|
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: 793.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 5 VQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPA 84
Cdd:cd07132 4 VRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 85 KKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVN 164
Cdd:cd07132 84 KKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 165 GGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAP 244
Cdd:cd07132 164 GGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 245 DYILCEASSQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLEGQKIAFGGETDEATRYIAPTILTDVDPN 324
Cdd:cd07132 244 DYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 325 SKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGA 404
Cdd:cd07132 324 DPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGN 403
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 399362 405 SGMGAYHGKYSFDTFSHQRPCLLKGLKGESVNKLRYPPNS 444
Cdd:cd07132 404 SGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
5-426 |
0e+00 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 696.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 5 VQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPA 84
Cdd:cd07087 4 VARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 85 KKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVN 164
Cdd:cd07087 84 SVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 165 GGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAP 244
Cdd:cd07087 164 GGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 245 DYILCEASSQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLEGQKIAFGGETDEATRYIAPTILTDVDPN 324
Cdd:cd07087 244 DYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSPD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 325 SKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGA 404
Cdd:cd07087 324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGN 403
|
410 420
....*....|....*....|..
gi 399362 405 SGMGAYHGKYSFDTFSHQRPCL 426
Cdd:cd07087 404 SGMGAYHGKAGFDTFSHLKSVL 425
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
5-465 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 629.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 5 VQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPA 84
Cdd:PTZ00381 13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 85 KKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVN 164
Cdd:PTZ00381 93 DTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 165 GGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAP 244
Cdd:PTZ00381 173 GGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 245 DYILCEASSQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLE--GQKIAFGGETDEATRYIAPTILTDVD 322
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDIENKYVAPTIIVNPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 323 PNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGV 402
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 399362 403 GASGMGAYHGKYSFDTFSHQRPCLLKGLKGESVNKLRYPPNSESKvSW--SKFFLLKQFNKGRLQ 465
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFK-SWvlSFLLKLSIPVQSEVL 476
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
2-447 |
0e+00 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 626.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASA 81
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYM 161
Cdd:cd07136 81 KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 162 IVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTC 241
Cdd:cd07136 161 VVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 242 IAPDYILCEASSQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLEGQKIAFGGETDEATRYIAPTILTDV 321
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 322 DPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGG 401
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 399362 402 VGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESvnKLRYPPNSESK 447
Cdd:cd07136 401 VGNSGMGSYHGKYSFDTFSHKKSILKKSTWFDL--PLRYPPYKGKK 444
|
|
| 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: 586.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASA 81
Cdd:cd07135 8 DSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAKD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 RPAKKNLLT-MMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLY 160
Cdd:cd07135 88 EKVKDGPLAfMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 161 MIVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQT 240
Cdd:cd07135 168 QVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 241 CIAPDYILCEASSQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLE--GQKIAFGGETDEATRYIAPTIL 318
Cdd:cd07135 248 CVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDttKGKVVIGGEMDEATRFIPPTIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 319 TDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLP 398
Cdd:cd07135 328 SDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAP 407
|
410 420
....*....|....*....|....*.
gi 399362 399 FGGVGASGMGAYHGKYSFDTFSHQRP 424
Cdd:cd07135 408 FGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
2-426 |
0e+00 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 518.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASA 81
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYM 161
Cdd:cd07134 81 KRVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 162 IVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTC 241
Cdd:cd07134 161 VFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 242 IAPDYILCEASSQDQIVQKIKDTVKDFYGEN--VKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETDEATRYIA 314
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAEIEKFYGKDaaRKASPDLARIVNDRHFDRLKGLLDdavakGAKVEFGGQFDAAQRYIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 315 PTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTV 394
Cdd:cd07134 321 PTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLN 400
|
410 420 430
....*....|....*....|....*....|..
gi 399362 395 NSLPFGGVGASGMGAYHGKYSFDTFSHQRPCL 426
Cdd:cd07134 401 PNLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
2-426 |
0e+00 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 517.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASA 81
Cdd:cd07137 2 PRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYM 161
Cdd:cd07137 82 EKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 162 IVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNC-GQT 240
Cdd:cd07137 162 VIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 241 CIAPDYILCEASSQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLE----GQKIAFGGETDEATRYIAPT 316
Cdd:cd07137 242 CIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDdpsvADKIVHGGERDEKNLYIEPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 317 ILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNS 396
Cdd:cd07137 322 ILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDT 401
|
410 420 430
....*....|....*....|....*....|
gi 399362 397 LPFGGVGASGMGAYHGKYSFDTFSHQRPCL 426
Cdd:cd07137 402 LPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
6-424 |
1.37e-175 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 499.70 E-value: 1.37e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 6 QRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADlskselnaYSH---------EVITILGEIDFMLGNLP 76
Cdd:cd07133 5 ERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISAD--------FGHrsrhetllaEILPSIAGIKHARKHLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 77 ELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLD 156
Cdd:cd07133 77 KWMKPSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 157 QDLYMIVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMN 236
Cdd:cd07133 157 EDEVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 237 CGQTCIAPDYILCEASSQDQIVQKIKDTVKDFYGeNVKASPDYERIINLRHFKRIKSLLE-----GQKI---AFGGETDE 308
Cdd:cd07133 237 AGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEdarakGARVielNPAGEDFA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 309 ATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDV 388
Cdd:cd07133 316 ATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDT 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 399362 389 IMHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRP 424
Cdd:cd07133 396 LLHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-449 |
4.47e-155 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 449.56 E-value: 4.47e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELAS 80
Cdd:PLN02203 8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 81 ARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLY 160
Cdd:PLN02203 88 PKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 161 MIVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYID---RDCDLDVACRRITWGKYMNC 237
Cdd:PLN02203 168 KVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 238 -GQTCIAPDYILCEASSQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLEGQKIA----FGGETDEATRY 312
Cdd:PLN02203 248 aGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAasivHGGSIDEKKLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 313 IAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHF 392
Cdd:PLN02203 328 IEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQY 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 399362 393 TVNSLPFGGVGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESvnKLRYPPNSESKVS 449
Cdd:PLN02203 408 ACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEF--EFRYPPWNDFKLG 462
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
5-448 |
8.14e-131 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 387.86 E-value: 8.14e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 5 VQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPA 84
Cdd:PLN02174 16 VTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 85 KKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVN 164
Cdd:PLN02174 96 KTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 165 GGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKY-MNCGQTCIA 243
Cdd:PLN02174 176 GAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACIS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 244 PDYILCEASSQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLE----GQKIAFGGETDEATRYIAPTILT 319
Cdd:PLN02174 256 PDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 320 DVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPF 399
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPF 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 399362 400 GGVGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESVnkLRYPPNSESKV 448
Cdd:PLN02174 416 GGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSA--VRYPPYSRGKL 462
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
2-427 |
3.99e-128 |
|
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: 378.86 E-value: 3.99e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAyshevitiLGEIDFMLGNL---PEL 78
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEA--------LGEVARAADTFryyAGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 79 ASARPAKKNLLTMMD-EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LD 156
Cdd:cd07078 73 ARRLHGEVIPSPDPGeLAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 157 QDLYMIVNGGVEETTELLR--QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKY 234
Cdd:cd07078 153 PGVLNVVTGDGDEVGAALAshPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 235 MNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDFYGEN-VKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETDE 308
Cdd:cd07078 233 GNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEdakaeGAKLLCGGKRLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 309 AT--RYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGN 386
Cdd:cd07078 313 GGkgYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 399362 387 DVIMHFTVNsLPFGGVGASGMGAYHGKYSFDTFSHQRPCLL 427
Cdd:cd07078 393 DYSVGAEPS-APFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
9-427 |
1.20e-103 |
|
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: 314.17 E-value: 1.20e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 9 RQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVITILGEIDFmlgnLPELASARPAKKNL 88
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRY----AAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 89 LTMMD-EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNG- 165
Cdd:cd06534 79 SPDPGgEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 166 GVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAP 244
Cdd:cd06534 159 GDEVGAALLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 245 DYILCEASSQDQIVQKIKdtvkdfygenvkaspdyeriinlrhfkriksllegqkiafggetdeatryiapTILTDVDPN 324
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV-----------------------------------------------------TVLVDVDPD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 325 SKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNsLPFGGVGA 404
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-APFGGVKN 344
|
410 420
....*....|....*....|...
gi 399362 405 SGMGAYHGKYSFDTFSHQRPCLL 427
Cdd:cd06534 345 SGIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
5-423 |
4.77e-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: 298.19 E-value: 4.77e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 5 VQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAyshevitiLGEIDFMLGNL---PELASA 81
Cdd:COG1012 49 VAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEA--------RGEVDRAADFLryyAGEARR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 RPAKKNLLTMMD-EAYVQPEPLGVVLIIGAWNYPFVLTLQP------------LvgaiaagnaaivKPSELSENTAKILA 148
Cdd:COG1012 121 LYGETIPSDAPGtRAYVRREPLGVVGAITPWNFPLALAAWKlapalaagntvvL------------KPAEQTPLSALLLA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 149 ELLPQY-LDQDLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVA 225
Cdd:COG1012 189 ELLEEAgLPAGVLNVVTGDGSEVGAALvaHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 226 CRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQK 299
Cdd:COG1012 269 VEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIedavaEGAE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 300 IAFGGE--TDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDE 377
Cdd:COG1012 349 LLTGGRrpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARR 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 399362 378 TSSGGVTGNDVIMHFTVNsLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:COG1012 429 LEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETK 473
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
3-423 |
1.53e-84 |
|
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: 267.55 E-value: 1.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 3 RQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSElNAYSHEVITILGEIDFMLGNLPELASAR 82
Cdd:cd07099 22 AAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPR-ADAGLEVLLALEAIDWAARNAPRVLAPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 83 PAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYM 161
Cdd:cd07099 101 KVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAgPPQGVLQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 162 IVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTC 241
Cdd:cd07099 181 VVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 242 IAPDYILCEASSQDQIVQKIKDTVKDF---YGENVKAspDYERIINLRHFKRIKSLLE-----GQKIAFGGE-TDEATRY 312
Cdd:cd07099 261 ISVERVYVHESVYDEFVARLVAKARALrpgADDIGDA--DIGPMTTARQLDIVRRHVDdavakGAKALTGGArSNGGGPF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 313 IAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHF 392
Cdd:cd07099 339 YEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTA 418
|
410 420 430
....*....|....*....|....*....|.
gi 399362 393 TVNSLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07099 419 GIPALPFGGVKDSGGGRRHGAEGLREFCRPK 449
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
2-423 |
5.90e-83 |
|
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: 263.62 E-value: 5.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYsHEVITILGEIDFMLGNLPELA-S 80
Cdd:pfam00171 32 DAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR-GEVDRAIDVLRYYAGLARRLDgE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 81 ARPAKKNLLtmmdeAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDL 159
Cdd:pfam00171 111 TLPSDPGRL-----AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 160 YMIVNGGVEETTELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNC 237
Cdd:pfam00171 186 LNVVTGSGAEVGEALVEhpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 238 GQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGETDEAT- 310
Cdd:pfam00171 266 GQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVedakeEGAKLLTGGEAGLDNg 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 311 RYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIM 390
Cdd:pfam00171 346 YFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTT 425
|
410 420 430
....*....|....*....|....*....|...
gi 399362 391 hFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:pfam00171 426 -GDADGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
2-413 |
7.93e-71 |
|
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: 232.58 E-value: 7.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASA 81
Cdd:cd07098 21 DEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL-----D 156
Cdd:cd07098 101 ESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLaacghD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 157 QDLYMIVNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYM 235
Cdd:cd07098 181 PDLVQLVTCLPETAEALTSHpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 236 NCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGE---- 305
Cdd:cd07098 261 SSGQNCIGIERVIVHEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVadaveKGARLLAGGKryph 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 306 -TDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVT 384
Cdd:cd07098 341 pEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVA 420
|
410 420
....*....|....*....|....*....
gi 399362 385 GNDVIMHFTVNSLPFGGVGASGMGAYHGK 413
Cdd:cd07098 421 INDFGVNYYVQQLPFGGVKGSGFGRFAGE 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
2-423 |
1.58e-62 |
|
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: 209.69 E-value: 1.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDIL-------------AAIAADLSKSELNAYSHEVITILGEI 68
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIAdwliresgstrpkAAFEVGAAIAILREAAGLPRRPEGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 69 dfmlgnlpeLASARPAKKNlltmmdeaYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENT----- 143
Cdd:cd07104 83 ---------LPSDVPGKES--------MVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgglli 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 144 AKILAEL-LPQyldqDLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDC 220
Cdd:cd07104 146 AEIFEEAgLPK----GVLNVVPGGGSEIGDALveHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 221 DLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLL 295
Cdd:cd07104 222 DLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKalpvgDPRDPDTVIGP----LINERQVDRVHAIV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 296 E-----GQKIAFGGETDEatRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKL 370
Cdd:cd07104 298 EdavaaGARLLTGGTYEG--LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLER 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 399362 371 IKRVIDETSSGGVTGNDVimhfTVNS---LPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07104 376 AMAFAERLETGMVHINDQ----TVNDephVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
1-377 |
7.05e-61 |
|
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: 206.35 E-value: 7.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPE--- 77
Cdd:cd07088 37 ADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARRieg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 78 --LASARPAKKnlltmmdeAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY- 154
Cdd:cd07088 116 eiIPSDRPNEN--------IFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAg 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 155 LDQDLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWG 232
Cdd:cd07088 188 LPAGVLNIVTGRGSVVGDALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 233 KYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGET 306
Cdd:cd07088 268 RIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVkVGDPFDAATDMGPLVNEAALDKVEEMVEraveaGATLLTGGKR 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 399362 307 DEATR--YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDE 377
Cdd:cd07088 348 PEGEKgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNE 420
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
2-423 |
1.95e-59 |
|
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: 202.02 E-value: 1.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFmlgnLPELASA 81
Cdd:cd07093 22 DAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIPRAAANFRF----FADYILQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 RPAkkNLLTMMDEA--YVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyLDQDL 159
Cdd:cd07093 98 LDG--ESYPQDGGAlnYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELA---NEAGL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 160 ----YMIVNGGVEETTELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGK 233
Cdd:cd07093 173 ppgvVNVVHGFGPEAGAALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 234 YMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YG----ENVKASPdyerIINLRHFKRIKSLL-----EGQKIAFG 303
Cdd:cd07093 253 FSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALkVGdpldPDTEVGP----LISKEHLEKVLGYVelaraEGATILTG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 304 GETDEATR-----YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDET 378
Cdd:cd07093 329 GGRPELPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRL 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 399362 379 SSGGVTGNDvimhFTVNSL--PFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07093 409 EAGTVWVNC----WLVRDLrtPFGGVKASGIGREGGDYSLEFYTELK 451
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
2-423 |
5.01e-59 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 201.02 E-value: 5.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYshevitilGEIDFMLGNLPELASA 81
Cdd:cd07150 24 ERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW--------FETTFTPELLRAAAGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 --RPAKKnllTMMDEA-----YVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY 154
Cdd:cd07150 96 crRVRGE---TLPSDSpgtvsMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 155 -LDQDLYMIVNGGVEETTELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITW 231
Cdd:cd07150 173 gLPKGVFNVVTGGGAEVGDELVDdpRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 232 GKYMNCGQTCIAPDYILCEASSQDQIVQKI-----KDTVKDFYGENVKASPdyerIINLRHFKRIKSLLE-----GQKIA 301
Cdd:cd07150 253 GAFMHQGQICMSASRIIVEEPVYDEFVKKFvarasKLKVGDPRDPDTVIGP----LISPRQVERIKRQVEdavakGAKLL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 302 FGGETDeaTRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSG 381
Cdd:cd07150 329 TGGKYD--GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESG 406
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 399362 382 GVTGNDVIMHFTVNsLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07150 407 MVHINDPTILDEAH-VPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
100-423 |
1.26e-56 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 194.48 E-value: 1.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 100 EPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL--RQ 176
Cdd:cd07118 118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMteHP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 177 RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQ 256
Cdd:cd07118 198 DVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 257 IVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGETDE--ATRYIAPTILTDVDPNSKVM 328
Cdd:cd07118 278 FVAAVVARSRKVrVGDPLDPETKVGAIINEAQLAKITDYVdagraEGATLLLGGERLAsaAGLFYQPTIFTDVTPDMAIA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 329 QEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTvnSLPFGGVGASGMG 408
Cdd:cd07118 358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIG 435
|
330
....*....|....*
gi 399362 409 AYHGKYSFDTFSHQR 423
Cdd:cd07118 436 RELGRYGVEEYTELK 450
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
1-419 |
6.08e-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: 6.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADL------SKSELNA-------YSHEVITILGE 67
Cdd:cd07103 21 ADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQgkplaeARGEVDYaasflewFAEEARRIYGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 68 IdfmlgnLPelaSARPAKKNLltmmdeayVQPEPLGVVLIIGAWNYP-----------------FVLtlqplvgaiaagn 130
Cdd:cd07103 101 T------IP---SPAPGKRIL--------VIKQPVGVVAAITPWNFPaamitrkiapalaagctVVL------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 131 aaivKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL----RQRfdHILYTGNTAVGKIVMEAAAKHLTPVT 205
Cdd:cd07103 151 ----KPAEETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEALcaspRVR--KISFTGSTAVGKLLMAQAADTVKRVS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 206 LELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-----YGENVKASPdye 280
Cdd:cd07103 225 LELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLkvgngLDEGTDMGP--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 281 rIINLRHFKRIKSLLE-----GQKIAFGGETDEAT-RYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFIND 354
Cdd:cd07103 302 -LINERAVEKVEALVEdavakGAKVLTGGKRLGLGgYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARAND 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 399362 355 REKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMhfTVNSLPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07103 381 TPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLI--SDAEAPFGGVKESGLGREGGKEGLEEY 443
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
36-419 |
9.45e-55 |
|
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: 190.31 E-value: 9.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 36 EREKDILAAI-AADLSKS-ELNAYSH--EVITIL----GEIDFMLGnlpELASARPAKknlltmmdEAYVQPEPLGVVLI 107
Cdd:cd07144 82 EKNRDLLAAIeALDSGKPyHSNALGDldEIIAVIryyaGWADKIQG---KTIPTSPNK--------LAYTLHEPYGVCGQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 108 IGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELLRQR--FDHILYT 184
Cdd:cd07144 151 IIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHpdVDKIAFT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 185 GNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDT 264
Cdd:cd07144 231 GSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEH 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 265 VK------DFYGENVKASPdyerIINLRHFKRIKSLLE-----GQKIAFGGE----TDEATRYIAPTILTDVDPNSKVMQ 329
Cdd:cd07144 311 VKqnykvgSPFDDDTVVGP----QVSKTQYDRVLSYIEkgkkeGAKLVYGGEkapeGLGKGYFIPPTIFTDVPQDMRIVK 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 330 EEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGV---TGNDviMHFTVnslPFGGVGASG 406
Cdd:cd07144 387 EEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVwinSSND--SDVGV---PFGGFKMSG 461
|
410
....*....|...
gi 399362 407 MGAYHGKYSFDTF 419
Cdd:cd07144 462 IGRELGEYGLETY 474
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
5-421 |
1.15e-54 |
|
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: 189.38 E-value: 1.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 5 VQRLRQTFRSGRSRPLRFRLqqlEALRRMVqerekDILAAIAADLSKS-------ELNAYSHEVITILGEIDFMLGNLPE 77
Cdd:cd07102 24 LERARAAQKGWRAVPLEERK---AIVTRAV-----ELLAANTDEIAEEltwqmgrPIAQAGGEIRGMLERARYMISIAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 78 -LASARPAKKNLLtmmdEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELS----ENTAKILAE-LL 151
Cdd:cd07102 96 aLADIRVPEKDGF----ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTplcgERFAAAFAEaGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 152 PQyldqDLYMIVNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIT 230
Cdd:cd07102 172 PE----GVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 231 WGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE-----GQKIAFGG 304
Cdd:cd07102 248 DGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIAdaiakGARALIDG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 305 ET----DEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSS 380
Cdd:cd07102 328 ALfpedKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLET 407
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 399362 381 GGVTGN--DvimhFTVNSLPFGGVGASGMGAYHGKYSFDTFSH 421
Cdd:cd07102 408 GTVFMNrcD----YLDPALAWTGVKDSGRGVTLSRLGYDQLTR 446
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
95-420 |
3.95e-54 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 187.83 E-value: 3.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 95 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNG-GVEETTE 172
Cdd:cd07109 111 VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGlGAEAGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 173 LLRQR-FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEA 251
Cdd:cd07109 191 LVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 252 SSQDQIVQKIkdtVKDFYGENVKAS---PDYERIINLRHFKRIKSLLE-----GQKIAFGGETDEATR----YIAPTILT 319
Cdd:cd07109 271 SIYDEVLERL---VERFRALRVGPGledPDLGPLISAKQLDRVEGFVArararGARIVAGGRIAEGAPaggyFVAPTLLD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 320 DVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDvimHFTVN--SL 397
Cdd:cd07109 348 DVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNN---YGAGGgiEL 424
|
330 340
....*....|....*....|...
gi 399362 398 PFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07109 425 PFGGVKKSGHGREKGLEALYNYT 447
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
100-419 |
2.37e-53 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 187.21 E-value: 2.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 100 EPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEE------TTE 172
Cdd:PLN02278 159 QPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEigdallASP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 173 LLRQrfdhILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEAS 252
Cdd:PLN02278 239 KVRK----ITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 253 SQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLL-----EGQKIAFGGE--TDEATRYiAPTILTD 320
Cdd:PLN02278 315 IYDKFAEAFSKAVQklvvgDGFEEGVTQGP----LINEAAVQKVESHVqdavsKGAKVLLGGKrhSLGGTFY-EPTVLGD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 321 VDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVnsLPFG 400
Cdd:PLN02278 390 VTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEV--APFG 467
|
330
....*....|....*....
gi 399362 401 GVGASGMGAYHGKYSFDTF 419
Cdd:PLN02278 468 GVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
100-420 |
3.22e-53 |
|
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: 185.09 E-value: 3.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 100 EPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyLDQDL----YMIVNGGVEETTELLR 175
Cdd:cd07105 97 EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVF---HEAGLpkgvLNVVTHSPEDAPEVVE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 176 QRFDH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07105 174 ALIAHpavrkVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVH 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 251 ASSQDQIVQKIKDTVKDFYGENVKASPdyerIINLRHFKRIKSLLE-----GQKIAFGGETD--EATRYIAPTILTDVDP 323
Cdd:cd07105 254 ESIADEFVEKLKAAAEKLFAGPVVLGS----LVSAAAADRVKELVDdalskGAKLVVGGLADesPSGTSMPPTILDNVTP 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 324 NSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHfTVNSLPFGGVG 403
Cdd:cd07105 330 DMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVH-DEPTLPHGGVK 408
|
330
....*....|....*..
gi 399362 404 ASGMGAYHGKYSFDTFS 420
Cdd:cd07105 409 SSGYGRFNGKWGIDEFT 425
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
95-417 |
5.49e-53 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 185.49 E-value: 5.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 95 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQD-LYMIVNG-----GVE 168
Cdd:cd07091 135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPgVVNIVPGfgptaGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 169 ETTELlrqRFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYI 247
Cdd:cd07091 215 ISSHM---DVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 248 LCEASSQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLL-----EGQKIAFGGET-DEATRYIAPT 316
Cdd:cd07091 292 FVQESIYDEFVEKFKARAEkrvvgDPFDPDTFQGP----QVSKAQFDKILSYIesgkkEGATLLTGGERhGSKGYFIQPT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 317 ILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGN--DVIMHftv 394
Cdd:cd07091 368 VFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtyNVFDA--- 444
|
330 340
....*....|....*....|...
gi 399362 395 nSLPFGGVGASGMGAYHGKYSFD 417
Cdd:cd07091 445 -AVPFGGFKQSGFGRELGEEGLE 466
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
2-420 |
9.03e-53 |
|
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: 184.45 E-value: 9.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGnlpelaSA 81
Cdd:cd07092 22 DAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFRFFAG------AA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 R----PAKKNLLTMMdEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQ 157
Cdd:cd07092 96 RtlegPAAGEYLPGH-TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 158 DLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYM 235
Cdd:cd07092 175 GVVNVVCGGGASAGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYY 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 236 NCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE----GQKIAFGGETDEAT 310
Cdd:cd07092 255 NAGQDCTAACRVYVHESVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVErapaHARVLTGGRRAEGP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 311 RY-IAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDvi 389
Cdd:cd07092 335 GYfYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNT-- 412
|
410 420 430
....*....|....*....|....*....|..
gi 399362 390 mHFT-VNSLPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07092 413 -HIPlAAEMPHGGFKQSGYGKDLSIYALEDYT 443
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
101-414 |
5.71e-52 |
|
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: 181.96 E-value: 5.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 101 PLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVNGGVEETTELLRQ-RFD 179
Cdd:cd07106 114 PLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGGDELGPALTSHpDIR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 180 HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQ 259
Cdd:cd07106 194 KISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCE 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 260 KIKDTVKDFY-GENVKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETDEATRY-IAPTILTDVDPNSKVMQEEI 332
Cdd:cd07106 274 ALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEdakakGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRIVDEEQ 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 333 FGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNdviMHFTVN-SLPFGGVGASGMGAYH 411
Cdd:cd07106 354 FGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN---THGALDpDAPFGGHKQSGIGVEF 430
|
...
gi 399362 412 GKY 414
Cdd:cd07106 431 GIE 433
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
1-419 |
1.52e-51 |
|
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: 181.55 E-value: 1.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELAS 80
Cdd:cd07138 38 VDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 81 ARPAKKNLLTMmdeayvqpEPLGVVLIIGAWNYPF-----------------VLtlqplvgaiaagnaaivKPSELSENT 143
Cdd:cd07138 118 EERRGNSLVVR--------EPIGVCGLITPWNWPLnqivlkvapalaagctvVL-----------------KPSEVAPLS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 144 AKILAELLpqyLDQDL----YMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYID 217
Cdd:cd07138 173 AIILAEIL---DEAGLpagvFNLVNGDGPVVGEALsaHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIIL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 218 RDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKD-----TVKDFYGENVKASPdyerIINLRHFKRIK 292
Cdd:cd07138 250 DDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAaaeayVVGDPRDPATTLGP----LASAAQFDRVQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 293 SLL-----EGQKIAFGG----ETDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYI 363
Cdd:cd07138 326 GYIqkgieEGARLVAGGpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYV 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 399362 364 FSHNNKLIKRVIDETSSGGVTGNDVIMHFtvnSLPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07138 406 WSADPERARAVARRLRAGQVHINGAAFNP---GAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
1-408 |
1.64e-51 |
|
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: 180.87 E-value: 1.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSelnaysheVITILGEIDFMLGNLpELaS 80
Cdd:cd07149 23 VEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKP--------IKDARKEVDRAIETL-RL-S 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 81 ARPAKKNLLTM--MDE--------AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAEL 150
Cdd:cd07149 93 AEEAKRLAGETipFDAspggegriGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 151 LPQ-YLDQDLYMIVNGGVEET-TELLR-QRFDHILYTGNTAVGKIVMEAAAkhLTPVTLELGGKSPCYIDRDCDLDVACR 227
Cdd:cd07149 173 LLEaGLPKGALNVVTGSGETVgDALVTdPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEKAVE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 228 RITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLLE-----G 297
Cdd:cd07149 251 RCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKklvvgDPLDEDTDVGP----MISEAEAERIEEWVEeavegG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 298 QKIAFGGETDEAtrYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDE 377
Cdd:cd07149 327 ARLLTGGKRDGA--ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARE 404
|
410 420 430
....*....|....*....|....*....|.
gi 399362 378 TSSGGVTGNDvIMHFTVNSLPFGGVGASGMG 408
Cdd:cd07149 405 LEVGGVMIND-SSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
1-423 |
1.82e-50 |
|
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: 178.21 E-value: 1.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTF-RSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELA 79
Cdd:cd07089 21 VDAAIAAARRAFdTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSFP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 80 --SARPAKkNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyLDQ 157
Cdd:cd07089 101 weFDLPVP-ALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEII---AET 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 158 DL----YMIVNGGVEETTELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITW 231
Cdd:cd07089 177 DLpagvVNVVTGSDNAVGEALTTdpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 232 GKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YG----ENVKASPdyerIINLRHFKRIKSLL-----EGQKIA 301
Cdd:cd07089 257 VCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGdpadPGTVMGP----LISAAQRDRVEGYIargrdEGARLV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 302 FGGETDEATR---YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDET 378
Cdd:cd07089 333 TGGGRPAGLDkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRI 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 399362 379 SSGGVTGNDViMHFTVNSlPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07089 413 RTGSVGINGG-GGYGPDA-PFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
95-423 |
2.47e-50 |
|
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: 177.74 E-value: 2.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 95 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAEL-----LPQYLDQdlymIVNGGVEE 169
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPPGVVN----VVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 170 TTELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYI 247
Cdd:cd07114 189 TGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 248 LCEASSQDQIVQKIKDTVKdfygeNVK-ASPDYER-----IINLRHFKRIKSLL-----EGQKIAFGGET-----DEATR 311
Cdd:cd07114 269 LVQRSIYDEFVERLVARAR-----AIRvGDPLDPEtqmgpLATERQLEKVERYVarareEGARVLTGGERpsgadLGAGY 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 312 YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDviMH 391
Cdd:cd07114 344 FFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YR 421
|
330 340 350
....*....|....*....|....*....|..
gi 399362 392 FTVNSLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07114 422 ALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
5-423 |
4.11e-50 |
|
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: 177.16 E-value: 4.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 5 VQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEReKDILAAIAADLSKSELNAYSHEVITILGEIDFMlgnlPELASARPA 84
Cdd:cd07110 25 VRAARRAFPRWKKTTGAERAKYLRAIAEGVRER-REELAELEARDNGKPLDEAAWDVDDVAGCFEYY----ADLAEQLDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 85 KKNL-LTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAE------LLPQY 154
Cdd:cd07110 100 KAERaVPLPSEdfkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEiaaeagLPPGV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 155 LDqdlymIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWG 232
Cdd:cd07110 180 LN-----VVTGTGDEAGAPLaaHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 233 KYMNCGQTCIAPDYILCEASSQDQIVQKIKD-----TVKDFYGENVKASP-----DYERIinLRHFKRIKSllEGQKIAF 302
Cdd:cd07110 255 CFWNNGQICSATSRLLVHESIADAFLERLATaaeaiRVGDPLEEGVRLGPlvsqaQYEKV--LSFIARGKE--EGARLLC 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 303 GGETDEATR---YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETS 379
Cdd:cd07110 331 GGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALE 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 399362 380 SGGVTGNDVIMHFTvnSLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:cd07110 411 AGIVWINCSQPCFP--QAPWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
101-423 |
4.88e-50 |
|
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: 176.72 E-value: 4.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 101 PLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENT-----AKILAEL-LPQYLDQdlymIVNGGVEETTELL 174
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSggvviARLFEEAgLPAGVLH----VLPGGADAGEALV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 175 R-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASS 253
Cdd:cd07152 186 EdPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 254 QDQIVQKIKD-----TVKDFYGENVKASPdyerIINLRHFKRIKSLLE-----GQKIAFGGETDEatRYIAPTILTDVDP 323
Cdd:cd07152 266 ADAYTAKLAAkakhlPVGDPATGQVALGP----LINARQLDRVHAIVDdsvaaGARLEAGGTYDG--LFYRPTVLSGVKP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 324 NSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVimhfTVNS---LPFG 400
Cdd:cd07152 340 GMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVNDephNPFG 415
|
330 340
....*....|....*....|....
gi 399362 401 GVGASGMGAYHG-KYSFDTFSHQR 423
Cdd:cd07152 416 GMGASGNGSRFGgPANWEEFTQWQ 439
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
96-420 |
7.56e-50 |
|
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: 176.48 E-value: 7.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 96 YVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL 174
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 175 RQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEAS 252
Cdd:cd07115 192 VEHpdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 253 SQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGETDEATR-YIAPTILTDVDPNS 325
Cdd:cd07115 272 IYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDRVLDYVdvgreEGARLLTGGKRPGARGfFVEPTIFAAVPPEM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 326 KVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNdvIMHFTVNSLPFGGVGAS 405
Cdd:cd07115 352 RIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQS 429
|
330
....*....|....*
gi 399362 406 GMGAYHGKYSFDTFS 420
Cdd:cd07115 430 GFGREMGREALDEYT 444
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
95-421 |
1.49e-49 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 175.96 E-value: 1.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 95 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGvEETTEL 173
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 174 LRQRFD--HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEA 251
Cdd:cd07090 189 LCEHPDvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 252 SSQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLL-----EGQKIAFGGE----TD--EATRYIAP 315
Cdd:cd07090 269 SIKDEFTERLVERTKkirigDPLDEDTQMGA----LISEEHLEKVLGYIesakqEGAKVLCGGErvvpEDglENGFYVSP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 316 TILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDvimhFTVN 395
Cdd:cd07090 345 CVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT----YNIS 420
|
330 340
....*....|....*....|....*...
gi 399362 396 S--LPFGGVGASGMGAYHGKYSFDTFSH 421
Cdd:cd07090 421 PveVPFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
3-408 |
2.12e-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: 175.24 E-value: 2.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 3 RQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPEL-ASA 81
Cdd:cd07108 23 RAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVLADLFRYFGGLAGELkGET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 RPAKKNLLTmmdeaYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYM 161
Cdd:cd07108 103 LPFGPDVLT-----YTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 162 IVNGGVEETTELLRQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWG-KYMNCG 238
Cdd:cd07108 178 VITGYGEECGAALVDHpdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGmRFTRQG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 239 QTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE------GQKIAFGGETDEATR 311
Cdd:cd07108 258 QSCTAGSRLFVHEDIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDlglstsGATVLRGGPLPGEGP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 312 -----YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGN 386
Cdd:cd07108 338 ladgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVN 417
|
410 420
....*....|....*....|..
gi 399362 387 DviMHFTVNSLPFGGVGASGMG 408
Cdd:cd07108 418 Q--GGGQQPGQSYGGFKQSGLG 437
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
36-420 |
1.38e-47 |
|
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: 171.17 E-value: 1.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 36 EREKDILAAIAA-DLSKSELNAYSHEVITILGEIDFMLGnlpelasarPAKKNLLTMMDE-----AYVQPEPLGVVLIIG 109
Cdd:cd07143 82 ERNLDYLASIEAlDNGKTFGTAKRVDVQASADTFRYYGG---------WADKIHGQVIETdikklTYTRHEPIGVCGQII 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 110 AWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL--RQRFDHILYTGN 186
Cdd:cd07143 153 PWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAIssHMDIDKVAFTGS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 187 TAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTV 265
Cdd:cd07143 233 TLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 266 K-----DFYGENVKASPDYERIinlrHFKRIKSLLE-----GQKIAFGGETDEATRY-IAPTILTDVDPNSKVMQEEIFG 334
Cdd:cd07143 313 KklkvgDPFAEDTFQGPQVSQI----QYERIMSYIEsgkaeGATVETGGKRHGNEGYfIEPTIFTDVTEDMKIVKEEIFG 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 335 PILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDV-IMHFTVnslPFGGVGASGMGAYHGK 413
Cdd:cd07143 389 PVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYnLLHHQV---PFGGYKQSGIGRELGE 465
|
....*..
gi 399362 414 YSFDTFS 420
Cdd:cd07143 466 YALENYT 472
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
2-421 |
2.24e-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: 170.61 E-value: 2.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSK--SELNAyshEVITILGEIDFMLGNLPEL- 78
Cdd:cd07131 40 DAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKplAEGRG---DVQEAIDMAQYAAGEGRRLf 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 79 ----ASARPAKknlltmmdEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY 154
Cdd:cd07131 117 getvPSELPNK--------DAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 155 -LDQDLYMIVNGGVEETTELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITW 231
Cdd:cd07131 189 gLPPGVVNVVHGRGEEVGEALVEhpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALW 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 232 GKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGE 305
Cdd:cd07131 269 SAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLNYNeigkeEGATLLLGGE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 306 -----TDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSS 380
Cdd:cd07131 349 rltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEA 428
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 399362 381 GGVTGNDVIMHFTVNsLPFGGVGASGMGAYHGKYS-FDTFSH 421
Cdd:cd07131 429 GITYVNAPTIGAEVH-LPFGGVKKSGNGHREAGTTaLDAFTE 469
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
94-420 |
5.50e-47 |
|
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: 169.41 E-value: 5.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 94 EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTE 172
Cdd:cd07119 127 ISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 173 LL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07119 207 ELaeSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 251 ASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGE--TDEATR---YIAPTILT 319
Cdd:cd07119 287 ESIHDKFVAALAERAKKIkLGNGLDADTEMGPLVSAEHREKVLSYIqlgkeEGARLVCGGKrpTGDELAkgyFVEPTIFD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 320 DVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDviMHFTVNSLPF 399
Cdd:cd07119 367 DVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPW 444
|
330 340
....*....|....*....|.
gi 399362 400 GGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07119 445 GGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
23-420 |
6.90e-47 |
|
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: 168.64 E-value: 6.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 23 RLQQLEALRRMVQEREKDILAAIAADLSKSELNAyshevitiLGEIDFMLGNLPELAS--ARPAKKNLLTMMD--EAYVQ 98
Cdd:cd07151 56 RAEILEKAAQILEERRDEIVEWLIRESGSTRIKA--------NIEWGAAMAITREAATfpLRMEGRILPSDVPgkENRVY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 99 PEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENT-----AKILAEL-LPQYLdqdLYMIVNGGVEETTE 172
Cdd:cd07151 128 REPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITgglllAKIFEEAgLPKGV---LNVVVGAGSEIGDA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 173 LLRQ---RFdhILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC 249
Cdd:cd07151 205 FVEHpvpRL--ISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 250 EASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETDEatRYIAPTILTDVDP 323
Cdd:cd07151 283 HEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIEqaveeGATLLVGGEAEG--NVLEPTVLSDVTN 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 324 NSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVimhfTVNS---LPFG 400
Cdd:cd07151 361 DMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQ----PVNDephVPFG 436
|
410 420
....*....|....*....|
gi 399362 401 GVGASGMGAYHGKYSFDTFS 420
Cdd:cd07151 437 GEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
1-419 |
8.90e-47 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 168.52 E-value: 8.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTFRSG--RSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLgnlpEL 78
Cdd:cd07139 38 VDAAVAAARRAFDNGpwPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRAQGPGPAALLRYYA----AL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 79 ASARPAKKNLLTM-MDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LD 156
Cdd:cd07139 114 ARDFPFEERRPGSgGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 157 QDLYMIVNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYM 235
Cdd:cd07139 194 PGVVNVVPADREVGEYLVRHpGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLM 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 236 NCGQTCIAPDYILCEASSQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRI-----KSLLEGQKIAFGGE 305
Cdd:cd07139 274 NNGQVCVALTRILVPRSRYDEVVEALAAAVAalkvgDPLDPATQIGP----LASARQRERVegyiaKGRAEGARLVTGGG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 306 T-DEATR--YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGG 382
Cdd:cd07139 350 RpAGLDRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGT 429
|
410 420 430
....*....|....*....|....*....|....*..
gi 399362 383 VTGNDVIMHFtvnSLPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07139 430 VGVNGFRLDF---GAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
93-420 |
6.17e-46 |
|
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: 166.14 E-value: 6.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 93 DEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETT 171
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 172 ELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC 249
Cdd:TIGR01804 205 PLLvnHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 250 EASSQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLL-----EGQKIAFGG------ETDEATrYI 313
Cdd:TIGR01804 285 HKKIKERFLARLVERTEriklgDPFDEATEMGP----LISAAHRDKVLSYIekgkaEGATLATGGgrpenvGLQNGF-FV 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 314 APTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDviMHFT 393
Cdd:TIGR01804 360 EPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLY 437
|
330 340
....*....|....*....|....*..
gi 399362 394 VNSLPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:TIGR01804 438 PAEAPFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
95-408 |
1.22e-45 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 165.21 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 95 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEET-TE 172
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVgDE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 173 LLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEA 251
Cdd:cd07145 197 IVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 252 SSQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLL-----EGQKIAFGGETDEATrYIAPTILTDV 321
Cdd:cd07145 277 EVYDKFLKLLVEKVKklkvgDPLDESTDLGP----LISPEAVERMENLVndaveKGGKILYGGKRDEGS-FFPPTVLEND 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 322 DPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMhFTVNSLPFGG 401
Cdd:cd07145 352 TPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR-FRWDNLPFGG 430
|
....*..
gi 399362 402 VGASGMG 408
Cdd:cd07145 431 FKKSGIG 437
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
79-408 |
1.50e-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: 165.59 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 79 ASARPAKKNLLTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL 155
Cdd:cd07559 111 AGVIRAQEGSLSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 156 DQDLYMIVNG-GVEETTELL-RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYI-----DRDCDLDVACRR 228
Cdd:cd07559 191 PKGVVNVVTGfGSEAGKPLAsHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 229 ITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVkdfygENVKA-SP-DYERII----NLRHFKRIKSLL-----EG 297
Cdd:cd07559 271 GQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERF-----EAIKVgNPlDPETMMgaqvSKDQLEKILSYVdigkeEG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 298 QKIAFGGE-----TDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIK 372
Cdd:cd07559 346 AEVLTGGErltlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRAL 425
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 399362 373 RVIDETSSGGVTGNdvimhfTVNSLP----FGGVGASGMG 408
Cdd:cd07559 426 RVARGIQTGRVWVN------CYHQYPahapFGGYKKSGIG 459
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
95-420 |
1.79e-45 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 165.08 E-value: 1.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 95 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAEL-----LPQyldqDLYMIVNGGVEE 169
Cdd:cd07112 118 ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLPA----GVLNVVPGFGHT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 170 TTELL--RQRFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDC-DLDVACRRITWGKYMNCGQTCIAPD 245
Cdd:cd07112 194 AGEALglHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 246 YILCEASSQDQIVQKIKDTVKDFY-GENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGETDEATR---YIAPT 316
Cdd:cd07112 274 RLLVHESIKDEFLEKVVAAAREWKpGDPLDPATRMGALVSEAHFDKVLGYIesgkaEGARLVAGGKRVLTETggfFVEPT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 317 ILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNdvimhfTVN- 395
Cdd:cd07112 354 VFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN------CFDe 427
|
330 340
....*....|....*....|....*...
gi 399362 396 ---SLPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07112 428 gdiTTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
2-412 |
1.66e-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: 1.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDiLAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELasa 81
Cdd:cd07107 22 DRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEE-LALIDALDCGNPVSAMLGDVMVAAALLDYFAGLVTEL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 rpaKKNLLTMMDEA--YVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDL 159
Cdd:cd07107 98 ---KGETIPVGGRNlhYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 160 YMIVNGGVEETTE-LLRQR-FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGkyMN- 236
Cdd:cd07107 175 FNILPGDGATAGAaLVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAG--MNf 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 237 --CGQTCIAPDYILCEASSQDQIVQKIKDTVKDFY-GENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGG--ET 306
Cdd:cd07107 253 twCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIdsakrEGARLVTGGgrPE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 307 DEATR---YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGV 383
Cdd:cd07107 333 GPALEggfYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYV 412
|
410 420
....*....|....*....|....*....
gi 399362 384 TGNDVIMHFTvnSLPFGGVGASGMGAYHG 412
Cdd:cd07107 413 WINGSSRHFL--GAPFGGVKNSGIGREEC 439
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
96-381 |
1.87e-43 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 158.36 E-value: 1.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 96 YVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL 174
Cdd:PRK10090 66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 175 --RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEAS 252
Cdd:PRK10090 146 agNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 253 SQDQIVQKIKDTVKDF-YGENVKAS-PDYERIINLRHFKRIKSLL-----EGQKIAFGGETDEATRYI-APTILTDVDPN 324
Cdd:PRK10090 226 IYDQFVNRLGEAMQAVqFGNPAERNdIAMGPLINAAALERVEQKVaraveEGARVALGGKAVEGKGYYyPPTLLLDVRQE 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 399362 325 SKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSG 381
Cdd:PRK10090 306 MSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFG 362
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
1-419 |
2.01e-43 |
|
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: 158.39 E-value: 2.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEReKDILAAIAAD-----LSKSelnayshevitiLGEI------- 68
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRER-KDELARLITLemgkpIAEA------------RAEVekcawic 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 69 DFMLGNLPELASARPAKknllTMMDEAYVQPEPLGVVLIIGAWNYPF---------------VLTLqplvgaiaagnaai 133
Cdd:cd07100 68 RYYAENAEAFLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFwqvfrfaapnlmagnTVLL-------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 134 vKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELLR-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGK 211
Cdd:cd07100 130 -KHASNVPGCALAIEELFREAgFPEGVFQNLLIDSDQVEAIIAdPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 212 SPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVK-----DFYGENVKASP--------D 278
Cdd:cd07100 209 DPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAalkvgDPMDEDTDLGPlarkdlrdE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 279 YERIINlrhfkriKSLLEGQKIAFGGET-DEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREK 357
Cdd:cd07100 289 LHEQVE-------EAVAAGATLLLGGKRpDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPF 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 399362 358 PLALYIFSHNNKLIKRVIDETSSGGVTGNDVimhftVNS---LPFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07100 362 GLGGSVFTTDLERAERVARRLEAGMVFINGM-----VKSdprLPFGGVKRSGYGRELGRFGIREF 421
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
2-413 |
2.33e-43 |
|
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: 159.01 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPELASA 81
Cdd:cd07101 21 EAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFE-EVLDVAIVARYYARRAERLLKP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 RPaKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLY 160
Cdd:cd07101 100 RR-RRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLPRDLW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 161 MIVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQT 240
Cdd:cd07101 179 QVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 241 CIAPDYILCEASSQDQIVQKIKDTVkdfygENVKASPDYE------RIINLRHFKRIKSLLE-----GQKIAFGGET--D 307
Cdd:cd07101 259 CVSIERIYVHESVYDEFVRRFVART-----RALRLGAALDygpdmgSLISQAQLDRVTAHVDdavakGATVLAGGRArpD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 308 EATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGND 387
Cdd:cd07101 334 LGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE 413
|
410 420
....*....|....*....|....*...
gi 399362 388 vIMHFTVNSL--PFGGVGASGMGAYHGK 413
Cdd:cd07101 414 -GYAAAWASIdaPMGGMKDSGLGRRHGA 440
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
94-409 |
2.67e-43 |
|
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: 159.34 E-value: 2.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 94 EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNG-GVEETT 171
Cdd:cd07097 128 EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGsGSEVGQ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 172 ELLR-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07097 208 ALVEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 251 ASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGET-DEATR--YIAPTILTDV 321
Cdd:cd07097 288 EGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIeiarsEGAKLVYGGERlKRPDEgyYLAPALFAGV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 322 DPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGN--DVIMHFTVnslPF 399
Cdd:cd07097 368 TNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlpTAGVDYHV---PF 444
|
330
....*....|
gi 399362 400 GGVGASGMGA 409
Cdd:cd07097 445 GGRKGSSYGP 454
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
95-408 |
4.60e-43 |
|
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: 158.76 E-value: 4.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 95 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGgveeTTEL 173
Cdd:cd07113 136 AFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNG----KGAV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 174 LRQRFDH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYIL 248
Cdd:cd07113 212 GAQLISHpdvakVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 249 CEASSQDQIVQKIKDTVKDFY-GENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGET-DEATRYIAPTILTDV 321
Cdd:cd07113 292 VHRSKFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEAlAGEGYFVQPTLVLAR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 322 DPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNdviMHFTVN-SLPFG 400
Cdd:cd07113 372 SADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDpAVPFG 448
|
....*...
gi 399362 401 GVGASGMG 408
Cdd:cd07113 449 GMKQSGIG 456
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
79-408 |
4.88e-43 |
|
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: 158.77 E-value: 4.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 79 ASARPAKKNLLTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL 155
Cdd:cd07117 111 AGVIRAEEGSANMIDEdtlSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 156 DQDLYMIVNGGVEETTELLRQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGK 233
Cdd:cd07117 191 PKGVVNIVTGKGSKSGEYLLNHpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 234 YMNCGQTCIAPDYILCEASSQDQIVQKIKdtvKDFygENVKA----SPDYE--RIINLRHFKRIKSLL-----EGQKIAF 302
Cdd:cd07117 271 LFNQGQVCCAGSRIFVQEGIYDEFVAKLK---EKF--ENVKVgnplDPDTQmgAQVNKDQLDKILSYVdiakeEGAKILT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 303 GGE-----TDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDE 377
Cdd:cd07117 346 GGHrltenGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARA 425
|
330 340 350
....*....|....*....|....*....|....*
gi 399362 378 TSSGGVTGNdvimhfTVNSLP----FGGVGASGMG 408
Cdd:cd07117 426 VETGRVWVN------TYNQIPagapFGGYKKSGIG 454
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
2-408 |
5.08e-43 |
|
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: 157.98 E-value: 5.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAyshevitiLGEIDFMLGNLpELASA 81
Cdd:cd07094 24 EEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA--------RVEVDRAIDTL-RLAAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 R---------PAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELL- 151
Cdd:cd07094 95 EaerirgeeiPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILv 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 152 PQYLDQDLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKhlTPVTLELGGKSPCYIDRDCDLDVACRRI 229
Cdd:cd07094 175 EAGVPEGVLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEAL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 230 TWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRI-----KSLLEGQKIAFG 303
Cdd:cd07094 253 AKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLkVGDPLDEDTDVGPLISEEAAERVerwveEAVEAGARLLCG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 304 GETDEATRYiaPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHN-NKLIKrVIDETSSGG 382
Cdd:cd07094 333 GERDGALFK--PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDlNVAFK-AAEKLEVGG 409
|
410 420
....*....|....*....|....*.
gi 399362 383 VTGNDViMHFTVNSLPFGGVGASGMG 408
Cdd:cd07094 410 VMVNDS-SAFRTDWMPFGGVKESGVG 434
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
2-420 |
2.84e-42 |
|
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: 155.98 E-value: 2.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRF-RLQQLEALRRMVQEREKDILAAIAADLSKS-------------ELNAYSHEVITILGE 67
Cdd:cd07146 20 EEALREALALAASYRSTLTRYqRSAILNKAAALLEARREEFARLITLESGLClkdtryevgraadVLRFAAAEALRDDGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 68 -IDFmlgnlpELASARPAKKnlltmmdeAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKI 146
Cdd:cd07146 100 sFSC------DLTANGKARK--------IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 147 LAELLPQY-LDQDLYMIVNGGVEETTELLRQ--RFDHILYTGNTAVGKIVMEAAA-KHLTpvtLELGGKSPCYIDRDCDL 222
Cdd:cd07146 166 LADLLYEAgLPPDMLSVVTGEPGEIGDELIThpDVDLVTFTGGVAVGKAIAATAGyKRQL---LELGGNDPLIVMDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 223 DVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIIN---LRHFKRI--KSLLE 296
Cdd:cd07146 243 ERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDeeaAIQIENRveEAIAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 297 GQKIAFGGETDEAtrYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVID 376
Cdd:cd07146 323 GARVLLGNQRQGA--LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 399362 377 ETSSGGVTGNDViMHFTVNSLPFGGVGASGMGAYHG-KYSFDTFS 420
Cdd:cd07146 401 RLDVGTVNVNEV-PGFRSELSPFGGVKDSGLGGKEGvREAMKEMT 444
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
95-419 |
1.57e-41 |
|
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: 154.57 E-value: 1.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 95 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNG-GVEETTE 172
Cdd:cd07142 135 VYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGfGPTAGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 173 LLRQR-FDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCE 250
Cdd:cd07142 215 IASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVH 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 251 ASSQDQIVQKIKD-----TVKDFYGENVKASPDyeriINLRHFKRIKSLL-----EGQKIAFGGE-TDEATRYIAPTILT 319
Cdd:cd07142 295 ESIYDEFVEKAKAralkrVVGDPFRKGVEQGPQ----VDKEQFEKILSYIehgkeEGATLITGGDrIGSKGYYIQPTIFS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 320 DVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGN--DVimhFTVnSL 397
Cdd:cd07142 371 DVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDV---FDA-SI 446
|
330 340
....*....|....*....|..
gi 399362 398 PFGGVGASGMGAYHGKYSFDTF 419
Cdd:cd07142 447 PFGGYKMSGIGREKGIYALNNY 468
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-409 |
8.19e-41 |
|
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: 153.15 E-value: 8.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKS--ELNAYSHEVItilgeiDF-------ML 72
Cdd:cd07124 72 EAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNwaEADADVAEAI------DFleyyareML 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 73 GNLPELASARPAKKNLLTMmdeayvqpEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLP 152
Cdd:cd07124 146 RLRGFPVEMVPGEDNRYVY--------RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 153 QY-LDQDLYMIVNGGVEETTELLrqrFDH-----ILYTGNTAVGKIVMEAAAK------HLTPVTLELGGKSPCYIDRDC 220
Cdd:cd07124 218 EAgLPPGVVNFLPGPGEEVGDYL---VEHpdvrfIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 221 DLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE--- 296
Cdd:cd07124 295 DLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALkVGDPEDPEVYMGPVIDKGARDRIRRYIEigk 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 297 -GQKIAFGGETDE-ATR--YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIK 372
Cdd:cd07124 375 sEGRLLLGGEVLElAAEgyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLE 454
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 399362 373 RVIDETSSG------GVTGNDVIMHftvnslPFGGVGASGMGA 409
Cdd:cd07124 455 RARREFEVGnlyanrKITGALVGRQ------PFGGFKMSGTGS 491
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
2-423 |
2.54e-40 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 151.95 E-value: 2.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPE-LAS 80
Cdd:PRK09407 57 EAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFE-EVLDVALTARYYARRAPKlLAP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 81 ARpaKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDL 159
Cdd:PRK09407 136 RR--RAGALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 160 YMIVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQ 239
Cdd:PRK09407 214 WQVVTGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 240 TCIAPDYILCEASSQDQIVQKIKDTVKDFygeNVKASPDYE----RIINLRHFKRIKSLLE-----GQKIAFGGET--DE 308
Cdd:PRK09407 294 LCISIERIYVHESIYDEFVRAFVAAVRAM---RLGAGYDYSadmgSLISEAQLETVSAHVDdavakGATVLAGGKArpDL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 309 ATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDV 388
Cdd:PRK09407 371 GPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEG 450
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 399362 389 IMH-FTVNSLPFGGVGASGMGAYHG-----KYS-FDTFSHQR 423
Cdd:PRK09407 451 YAAaWGSVDAPMGGMKDSGLGRRHGaegllKYTeSQTIATQR 492
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
2-408 |
7.69e-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: 7.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRS--RPLRFrlqqlEALRRMVQEREKDiLAAIAADLSKselnayshEVITIL----GEI------- 68
Cdd:cd07086 38 EAAVAAAREAFKEWRKvpAPRRG-----EIVRQIGEALRKK-KEALGRLVSL--------EMGKILpeglGEVqemidic 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 69 DFMLG-----NLPELASARPAKKnlltMMDeayvQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSE----L 139
Cdd:cd07086 104 DYAVGlsrmlYGLTIPSERPGHR----LME----QWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSEttplT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 140 SENTAKILAELLPQY-LDQDLYMIVNGGVEeTTELLR--QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYI 216
Cdd:cd07086 176 AIAVTKILAEVLEKNgLPPGVVNLVTGGGD-GGELLVhdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 217 DRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL 295
Cdd:cd07086 255 MDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNAI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 296 E-----GQKIAFGGET---DEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHN 367
Cdd:cd07086 335 EiaksqGGTVLTGGKRidgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTED 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 399362 368 NKLIKRVIDETSS--------GGVTGNDVimhftvnSLPFGGVGASGMG 408
Cdd:cd07086 415 LREAFRWLGPKGSdcgivnvnIPTSGAEI-------GGAFGGEKETGGG 456
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
92-423 |
1.68e-39 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 149.50 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 92 MDE--AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAE------LLPQYLDqdlymIV 163
Cdd:PLN02467 140 METfkGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADicrevgLPPGVLN-----VV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 164 NG-GVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTC 241
Cdd:PLN02467 215 TGlGTEAGAPLASHpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQIC 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 242 IAPDYILCEASSQDQIVQKIKDTVKdfygeNVKASPDYER------IINLRHFKRIKSLL-----EGQKIAFGGETDEAT 310
Cdd:PLN02467 295 SATSRLLVHERIASEFLEKLVKWAK-----NIKISDPLEEgcrlgpVVSEGQYEKVLKFIstaksEGATILCGGKRPEHL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 311 R---YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGND 387
Cdd:PLN02467 370 KkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINC 449
|
330 340 350
....*....|....*....|....*....|....*.
gi 399362 388 VIMHFTvnSLPFGGVGASGMGAYHGKYSFDTFSHQR 423
Cdd:PLN02467 450 SQPCFC--QAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
10-408 |
2.04e-39 |
|
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: 148.16 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 10 QTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAY-------------SHEVITILGEIdfmlgnLP 76
Cdd:cd07147 32 KAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARgevaraidtfriaAEEATRIYGEV------LP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 77 ELASARPAKKnlltmmdEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELL-PQYL 155
Cdd:cd07147 106 LDISARGEGR-------QGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaETGL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 156 DQDLYMIVNGGVEETTELLR-QRFDHILYTGNTAVG-KIVMEAAAKHltpVTLELGGKSPCYIDRDCDLDVACRRITWGK 233
Cdd:cd07147 179 PKGAFSVLPCSRDDADLLVTdERIKLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDADLDFAAQRIIFGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 234 YMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETD 307
Cdd:cd07147 256 FYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALkTGDPKDDATDVGPMISESEAERVEGWVNeavdaGAKLLTGGKRD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 308 EATryIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGND 387
Cdd:cd07147 336 GAL--LEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVIND 413
|
410 420
....*....|....*....|.
gi 399362 388 ViMHFTVNSLPFGGVGASGMG 408
Cdd:cd07147 414 V-PTFRVDHMPYGGVKDSGIG 433
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
100-406 |
1.10e-38 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 147.39 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 100 EPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL---- 174
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYLvdhp 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 175 RQRFdhILYTGNTAVGKIVMEAAAK------HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYIL 248
Cdd:PRK03137 250 KTRF--ITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 249 CEASSQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLE-GQ---KIAFGGETDEATRY-IAPTILTDVDP 323
Cdd:PRK03137 328 VHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEiGKeegRLVLGGEGDDSKGYfIQPTIFADVDP 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 324 NSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSG------GVTGNDVIMHftvnsl 397
Cdd:PRK03137 408 KARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGnlyfnrGCTGAIVGYH------ 481
|
....*....
gi 399362 398 PFGGVGASG 406
Cdd:PRK03137 482 PFGGFNMSG 490
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
94-420 |
1.35e-38 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 146.18 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 94 EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVgaiaagnaaivkPSELSENT-----AK---ILAELLPQYLDQ-----DLY 160
Cdd:cd07082 134 IAQVRREPLGVVLAIGPFNYPLNLTVSKLI------------PALIMGNTvvfkpATqgvLLGIPLAEAFHDagfpkGVV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 161 MIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKhlTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCG 238
Cdd:cd07082 202 NVVTGRGREIGDPLvtHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSG 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 239 QTCIAPDYILCEASSQDQIVQKIKD-----TVKDFYGENV-------KASPDYeriinlrhfkrIKSLLE-----GQKIA 301
Cdd:cd07082 280 QRCTAIKRVLVHESVADELVELLKEevaklKVGMPWDNGVditplidPKSADF-----------VEGLIDdavakGATVL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 302 FGGETDEATrYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSG 381
Cdd:cd07082 349 NGGGREGGN-LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVG 427
|
330 340 350
....*....|....*....|....*....|....*....
gi 399362 382 GVTGNDVIMHfTVNSLPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07082 428 TVNINSKCQR-GPDHFPFLGRKDSGIGTQGIGDALRSMT 465
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
96-417 |
2.21e-38 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 145.82 E-value: 2.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 96 YVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVNGGVEETTELL- 174
Cdd:PRK13473 133 MIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALv 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 175 -RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASS 253
Cdd:PRK13473 213 gHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGI 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 254 QDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE------GQKIAFGGET-DEATRYIAPTILTDVDPNS 325
Cdd:PRK13473 293 YDDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFVErakalgHIRVVTGGEApDGKGYYYEPTLLAGARQDD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 326 KVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMhfTVNSLPFGGVGAS 405
Cdd:PRK13473 373 EIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQS 450
|
330
....*....|....*.
gi 399362 406 GmgayHGK----YSFD 417
Cdd:PRK13473 451 G----YGKdmslYGLE 462
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
95-420 |
5.51e-38 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 144.80 E-value: 5.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 95 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAEL-------------LPQYLDQDLYM 161
Cdd:cd07141 139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLikeagfppgvvnvVPGYGPTAGAA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 162 IVNggveettellRQRFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQT 240
Cdd:cd07141 219 ISS----------HPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQC 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 241 CIAPDYILCEASSQDQIVQKI-----KDTVKDFYGENVKASPDyeriINLRHFKRIKSLL-----EGQKIAFGGET-DEA 309
Cdd:cd07141 289 CCAGSRTFVQESIYDEFVKRSverakKRVVGNPFDPKTEQGPQ----IDEEQFKKILELIesgkkEGAKLECGGKRhGDK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 310 TRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNnklIKRVIdeTSSGGVTGNDVI 389
Cdd:cd07141 365 GYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD---IDKAI--TFSNALRAGTVW 439
|
330 340 350
....*....|....*....|....*....|....*
gi 399362 390 M----HFTVNSlPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07141 440 VncynVVSPQA-PFGGYKMSGNGRELGEYGLQEYT 473
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
94-421 |
1.28e-37 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 144.19 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 94 EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVNGGVEETTEL 173
Cdd:PLN02766 151 QGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 174 L---RQRFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC 249
Cdd:PLN02766 231 AiasHMDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 250 EASSQDQIVQKIKDTVKDF-----YGENVKASP-----DYERIIN-LRHFKRiksllEGQKIAFGGE-TDEATRYIAPTI 317
Cdd:PLN02766 311 QEGIYDEFVKKLVEKAKDWvvgdpFDPRARQGPqvdkqQFEKILSyIEHGKR-----EGATLLTGGKpCGDKGYYIEPTI 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 318 LTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNdviMHFTV-NS 396
Cdd:PLN02766 386 FTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYFAFdPD 462
|
330 340
....*....|....*....|....*
gi 399362 397 LPFGGVGASGMGAYHGKYSFDTFSH 421
Cdd:PLN02766 463 CPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
1-420 |
7.12e-37 |
|
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: 141.33 E-value: 7.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTFRSG---RSRPLRFRlqqleALRRMVQ--EREKDILAAIAA--------------DLSKSELNAYSHEV 61
Cdd:cd07120 21 AEAAIAAARRAFDETdwaHDPRLRAR-----VLLELADafEANAERLARLLAlengkilgearfeiSGAISELRYYAGLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 62 ITILGeidfmlgnlpelASARPAKKNLLTMMDEayvqpePLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSE 141
Cdd:cd07120 96 RTEAG------------RMIEPEPGSFSLVLRE------PMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 142 NTAKILAELLPQ--YLDQDLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYID 217
Cdd:cd07120 158 QINAAIIRILAEipSLPAGVVNLFTESGSEGAAHLvaSPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 218 RDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDtvkdfYGENVKASPDYER------IINLRHFKRI 291
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAA-----RLAAVKVGPGLDPasdmgpLIDRANVDRV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 292 KSLLE------GQKIAFGGETDEATR---YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALY 362
Cdd:cd07120 313 DRMVEraiaagAEVVLRGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAAS 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 399362 363 IFSHNNKLIKRVIDETSSGGVTGNDVIMHFtvNSLPFGGVGASGMGAYHGKYSFDTFS 420
Cdd:cd07120 393 VWTRDLARAMRVARAIRAGTVWINDWNKLF--AEAEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
1-419 |
2.23e-36 |
|
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: 140.34 E-value: 2.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVITILGEIDFMLGnLPELAS 80
Cdd:cd07085 40 VDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARG-DVLRGLEVVEFACS-IPHLLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 81 ARPAKkNLLTMMDeAYVQPEPLGVVLIIGAWNYP-----------------FVLtlqplvgaiaagnaaivKPSELSENT 143
Cdd:cd07085 118 GEYLE-NVARGID-TYSYRQPLGVVAGITPFNFPamiplwmfpmaiacgntFVL-----------------KPSERVPGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 144 AKILAELLPQY-LDQDLYMIVNGGVEETTELLrqrfDH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYID 217
Cdd:cd07085 179 AMRLAELLQEAgLPDGVLNVVHGGKEAVNALL----DHpdikaVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 218 RDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL- 295
Cdd:cd07085 255 PDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLkVGAGDDPGADMGPVISPAAKERIEGLIe 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 296 ----EGQKIAFGGETDEATRY-----IAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSH 366
Cdd:cd07085 335 sgveEGAKLVLDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTR 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 367 NNKLIKRVIDETSSGGVTGNDVI-----MHftvnslPFGGVGASGMGAYH--GKYSFDTF 419
Cdd:cd07085 415 SGAAARKFQREVDAGMVGINVPIpvplaFF------SFGGWKGSFFGDLHfyGKDGVRFY 468
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
66-408 |
1.11e-35 |
|
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: 138.40 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 66 GEIDFMLGNLPELASARPaKKNLltmmdeAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAK 145
Cdd:cd07140 119 GWCDKIQGKTIPINQARP-NRNL------TLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 146 ILAEL-LPQYLDQDLYMIVNGgveeTTELLRQRF-DH-----ILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYID 217
Cdd:cd07140 192 KFAELtVKAGFPKGVINILPG----SGSLVGQRLsDHpdvrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIF 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 218 RDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRI----- 291
Cdd:cd07140 268 ADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLveyce 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 292 KSLLEGQKIAFGG-ETDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKN--VEEAINFINDREKPLALYIFSHNN 368
Cdd:cd07140 348 RGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDI 427
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 399362 369 KLIKRVIDETSSGGVTGNdvIMHFTVNSLPFGGVGASGMG 408
Cdd:cd07140 428 NKALYVSDKLEAGTVFVN--TYNKTDVAAPFGGFKQSGFG 465
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
97-419 |
2.22e-35 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 137.35 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 97 VQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNG-----GVEET 170
Cdd:PRK11241 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGsagavGGELT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 171 TELLRQRFDhilYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCE 250
Cdd:PRK11241 222 SNPLVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 251 ASSQDQIVQKIKDTVKDFY-GENVKASPDYERIINLRHFKRIK-----SLLEGQKIAFGGETDE-ATRYIAPTILTDVDP 323
Cdd:PRK11241 299 DGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 324 NSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVnsLPFGGVG 403
Cdd:PRK11241 379 NAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV--APFGGIK 456
|
330
....*....|....*.
gi 399362 404 ASGMGAYHGKYSFDTF 419
Cdd:PRK11241 457 ASGLGREGSKYGIEDY 472
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
95-420 |
9.36e-35 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 135.79 E-value: 9.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 95 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAEL-----LPqylDQDLYMIVNGGVEE 169
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLakeagLP---DGVLNVVTGFGHEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 170 TTEL-LRQRFDHILYTGNTAVGKIVM-EAAAKHLTPVTLELGGKSPCYIDRDC-DLDVACRRITWGKYMNCGQTCIAPDY 246
Cdd:PRK09847 228 GQALsRHNDIDAIAFTGSTRTGKQLLkDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 247 ILCEASSQDQIVQKIKDTVKDFY-GENVKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETDEATrYIAPTILTD 320
Cdd:PRK09847 308 LLLEESIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIRegeskGQLLLDGRNAGLAA-AIGPTIFVD 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 321 VDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGV---TGNDVIMhftvnSL 397
Cdd:PRK09847 387 VDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVfvnNYNDGDM-----TV 461
|
330 340
....*....|....*....|...
gi 399362 398 PFGGVGASGMGAYHGKYSFDTFS 420
Cdd:PRK09847 462 PFGGYKQSGNGRDKSLHALEKFT 484
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
100-419 |
8.55e-34 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 133.78 E-value: 8.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 100 EPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNG-GVEETTELLRQR 177
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGfGPTAGAALASHM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 178 -FDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQD 255
Cdd:PLN02466 274 dVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 256 QIVQK-----IKDTVKDFYGENVKASPDyeriINLRHFKR----IKSLLE-GQKIAFGGETDEATRY-IAPTILTDVDPN 324
Cdd:PLN02466 354 EFVEKakaraLKRVVGDPFKKGVEQGPQ----IDSEQFEKilryIKSGVEsGATLECGGDRFGSKGYyIQPTVFSNVQDD 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 325 SKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGN--DVimhFTVnSLPFGGV 402
Cdd:PLN02466 430 MLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDV---FDA-AIPFGGY 505
|
330
....*....|....*..
gi 399362 403 GASGMGAYHGKYSFDTF 419
Cdd:PLN02466 506 KMSGIGREKGIYSLNNY 522
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
92-413 |
5.18e-32 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 127.90 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 92 MDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEET 170
Cdd:cd07111 138 LDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGSFG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 171 TELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC 249
Cdd:cd07111 218 SALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLV 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 250 EASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLEGQKiAFGGETDEATR-------YIAPTILTDV 321
Cdd:cd07111 298 QESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADVFQPGAdlpskgpFYPPTLFTNV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 322 DPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMhFTVNSlPFGG 401
Cdd:cd07111 377 PPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNL-FDAAA-GFGG 454
|
330
....*....|..
gi 399362 402 VGASGMGAYHGK 413
Cdd:cd07111 455 YRESGFGREGGK 466
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
1-408 |
3.21e-31 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 125.36 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPELAS 80
Cdd:PRK13968 31 IENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-EVAKSANLCDWYAEHGPAMLK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 81 ARPAkknlLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELlpqYLDQDLY 160
Cdd:PRK13968 110 AEPT----LVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQV---FKDAGIP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 161 MIVNGGVEETTELLRQ-----RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYM 235
Cdd:PRK13968 183 QGVYGWLNADNDGVSQmindsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 236 NCGQTCIAPDYILCEASSQDQIVQKIKDTVKDFygeNVKASPDYERII------NLR---HFKRIKSLLEGQKIAFGGET 306
Cdd:PRK13968 263 NTGQVCAAAKRFIIEEGIASAFTERFVAAAAAL---KMGDPRDEENALgpmarfDLRdelHHQVEATLAEGARLLLGGEK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 307 DE-ATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVtg 385
Cdd:PRK13968 340 IAgAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGV-- 417
|
410 420
....*....|....*....|....*
gi 399362 386 ndVIMHFTVNS--LPFGGVGASGMG 408
Cdd:PRK13968 418 --FINGYCASDarVAFGGVKKSGFG 440
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
1-412 |
2.46e-30 |
|
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: 123.46 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAySHEVITILGEIDFMLGNLPELAS 80
Cdd:cd07083 57 AEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA-IDDVAEAIDFIRYYARAALRLRY 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 81 ARPAKKNLLTMMDEAYVQPepLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDL 159
Cdd:cd07083 136 PAVEVVPYPGEDNESFYVG--LGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 160 YMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLT------PVTLELGGKSPCYIDRDCDLDVACRRITW 231
Cdd:cd07083 214 VQFLPGVGEEVGAYLteHERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 232 GKYMNCGQTCIAPDYILCEASSQDQI---VQKIKDTVKdfYGENVKASPDYERIINLRHFKRIKSLLEGQK----IAFGG 304
Cdd:cd07083 294 SAFGFQGQKCSAASRLILTQGAYEPVlerLLKRAERLS--VGPPEENGTDLGPVIDAEQEAKVLSYIEHGKnegqLVLGG 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 305 ETDEATRY-IAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVE--EAINFINDREKPLALYIFSHNNKLIKRVIDETSSG 381
Cdd:cd07083 372 KRLEGEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVG 451
|
410 420 430
....*....|....*....|....*....|.
gi 399362 382 GVTGNDVIMHFTVNSLPFGGVGASGMGAYHG 412
Cdd:cd07083 452 NLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
5-406 |
1.84e-29 |
|
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: 119.68 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 5 VQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEReKDILA-AIAADLSKSELNAYShEVITILGEIDFMLGNLPElasaRP 83
Cdd:cd07095 6 VAAARAAFPGWAALSLEERAAILRRFAELLKAN-KEELArLISRETGKPLWEAQT-EVAAMAGKIDISIKAYHE----RT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 84 AKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELL-PQYLDQDLYMI 162
Cdd:cd07095 80 GERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 163 VNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHltP---VTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCG 238
Cdd:cd07095 160 VQGGRETGEALAAHeGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 239 QTCIAPDYILCEASSQ-----DQIVQKIK-------DTVKDFYGENV--KASPDYERIINLRHFKRIKSLLEGQKIafgg 304
Cdd:cd07095 238 QRCTCARRLIVPDGAVgdaflERLVEAAKrlrigapDAEPPFMGPLIiaAAAARYLLAQQDLLALGGEPLLAMERL---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 305 etDEATRYIAPTILtDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVT 384
Cdd:cd07095 314 --VAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
|
410 420
....*....|....*....|..
gi 399362 385 GNDVIMhFTVNSLPFGGVGASG 406
Cdd:cd07095 391 WNRPTT-GASSTAPFGGVGLSG 411
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
93-408 |
5.62e-29 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 119.21 E-value: 5.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 93 DEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGgVEETT 171
Cdd:PRK13252 134 SFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVVQG-DGRVG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 172 ELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC 249
Cdd:PRK13252 213 AWLTEhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 250 EASSQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRI-----KSLLEGQKIAFGGE--TDEATR---YIA 314
Cdd:PRK13252 293 QKSIKAAFEARLLERVEririgDPMDPATNFGP----LVSFAHRDKVlgyieKGKAEGARLLCGGErlTEGGFAngaFVA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 315 PTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVtgndvimhfTV 394
Cdd:PRK13252 369 PTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGIC---------WI 439
|
330 340
....*....|....*....|.
gi 399362 395 NS-------LPFGGVGASGMG 408
Cdd:PRK13252 440 NTwgespaeMPVGGYKQSGIG 460
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
79-408 |
1.78e-27 |
|
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: 114.86 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 79 ASARPAKKNLLTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL 155
Cdd:cd07116 111 AGCIRAQEGSISEIDEntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 156 DQDLYMIVNG-GVEETTELL-RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSP-CYIDRDCDLDVA-CRRITW 231
Cdd:cd07116 191 PPGVVNVVNGfGLEAGKPLAsSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPnIFFADVMDADDAfFDKALE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 232 GKYM---NCGQTCIAPDYILCEASSQDQIVQKIKDTVKDFygenVKASP-DYERII----NLRHFKRIKSLL-----EGQ 298
Cdd:cd07116 271 GFVMfalNQGEVCTCPSRALIQESIYDRFMERALERVKAI----KQGNPlDTETMIgaqaSLEQLEKILSYIdigkeEGA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 299 KIAFGGE-----TDEATRYIAPTILTDVDpNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKR 373
Cdd:cd07116 347 EVLTGGErnelgGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYR 425
|
330 340 350
....*....|....*....|....*....|....*
gi 399362 374 VIDETSSGGVTGNdvIMHFTVNSLPFGGVGASGMG 408
Cdd:cd07116 426 MGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIG 458
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
1-411 |
2.87e-26 |
|
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: 111.13 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 1 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSH-----EVITILGEID-FMLGN 74
Cdd:TIGR01722 40 VDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDvarglEVVEHACGVNsLLKGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 75 LPElasarpakkNLLTMMDeAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY 154
Cdd:TIGR01722 120 TST---------QVATRVD-VYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 155 -LDQDLYMIVNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWG 232
Cdd:TIGR01722 190 gAPDGVLNVVHGDKEAVDRLLEHpDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 233 KYMNCGQTCIAPDYILCeASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGG-- 304
Cdd:TIGR01722 270 AYGAAGQRCMAISAAVL-VGAADEWVPEIRERAEKIrIGPGDDPGAEMGPLITPQAKDRVASLIaggaaEGAEVLLDGrg 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 305 ---ETDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSG 381
Cdd:TIGR01722 349 ykvDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVG 428
|
410 420 430
....*....|....*....|....*....|
gi 399362 382 GVtGNDVIMHFTVNSLPFGGVGASGMGAYH 411
Cdd:TIGR01722 429 QV-GVNVPIPVPLPYFSFTGWKDSFFGDHH 457
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
2-416 |
6.62e-25 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 107.13 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSeLNAYSHEVITILGEIDFMLGNLPELASA 81
Cdd:PRK09406 26 DAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LASAKAEALKCAKGFRYYAEHAEALLAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 RPAKKNLLTMmDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELL-----PQYLD 156
Cdd:PRK09406 105 EPADAAAVGA-SRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFrragfPDGCF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 157 QDLyMIVNGGVEEtteLLR-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYM 235
Cdd:PRK09406 184 QTL-LVGSGAVEA---ILRdPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 236 NCGQTCIAPDYILCEASSQDQIVQKIKD-----TVKDFYGENVKASP--------DYERIINlrhfkriKSLLEGQKIAF 302
Cdd:PRK09406 260 NNGQSCIAAKRFIVHADVYDAFAEKFVArmaalRVGDPTDPDTDVGPlateqgrdEVEKQVD-------DAVAAGATILC 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 303 GGET-DEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSG 381
Cdd:PRK09406 333 GGKRpDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAG 412
|
410 420 430
....*....|....*....|....*....|....*...
gi 399362 382 GVTGNDviMHFTVNSLPFGGVGASGMG---AYHGKYSF 416
Cdd:PRK09406 413 QVFING--MTVSYPELPFGGVKRSGYGrelSAHGIREF 448
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
2-367 |
4.66e-23 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 101.51 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFR---LQQL-EALRRmvqerEKDILAAIAadlskselnaySHEVITI----LGEI----- 68
Cdd:cd07130 37 ESTIKAAQEAFKEWRDVPAPKRgeiVRQIgDALRK-----KKEALGKLV-----------SLEMGKIlpegLGEVqemid 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 69 --DFMLG-----NLPELASARPAKKnlltMMDeayvQPEPLGVVLIIGAWNYP-------FVLTLqplvgaiAAGNAAIV 134
Cdd:cd07130 101 icDFAVGlsrqlYGLTIPSERPGHR----MME----QWNPLGVVGVITAFNFPvavwgwnAAIAL-------VCGNVVVW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 135 KPSELSENTA----KILAELLPQY-LDQDLYMIVNGGVEETTELLR-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLEL 208
Cdd:cd07130 166 KPSPTTPLTAiavtKIVARVLEKNgLPGAIASLVCGGADVGEALVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 209 GGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKD---TVK--DFYGENVKASP------ 277
Cdd:cd07130 246 GGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKaykQVRigDPLDDGTLVGPlhtkaa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 278 --DYERIINlrhfkRIKSllEGQKIAFGGE-TDEATRYIAPTILTdVDPNSKVMQEEIFGPILPIVSVKNVEEAINFIND 354
Cdd:cd07130 326 vdNYLAAIE-----EAKS--QGGTVLFGGKvIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNE 397
|
410
....*....|...
gi 399362 355 REKPLALYIFSHN 367
Cdd:cd07130 398 VPQGLSSSIFTTD 410
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
95-408 |
7.33e-22 |
|
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: 97.87 E-value: 7.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 95 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSE---LS-ENTAKILAEL-LPQYLDQDLYMIVNGGVEE 169
Cdd:cd07148 118 AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALatpLScLAFVDLLHEAgLPEGWCQAVPCENAVAEKL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 170 TTEllrQRFDHILYTGNTAVGKIVMEAAAKHlTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC 249
Cdd:cd07148 198 VTD---PRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 250 EASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETDEATRYiAPTILTDVDP 323
Cdd:cd07148 274 PAEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVEEWVNeavaaGARLLCGGKRLSDTTY-APTVLLDPPR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 324 NSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDvimH--FTVNSLPFGG 401
Cdd:cd07148 353 DAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND---HtaFRVDWMPFAG 429
|
....*..
gi 399362 402 VGASGMG 408
Cdd:cd07148 430 RRQSGYG 436
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
2-406 |
4.92e-19 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 89.63 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPElasa 81
Cdd:PRK09457 40 DAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAAT-EVTAMINKIAISIQAYHE---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLY 160
Cdd:PRK09457 115 RTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 161 MIVNGGVEETTELLRQR-FDHILYTGNTAVGKIVMEAAAKHltP---VTLELGGKSPCYIDRDCDLDVACRRITWGKYMN 236
Cdd:PRK09457 195 NLVQGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFIS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 237 CGQTCIAPDYILCEASSQ-DQIVQKIKDTVK-----DFYGENvkaSPDYERIINLRHFKRiksLLEGQK--IAFGGET-- 306
Cdd:PRK09457 273 AGQRCTCARRLLVPQGAQgDAFLARLVAVAKrltvgRWDAEP---QPFMGAVISEQAAQG---LVAAQAqlLALGGKSll 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 307 -----DEATRYIAPTILtDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSG 381
Cdd:PRK09457 347 emtqlQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAG 425
|
410 420
....*....|....*....|....*
gi 399362 382 GVTGNDVIMHFTvNSLPFGGVGASG 406
Cdd:PRK09457 426 IVNWNKPLTGAS-SAAPFGGVGASG 449
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
28-409 |
1.73e-18 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 87.89 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 28 EALRRMVQEREKDilaAIAADLSKSELNAYS-HEVITILGEIDFMLGNlpelaSARPAKKNLLTMMDEAyvqpePLGVVL 106
Cdd:PLN00412 97 ECLVKEIAKPAKD---AVTEVVRSGDLISYTaEEGVRILGEGKFLVSD-----SFPGNERNKYCLTSKI-----PLGVVL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 107 IIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELLRQR--FDHILY 183
Cdd:PLN00412 164 AIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAgFPKGLISCVTGKGSEIGDFLTMHpgVNCISF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 184 TGNTAVGKIVMEAAakhLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKD 263
Cdd:PLN00412 244 TGGDTGIAISKKAG---MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 264 TVKDFYGENVKASPDYERIINLRHFKRIKSLLEG--QKIA-FGGETDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIV 340
Cdd:PLN00412 321 KVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDakEKGAtFCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVI 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 399362 341 SVKNVEEAINFINDREKPLALYIFSHN-NKLIkRVIDETSSGGVTGNDVIM----HFtvnslPFGGVGASGMGA 409
Cdd:PLN00412 401 RINSVEEGIHHCNASNFGLQGCVFTRDiNKAI-LISDAMETGTVQINSAPArgpdHF-----PFQGLKDSGIGS 468
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
94-421 |
1.92e-16 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 82.10 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 94 EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVNGGVEETTEL 173
Cdd:PLN02419 242 DTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 174 LRQRFD--HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC-- 249
Cdd:PLN02419 322 ICDDEDirAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvg 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 250 -EASSQDQIVQKIKdTVKDFYGENVKAspDYERIINLRHFKRI------------KSLLEGQKIAFGGEtdEATRYIAPT 316
Cdd:PLN02419 402 dAKSWEDKLVERAK-ALKVTCGSEPDA--DLGPVISKQAKERIcrliqsgvddgaKLLLDGRDIVVPGY--EKGNFIGPT 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 317 ILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVtGNDVIMHFTVNS 396
Cdd:PLN02419 477 ILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQI-GINVPIPVPLPF 555
|
330 340
....*....|....*....|....*..
gi 399362 397 LPFGGVGASGMG--AYHGKYSFDTFSH 421
Cdd:PLN02419 556 FSFTGNKASFAGdlNFYGKAGVDFFTQ 582
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
60-425 |
3.23e-16 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 81.03 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 60 EVITILGEIDFMLG-----NLPELASARPAKknlltMMDEAYvqpEPLGVVLIIGAWNYP-FVLTLQP-LVGAIAAGNAA 132
Cdd:PLN02315 116 EVQEIIDMCDFAVGlsrqlNGSIIPSERPNH-----MMMEVW---NPLGIVGVITAFNFPcAVLGWNAcIALVCGNCVVW 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 133 IVKPSE--LSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLEL 208
Cdd:PLN02315 188 KGAPTTplITIAMTKLVAEVLEKNnLPGAIFTSFCGGAEIGEAIAKDtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLEL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 209 GGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKAS-------PDYE 280
Cdd:PLN02315 268 SGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVkIGDPLEKGtllgplhTPES 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 281 RIINLRHFKRIKSllEGQKIAFGGETDEAT-RYIAPTILtDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPL 359
Cdd:PLN02315 348 KKNFEKGIEIIKS--QGGKILTGGSAIESEgNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGL 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 399362 360 ALYIFSHNNKLIKRVIdetssgGVTGND---VIMHFTVNSL----PFGGVGASGMGAYHGKYSFDTFSHQRPC 425
Cdd:PLN02315 425 SSSIFTRNPETIFKWI------GPLGSDcgiVNVNIPTNGAeiggAFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
101-409 |
6.53e-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: 79.59 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 101 PLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQ--YLDQDLYMIVNGGVEETTELLRQ-R 177
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGKTMQALLLHpN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 178 FDHILYTGNTAVGKIVmeAAAKHLTPVTLELGGKSPCYIDRDCD-LDVACRRITWGKYMNCGQTCIAPDYILCEASSQdq 256
Cdd:cd07084 180 PKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWS-- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 257 iVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSL--LEGQKIAFGGETDEATRY-------IAPTILTDVDPN--- 324
Cdd:cd07084 256 -KTPLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMenLLGSVLLFSGKELKNHSIpsiygacVASALFVPIDEIlkt 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 325 SKVMQEEIFGPILPIVSVKNVEEA--INFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTV--NSLPFG 400
Cdd:cd07084 335 YELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVapNQNHGG 414
|
....*....
gi 399362 401 GVGASGMGA 409
Cdd:cd07084 415 GPAADPRGA 423
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
2-409 |
9.22e-16 |
|
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: 79.55 E-value: 9.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 2 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVitilGE-IDF-------MLG 73
Cdd:cd07125 72 DAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADA-EV----REaIDFcryyaaqARE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 74 NLPELASARP-AKKNLLTMmdeayvqpEPLGVVLIIGAWNYPF----------------VLTlqplvgaiaagnaaivKP 136
Cdd:cd07125 147 LFSDPELPGPtGELNGLEL--------HGRGVFVCISPWNFPLaiftgqiaaalaagntVIA----------------KP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 137 SELSENTAKILAELL-----PQYLdqdLYMIVNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKH---LTPVTLE 207
Cdd:cd07125 203 AEQTPLIAARAVELLheagvPRDV---LQLVPGDGEEIGEALVAHpRIDGVIFTGSTETAKLINRALAERdgpILPLIAE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 208 LGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINLR 286
Cdd:cd07125 280 TGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLkVGDPWDLSTDVGPLIDKP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 287 HFKRIKS---LLEGQK--IAFGGETDEATRYIAPTILTDVdpNSKVMQEEIFGPILPIVSVK--NVEEAINFINDREKPL 359
Cdd:cd07125 360 AGKLLRAhteLMRGEAwlIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 399362 360 ALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMGA 409
Cdd:cd07125 438 TLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGP 487
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
100-412 |
2.75e-12 |
|
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: 68.78 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 100 EPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL--RQ 176
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRGADVGAALtsDP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 177 RFDHILYTGNTAVGKIVMEAAAKHL---TPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDyILCeasS 253
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALR-VLC---V 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 254 QDQIVQKIKDTVKDFYGENVKASP-----DYERIIN-------LRHFKRIKSllEGQKIA-FGGETDEATR---YIAPTi 317
Cdd:TIGR01238 315 QEDVADRVLTMIQGAMQELKVGVPhllttDVGPVIDaeakqnlLAHIEHMSQ--TQKKIAqLTLDDSRACQhgtFVAPT- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 318 LTDVDpNSKVMQEEIFGPILPIVSVK--NVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVN 395
Cdd:TIGR01238 392 LFELD-DIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVG 470
|
330
....*....|....*..
gi 399362 396 SLPFGGVGASGMGAYHG 412
Cdd:TIGR01238 471 VQPFGGQGLSGTGPKAG 487
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
207-406 |
3.89e-12 |
|
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: 68.38 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 207 ELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQKIKDTVKDF-YGENVKASPDYERIINL 285
Cdd:cd07123 284 ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIkMGDPDDFSNFMGAVIDE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 286 RHFKRIKSLLE------GQKIAFGGETDEATRY-IAPTILTDVDPNSKVMQEEIFGPILpIVSV---KNVEEAINFINDR 355
Cdd:cd07123 364 KAFDRIKGYIDhaksdpEAEIIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFGPVL-TVYVypdSDFEETLELVDTT 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 399362 356 EkPLALY--IFSHNNKLIKRV------------IDETSSGGVTGNDvimhftvnslPFGGVGASG 406
Cdd:cd07123 443 S-PYALTgaIFAQDRKAIREAtdalrnaagnfyINDKPTGAVVGQQ----------PFGGARASG 496
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
285-408 |
2.34e-06 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 50.20 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 285 LRHFKRIKSllEGQKIA---FGGETDEATrYIAPTI--LTDVDpnskVMQEEIFGPILPIVSVK--NVEEAINFINDREK 357
Cdd:PRK11904 882 DAHIERMKR--EARLLAqlpLPAGTENGH-FVAPTAfeIDSIS----QLEREVFGPILHVIRYKasDLDKVIDAINATGY 954
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 399362 358 PLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMG 408
Cdd:PRK11904 955 GLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
299-408 |
5.56e-04 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 42.54 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 299 KIAFGGETDEATrYIAPTILtDVDpNSKVMQEEIFGPILPIVSVK--NVEEAINFINDREKPLALYIFSHNNKLIKRVID 376
Cdd:PRK11905 889 QLPLPAETEKGT-FVAPTLI-EID-SISDLEREVFGPVLHVVRFKadELDRVIDDINATGYGLTFGLHSRIDETIAHVTS 965
|
90 100 110
....*....|....*....|....*....|..
gi 399362 377 ETSSGGVTGNDVIMHFTVNSLPFGGVGASGMG 408
Cdd:PRK11905 966 RIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTG 997
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
289-375 |
5.69e-04 |
|
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: 42.26 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 289 KRIKSLLEGQKIAFGGETDEATR--------YIAPTILT--DVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKP 358
Cdd:cd07128 345 AAVATLLAEAEVVFGGPDRFEVVgadaekgaFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGS 424
|
90
....*....|....*..
gi 399362 359 LALYIFSHNNKLIKRVI 375
Cdd:cd07128 425 LVASVVTNDPAFARELV 441
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
82-383 |
8.07e-04 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 42.08 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 82 RPAKKNLLTMMDEAYvQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELS----ENTAKILAELLPQY-LD 156
Cdd:cd07127 175 KPQGKHDPLAMEKTF-TVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAilplAITVQVAREVLAEAgFD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 157 QDLYMIVNGGVEE--TTEL-LRQRFDHILYTGNTAVGKIvMEAAAKHLTPVTlELGGKSPCYIDRDCDLDVACRRITWGK 233
Cdd:cd07127 254 PNLVTLAADTPEEpiAQTLaTRPEVRIIDFTGSNAFGDW-LEANARQAQVYT-EKAGVNTVVVDSTDDLKAMLRNLAFSL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 234 YMNCGQTCIAPDYILC---------EASSQDQIVQKIKDTVKDFYGENVKA--------SPD-YERIINLRHFKRIksLL 295
Cdd:cd07127 332 SLYSGQMCTTPQNIYVprdgiqtddGRKSFDEVAADLAAAIDGLLADPARAaallgaiqSPDtLARIAEARQLGEV--LL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 296 EGQKIAFGGETDEATRyiAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFIND--REK-PLALYIFSHNNKLIK 372
Cdd:cd07127 410 ASEAVAHPEFPDARVR--TPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELAREsvREHgAMTVGVYSTDPEVVE 487
|
330
....*....|.
gi 399362 373 RVIDETSSGGV 383
Cdd:cd07127 488 RVQEAALDAGV 498
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
94-349 |
1.13e-03 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 41.05 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 94 EAYVQPEPLGVVLIIGAWNYPfVLTLQPLVGAIAAGNAAIVKPSELSENTAKILA----ELLPQYLDQDLYMIVN-GGVE 168
Cdd:cd07077 93 ETYVRAFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTNRALAllfqAADAAHGPKILVLYVPhPSDE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 169 ETTELLRQ-RFDHILYTGntavGKIVMEAAAKH--LTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMncgqtciapD 245
Cdd:cd07077 172 LAEELLSHpKIDLIVATG----GRDAVDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFF---------D 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 246 YILCeASSQDQIVqkikdtVKDFYgenvkaSPDYERIInLRHFKRIKSLLEGQKIAFGGETDEATRYIaptiltdvdpns 325
Cdd:cd07077 239 QNAC-ASEQNLYV------VDDVL------DPLYEEFK-LKLVVEGLKVPQETKPLSKETTPSFDDEA------------ 292
|
250 260
....*....|....*....|....
gi 399362 326 kvmqEEIFGPILPIVSVKNVEEAI 349
Cdd:cd07077 293 ----LESMTPLECQFRVLDVISAV 312
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
285-408 |
1.37e-03 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 41.46 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 285 LRHFKRIKSllEGQKIA---FGGETDEATrYIAPTI--LTDVDpnskVMQEEIFGPILPIVSVK--NVEEAINFINDREK 357
Cdd:COG4230 878 EAHIERMRA--EGRLVHqlpLPEECANGT-FVAPTLieIDSIS----DLEREVFGPVLHVVRYKadELDKVIDAINATGY 950
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 358 PLALYIFSHNNKLIKRVIDETSsggvTGNdvimhFTVN---------SLPFGGVGASGMG 408
Cdd:COG4230 951 GLTLGVHSRIDETIDRVAARAR----VGN-----VYVNrniigavvgVQPFGGEGLSGTG 1001
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
301-349 |
1.40e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 41.04 E-value: 1.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 399362 301 AFGGETDEATRyiapTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAI 349
Cdd:PRK15398 334 AAGINVPKDTR----LLIVETDANHPFVVTELMMPVLPVVRVKDVDEAI 378
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
101-408 |
2.02e-03 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 40.73 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 101 PLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTA----KILAE---------LLPqyldqdlymivngGV 167
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAaqavRILLEagvpagvvqLLP-------------GR 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 168 EET--TELLR-QRFDHILYTGNTAVGKIVMEAAAKHL------TPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCG 238
Cdd:PRK11809 835 GETvgAALVAdARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAG 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 239 QTCIAPDyILCeasSQDQIVQKIKDTVKDFYGENVKASPDY-----------ERIINL-RHFKRIKSllEGQKI---AFG 303
Cdd:PRK11809 915 QRCSALR-VLC---LQDDVADRTLKMLRGAMAECRMGNPDRlstdigpvidaEAKANIeRHIQAMRA--KGRPVfqaARE 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 304 GETDEAT-RYIAPTI--LTDVDPnskvMQEEIFGPILPIVSVK--NVEEAINFINDREKPLALYIFSHNNKLIKRVIDET 378
Cdd:PRK11809 989 NSEDWQSgTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSA 1064
|
330 340 350
....*....|....*....|....*....|
gi 399362 379 SSGGVTGNDVIMHFTVNSLPFGGVGASGMG 408
Cdd:PRK11809 1065 HVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
161-373 |
2.35e-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: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 161 MIVNGGVEETTELLRQR-FDHILYTGNTAVGKivmeAAAKHLTPVtleLG---GKSPCYIDRDCDLDVACRRITWGKYMN 236
Cdd:cd07122 161 WIEEPSIELTQELMKHPdVDLILATGGPGMVK----AAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 237 CGQTCiapdyilceASSQDQIVQK-IKDTVKDFYGEN--VKASPD-YERIIN--LRHFKRIKSLLEGQ---KIA--FGGE 305
Cdd:cd07122 234 NGTIC---------ASEQSVIVDDeIYDEVRAELKRRgaYFLNEEeKEKLEKalFDDGGTLNPDIVGKsaqKIAelAGIE 304
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 399362 306 TDEATRYIAPTIlTDVDPNSKVMQEEIFgPILPIVSVKNVEEAInfindrEKPLALY----------IFSHNNKLIKR 373
Cdd:cd07122 305 VPEDTKVLVAEE-TGVGPEEPLSREKLS-PVLAFYRAEDFEEAL------EKARELLeyggaghtavIHSNDEEVIEE 374
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
101-409 |
2.80e-03 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 40.17 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 101 PLGVVLIIGAWNYPFVLTLQPLVGAIAAGnaaiVKPSELSENTAKILAELLPQYL------DQDLYMIVNGGVEETTELL 174
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMG----NKPLLKVDSKVSVVMEQFLRLLhlcgmpATDVDLIHSDGPTMNKILL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 175 RQRFDHILYTGNTAV---------GKIVMEAAA---KHLTPVTLELGgkspcYIDRDCDLDVacrritwgkYMNCGQTCI 242
Cdd:cd07126 218 EANPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQDA---------YACSGQKCS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 243 APDYILC-EASSQDQIVQKIKDTVKDFYGENVKASP----DYERIINlrHFKRIKSlLEGQKIAFGGEtdEATRYIAPTI 317
Cdd:cd07126 284 AQSILFAhENWVQAGILDKLKALAEQRKLEDLTIGPvltwTTERILD--HVDKLLA-IPGAKVLFGGK--PLTNHSIPSI 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 318 LTDVDP--------------NSKVMQEEIFGPILPIVSVKNVEEainfindrekPLALYIFSHnnklikrvIDETSSGGV 383
Cdd:cd07126 359 YGAYEPtavfvpleeiaieeNFELVTTEVFGPFQVVTEYKDEQL----------PLVLEALER--------MHAHLTAAV 420
|
330 340 350
....*....|....*....|....*....|.
gi 399362 384 TGNDV-----IMHFTVNSLPFGGVGASGMGA 409
Cdd:cd07126 421 VSNDIrflqeVLANTVNGTTYAGIRARTTGA 451
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
184-350 |
2.97e-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: 39.91 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 184 TGNTAVGKIVMEAAAKhltpvtlELG---GKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASSQDQIVQK 260
Cdd:cd07121 187 TGGPAVVKAALSSGKK-------AIGagaGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399362 261 IKDtvkdfYGENVKASPDYERIINL----RHFKRIKSLLEGQ---KIA--FGGETDEATRyiapTILTDVDPNSKVMQEE 331
Cdd:cd07121 260 MQR-----NGAYVLNDEQAEQLLEVvlltNKGATPNKKWVGKdasKILkaAGIEVPADIR----LIIVETDKDHPFVVEE 330
|
170
....*....|....*....
gi 399362 332 IFGPILPIVSVKNVEEAIN 350
Cdd:cd07121 331 QMMPILPVVRVKNFDEAIE 349
|
|
| |
