIK 262
Cdd:cd07134 182 FTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 263 ETVKEFYGEN--VKESPDYERIINLRHFKRIQSLLE-----GQKIAFGGETDEATRYIAPTILTDVDPKSRVMQEEIFGP 335
Cdd:cd07134 262 AEIEKFYGKDaaRKASPDLARIVNDRHFDRLKGLLDdavakGAKVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 336 VLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNALPFGGVGASGMGAYHGKYS 415
Cdd:cd07134 342 VLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGSYHGVYG 421
|
410
....*....|.
gi 514452363 416 FDTFSHHRACL 426
Cdd:cd07134 422 FKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
6-424 |
1.03e-175 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 500.09 E-value: 1.03e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 6 QRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADL-CKSEFNGFNQEVITVLGEIGFMLANLPEWVTPTPA 84
Cdd:cd07133 5 ERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMKPSRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 85 KKNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLYAVIN 164
Cdd:cd07133 85 HVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAVVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 165 GGVEETTELLKHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAP 244
Cdd:cd07133 165 GGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 245 DYVLCEASLQNQIVQKIKETVKEFYGeNVKESPDYERIINLRHFKRIQSLLE-----GQKI---AFGGETDEATRYIAPT 316
Cdd:cd07133 245 DYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEdarakGARVielNPAGEDFAATRKLPPT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 317 ILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNA 396
Cdd:cd07133 324 LVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVAQDD 403
|
410 420
....*....|....*....|....*...
gi 514452363 397 LPFGGVGASGMGAYHGKYSFDTFSHHRA 424
Cdd:cd07133 404 LPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-469 |
2.35e-158 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 458.04 E-value: 2.35e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 1 MEREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPEWVT 80
Cdd:PLN02203 8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 81 PTPAKKNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLY 160
Cdd:PLN02203 88 PKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 161 AVINGGVEETTELLKHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVD---KDCDLDVVCRRITWGKWMNC 237
Cdd:PLN02203 168 KVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 238 -GQTCIAPDYVLCEASLQNQIVQKIKETVKEFYGENVKESPDYERIINLRHFKRIQSLLEGQKIA----FGGETDEATRY 312
Cdd:PLN02203 248 aGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAasivHGGSIDEKKLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 313 IAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHF 392
Cdd:PLN02203 328 IEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQY 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514452363 393 TLNALPFGGVGASGMGAYHGKYSFDTFSHHRACLLKSLKREgaNKLRYPPNSQSKVNLAKflLLKQFSRGKLGLLML 469
Cdd:PLN02203 408 ACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTE--FEFRYPPWNDFKLGFLR--LVYRFDYFGLLLLLL 480
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
5-455 |
8.07e-140 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 410.98 E-value: 8.07e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 5 VQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPEWVTPTPA 84
Cdd:PLN02174 16 VTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 85 KKNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLYAVIN 164
Cdd:PLN02174 96 KTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 165 GGVEETTELLKHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKW-MNCGQTCIA 243
Cdd:PLN02174 176 GAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACIS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 244 PDYVLCEASLQNQIVQKIKETVKEFYGENVKESPDYERIINLRHFKRIQSLLE----GQKIAFGGETDEATRYIAPTILT 319
Cdd:PLN02174 256 PDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 320 DVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNALPF 399
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPF 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 514452363 400 GGVGASGMGAYHGKYSFDTFSHHRACLLKSLKreGANKLRYPPNSQSKVNLAKFLL 455
Cdd:PLN02174 416 GGVGESGMGAYHGKFSFDAFSHKKAVLYRSLF--GDSAVRYPPYSRGKLRLLKALV 469
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
2-427 |
2.37e-127 |
|
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: 376.93 E-value: 2.37e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSefngfnqeVITVLGEIGFMLANL------ 75
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKP--------IEEALGEVARAADTFryyagl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 76 ---PEWVTPTPAKKNLLTlldevYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLP 152
Cdd:cd07078 73 arrLHGEVIPSPDPGELA-----IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 153 QY-LDQDLYAVINGGVEET-TELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRI 229
Cdd:cd07078 148 EAgLPPGVLNVVTGDGDEVgAALASHpRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 230 TWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEFYGEN-VKESPDYERIINLRHFKRIQSLLE-----GQKIAFG 303
Cdd:cd07078 228 VFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEdakaeGAKLLCG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 304 GETDEAT--RYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSG 381
Cdd:cd07078 308 GKRLEGGkgYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAG 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 514452363 382 GVTVNDVVMHFTLNAlPFGGVGASGMGAYHGKYSFDTFSHHRACLL 427
Cdd:cd07078 388 TVWINDYSVGAEPSA-PFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
9-427 |
4.94e-102 |
|
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: 309.93 E-value: 4.94e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 9 RQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEfngfnqevITVLGEIGFMLANL----------PEW 78
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPI--------EEALGEVARAIDTFryaagladklGGP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 79 VTPTPAKKNLLtlldevYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQ 157
Cdd:cd06534 76 ELPSPDPGGEA------YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 158 DLYAVING-GVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWM 235
Cdd:cd06534 150 GVVNVVPGgGDEVGAALLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 236 NCGQTCIAPDYVLCEASLQNQIVQKIKetvkefygenvkespdyeriinlrhfkriqsllegqkiafggetdeatryiap 315
Cdd:cd06534 230 NAGQICTAASRLLVHESIYDEFVEKLV----------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 316 TILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLN 395
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE 336
|
410 420 430
....*....|....*....|....*....|..
gi 514452363 396 AlPFGGVGASGMGAYHGKYSFDTFSHHRACLL 427
Cdd:cd06534 337 A-PFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
5-421 |
9.88e-96 |
|
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: 297.42 E-value: 9.88e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 5 VQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSefngfnqeVITVLGEIGFMLANLpEW------ 78
Cdd:COG1012 49 VAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKP--------LAEARGEVDRAADFL-RYyagear 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 79 -----VTPTPAKKNLltlldeVYVQPEPLGVVLIIGAWNYPFVLTMHPL----------VGaiaagnaaiiKPSELSENT 143
Cdd:COG1012 120 rlygeTIPSDAPGTR------AYVRREPLGVVGAITPWNFPLALAAWKLapalaagntvVL----------KPAEQTPLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 144 AKILTKLLPQY-LDQDLYAVINGGVEETTE-LLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDC 220
Cdd:COG1012 184 ALLLAELLEEAgLPAGVLNVVTGDGSEVGAaLVAHpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 221 DLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL---- 295
Cdd:COG1012 264 DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIedav 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 296 -EGQKIAFGGE--TDEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIK 372
Cdd:COG1012 344 aEGAELLTGGRrpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARAR 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 514452363 373 RMIDETSSGGVTVNDVVMHFTLNAlPFGGVGASGMGAYHGKYSFDTFSH 421
Cdd:COG1012 424 RVARRLEAGMVWINDGTTGAVPQA-PFGGVKQSGIGREGGREGLEEYTE 471
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
2-420 |
3.73e-82 |
|
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: 261.70 E-value: 3.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHeKDILAAI-----GADLCKSEFNgfNQEVITVLGEIGFMLANLP 76
Cdd:pfam00171 32 DAAIAAARAAFPAWRKTPAAERAAILRKAADLLEER-KDELAELetlenGKPLAEARGE--VDRAIDVLRYYAGLARRLD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 77 EWVTPTPAKKnlltlldEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-L 155
Cdd:pfam00171 109 GETLPSDPGR-------LAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 156 DQDLYAVINGGVEETTE-LLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGK 233
Cdd:pfam00171 182 PAGVLNVVTGSGAEVGEaLVEHpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 234 WMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGGETD 307
Cdd:pfam00171 262 FGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 308 EAT-RYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVN 386
Cdd:pfam00171 342 LDNgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWIN 421
|
410 420 430
....*....|....*....|....*....|....
gi 514452363 387 DVVMhFTLNALPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:pfam00171 422 DYTT-GDADGLPFGGFKQSGFGREGGPYGLEEYT 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
5-424 |
1.51e-80 |
|
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: 257.53 E-value: 1.51e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 5 VQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFnQEVITVLGEIGFMLANLPEWVTPTPA 84
Cdd:cd07099 24 VARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEVLLALEAIDWAARNAPRVLAPRKV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 85 KKNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVI 163
Cdd:cd07099 103 PTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAgPPQGVLQVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 164 NGGVEETTELLKHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIA 243
Cdd:cd07099 183 TGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCIS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 244 PDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE-----GQKIAFGGE-TDEATRYIAPT 316
Cdd:cd07099 263 VERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRRHVDdavakGAKALTGGArSNGGGPFYEPT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 317 ILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNA 396
Cdd:cd07099 343 VLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPA 422
|
410 420
....*....|....*....|....*...
gi 514452363 397 LPFGGVGASGMGAYHGKYSFDTFSHHRA 424
Cdd:cd07099 423 LPFGGVKDSGGGRRHGAEGLREFCRPKA 450
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
2-413 |
5.31e-70 |
|
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: 230.26 E-value: 5.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPEWVTP 81
Cdd:cd07098 21 DEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 82 TPAKKNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYL-----D 156
Cdd:cd07098 101 ESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLaacghD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 157 QDLYAVINGGVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWM 235
Cdd:cd07098 181 PDLVQLVTCLPETAEALTSHpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 236 NCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGGE---- 305
Cdd:cd07098 261 SSGQNCIGIERVIVHEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVadaveKGARLLAGGKryph 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 306 -TDEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVT 384
Cdd:cd07098 341 pEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVA 420
|
410 420
....*....|....*....|....*....
gi 514452363 385 VNDVVMHFTLNALPFGGVGASGMGAYHGK 413
Cdd:cd07098 421 INDFGVNYYVQQLPFGGVKGSGFGRFAGE 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
2-421 |
1.00e-58 |
|
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: 199.68 E-value: 1.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAI----GADLCKSEFN-----GFNQEVIT----VLGEI 68
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLiresGSTRPKAAFEvgaaiAILREAAGlprrPEGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 69 gfmlanLPewvTPTPAKKNlltlldevYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENT----- 143
Cdd:cd07104 83 ------LP---SDVPGKES--------MVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgglli 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 144 AKILTKL-LPQyldqDLYAVINGGVEETTE-LLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDC 220
Cdd:cd07104 146 AEIFEEAgLPK----GVLNVVPGGGSEIGDaLVEHpRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 221 DLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YG----ENVKESPdyerIINLRHFKRIQSLL 295
Cdd:cd07104 222 DLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALpVGdprdPDTVIGP----LINERQVDRVHAIV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 296 E-----GQKIAFGGETDEatRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKL 370
Cdd:cd07104 298 EdavaaGARLLTGGTYEG--LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLER 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 514452363 371 IKRMIDETSSGGVTVNDVVMHFTLNAlPFGGVGASGMGAYHGKYSFDTFSH 421
Cdd:cd07104 376 AMAFAERLETGMVHINDQTVNDEPHV-PFGGVKASGGGRFGGPASLEEFTE 425
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
5-422 |
7.10e-57 |
|
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: 195.16 E-value: 7.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 5 VQRLRQAFRSGRSRPLQFRLQ----QLEALRRMVQEHEKDILAAIGADL--CKSEFNGFNQEVitvlgeiGFMLANLPEW 78
Cdd:cd07102 24 LERARAAQKGWRAVPLEERKAivtrAVELLAANTDEIAEELTWQMGRPIaqAGGEIRGMLERA-------RYMISIAEEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 79 V--TPTPAKKNLltlldEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELS----ENTAKILTK-LL 151
Cdd:cd07102 97 LadIRVPEKDGF-----ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTplcgERFAAAFAEaGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 152 PQyldqDLYAVINGGVEETTELLK-HRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRIT 230
Cdd:cd07102 172 PE----GVFQVLHLSHETSAALIAdPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 231 WGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE-----GQKIAFGG 304
Cdd:cd07102 248 DGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIAdaiakGARALIDG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 305 ET----DEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSS 380
Cdd:cd07102 328 ALfpedKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLET 407
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 514452363 381 GGVTVN--DVVMhftlNALPFGGVGASGMGAYHGKYSFDTF----SHH 422
Cdd:cd07102 408 GTVFMNrcDYLD----PALAWTGVKDSGRGVTLSRLGYDQLtrpkSYH 451
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
2-420 |
1.21e-56 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 194.71 E-value: 1.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFNQEVITVLGEIGF---MLANLPEW 78
Cdd:cd07093 22 DAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIPRAAANFRFfadYILQLDGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 79 VTPTPAkkNLLTlldevYVQPEPLGVVLIIGAWNYPFVLT---MHP-------LVGaiaagnaaiiKPSELSENTAKILT 148
Cdd:cd07093 102 SYPQDG--GALN-----YVLRQPVGVAGLITPWNLPLMLLtwkIAPalafgntVVL----------KPSEWTPLTAWLLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 149 KLLpqyLDQDL----YAVINGGVEETTELL-KH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDL 222
Cdd:cd07093 165 ELA---NEAGLppgvVNVVHGFGPEAGAALvAHpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 223 DVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----E 296
Cdd:cd07093 242 DRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALkVGDPLDPDTEVGPLISKEHLEKVLGYVelaraE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 297 GQKIAFGGETDEATR-----YIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLI 371
Cdd:cd07093 322 GATILTGGGRPELPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 514452363 372 KRMIDETSSGGVTVNDvvmHFT--LNAlPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07093 402 HRVARRLEAGTVWVNC---WLVrdLRT-PFGGVKASGIGREGGDYSLEFYT 448
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
100-420 |
1.53e-56 |
|
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: 194.47 E-value: 1.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 100 EPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVINGGVEET-TELLKH- 176
Cdd:cd07150 118 RPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVgDELVDDp 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 177 RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQ 256
Cdd:cd07150 198 RVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 257 IVQKIKETVKEF-YG----ENVKESPdyerIINLRHFKRIQSLLE-----GQKIAFGGETDeaTRYIAPTILTDVDPKSR 326
Cdd:cd07150 278 FVKKFVARASKLkVGdprdPDTVIGP----LISPRQVERIKRQVEdavakGAKLLTGGKYD--GNFYQPTVLTDVTPDMR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 327 VMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNAlPFGGVGASG 406
Cdd:cd07150 352 IFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILDEAHV-PFGGVKASG 430
|
330
....*....|....
gi 514452363 407 MGAYHGKYSFDTFS 420
Cdd:cd07150 431 FGREGGEWSMEEFT 444
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
95-420 |
2.08e-56 |
|
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: 193.99 E-value: 2.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 95 VYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVING-GVEETTE 172
Cdd:cd07109 111 VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGlGAEAGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 173 LLKHR-FDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEA 251
Cdd:cd07109 191 LVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 252 SLQNQIVQKIKETVKEF---YGEnvkESPDYERIINLRHFKRIQSLLE-----GQKIAFGGETDEATR----YIAPTILT 319
Cdd:cd07109 271 SIYDEVLERLVERFRALrvgPGL---EDPDLGPLISAKQLDRVEGFVArararGARIVAGGRIAEGAPaggyFVAPTLLD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 320 DVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVND------Vvmhft 393
Cdd:cd07109 348 DVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNNygagggI----- 422
|
330 340
....*....|....*....|....*..
gi 514452363 394 lnALPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07109 423 --ELPFGGVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
1-419 |
6.91e-56 |
|
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: 192.65 E-value: 6.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 1 MEREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDI-----------LA-AIG-ADLCKSEFNGFNQEVITVLGE 67
Cdd:cd07103 21 ADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLarlltleqgkpLAeARGeVDYAASFLEWFAEEARRIYGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 68 IgfmlanLPewvTPTPAKKNLltlldevyVQPEPLGVVLIIGAWNYPFVL-------------TMhplvgaiaagnaaII 134
Cdd:cd07103 101 T------IP---SPAPGKRIL--------VIKQPVGVVAAITPWNFPAAMitrkiapalaagcTV-------------VL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 135 KPSELSENTAKILTKLLPQY-LDQDLYAVINGGVEETTE-LLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGK 211
Cdd:cd07103 151 KPAEETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEaLCASpRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 212 SPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKR 290
Cdd:cd07103 231 APFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 291 IQSLLE-----GQKIAFGGETDEAT-RYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIF 364
Cdd:cd07103 311 VEALVEdavakGAKVLTGGKRLGLGgYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 514452363 365 SHNNKLIKRMIDETSSGGVTVNDVVMhfTLNALPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07103 391 TRDLARAWRVAEALEAGMVGINTGLI--SDAEAPFGGVKESGLGREGGKEGLEEY 443
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
95-386 |
1.26e-55 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 192.48 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 95 VYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVING-GVEETTE 172
Cdd:cd07088 127 IFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGrGSVVGDA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 173 LLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEA 251
Cdd:cd07088 207 LVAHpKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 252 SLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE-----GQKIAFGGETDEATR--YIAPTILTDVDP 323
Cdd:cd07088 287 DIYDEFMEKLVEKMKAVkVGDPFDAATDMGPLVNEAALDKVEEMVEraveaGATLLTGGKRPEGEKgyFYEPTVLTNVRQ 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514452363 324 KSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVN 386
Cdd:cd07088 367 DMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYIN 429
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
1-424 |
3.22e-54 |
|
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: 188.12 E-value: 3.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 1 MEREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDiLAAI-----GADLCKSEFngfnqevitvlgEIGFMLAnl 75
Cdd:cd07106 21 LDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEE-LARLltleqGKPLAEAQF------------EVGGAVA-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 76 peWVTPTPAkknlLTLLDEVYVQPE---------PLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKI 146
Cdd:cd07106 86 --WLRYTAS----LDLPDEVIEDDDtrrvelrrkPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 147 LTKLLPQYLDQDLYAVINGGVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVV 225
Cdd:cd07106 160 LGELAQEVLPPGVLNVVSGGDELGPALTSHpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 226 CRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEFY-GENVKESPDYERIINLRHFKRIQSLLE-----GQK 299
Cdd:cd07106 240 APKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEdakakGAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 300 IAFGGETDEATRY-IAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDET 378
Cdd:cd07106 320 VLAGGEPLDGPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 514452363 379 SSGGVTVNdvvMHFTLN-ALPFGGVGASGMGAYHGKYSFDTFSHHRA 424
Cdd:cd07106 400 EAGTVWIN---THGALDpDAPFGGHKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
1-424 |
3.35e-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: 185.52 E-value: 3.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 1 MEREVQRLRQAF-RSGRSRPLQFR---LQQL-EALRRMVQEHEKDILAAIGADLCKSEFngfnQEVITVLGEIGFM--LA 73
Cdd:cd07089 21 VDAAIAAARRAFdTGDWSTDAEERarcLRQLhEALEARKEELRALLVAEVGAPVMTARA----MQVDGPIGHLRYFadLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 74 NLPEWVTPTPAKkNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLpq 153
Cdd:cd07089 97 DSFPWEFDLPVP-ALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEII-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 154 yLDQDLYA-VIN---GGVEETTELL--KHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCR 227
Cdd:cd07089 174 -AETDLPAgVVNvvtGSDNAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 228 RITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQKIA 301
Cdd:cd07089 253 AAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGDPADPGTVMGPLISAAQRDRVEGYIargrdEGARLV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 302 FGGETDEATR---YIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDET 378
Cdd:cd07089 333 TGGGRPAGLDkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRI 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 514452363 379 SSGGVTVNDVVmHFTLNAlPFGGVGASGMGAYHGKYSFDTFSHHRA 424
Cdd:cd07089 413 RTGSVGINGGG-GYGPDA-PFGGYKQSGLGRENGIEGLEEFLETKS 456
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
2-408 |
2.43e-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: 183.14 E-value: 2.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSG--RSRPLQFRLQQLEALRRMVQEHeKDILAAIgadlcKSEFNGfnqeviTVLGEIGFMLANLPEW- 78
Cdd:cd07114 22 DRAVAAARAAFEGGawRKLTPTERGKLLRRLADLIEAN-AEELAEL-----ETRDNG------KLIRETRAQVRYLAEWy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 79 -------------VTPTpAKKNLLtlldeVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAK 145
Cdd:cd07114 90 ryyagladkiegaVIPV-DKGDYL-----NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 146 ILTKL-----LPQyldqDLYAVINGGVEETTELL-KH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDK 218
Cdd:cd07114 164 ELAKLaeeagFPP----GVVNVVTGFGPETGEALvEHpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 219 DCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-- 295
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIrVGDPLDPETQMGPLATERQLEKVERYVar 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 296 ---EGQKIAFGGET-----DEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHN 367
Cdd:cd07114 320 areEGARVLTGGERpsgadLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 514452363 368 NKLIKRMIDETSSGGVTVNDvvMHFTLNALPFGGVGASGMG 408
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNT--YRALSPSSPFGGFKDSGIG 438
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
100-420 |
2.21e-50 |
|
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: 177.91 E-value: 2.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 100 EPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVING-GVEETTELLKH- 176
Cdd:cd07118 118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGyGATVGQAMTEHp 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 177 RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQ 256
Cdd:cd07118 198 DVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 257 IVQKIKE-TVKEFYGENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGGETDE--ATRYIAPTILTDVDPKSRVM 328
Cdd:cd07118 278 FVAAVVArSRKVRVGDPLDPETKVGAIINEAQLAKITDYVdagraEGATLLLGGERLAsaAGLFYQPTIFTDVTPDMAIA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 329 QEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTlnALPFGGVGASGMG 408
Cdd:cd07118 358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIG 435
|
330
....*....|..
gi 514452363 409 AYHGKYSFDTFS 420
Cdd:cd07118 436 RELGRYGVEEYT 447
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
2-424 |
2.28e-50 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 178.76 E-value: 2.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSR-PLQFRLQQLEALRRMVQEHeKDILAAIGA-DLCK---SEFNGFNQEVITVLGEIGFMLANLP 76
Cdd:cd07144 48 DKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKN-RDLLAAIEAlDSGKpyhSNALGDLDEIIAVIRYYAGWADKIQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 77 EWVTPTPAKKnlltlldEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-L 155
Cdd:cd07144 127 GKTIPTSPNK-------LAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 156 DQDLYAVING-GVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGK 233
Cdd:cd07144 200 PPGVVNIIPGyGAVAGSALAEHpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 234 WMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEFY--GENVKESPDYERIINLRHFKRIQSLLE-----GQKIAFGGE- 305
Cdd:cd07144 280 MYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEkgkkeGAKLVYGGEk 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 306 ---TDEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGG 382
Cdd:cd07144 360 apeGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGM 439
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 514452363 383 VTVN-----DVVMhftlnalPFGGVGASGMGAYHGKYSFDTFSHHRA 424
Cdd:cd07144 440 VWINssndsDVGV-------PFGGFKMSGIGRELGEYGLETYTQTKA 479
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
100-420 |
8.36e-50 |
|
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: 175.84 E-value: 8.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 100 EPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLpqyLDQDLYA----VINGGVE---ETTE 172
Cdd:cd07105 97 EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVF---HEAGLPKgvlnVVTHSPEdapEVVE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 173 -LLKH---RFdhILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVL 248
Cdd:cd07105 174 aLIAHpavRK--VNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERII 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 249 CEASLQNQIVQKIKETVKEFYGENVKESPdyerIINLRHFKRIQSLLE-----GQKIAFGGETD--EATRYIAPTILTDV 321
Cdd:cd07105 252 VHESIADEFVEKLKAAAEKLFAGPVVLGS----LVSAAAADRVKELVDdalskGAKLVVGGLADesPSGTSMPPTILDNV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 322 DPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHfTLNALPFGG 401
Cdd:cd07105 328 TPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVH-DEPTLPHGG 406
|
330
....*....|....*....
gi 514452363 402 VGASGMGAYHGKYSFDTFS 420
Cdd:cd07105 407 VKSSGYGRFNGKWGIDEFT 425
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
2-419 |
2.17e-49 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 176.42 E-value: 2.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCK--SEFNG-----------FNQEVITVLGEI 68
Cdd:PLN02278 65 NDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKplKEAIGevaygasfleyFAEEAKRVYGDI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 69 gfmlanLPewvTPTPAKKnlltlldeVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILT 148
Cdd:PLN02278 145 ------IP---SPFPDRR--------LLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 149 KLLPQY-LDQDLYAVINGGVEETTELL--KHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVV 225
Cdd:PLN02278 208 ELALQAgIPPGVLNVVMGDAPEIGDALlaSPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 226 CRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQK 299
Cdd:PLN02278 288 VKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVESHVqdavsKGAK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 300 IAFGGE--TDEATRYiAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDE 377
Cdd:PLN02278 368 VLLGGKrhSLGGTFY-EPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEA 446
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 514452363 378 TSSGGVTVNDVVMHfTLNAlPFGGVGASGMGAYHGKYSFDTF 419
Cdd:PLN02278 447 LEYGIVGVNEGLIS-TEVA-PFGGVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
2-420 |
3.16e-49 |
|
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: 174.82 E-value: 3.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPewVTP 81
Cdd:cd07092 22 DAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFRFFAGAAR--TLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 82 TPAKKNLLTLLdEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLYA 161
Cdd:cd07092 100 GPAAGEYLPGH-TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 162 VINGGVEETTELL--KHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQ 239
Cdd:cd07092 179 VVCGGGASAGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 240 TCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE----GQKIAFGGETDEATRY-I 313
Cdd:cd07092 259 DCTAACRVYVHESVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVErapaHARVLTGGRRAEGPGYfY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 314 APTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDvvmHFT 393
Cdd:cd07092 339 EPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT---HIP 415
|
410 420
....*....|....*....|....*...
gi 514452363 394 LNA-LPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07092 416 LAAeMPHGGFKQSGYGKDLSIYALEDYT 443
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
83-408 |
6.40e-49 |
|
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: 174.09 E-value: 6.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 83 PAKKNLLTlldevYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLYAV 162
Cdd:cd07108 104 PFGPDVLT-----YTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 163 INGGVEETTE-LLKHR-FDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWG-KWMNCGQ 239
Cdd:cd07108 179 ITGYGEECGAaLVDHPdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGmRFTRQGQ 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 240 TCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE------GQKIAFGGETDEATR- 311
Cdd:cd07108 259 SCTAGSRLFVHEDIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDlglstsGATVLRGGPLPGEGPl 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 312 ----YIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVND 387
Cdd:cd07108 339 adgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQ 418
|
330 340
....*....|....*....|.
gi 514452363 388 vvMHFTLNALPFGGVGASGMG 408
Cdd:cd07108 419 --GGGQQPGQSYGGFKQSGLG 437
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
100-408 |
7.03e-49 |
|
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: 173.94 E-value: 7.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 100 EPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQ-YLDQDLYAVINGGVEET-TELLKH- 176
Cdd:cd07149 122 EPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEaGLPKGALNVVTGSGETVgDALVTDp 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 177 RFDHILYTGNATVGKIVMAAAAkhLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQ 256
Cdd:cd07149 202 RVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 257 IVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE-----GQKIAFGGETDEAtrYIAPTILTDVDPKSRVMQE 330
Cdd:cd07149 280 FLERFVAATKKLvVGDPLDEDTDVGPMISEAEAERIEEWVEeavegGARLLTGGKRDGA--ILEPTVLTDVPPDMKVVCE 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514452363 331 EIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDvVMHFTLNALPFGGVGASGMG 408
Cdd:cd07149 358 EVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMIND-SSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
96-424 |
4.07e-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: 171.85 E-value: 4.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 96 YVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVINGGVEETTE-L 173
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAaL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 174 LKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEAS 252
Cdd:cd07115 192 VEHpDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 253 LQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGGETDEATR-YIAPTILTDVDPKS 325
Cdd:cd07115 272 IYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDRVLDYVdvgreEGARLLTGGKRPGARGfFVEPTIFAAVPPEM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 326 RVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNdvVMHFTLNALPFGGVGAS 405
Cdd:cd07115 352 RIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQS 429
|
330
....*....|....*....
gi 514452363 406 GMGAYHGKYSFDTFSHHRA 424
Cdd:cd07115 430 GFGREMGREALDEYTEVKS 448
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
1-419 |
4.41e-48 |
|
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: 171.92 E-value: 4.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 1 MEREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAI----GADLCKSEfngfNQEVITVLGEIGFMLANLP 76
Cdd:cd07138 38 VDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAItlemGAPITLAR----AAQVGLGIGHLRAAADALK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 77 EWVTPTPAKKNLltlldevyVQPEPLGVVLIIGAWNYPF-----------------VLtmhplvgaiaagnaaiiKPSEL 139
Cdd:cd07138 114 DFEFEERRGNSL--------VVREPIGVCGLITPWNWPLnqivlkvapalaagctvVL-----------------KPSEV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 140 SENTAKILTKLLpqyLDQDLYA----VING-GVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSP 213
Cdd:cd07138 169 APLSAIILAEIL---DEAGLPAgvfnLVNGdGPVVGEALSAHpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 214 CYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQ 292
Cdd:cd07138 246 NIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 293 SLL-----EGQKIAFGG----ETDEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYI 363
Cdd:cd07138 326 GYIqkgieEGARLVAGGpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYV 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 514452363 364 FSHNNKLIKRMIDETSSGGVTVNDVVmhFTLNAlPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07138 406 WSADPERARAVARRLRAGQVHINGAA--FNPGA-PFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
1-419 |
8.45e-48 |
|
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: 171.60 E-value: 8.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 1 MEREVQRLRQAFRSG--RSRPLQFRLQQLEALRRMVQEHEKDILAAI----GADLCKSEfNGFNQEVITVLGEIGFMLAN 74
Cdd:cd07139 38 VDAAVAAARRAFDNGpwPRLSPAERAAVLRRLADALEARADELARLWtaenGMPISWSR-RAQGPGPAALLRYYAALARD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 75 LPeWVTPTPAKknlltLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY 154
Cdd:cd07139 117 FP-FEERRPGS-----GGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 155 -LDQDLYAVINGGVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWG 232
Cdd:cd07139 191 gLPPGVVNVVPADREVGEYLVRHpGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 233 KWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGGET 306
Cdd:cd07139 271 SLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALkVGDPLDPATQIGPLASARQRERVEGYIakgraEGARLVTGGGR 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 307 -DEATR--YIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFS----HNNKLIKRMidetS 379
Cdd:cd07139 351 pAGLDRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTadveRGLAVARRI----R 426
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 514452363 380 SGGVTVNDVVMHFtlnALPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07139 427 TGTVGVNGFRLDF---GAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
95-408 |
1.06e-47 |
|
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: 170.99 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 95 VYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVINGGVEET-TE 172
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVgDE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 173 LLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEA 251
Cdd:cd07145 197 IVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 252 SLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGGETDEATrYIAPTILTDVDPKS 325
Cdd:cd07145 277 EVYDKFLKLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVndaveKGGKILYGGKRDEGS-FFPPTVLENDTPDM 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 326 RVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMhFTLNALPFGGVGAS 405
Cdd:cd07145 356 IVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR-FRWDNLPFGGFKKS 434
|
...
gi 514452363 406 GMG 408
Cdd:cd07145 435 GIG 437
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
95-417 |
1.34e-47 |
|
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: 170.85 E-value: 1.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 95 VYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQyldqdlyA-----VIN--GGV 167
Cdd:cd07091 135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKE-------AgfppgVVNivPGF 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 168 EETT--ELLKH-RFDHILYTGNATVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIA 243
Cdd:cd07091 208 GPTAgaAISSHmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 244 PDYVLCEASLQNQIVQKIKETVKEFY-GENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGGET-DEATRYIAPT 316
Cdd:cd07091 288 GSRIFVQESIYDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIesgkkEGATLLTGGERhGSKGYFIQPT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 317 ILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVN--DVVMHftl 394
Cdd:cd07091 368 VFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtyNVFDA--- 444
|
330 340
....*....|....*....|...
gi 514452363 395 nALPFGGVGASGMGAYHGKYSFD 417
Cdd:cd07091 445 -AVPFGGFKQSGFGRELGEEGLE 466
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
2-423 |
4.80e-47 |
|
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: 168.63 E-value: 4.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAI----GADLCKSEFngfnqEVITVLGEIgFMLANLP- 76
Cdd:cd07152 16 DRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIvresGSIRPKAGF-----EVGAAIGEL-HEAAGLPt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 77 ----EWVTPTPAKKNlltlldevYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKL-- 150
Cdd:cd07152 90 qpqgEILPSAPGRLS--------LARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARlf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 151 ----LPQYLDQdlyaVINGGVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVV 225
Cdd:cd07152 162 eeagLPAGVLH----VLPGGADAGEALVEDpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 226 CRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-----YGENVKESPdyerIINLRHFKRIQSLLE---- 296
Cdd:cd07152 238 ASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLpvgdpATGQVALGP----LINARQLDRVHAIVDdsva 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 297 -GQKIAFGGETDEatRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMI 375
Cdd:cd07152 314 aGARLEAGGTYDG--LFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 514452363 376 DETSSGGVTVNDV-VMHFTLNalPFGGVGASGMGAYHG-KYSFDTFSHHR 423
Cdd:cd07152 392 DRLRTGMLHINDQtVNDEPHN--PFGGMGASGNGSRFGgPANWEEFTQWQ 439
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
2-424 |
9.87e-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: 168.68 E-value: 9.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCK--SEFNGFNQEVIT----VLGEIGFMLANl 75
Cdd:cd07131 40 DAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKplAEGRGDVQEAIDmaqyAAGEGRRLFGE- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 76 pewVTPTP-AKKNLLTLLdevyvqpEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSElseNTAKILTKLLPQY 154
Cdd:cd07131 119 ---TVPSElPNKDAMTRR-------QPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAE---DTPACALKLVELF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 155 LDQDLYA-VIN---GGVEETTE-LLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRR 228
Cdd:cd07131 186 AEAGLPPgVVNvvhGRGEEVGEaLVEHpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 229 ITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQKIAF 302
Cdd:cd07131 266 ALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLNYNeigkeEGATLLL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 303 GGE-----TDEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDE 377
Cdd:cd07131 346 GGErltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRD 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 514452363 378 TSSGGVTVNDVvmhfTLNA---LPFGGVGASGMGAYHGKYS-FDTFSHHRA 424
Cdd:cd07131 426 LEAGITYVNAP----TIGAevhLPFGGVKKSGNGHREAGTTaLDAFTEWKA 472
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
96-420 |
6.04e-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: 166.72 E-value: 6.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 96 YVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLpqyLDQDLYA-VIN----GGVEET 170
Cdd:cd07119 129 RTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELI---EEAGLPAgVVNlvtgSGATVG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 171 TELLKHR-FDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLC 249
Cdd:cd07119 206 AELAESPdVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLV 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 250 EASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGGE--TDEATR---YIAPTIL 318
Cdd:cd07119 286 EESIHDKFVAALAERAKKIkLGNGLDADTEMGPLVSAEHREKVLSYIqlgkeEGARLVCGGKrpTGDELAkgyFVEPTIF 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 319 TDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDvvMHFTLNALP 398
Cdd:cd07119 366 DDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAP 443
|
330 340
....*....|....*....|..
gi 514452363 399 FGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07119 444 WGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
95-429 |
9.57e-46 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 165.55 E-value: 9.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 95 VYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVINGGVEETTEL 173
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGGGETGQLL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 174 LKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEAS 252
Cdd:cd07090 190 CEHpDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 253 LQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGGE----TD--EATRYIAPTILTD 320
Cdd:cd07090 270 IKDEFTERLVERTKKIrIGDPLDEDTQMGALISEEHLEKVLGYIesakqEGAKVLCGGErvvpEDglENGFYVSPCVLTD 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 321 VDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDvvmhFTLNA--LP 398
Cdd:cd07090 350 CTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT----YNISPveVP 425
|
330 340 350
....*....|....*....|....*....|.
gi 514452363 399 FGGVGASGMGAYHGKYSFDTFSHhraclLKS 429
Cdd:cd07090 426 FGGYKQSGFGRENGTAALEHYTQ-----LKT 451
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
93-420 |
1.14e-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: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 93 DEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVINGGVEETT 171
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 172 ELL-KHR-FDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLC 249
Cdd:TIGR01804 205 PLLvNHPdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 250 EASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGG------ETDEATrYIAPTI 317
Cdd:TIGR01804 285 HKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIekgkaEGATLATGGgrpenvGLQNGF-FVEPTV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 318 LTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDvvMHFTLNAL 397
Cdd:TIGR01804 364 FADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEA 441
|
330 340
....*....|....*....|...
gi 514452363 398 PFGGVGASGMGAYHGKYSFDTFS 420
Cdd:TIGR01804 442 PFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
96-408 |
1.48e-45 |
|
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: 165.69 E-value: 1.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 96 YVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVINGGVEETTELL 174
Cdd:cd07113 137 FTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKGAVGAQLI 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 175 KH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASL 253
Cdd:cd07113 217 SHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSK 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 254 QNQIVQKIKETVKEFY-GENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGGET-DEATRYIAPTILTDVDPKSR 326
Cdd:cd07113 297 FDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEAlAGEGYFVQPTLVLARSADSR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 327 VMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNdvvMHFTLN-ALPFGGVGAS 405
Cdd:cd07113 377 LMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDpAVPFGGMKQS 453
|
...
gi 514452363 406 GMG 408
Cdd:cd07113 454 GIG 456
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
89-408 |
4.15e-45 |
|
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: 164.44 E-value: 4.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 89 LTLLDE---VYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLYAVING 165
Cdd:cd07559 121 LSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 166 -GVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYV-----DKDCDLDVVCRRITWGKWMNCG 238
Cdd:cd07559 201 fGSEAGKPLASHpRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFAFNQG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 239 QTCIAPDYVLCEASLQNQIVQKIKETVkefygENVKE-SP-DYERII----NLRHFKRIQSLL-----EGQKIAFGGE-- 305
Cdd:cd07559 281 EVCTCPSRALVQESIYDEFIERAVERF-----EAIKVgNPlDPETMMgaqvSKDQLEKILSYVdigkeEGAEVLTGGErl 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 306 ---TDEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGG 382
Cdd:cd07559 356 tlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGR 435
|
330 340 350
....*....|....*....|....*....|
gi 514452363 383 VTVNdvvmhfTLNALP----FGGVGASGMG 408
Cdd:cd07559 436 VWVN------CYHQYPahapFGGYKKSGIG 459
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
1-419 |
1.21e-44 |
|
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: 161.86 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 1 MEREVQRLRQAFRSGRSRPLQFRLQQL----EALRR--------MVQEHEKDILAAIG-----ADLCKsefngfnqevit 63
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLrklaDLLRErkdelarlITLEMGKPIAEARAevekcAWICR------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 64 vlgeigFMLANLPEWVTPTPAKknllTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENT 143
Cdd:cd07100 69 ------YYAENAEAFLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 144 AKILTKLLPQY-LDQDLYAVINGGVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCD 221
Cdd:cd07100 139 ALAIEELFREAgFPEGVFQNLLIDSDQVEAIIADpRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 222 LDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDY-----ERIINLRHfKRIQ-SL 294
Cdd:cd07100 219 LDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALkVGDPMDEDTDLgplarKDLRDELH-EQVEeAV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 295 LEGQKIAFGGET-DEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKR 373
Cdd:cd07100 298 AAGATLLLGGKRpDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAER 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 514452363 374 MIDETSSGGVTVNDVVmhFTLNALPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07100 378 VARRLEAGMVFINGMV--KSDPRLPFGGVKRSGYGRELGRFGIREF 421
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
2-412 |
1.99e-44 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 162.16 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDiLAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPEWVTP 81
Cdd:cd07107 22 DRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEE-LALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTELKGE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 82 T-PAKKNLLTlldevYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLY 160
Cdd:cd07107 101 TiPVGGRNLH-----YTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 161 AVINGGVEETTE-LLKHR-FDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGkwMN-- 236
Cdd:cd07107 176 NILPGDGATAGAaLVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAG--MNft 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 237 -CGQTCIAPDYVLCEASLQNQIVQKIKETVKEFY-GENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGG--ETD 307
Cdd:cd07107 254 wCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIdsakrEGARLVTGGgrPEG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 308 EATR---YIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVT 384
Cdd:cd07107 334 PALEggfYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVW 413
|
410 420
....*....|....*....|....*...
gi 514452363 385 VNDVVMHFTlnALPFGGVGASGMGAYHG 412
Cdd:cd07107 414 INGSSRHFL--GAPFGGVKNSGIGREEC 439
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
8-420 |
2.34e-44 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 162.09 E-value: 2.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 8 LRQAFRSGR-------SRPLQFRLQQLEALRRMVQEHEKDILAAI----GADLCKSEFngfnqevitvlgEIGFMLANLP 76
Cdd:cd07151 34 VDEAYRAAAaaqkewaATLPQERAEILEKAAQILEERRDEIVEWLiresGSTRIKANI------------EWGAAMAITR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 77 EWVT------------PTPAKKNlltlldevYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENT- 143
Cdd:cd07151 102 EAATfplrmegrilpsDVPGKEN--------RVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITg 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 144 ----AKILTKL-LPQYLdqdLYAVINGGVEETTELLKH---RFdhILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCY 215
Cdd:cd07151 174 glllAKIFEEAgLPKGV---LNVVVGAGSEIGDAFVEHpvpRL--ISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 216 VDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSL 294
Cdd:cd07151 249 VLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 295 LE-----GQKIAFGGETDEatRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNK 369
Cdd:cd07151 329 IEqaveeGATLLVGGEAEG--NVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLE 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 514452363 370 LIKRMIDETSSGGVTVNDVVMHFTLNAlPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07151 407 RGVQFARRIDAGMTHINDQPVNDEPHV-PFGGEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
94-409 |
3.55e-44 |
|
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: 161.65 E-value: 3.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 94 EVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQyldQDLYA-VIN----GGVE 168
Cdd:cd07097 128 EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEE---AGLPAgVFNlvmgSGSE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 169 ETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYV 247
Cdd:cd07097 205 VGQALVEHpDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 248 LCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGGET-DEATR--YIAPTIL 318
Cdd:cd07097 285 IVTEGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIeiarsEGAKLVYGGERlKRPDEgyYLAPALF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 319 TDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNAlP 398
Cdd:cd07097 365 AGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGVDYHV-P 443
|
330
....*....|.
gi 514452363 399 FGGVGASGMGA 409
Cdd:cd07097 444 FGGRKGSSYGP 454
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
2-408 |
6.38e-44 |
|
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: 160.68 E-value: 6.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDI--LAAIGADLCKSEFNGFNQEVITVLGEIGFMLANLPEWV 79
Cdd:cd07094 24 EEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFakIIACEGGKPIKDARVEVDRAIDTLRLAAEEAERIRGEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 80 TPTPAKKNLLTLLdeVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLL-PQYLDQD 158
Cdd:cd07094 104 IPLDATQGSDNRL--AWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 159 LYAVING-GVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKhlTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMN 236
Cdd:cd07094 182 VLQVVTGeREVLGDAFAADeRVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 237 CGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE-----GQKIAFGGETDEAT 310
Cdd:cd07094 260 AGQVCISVQRIYVHEELYDEFIEAFVAAVKKLkVGDPLDEDTDVGPLISEEAAERVERWVEeaveaGARLLCGGERDGAL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 311 RYiaPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHN-NKLIKrMIDETSSGGVTVNDVV 389
Cdd:cd07094 340 FK--PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDlNVAFK-AAEKLEVGGVMVNDSS 416
|
410
....*....|....*....
gi 514452363 390 mHFTLNALPFGGVGASGMG 408
Cdd:cd07094 417 -AFRTDWMPFGGVKESGVG 434
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
5-421 |
8.40e-44 |
|
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: 160.21 E-value: 8.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 5 VQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHeKDILAAIGADLCKSEFNGFNQEVITVLGEIGFMlANLPEWVTPTPA 84
Cdd:cd07110 25 VRAARRAFPRWKKTTGAERAKYLRAIAEGVRER-REELAELEARDNGKPLDEAAWDVDDVAGCFEYY-ADLAEQLDAKAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 85 KKnlLTLLDE---VYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKL-----LPQyld 156
Cdd:cd07110 103 RA--VPLPSEdfkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIaaeagLPP--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 157 qDLYAVINGGVEET-TELLKHR-FDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKW 234
Cdd:cd07110 178 -GVLNVVTGTGDEAgAPLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 235 MNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-----YGENVKESP-----DYERIinLRHFKRIQSllEGQKIAFGG 304
Cdd:cd07110 257 WNNGQICSATSRLLVHESIADAFLERLATAAEAIrvgdpLEEGVRLGPlvsqaQYEKV--LSFIARGKE--EGARLLCGG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 305 ETDEATR---YIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSG 381
Cdd:cd07110 333 RRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAG 412
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 514452363 382 GVTVNDVVMHFTlnALPFGGVGASGMGAYHGKYSFDTFSH 421
Cdd:cd07110 413 IVWINCSQPCFP--QAPWGGYKRSGIGRELGEWGLDNYLE 450
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
96-424 |
1.49e-43 |
|
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: 160.00 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 96 YVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVING-GVEETTEL 173
Cdd:cd07143 139 YTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGyGRTCGNAI 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 174 LKH-RFDHILYTGNATVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEA 251
Cdd:cd07143 219 SSHmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 252 SLQNQIVQKIKETVKEF-----YGENVKESPDYERIinlrHFKRIQSLLE-----GQKIAFGGETDEATRY-IAPTILTD 320
Cdd:cd07143 299 GIYDKFVKRFKEKAKKLkvgdpFAEDTFQGPQVSQI----QYERIMSYIEsgkaeGATVETGGKRHGNEGYfIEPTIFTD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 321 VDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDvvmHFTLNA-LPF 399
Cdd:cd07143 375 VTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNC---YNLLHHqVPF 451
|
330 340
....*....|....*....|....*
gi 514452363 400 GGVGASGMGAYHGKYSFDTFSHHRA 424
Cdd:cd07143 452 GGYKQSGIGRELGEYALENYTQIKA 476
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
79-420 |
1.87e-43 |
|
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: 159.30 E-value: 1.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 79 VTPTPAkkNLLTLldevyVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKL-----LPQ 153
Cdd:cd07112 109 VAPTGP--DALAL-----ITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLPA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 154 yldqDLYAVINGGVEETTELL-KHR-FDHILYTGNATVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDC-DLDVVCRRI 229
Cdd:cd07112 182 ----GVLNVVPGFGHTAGEALgLHMdVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 230 TWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEFY-GENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFG 303
Cdd:cd07112 258 AAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKpGDPLDPATRMGALVSEAHFDKVLGYIesgkaEGARLVAG 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 304 GETDEATR---YIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSS 380
Cdd:cd07112 338 GKRVLTETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRA 417
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 514452363 381 GGVTVNdvvmhfTLNAL----PFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07112 418 GTVWVN------CFDEGdittPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
95-420 |
2.00e-43 |
|
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: 159.06 E-value: 2.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 95 VYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVINGGVEE-TTE 172
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEiGDE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 173 LLKH-RFDHILYTGNATVGKIVMAAAA-KHLTpvtLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCE 250
Cdd:cd07146 194 LITHpDVDLVTFTGGVAVGKAIAATAGyKRQL---LELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVH 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 251 ASLQNQIVQKIKETVKEF-YGENVKESPDYERIIN---LRHFKRI--QSLLEGQKIAFGGETDEAtrYIAPTILTDVDPK 324
Cdd:cd07146 271 ESVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDeeaAIQIENRveEAIAQGARVLLGNQRQGA--LYAPTVLDHVPPD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 325 SRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVmHFTLNALPFGGVGA 404
Cdd:cd07146 349 AELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVP-GFRSELSPFGGVKD 427
|
330
....*....|....*..
gi 514452363 405 SGMGAYHG-KYSFDTFS 420
Cdd:cd07146 428 SGLGGKEGvREAMKEMT 444
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
95-386 |
1.06e-42 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 156.05 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 95 VYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVING-GVEETTE 172
Cdd:PRK10090 65 ILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGrGETVGQE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 173 LLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEA 251
Cdd:PRK10090 145 LAGNpKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 252 SLQNQIVQKIKETVKEF-YGENVKES-PDYERIINLRHFKRIQSLL-----EGQKIAFGGETDEATRYI-APTILTDVDP 323
Cdd:PRK10090 225 GIYDQFVNRLGEAMQAVqFGNPAERNdIAMGPLINAAALERVEQKVaraveEGARVALGGKAVEGKGYYyPPTLLLDVRQ 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514452363 324 KSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVN 386
Cdd:PRK10090 305 EMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
2-413 |
1.04e-41 |
|
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: 154.39 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFnQEVITVLGEIGFMLANLPEWVTP 81
Cdd:cd07101 21 EAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAF-EEVLDVAIVARYYARRAERLLKP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 82 TPaKKNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLY 160
Cdd:cd07101 100 RR-RRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLPRDLW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 161 AVINGGVEETTELLKHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQT 240
Cdd:cd07101 179 QVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 241 CIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE-----GQKIAFGGET--DEATRY 312
Cdd:cd07101 259 CVSIERIYVHESVYDEFVRRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVDdavakGATVLAGGRArpDLGPYF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 313 IAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVND-VVMH 391
Cdd:cd07101 339 YEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEgYAAA 418
|
410 420
....*....|....*....|..
gi 514452363 392 FTLNALPFGGVGASGMGAYHGK 413
Cdd:cd07101 419 WASIDAPMGGMKDSGLGRRHGA 440
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
100-408 |
1.28e-41 |
|
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: 154.53 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 100 EPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLYAVINGGVEETTELLKHR-- 177
Cdd:cd07117 135 EPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHpg 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 178 FDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQI 257
Cdd:cd07117 215 LDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEF 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 258 VQKIKEtvkEFygENVK----ESPDYE--RIINLRHFKRIQSLL-----EGQKIAFGGE-----TDEATRYIAPTILTDV 321
Cdd:cd07117 295 VAKLKE---KF--ENVKvgnpLDPDTQmgAQVNKDQLDKILSYVdiakeEGAKILTGGHrltenGLDKGFFIEPTLIVNV 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 322 DPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNdvvmhfTLNALP--- 398
Cdd:cd07117 370 TNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN------TYNQIPaga 443
|
330
....*....|.
gi 514452363 399 -FGGVGASGMG 408
Cdd:cd07117 444 pFGGYKKSGIG 454
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
101-408 |
8.49e-40 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 149.32 E-value: 8.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 101 PLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLL-PQYLDQDLYAVINGGVEETTELLKH-RF 178
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaETGLPKGAFSVLPCSRDDADLLVTDeRI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 179 DHILYTGNATVG-KIVMAAAAKHltpVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQI 257
Cdd:cd07147 203 KLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 258 VQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE-----GQKIAFGGETDEATryIAPTILTDVDPKSRVMQEE 331
Cdd:cd07147 280 KSRLVARVKALkTGDPKDDATDVGPMISESEAERVEGWVNeavdaGAKLLTGGKRDGAL--LEPTILEDVPPDMEVNCEE 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514452363 332 IFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMhFTLNALPFGGVGASGMG 408
Cdd:cd07147 358 VFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDVPT-FRVDHMPYGGVKDSGIG 433
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
2-425 |
9.28e-40 |
|
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: 149.64 E-value: 9.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPlqfRLQQLEALRRMVQEHEKDiLAAIGADLCK------SEFNGFNQEVITV----LGEiGFM 71
Cdd:cd07086 38 EAAVAAAREAFKEWRKVP---APRRGEIVRQIGEALRKK-KEALGRLVSLemgkilPEGLGEVQEMIDIcdyaVGL-SRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 72 LANLpewVTPT--PAKKNlltlldevYVQPEPLGVVLIIGAWNYPFVL----TMHPLVGAIAAGNaaiiKPSELSENTAK 145
Cdd:cd07086 113 LYGL---TIPSerPGHRL--------MEQWNPLGVVGVITAFNFPVAVpgwnAAIALVCGNTVVW----KPSETTPLTAI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 146 ILTKLLPQYLDQD-----LYAVINGGVEeTTELLKH--RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDK 218
Cdd:cd07086 178 AVTKILAEVLEKNglppgVVNLVTGGGD-GGELLVHdpRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 219 DCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE- 296
Cdd:cd07086 257 DADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNAIEi 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 297 ----GQKIAFGGET---DEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNK 369
Cdd:cd07086 337 aksqGGTVLTGGKRidgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLR 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514452363 370 LIKRMIDETSS--GGVTVNDVvmhfTLNA---LPFGGVGASGMGAYHGKYSFDTFSHHRAC 425
Cdd:cd07086 417 EAFRWLGPKGSdcGIVNVNIP----TSGAeigGAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
94-421 |
1.40e-39 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 149.50 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 94 EVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTK------LLPQYLDqdlyaVING-G 166
Cdd:PLN02467 144 KGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADicrevgLPPGVLN-----VVTGlG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 167 VEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPD 245
Cdd:PLN02467 219 TEAGAPLASHpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 246 YVLCEASLQNQIVQKIKETVKefygeNVKESPDYER------IINLRHFKRIQSLL-----EGQKIAFGGETDEATR--- 311
Cdd:PLN02467 299 RLLVHERIASEFLEKLVKWAK-----NIKISDPLEEgcrlgpVVSEGQYEKVLKFIstaksEGATILCGGKRPEHLKkgf 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 312 YIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMH 391
Cdd:PLN02467 374 FIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPC 453
|
330 340 350
....*....|....*....|....*....|
gi 514452363 392 FTlnALPFGGVGASGMGAYHGKYSFDTFSH 421
Cdd:PLN02467 454 FC--QAPWGGIKRSGFGRELGEWGLENYLS 481
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
95-424 |
1.44e-39 |
|
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: 149.18 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 95 VYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVING-GVEETTE 172
Cdd:cd07142 135 VYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGfGPTAGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 173 LLKHR-FDHILYTGNATVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCE 250
Cdd:cd07142 215 IASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVH 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 251 ASLQNQIVQKIKE-----TVKEFYGENVKESPDyeriINLRHFKRIQSLL-----EGQKIAFGGE-TDEATRYIAPTILT 319
Cdd:cd07142 295 ESIYDEFVEKAKAralkrVVGDPFRKGVEQGPQ----VDKEQFEKILSYIehgkeEGATLITGGDrIGSKGYYIQPTIFS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 320 DVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVN--DVvmhFTLnAL 397
Cdd:cd07142 371 DVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDV---FDA-SI 446
|
330 340
....*....|....*....|....*..
gi 514452363 398 PFGGVGASGMGAYHGKYSFDTFSHHRA 424
Cdd:cd07142 447 PFGGYKMSGIGREKGIYALNNYLQVKA 473
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
96-417 |
2.45e-37 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 142.74 E-value: 2.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 96 YVQPEPLGVVLIIGAWNYPfvLTM------------HPLVGaiaagnaaiiKPSELSENT----AKILTKLLPQyldqdl 159
Cdd:PRK13473 133 MIRRDPVGVVASIAPWNYP--LMMaawklapalaagNTVVL----------KPSEITPLTalklAELAADILPP------ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 160 yAVIN---GGVEETTE-LLKHR-FDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKW 234
Cdd:PRK13473 195 -GVLNvvtGRGATVGDaLVGHPkVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 235 MNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE------GQKIAFGGET- 306
Cdd:PRK13473 274 YNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFVErakalgHIRVVTGGEAp 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 307 DEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVN 386
Cdd:PRK13473 354 DGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVN 433
|
330 340 350
....*....|....*....|....*....|....*.
gi 514452363 387 DvvmHFTL-NALPFGGVGASGmgayHGK----YSFD 417
Cdd:PRK13473 434 T---HFMLvSEMPHGGQKQSG----YGKdmslYGLE 462
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-409 |
4.56e-37 |
|
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: 142.75 E-value: 4.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQL----EALRR--------MVQEHEK-------DILAAIgaDLCksEFngFNQEvi 62
Cdd:cd07124 72 EAAVQAARAAFPTWRRTPPEERARLLlraaALLRRrrfelaawMVLEVGKnwaeadaDVAEAI--DFL--EY--YARE-- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 63 tvlgeigfMLANLPEWVTPTPAKKNLLTLldevyvqpEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSEN 142
Cdd:cd07124 144 --------MLRLRGFPVEMVPGEDNRYVY--------RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 143 TAKILTKL-----LPQyldqdlyAVIN---GGVEETTE-LLKH-RFDHILYTGNATVGKIVMAAAAK------HLTPVTL 206
Cdd:cd07124 208 IAAKLVEIleeagLPP-------GVVNflpGPGEEVGDyLVEHpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 207 ELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINL 285
Cdd:cd07124 281 EMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALkVGDPEDPEVYMGPVIDK 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 286 RHFKRIQSLLE----GQKIAFGGETDE-ATR--YIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKP 358
Cdd:cd07124 361 GARDRIRRYIEigksEGRLLLGGEVLElAAEgyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYG 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 514452363 359 LALYIFSHNNKLIKRMIDETSSGGVTVND------VVMHftlnalPFGGVGASGMGA 409
Cdd:cd07124 441 LTGGVFSRSPEHLERARREFEVGNLYANRkitgalVGRQ------PFGGFKMSGTGS 491
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
2-412 |
1.00e-36 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 141.94 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFnQEVITVLGEIGFMLANLPEWVTP 81
Cdd:PRK09407 57 EAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAF-EEVLDVALTARYYARRAPKLLAP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 82 TPaKKNLLTLLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLY 160
Cdd:PRK09407 136 RR-RAGALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLW 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 161 AVING-GVEETTELLKHRfDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQ 239
Cdd:PRK09407 215 QVVTGpGPVVGTALVDNA-DYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 240 TCIAPD--YVlceaslqnqiVQKIKETVKEFYGENVKE---------SPDYERIINLRHFKRIQSLLE-----GQKIAFG 303
Cdd:PRK09407 294 LCISIEriYV----------HESIYDEFVRAFVAAVRAmrlgagydySADMGSLISEAQLETVSAHVDdavakGATVLAG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 304 GET--DEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSG 381
Cdd:PRK09407 364 GKArpDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAG 443
|
410 420 430
....*....|....*....|....*....|...
gi 514452363 382 GVTVND--VVMHFTLNAlPFGGVGASGMGAYHG 412
Cdd:PRK09407 444 TVNVNEgyAAAWGSVDA-PMGGMKDSGLGRRHG 475
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
100-420 |
1.16e-36 |
|
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: 140.56 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 100 EPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQ--YLDQdlyAVINGGVEETTELLKH- 176
Cdd:cd07120 116 EPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEipSLPA---GVVNLFTESGSEGAAHl 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 177 ----RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEAS 252
Cdd:cd07120 193 vaspDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 253 LQNQIVQKIKEtvkefYGENVKESPDYER------IINLRHFKRIQSLLE------GQKIAFGGETDEATR---YIAPTI 317
Cdd:cd07120 273 IADEVRDRLAA-----RLAAVKVGPGLDPasdmgpLIDRANVDRVDRMVEraiaagAEVVLRGGPVTEGLAkgaFLRPTL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 318 LTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDvvmHFTLNA- 396
Cdd:cd07120 348 LEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND---WNKLFAe 424
|
330 340
....*....|....*....|....
gi 514452363 397 LPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07120 425 AEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
79-406 |
1.20e-36 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 141.61 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 79 VTPTPAKKNLLtlldeVYvqpEPLGVVLIIGAWNYPFVL----TMHPLVGAIAAGNaaiiKPSELSENTAKILTKL---- 150
Cdd:PRK03137 157 VESRPGEHNRY-----FY---IPLGVGVVISPWNFPFAImagmTLAAIVAGNTVLL----KPASDTPVIAAKFVEVleea 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 151 -LPQyldqdlyAVIN----GGVEETTELLKH---RFdhILYTGNATVGKIVMAAAAK------HLTPVTLELGGKSPCYV 216
Cdd:PRK03137 225 gLPA-------GVVNfvpgSGSEVGDYLVDHpktRF--ITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 217 DKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEFYGENVKESPDYERIINLRHFKRIQSLLE 296
Cdd:PRK03137 296 DEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 297 -GQ---KIAFGGETDEATRY-IAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLI 371
Cdd:PRK03137 376 iGKeegRLVLGGEGDDSKGYfIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHL 455
|
330 340 350
....*....|....*....|....*....|....*
gi 514452363 372 KRMIDETSSGGVTVNDVVMHFTLNALPFGGVGASG 406
Cdd:PRK03137 456 EKARREFHVGNLYFNRGCTGAIVGYHPFGGFNMSG 490
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
96-420 |
1.54e-35 |
|
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: 137.70 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 96 YVQPEPLGVVLIIGAWNYPFVLTMHPLVgaiaagnaaiikPSELSENT-----AK---ILTKLLPQYLDQ-----DLYAV 162
Cdd:cd07082 136 QVRREPLGVVLAIGPFNYPLNLTVSKLI------------PALIMGNTvvfkpATqgvLLGIPLAEAFHDagfpkGVVNV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 163 INGGVEETTE-LLKH-RFDHILYTGNATVGKIVMAAAAKhlTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQT 240
Cdd:cd07082 204 VTGRGREIGDpLVTHgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQR 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 241 CIAPDYVLCEASLQNQIVQKIKE-----TVKEFYGENV-------KESPDYeriinlrhfkrIQSLLE-----GQKIAFG 303
Cdd:cd07082 282 CTAIKRVLVHESVADELVELLKEevaklKVGMPWDNGVditplidPKSADF-----------VEGLIDdavakGATVLNG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 304 GETDEATrYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGV 383
Cdd:cd07082 351 GGREGGN-LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTV 429
|
330 340 350
....*....|....*....|....*....|....*..
gi 514452363 384 TVNDVVMHFTlNALPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07082 430 NINSKCQRGP-DHFPFLGRKDSGIGTQGIGDALRSMT 465
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
96-421 |
1.52e-34 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 135.33 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 96 YVQPEPLGVVLIIGAWNYP---FVLTMHPLVGAIAAGNAaiiKPSELSENTAKILTKLLPQY-LDQDLYAVING-GVEET 170
Cdd:PLN02766 153 YTLKEPIGVVGHIIPWNFPstmFFMKVAPALAAGCTMVV---KPAEQTPLSALFYAHLAKLAgVPDGVINVVTGfGPTAG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 171 TELLKHR-FDHILYTGNATVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVL 248
Cdd:PLN02766 230 AAIASHMdVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVY 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 249 CEASLQNQIVQKIKETVKEF-----YGENVKESP-----DYERIIN-LRHFKRiqsllEGQKIAFGGE-TDEATRYIAPT 316
Cdd:PLN02766 310 VQEGIYDEFVKKLVEKAKDWvvgdpFDPRARQGPqvdkqQFEKILSyIEHGKR-----EGATLLTGGKpCGDKGYYIEPT 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 317 ILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNdvvMHFTL-N 395
Cdd:PLN02766 385 IFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYFAFdP 461
|
330 340
....*....|....*....|....*.
gi 514452363 396 ALPFGGVGASGMGAYHGKYSFDTFSH 421
Cdd:PLN02766 462 DCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
96-420 |
2.35e-34 |
|
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: 134.40 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 96 YVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQyldqdlyA-----VIN--GGVE 168
Cdd:cd07141 140 YTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKE-------AgfppgVVNvvPGYG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 169 ETT--ELLKH-RFDHILYTGNATVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAP 244
Cdd:cd07141 213 PTAgaAISSHpDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 245 DYVLCEASLQNQIVQKI-----KETVKEFYGENVKESPDyeriINLRHFKRIQSLL-----EGQKIAFGGET-DEATRYI 313
Cdd:cd07141 293 SRTFVQESIYDEFVKRSverakKRVVGNPFDPKTEQGPQ----IDEEQFKKILELIesgkkEGAKLECGGKRhGDKGYFI 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 314 APTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNnklIKRMIDETSS---GGVTVNdVVM 390
Cdd:cd07141 369 QPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD---IDKAITFSNAlraGTVWVN-CYN 444
|
330 340 350
....*....|....*....|....*....|
gi 514452363 391 HFTLNAlPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07141 445 VVSPQA-PFGGYKMSGNGRELGEYGLQEYT 473
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
91-413 |
2.42e-33 |
|
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: 131.75 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 91 LLDEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVINGGVEE 169
Cdd:cd07111 137 LLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGSF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 170 TTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVL 248
Cdd:cd07111 217 GSALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 249 CEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLEGQKiAFGGETDEATR-------YIAPTILTD 320
Cdd:cd07111 297 VQESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADVFQPGAdlpskgpFYPPTLFTN 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 321 VDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNdvvmhfTLN----A 396
Cdd:cd07111 376 VPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN------GHNlfdaA 449
|
330
....*....|....*..
gi 514452363 397 LPFGGVGASGMGAYHGK 413
Cdd:cd07111 450 AGFGGYRESGFGREGGK 466
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
1-419 |
1.11e-32 |
|
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: 129.56 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 1 MEREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDIlaaigADLCKSEfNG--FNQevitVLGEIGFMLANLpEW 78
Cdd:cd07085 40 VDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL-----ARLITLE-HGktLAD----ARGDVLRGLEVV-EF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 79 VTPTPakkNLLT--LLDEV------YVQPEPLGVVLIIGAWNYPFV--LTMHPL--------VGaiaagnaaiiKPSELS 140
Cdd:cd07085 109 ACSIP---HLLKgeYLENVargidtYSYRQPLGVVAGITPFNFPAMipLWMFPMaiacgntfVL----------KPSERV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 141 ENTAKILTKLLPQY-LDQDLYAVINGGVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDK 218
Cdd:cd07085 176 PGAAMRLAELLQEAgLPDGVLNVVHGGKEAVNALLDHpDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 219 DCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-- 295
Cdd:cd07085 256 DADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLkVGAGDDPGADMGPVISPAAKERIEGLIes 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 296 ---EGQKIAFGGETDEATRY-----IAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHN 367
Cdd:cd07085 336 gveEGAKLVLDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRS 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 514452363 368 NKLIKRMIDETSSGGVTVN-----DVVMHftlnalPFGGVGASGMGAYH--GKYSFDTF 419
Cdd:cd07085 416 GAAARKFQREVDAGMVGINvpipvPLAFF------SFGGWKGSFFGDLHfyGKDGVRFY 468
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
100-420 |
2.23e-32 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 129.25 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 100 EPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKL-----LPqylDQDLYAVINGGVEETTELL 174
Cdd:PRK09847 156 EPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLakeagLP---DGVLNVVTGFGHEAGQALS 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 175 KH-RFDHILYTGNATVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDC-DLDVVCRRITWGKWMNCGQTCIAPDYVLCEA 251
Cdd:PRK09847 233 RHnDIDAIAFTGSTRTGKQLLKDAGDsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 252 SLQNQIVQKIKETVKEFY-GENVKESPDYERIINLRHFKRIQSLLE-----GQKIAFGGETDEATrYIAPTILTDVDPKS 325
Cdd:PRK09847 313 SIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIRegeskGQLLLDGRNAGLAA-AIGPTIFVDVDPNA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 326 RVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTV---NDVVMhftlnALPFGGV 402
Cdd:PRK09847 392 SLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVnnyNDGDM-----TVPFGGY 466
|
330
....*....|....*...
gi 514452363 403 GASGMGAYHGKYSFDTFS 420
Cdd:PRK09847 467 KQSGNGRDKSLHALEKFT 484
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
100-424 |
4.41e-32 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 128.77 E-value: 4.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 100 EPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVING-GVEETTELLKHR 177
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGfGPTAGAALASHM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 178 -FDHILYTGNATVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQN 255
Cdd:PLN02466 274 dVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 256 QIVQK-----IKETVKEFYGENVKESPDyeriINLRHFKR----IQSLLE-GQKIAFGGETDEATRY-IAPTILTDVDPK 324
Cdd:PLN02466 354 EFVEKakaraLKRVVGDPFKKGVEQGPQ----IDSEQFEKilryIKSGVEsGATLECGGDRFGSKGYyIQPTVFSNVQDD 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 325 SRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVN--DVvmhFTLnALPFGGV 402
Cdd:PLN02466 430 MLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDV---FDA-AIPFGGY 505
|
330 340
....*....|....*....|..
gi 514452363 403 GASGMGAYHGKYSFDTFSHHRA 424
Cdd:PLN02466 506 KMSGIGREKGIYSLNNYLQVKA 527
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
93-408 |
3.44e-31 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 125.76 E-value: 3.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 93 DEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENT----AKILTKL-LPQyldqDLYAVINGGV 167
Cdd:PRK13252 134 SFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTalklAEIYTEAgLPD----GVFNVVQGDG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 168 EETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDY 246
Cdd:PRK13252 210 RVGAWLTEHpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTR 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 247 VLCEASLQNQIVQKIKETVKEFY-GENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFGGE--TDEATR---YIAP 315
Cdd:PRK13252 290 VFVQKSIKAAFEARLLERVERIRiGDPMDPATNFGPLVSFAHRDKVLGYIekgkaEGARLLCGGErlTEGGFAngaFVAP 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 316 TILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNdvvmhfTLN 395
Cdd:PRK13252 370 TVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWIN------TWG 443
|
330
....*....|....*..
gi 514452363 396 A----LPFGGVGASGMG 408
Cdd:PRK13252 444 EspaeMPVGGYKQSGIG 460
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
97-419 |
5.95e-31 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 125.02 E-value: 5.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 97 VQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-LDQDLYAVING-----GVEET 170
Cdd:PRK11241 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGsagavGGELT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 171 TELLKHRFDhilYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCE 250
Cdd:PRK11241 222 SNPLVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 251 ASLQNQIVQKIKETVKEFY-GENVKESPDYERIINLRHFKRIQ-----SLLEGQKIAFGGETDE-ATRYIAPTILTDVDP 323
Cdd:PRK11241 299 DGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 324 KSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMhfTLNALPFGGVG 403
Cdd:PRK11241 379 NAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGII--SNEVAPFGGIK 456
|
330
....*....|....*.
gi 514452363 404 ASGMGAYHGKYSFDTF 419
Cdd:PRK11241 457 ASGLGREGSKYGIEDY 472
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
1-408 |
5.70e-30 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 121.89 E-value: 5.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 1 MEREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSefngfnqeVITVLGEIGfMLANLPEWVT 80
Cdd:PRK13968 31 IENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKP--------INQARAEVA-KSANLCDWYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 81 P-TPAKKNLLTLLDE---VYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQY-L 155
Cdd:PRK13968 102 EhGPAMLKAEPTLVEnqqAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAgI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 156 DQDLYAVINGGVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKW 234
Cdd:PRK13968 182 PQGVYGWLNADNDGVSQMINDsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 235 MNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERI--INLR---HFKRIQSLLEGQKIAFGGETDE 308
Cdd:PRK13968 262 QNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALkMGDPRDEENALGPMarFDLRdelHHQVEATLAEGARLLLGGEKIA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 309 -ATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVND 387
Cdd:PRK13968 342 gAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVFING 421
|
410 420
....*....|....*....|.
gi 514452363 388 VVMHFTLNAlpFGGVGASGMG 408
Cdd:PRK13968 422 YCASDARVA--FGGVKKSGFG 440
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
96-408 |
2.04e-29 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 120.68 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 96 YVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKL-----LPQyldqdlyAVINGGVEET 170
Cdd:cd07140 142 LTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELtvkagFPK-------GVINILPGSG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 171 TELLKHRFDH-----ILYTGNATVGKIVMAAAAK-HLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAP 244
Cdd:cd07140 215 SLVGQRLSDHpdvrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 245 DYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRI-----QSLLEGQKIAFGG-ETDEATRYIAPTI 317
Cdd:cd07140 295 GRLFVEESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLveyceRGVKEGATLVYGGkQVDRPGFFFEPTV 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 318 LTDVDPKSRVMQEEIFGPVLPLVPVKNAD--EAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNdvVMHFTLN 395
Cdd:cd07140 375 FTDVEDHMFIAKEESFGPIMIISKFDDGDvdGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN--TYNKTDV 452
|
330
....*....|...
gi 514452363 396 ALPFGGVGASGMG 408
Cdd:cd07140 453 AAPFGGFKQSGFG 465
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
1-412 |
1.77e-28 |
|
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: 118.07 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 1 MEREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSefngFNQEVITVLGEIGFM--------- 71
Cdd:cd07083 57 AEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKN----WVEAIDDVAEAIDFIryyaraalr 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 72 LANLPEWVTPTPAKKNlltllDEVYVqpePLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSE----LSENTAKIL 147
Cdd:cd07083 133 LRYPAVEVVPYPGEDN-----ESFYV---GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEdavvVGYKVFEIF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 148 TKL-LPQYLDQDLYAVingGVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLT------PVTLELGGKSPCYVDKD 219
Cdd:cd07083 205 HEAgFPPGVVQFLPGV---GEEVGAYLTEHeRIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDET 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 220 CDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLEGQ 298
Cdd:cd07083 282 ADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEHG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 299 K----IAFGGETDEATRY-IAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNAD--EAINFINEREKPLALYIFSHNNKLI 371
Cdd:cd07083 362 KnegqLVLGGKRLEGEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHL 441
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 514452363 372 KRMIDETSSGGVTVNDVVMHFTLNALPFGGVGASGMGAYHG 412
Cdd:cd07083 442 EEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
84-429 |
2.98e-28 |
|
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: 117.17 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 84 AKKNLLTLLDE---VYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLY 160
Cdd:cd07116 116 AQEGSISEIDEntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 161 AVING-GVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSP-----CYVDKDcdlDVVCRRITWGK 233
Cdd:cd07116 196 NVVNGfGLEAGKPLASSkRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniffaDVMDAD---DAFFDKALEGF 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 234 WM---NCGQTCIAPDYVLCEASLQNQIVQKIKETVKEFYGENvkesP-DYERII----NLRHFKRIQSLL-----EGQKI 300
Cdd:cd07116 273 VMfalNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGN----PlDTETMIgaqaSLEQLEKILSYIdigkeEGAEV 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 301 AFGGE-----TDEATRYIAPTILTDVDpKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMI 375
Cdd:cd07116 349 LTGGErnelgGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMG 427
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 514452363 376 DETSSGGVTVNdvVMHFTLNALPFGGVGASGMGAYHGKYSFDTFSHHRaCLLKS 429
Cdd:cd07116 428 RGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK-NLLVS 478
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
5-406 |
3.98e-28 |
|
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: 116.22 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 5 VQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHeKDILA-AIGADLCKS--EFNGfnqEVITVLGEIGFMLAN----LPE 77
Cdd:cd07095 6 VAAARAAFPGWAALSLEERAAILRRFAELLKAN-KEELArLISRETGKPlwEAQT---EVAAMAGKIDISIKAyherTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 78 WVTPTPAKKNLLTLldevyvqpEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLL-PQYLD 156
Cdd:cd07095 82 RATPMAQGRAVLRH--------RPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 157 QDLYAVINGGVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHltP---VTLELGGKSPCYVDKDCDLDVVCRRITWG 232
Cdd:cd07095 154 PGVLNLVQGGRETGEALAAHeGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 233 KWMNCGQTC------IAPDYVLCEASLQnQIVQKIKETV-------KEFYG----ENVKEspDYERIINLRHFKRIQSLL 295
Cdd:cd07095 232 AFLTAGQRCtcarrlIVPDGAVGDAFLE-RLVEAAKRLRigapdaePPFMGpliiAAAAA--RYLLAQQDLLALGGEPLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 296 EGQKIafggetDEATRYIAPTILtDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMI 375
Cdd:cd07095 309 AMERL------VAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFL 381
|
410 420 430
....*....|....*....|....*....|....*
gi 514452363 376 DETSSGGVTVNDvvmhfTLN----ALPFGGVGASG 406
Cdd:cd07095 382 ARIRAGIVNWNR-----PTTgassTAPFGGVGLSG 411
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
2-416 |
1.74e-24 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 105.59 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSeFNGFNQEVITVLGEIGFMLANLPEWVTP 81
Cdd:PRK09406 26 DAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LASAKAEALKCAKGFRYYAEHAEALLAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 82 TPAKKNLLTLlDEVYVQPEPLGVVLIIGAWNYPFVLTMHplvgaiaagnaaIIKPSELSENTAkiLTKL---LPQ---YL 155
Cdd:PRK09406 105 EPADAAAVGA-SRAYVRYQPLGVVLAVMPWNFPLWQVVR------------FAAPALMAGNVG--LLKHasnVPQtalYL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 156 dQDLYA-------------VINGGVEETteLLKHRFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDL 222
Cdd:PRK09406 170 -ADLFRragfpdgcfqtllVGSGAVEAI--LRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 223 DVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE----- 296
Cdd:PRK09406 247 DRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALrVGDPTDPDTDVGPLATEQGRDEVEKQVDdavaa 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 297 GQKIAFGGET-DEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMI 375
Cdd:PRK09406 327 GATILCGGKRpDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFI 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 514452363 376 DETSSGGVTVNDVVMHFTlnALPFGGVGASGMG---AYHGKYSF 416
Cdd:PRK09406 407 DDLEAGQVFINGMTVSYP--ELPFGGVKRSGYGrelSAHGIREF 448
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
96-408 |
3.32e-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: 104.81 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 96 YVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKL-----LPQYLDQDLYAVINGGVEET 170
Cdd:cd07148 119 FTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLlheagLPEGWCQAVPCENAVAEKLV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 171 TEllkHRFDHILYTGNATVGKIVMAAAAKHlTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCE 250
Cdd:cd07148 199 TD---PRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 251 ASLQNQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLLE-----GQKIAFGGETDEATRYiAPTILTDVDPK 324
Cdd:cd07148 275 AEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVEEWVNeavaaGARLLCGGKRLSDTTY-APTVLLDPPRD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 325 SRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDvvmH--FTLNALPFGGV 402
Cdd:cd07148 354 AKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND---HtaFRVDWMPFAGR 430
|
....*.
gi 514452363 403 GASGMG 408
Cdd:cd07148 431 RQSGYG 436
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
1-411 |
4.69e-24 |
|
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: 104.58 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 1 MEREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSE-------FNGFnQEVITVLGEIGFMLA 73
Cdd:TIGR01722 40 VDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHsdalgdvARGL-EVVEHACGVNSLLKG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 74 NLPEWVTptpakKNLltlldEVYVQPEPLGVVLIIGAWNYPFV--LTMHPLVGAIAAGNAaiIKPSELSENTAKILTKLL 151
Cdd:TIGR01722 119 ETSTQVA-----TRV-----DVYSIRQPLGVCAGITPFNFPAMipLWMFPIAIACGNTFV--LKPSEKVPSAAVKLAELF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 152 PQY-LDQDLYAVINGGVEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRI 229
Cdd:TIGR01722 187 SEAgAPDGVLNVVHGDKEAVDRLLEHpDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADAL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 230 TWGKWMNCGQTCIAPDYVLCEASLQnQIVQKIKETVKEF-YGENVKESPDYERIINLRHFKRIQSLL-----EGQKIAFG 303
Cdd:TIGR01722 267 VGAAYGAAGQRCMAISAAVLVGAAD-EWVPEIRERAEKIrIGPGDDPGAEMGPLITPQAKDRVASLIaggaaEGAEVLLD 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 304 G-----ETDEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDET 378
Cdd:TIGR01722 346 GrgykvDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEI 425
|
410 420 430
....*....|....*....|....*....|...
gi 514452363 379 SSGGVTVNdVVMHFTLNALPFGGVGASGMGAYH 411
Cdd:TIGR01722 426 EVGQVGVN-VPIPVPLPYFSFTGWKDSFFGDHH 457
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
96-386 |
4.41e-21 |
|
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: 95.74 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 96 YVQPEPLGVVLIIGAWNYPFVL----TMHPLVGAIAAGNaaiiKPSELSENTAKILTKLLPQYLDQ-----DLYAVINGG 166
Cdd:cd07130 127 MEQWNPLGVVGVITAFNFPVAVwgwnAAIALVCGNVVVW----KPSPTTPLTAIAVTKIVARVLEKnglpgAIASLVCGG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 167 VEETTELLKH-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPD 245
Cdd:cd07130 203 ADVGEALVKDpRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 246 YVLceasLQNQIVQKIKETVKEFY-----GENVKESPDYERIINLRHFKRIQSLLE-----GQKIAFGGE-TDEATRYIA 314
Cdd:cd07130 283 RLI----VHESIYDEVLERLKKAYkqvriGDPLDDGTLVGPLHTKAAVDNYLAAIEeaksqGGTVLFGGKvIDGPGNYVE 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514452363 315 PTILTdVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSS--GGVTVN 386
Cdd:cd07130 359 PTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVN 431
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
101-409 |
8.69e-21 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 94.82 E-value: 8.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 101 PLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKP-SELSENTAKILTKLLPQYLDQDLYAVING-GVEETTELLKHR- 177
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPpTQGAVAALHMVHCFHLAGFPKGLISCVTGkGSEIGDFLTMHPg 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 178 FDHILYTGNATVGKIVMAAAakhLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQI 257
Cdd:PLN00412 238 VNCISFTGGDTGIAISKKAG---MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADAL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 258 VQKIKETVKEFYGENVKESPDYERIINLRHFKRIQSLLEG--QKIA-FGGETDEATRYIAPTILTDVDPKSRVMQEEIFG 334
Cdd:PLN00412 315 VEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDakEKGAtFCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 335 PVLPLVPVKNADEAINFINEREKPLALYIFSHN-NKLIkRMIDETSSGGVTVNDVVM----HFtlnalPFGGVGASGMGA 409
Cdd:PLN00412 395 PVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDiNKAI-LISDAMETGTVQINSAPArgpdHF-----PFQGLKDSGIGS 468
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
2-406 |
4.60e-20 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 92.71 E-value: 4.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSEFNGfNQEVITVLGEIGFMLANL----PE 77
Cdd:PRK09457 40 DAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEA-ATEVTAMINKIAISIQAYhertGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 78 WVTPTPAKKNLLtlldevyvQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKL-----LP 152
Cdd:PRK09457 119 KRSEMADGAAVL--------RHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLwqqagLP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 153 QyldqdlyAVIN---GGVEETTELLKHR-FDHILYTGNATVGKIVMAAAAKHltP---VTLELGGKSPCYVDKDCDLDVV 225
Cdd:PRK09457 191 A-------GVLNlvqGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 226 CRRITWGKWMNCGQTCIAPDYVLCEASLQNQ-IVQKIKETVKEF-YGE-NVKESPDYERIINLRHFKRiqsLLEGQK--I 300
Cdd:PRK09457 262 VHLIIQSAFISAGQRCTCARRLLVPQGAQGDaFLARLVAVAKRLtVGRwDAEPQPFMGAVISEQAAQG---LVAAQAqlL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 301 AFGGET-------DEATRYIAPTILtDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKR 373
Cdd:PRK09457 339 ALGGKSllemtqlQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQ 417
|
410 420 430
....*....|....*....|....*....|....*..
gi 514452363 374 MIDETSSGGVTVNDvvmhfTLN----ALPFGGVGASG 406
Cdd:PRK09457 418 FLLEIRAGIVNWNK-----PLTgassAAPFGGVGASG 449
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
5-421 |
1.27e-16 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 82.49 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 5 VQRLRQAFRSGRSRPLQFR----LQQLEALRRMVQEHEKDILAAIGADLCKSEFNGFnQEVITVLGEIGFMLANLPEWVt 80
Cdd:PLN02419 157 VSAAKQAFPLWRNTPITTRqrvmLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIF-RGLEVVEHACGMATLQMGEYL- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 81 ptPAKKNLLtlldEVYVQPEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQDLY 160
Cdd:PLN02419 235 --PNVSNGV----DTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGV 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 161 AVINGGVEETTELLKHRFD--HILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCG 238
Cdd:PLN02419 309 LNIVHGTNDTVNAICDDEDirAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAG 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 239 QTCIAPDYVLC---EASLQNQIVQKIKeTVKEFYGE--NVKESPDYERIINLRHFKRIQS--------LLEGQKIAFGGE 305
Cdd:PLN02419 389 QRCMALSTVVFvgdAKSWEDKLVERAK-ALKVTCGSepDADLGPVISKQAKERICRLIQSgvddgaklLLDGRDIVVPGY 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 306 tdEATRYIAPTILTDVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTV 385
Cdd:PLN02419 468 --EKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGI 545
|
410 420 430
....*....|....*....|....*....|....*...
gi 514452363 386 NdVVMHFTLNALPFGGVGASGMG--AYHGKYSFDTFSH 421
Cdd:PLN02419 546 N-VPIPVPLPFFSFTGNKASFAGdlNFYGKAGVDFFTQ 582
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
101-409 |
4.00e-16 |
|
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: 80.36 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 101 PLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQ--YLDQDLYAVINGGVEETTELLKH-R 177
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGKTMQALLLHpN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 178 FDHILYTGNATVGKIVMAAAakHLTPVTLELGGKSPCYVDKDCD-LDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNq 256
Cdd:cd07084 180 PKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWSK- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 257 ivQKIKETVKEFYGENVKESPDYERIINLRHFKRIQSL--LEGQKIAFGGETDEATRY-------IAPTILTDVDP---K 324
Cdd:cd07084 257 --TPLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMenLLGSVLLFSGKELKNHSIpsiygacVASALFVPIDEilkT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 325 SRVMQEEIFGPVLPLVPVKNADEA-INFINEREK-PLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTL--NALPFG 400
Cdd:cd07084 335 YELVTEEIFGPFAIVVEYKKDQLAlVLELLERMHgSLTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVapNQNHGG 414
|
....*....
gi 514452363 401 GVGASGMGA 409
Cdd:cd07084 415 GPAADPRGA 423
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
207-406 |
2.08e-15 |
|
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: 78.40 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 207 ELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQNQIVQKIKETVKEF-YGENVKESPDYERIINL 285
Cdd:cd07123 284 ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIkMGDPDDFSNFMGAVIDE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 286 RHFKRIQSLLE------GQKIAFGGETDEATRY-IAPTILTDVDPKSRVMQEEIFGPVLPL--VPVKNADEAINFINERE 356
Cdd:cd07123 364 KAFDRIKGYIDhaksdpEAEIIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFGPVLTVyvYPDSDFEETLELVDTTS 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 514452363 357 kPLALY--IFSHNNKLIKRMIDE--TSSGGVTVND-----VVmhftlNALPFGGVGASG 406
Cdd:cd07123 444 -PYALTgaIFAQDRKAIREATDAlrNAAGNFYINDkptgaVV-----GQQPFGGARASG 496
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
101-425 |
7.93e-15 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 76.80 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 101 PLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQYLDQD-----LYAVINGGVEETTELLK 175
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNnlpgaIFTSFCGGAEIGEAIAK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 176 H-RFDHILYTGNATVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASLQ 254
Cdd:PLN02315 234 DtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIY 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 255 NQIVQKIKETVKEF-YGENVKES----PDYERIINLRHFKRIQSL-LEGQKIAFGGETDEAT-RYIAPTILtDVDPKSRV 327
Cdd:PLN02315 314 DDVLEQLLTVYKQVkIGDPLEKGtllgPLHTPESKKNFEKGIEIIkSQGGKILTGGSAIESEgNFVQPTIV-EISPDADV 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 328 MQEEIFGPVLPLVPVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSS--GGVTVNDVVMHFTLNAlPFGGVGAS 405
Cdd:PLN02315 393 VKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVNIPTNGAEIGG-AFGGEKAT 471
|
330 340
....*....|....*....|
gi 514452363 406 GMGAYHGKYSFDTFSHHRAC 425
Cdd:PLN02315 472 GGGREAGSDSWKQYMRRSTC 491
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
2-409 |
5.35e-12 |
|
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: 67.99 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 2 EREVQRLRQAFRSGRSRPLQFRLQQLEALRRMVQEHEKDILAAIGADLCKSefngfnqeVITVLGE----IGF------- 70
Cdd:cd07125 72 DAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKT--------LADADAEvreaIDFcryyaaq 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 71 MLANLPEWVTPTP-AKKNLLTLldevyvqpEPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTK 149
Cdd:cd07125 144 ARELFSDPELPGPtGELNGLEL--------HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 150 LL-----PQYLdqdLYAVINGGVEETTELLKH-RFDHILYTG-NATVGKIVMAAAAKH--LTPVTLELGGKSPCYVDKDC 220
Cdd:cd07125 216 LLheagvPRDV---LQLVPGDGEEIGEALVAHpRIDGVIFTGsTETAKLINRALAERDgpILPLIAETGGKNAMIVDSTA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 221 DLDVVCRRITWGKWMNCGQTCIAPDyVLCeasLQNQIVQKIKETVKefygENVKE----SP-----DYERIINLRHFKRI 291
Cdd:cd07125 293 LPEQAVKDVVQSAFGSAGQRCSALR-LLY---LQEEIAERFIEMLK----GAMASlkvgDPwdlstDVGPLIDKPAGKLL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 292 QS---LLEGQK--IAFGGETDEATRYIAPTILTDVdpKSRVMQEEIFGPVLPLV--PVKNADEAINFINEREKPLALYIF 364
Cdd:cd07125 365 RAhteLMRGEAwlIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIH 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 514452363 365 SHNNKLIKRMIDETSSGGVTVND-----VVmhftlNALPFGGVGASGMGA 409
Cdd:cd07125 443 SRDEREIEYWRERVEAGNLYINRnitgaIV-----GRQPFGGWGLSGTGP 487
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
100-412 |
1.85e-11 |
|
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: 66.09 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 100 EPLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLLPQ--YLDQDLYAVINGGVEETTELLKH- 176
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEagFPAGTIQLLPGRGADVGAALTSDp 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 177 RFDHILYTGNATVGKIVMAAAAKHL---TPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDYVLCEASL 253
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 254 QNQIVQKIKETVKEF-YGENVKESPDYERIIN-------LRHfkrIQSLLEGQKIAFGGETD-----EATRYIAPTI--L 318
Cdd:TIGR01238 319 ADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDaeakqnlLAH---IEHMSQTQKKIAQLTLDdsracQHGTFVAPTLfeL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 319 TDVDPksrvMQEEIFGPVLPLVPVK--NADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVNDVVMHFTLNA 396
Cdd:TIGR01238 396 DDIAE----LSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGV 471
|
330
....*....|....*.
gi 514452363 397 LPFGGVGASGMGAYHG 412
Cdd:TIGR01238 472 QPFGGQGLSGTGPKAG 487
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
289-375 |
1.20e-05 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 47.65 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 289 KRIQSLLEGQKIAFGGETDEATR--------YIAPTILT--DVDPKSRVMQEEIFGPVLPLVPVKNADEAINFINEREKP 358
Cdd:cd07128 345 AAVATLLAEAEVVFGGPDRFEVVgadaekgaFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGS 424
|
90
....*....|....*..
gi 514452363 359 LALYIFSHNNKLIKRMI 375
Cdd:cd07128 425 LVASVVTNDPAFARELV 441
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
285-408 |
1.12e-04 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 44.80 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 285 LRHFKRIQSllEGQKIA---FGGETDEATrYIAPTI--LTDVDpksrVMQEEIFGPVLPLVPVKNA--DEAINFINEREK 357
Cdd:PRK11904 882 DAHIERMKR--EARLLAqlpLPAGTENGH-FVAPTAfeIDSIS----QLEREVFGPILHVIRYKASdlDKVIDAINATGY 954
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 514452363 358 PLALYIFSHNNKLIKRMIDETSSGGVTVND-----VVmhftlNALPFGGVGASGMG 408
Cdd:PRK11904 955 GLTLGIHSRIEETADRIADRVRVGNVYVNRnqigaVV-----GVQPFGGQGLSGTG 1005
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
101-452 |
1.69e-04 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 44.19 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 101 PLGVVLIIGAWNYPFVLTMHPLVGAIAAGNAAIIKPSELSENTAKILTKLL-----PQYLDQDLyavinGGVEET--TEL 173
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILleagvPAGVVQLL-----PGRGETvgAAL 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 174 LKH-RFDHILYTGNATVGKIVMAAAAKHL------TPVTLELGGKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCIAPDy 246
Cdd:PRK11809 843 VADaRVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALR- 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 247 VLCeasLQNQIVQKIKETVKEFYGENVKESPDY-----------ERIINL-RHFKRIQSllEGQKI---AFGGETDEAT- 310
Cdd:PRK11809 922 VLC---LQDDVADRTLKMLRGAMAECRMGNPDRlstdigpvidaEAKANIeRHIQAMRA--KGRPVfqaARENSEDWQSg 996
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 311 RYIAPTI--LTDVDPksrvMQEEIFGPVLPLV--PVKNADEAINFINEREKPLALYIFSHNNKLIKRMIDETSSGGVTVN 386
Cdd:PRK11809 997 TFVPPTLieLDSFDE----LKREVFGPVLHVVryNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1072
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514452363 387 DVVMHFTLNALPFGGVGASGMGAYHGK--YSFDTFSHHRA-CLLKSLKREGANklrYPPNSQSKVNLAK 452
Cdd:PRK11809 1073 RNMVGAVVGVQPFGGEGLSGTGPKAGGplYLYRLLATRPEdALAVTLARQDAE---YPVDAQLRAALLA 1138
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
167-394 |
2.86e-03 |
|
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: 40.17 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 167 VEETTELLKHR-FDHILYTGnatvGKIVMAAAAKHLTPVtleLG---GKSPCYVDKDCDLDVVCRRITWGKWMNCGQTCi 242
Cdd:cd07122 167 IELTQELMKHPdVDLILATG----GPGMVKAAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTIC- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 243 apdyvlceASLQNQIVQK-IKETVKEFYGEN----VKESpDYERIIN--LRHFKRIQSLLEGQ---KIA--FGGETDEAT 310
Cdd:cd07122 239 --------ASEQSVIVDDeIYDEVRAELKRRgayfLNEE-EKEKLEKalFDDGGTLNPDIVGKsaqKIAelAGIEVPEDT 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 311 RYIAPTIlTDVDPKSRVMQEEIFgPVLPLVPVKNADEAInfinerEKPLALY----------IFSHNNKLIK-------- 372
Cdd:cd07122 310 KVLVAEE-TGVGPEEPLSREKLS-PVLAFYRAEDFEEAL------EKARELLeyggaghtavIHSNDEEVIEefalrmpv 381
|
250 260
....*....|....*....|....*..
gi 514452363 373 -RMIDETSS----GGVTVNDVVMHFTL 394
Cdd:cd07122 382 sRILVNTPSslggIGDTYNGLAPSLTL 408
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
101-356 |
7.78e-03 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 38.68 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 101 PLGVVLIIGAWNYPF------------------VL----TMHPlvgaiaagnaaiikpsELSENTAKILTK-LLPQYLDQ 157
Cdd:cd07129 105 PLGPVAVFGASNFPLafsvaggdtasalaagcpVVvkahPAHP----------------GTSELVARAIRAaLRATGLPA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 158 DLYAVINGGVEET-TELLKH-RFDHILYTGNATVGKIVMAAAAKHLT--PVTLELGGKSPcyvdkdcdldVVcrrITWGK 233
Cdd:cd07129 169 GVFSLLQGGGREVgVALVKHpAIKAVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNP----------VF---ILPGA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 234 W----------------MNCGQTCIAPDYVLCEASLQNQ-IVQKIKETVKEFYG-----ENVKESpdYERIINlrhfkRI 291
Cdd:cd07129 236 LaergeaiaqgfvgsltLGAGQFCTNPGLVLVPAGPAGDaFIAALAEALAAAPAqtmltPGIAEA--YRQGVE-----AL 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514452363 292 QSLLEGQKIAFGGETDEATRYiAPTIL-TDVDP--KSRVMQEEIFGPVLPLVPVKNADEAINFINERE 356
Cdd:cd07129 309 AAAPGVRVLAGGAAAEGGNQA-APTLFkVDAAAflADPALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
311-408 |
8.69e-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: 38.37 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514452363 311 RYIAPTILTDVDPKSRVM-----------QEEIFGPVLPLVPVKNADEAINFINEREKPL--ALYIFSHN----NKLIKR 373
Cdd:cd07121 299 SKILKAAGIEVPADIRLIivetdkdhpfvVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNvenlTKMARA 378
|
90 100 110
....*....|....*....|....*....|....*
gi 514452363 374 MidETSSggvtvndvvmhFTLNALPFGGVGASGMG 408
Cdd:cd07121 379 M--QTTI-----------FVKNGPSYAGLGVGGEG 400
|
|
| |
