|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
82-521 |
0e+00 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 800.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 82 VQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPA 161
Cdd:cd07132 4 VRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 162 KKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVN 241
Cdd:cd07132 84 KKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 242 GGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAP 321
Cdd:cd07132 164 GGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 322 DYILCEASLQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLEGQKIAFGGETDEATRYIAPTILTDVDPN 401
Cdd:cd07132 244 DYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDVKPS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 402 SKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGA 481
Cdd:cd07132 324 DPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGN 403
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 564372361 482 SGMGAYHGKYSFDTFSHQRPCLLKGLKGESVNKLRYPPNS 521
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 ... |
82-503 |
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: 697.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 82 VQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPA 161
Cdd:cd07087 4 VARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 162 KKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVN 241
Cdd:cd07087 84 SVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 242 GGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAP 321
Cdd:cd07087 164 GGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 322 DYILCEASLQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLEGQKIAFGGETDEATRYIAPTILTDVDPN 401
Cdd:cd07087 244 DYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDVSPD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 402 SKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGA 481
Cdd:cd07087 324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGN 403
|
410 420
....*....|....*....|..
gi 564372361 482 SGMGAYHGKYSFDTFSHQRPCL 503
Cdd:cd07087 404 SGMGAYHGKAGFDTFSHLKSVL 425
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
79-524 |
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: 633.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASA 158
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 159 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYM 238
Cdd:cd07136 81 KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 239 IVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTC 318
Cdd:cd07136 161 VVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 319 IAPDYILCEASLQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLEGQKIAFGGETDEATRYIAPTILTDV 398
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 399 DPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGG 478
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 564372361 479 VGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESvnKLRYPPNSESK 524
Cdd:cd07136 401 VGNSGMGSYHGKYSFDTFSHKKSILKKSTWFDL--PLRYPPYKGKK 444
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
82-542 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 631.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 82 VQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPA 161
Cdd:PTZ00381 13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 162 KKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVN 241
Cdd:PTZ00381 93 DTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 242 GGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAP 321
Cdd:PTZ00381 173 GGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 322 DYILCEASLQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLE--GQKIAFGGETDEATRYIAPTILTDVD 399
Cdd:PTZ00381 253 DYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKdhGGKVVYGGEVDIENKYVAPTIIVNPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 400 PNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGV 479
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGGV 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564372361 480 GASGMGAYHGKYSFDTFSHQRPCLLKGLKGESVNKLRYPPNSESKvSW--SKFFLLKQFNKGRLQ 542
Cdd:PTZ00381 413 GNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFK-SWvlSFLLKLSIPVQSEVL 476
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
79-501 |
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: 587.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASA 158
Cdd:cd07135 8 DSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAKD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 159 RPAKKNLLT-MMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLY 237
Cdd:cd07135 88 EKVKDGPLAfMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 238 MIVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQT 317
Cdd:cd07135 168 QVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 318 CIAPDYILCEASLQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLE--GQKIAFGGETDEATRYIAPTIL 395
Cdd:cd07135 248 CVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDttKGKVVIGGEMDEATRFIPPTIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 396 TDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLP 475
Cdd:cd07135 328 SDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAP 407
|
410 420
....*....|....*....|....*.
gi 564372361 476 FGGVGASGMGAYHGKYSFDTFSHQRP 501
Cdd:cd07135 408 FGGVGDSGYGAYHGKYGFDTFTHERT 433
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
79-503 |
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: 519.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASA 158
Cdd:cd07134 1 RRVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 159 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYM 238
Cdd:cd07134 81 KRVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 239 IVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTC 318
Cdd:cd07134 161 VFEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 319 IAPDYILCEASLQDQIVQKIKDTVKDFYGEN--VKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETDEATRYIA 391
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAEIEKFYGKDaaRKASPDLARIVNDRHFDRLKGLLDdavakGAKVEFGGQFDAAQRYIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 392 PTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTV 471
Cdd:cd07134 321 PTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLN 400
|
410 420 430
....*....|....*....|....*....|..
gi 564372361 472 NSLPFGGVGASGMGAYHGKYSFDTFSHQRPCL 503
Cdd:cd07134 401 PNLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
79-503 |
0e+00 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 517.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASA 158
Cdd:cd07137 2 PRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 159 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYM 238
Cdd:cd07137 82 EKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 239 IVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNC-GQT 317
Cdd:cd07137 162 VIEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGCNnGQA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 318 CIAPDYILCEASLQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLE----GQKIAFGGETDEATRYIAPT 393
Cdd:cd07137 242 CIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDdpsvADKIVHGGERDEKNLYIEPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 394 ILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNS 473
Cdd:cd07137 322 ILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDT 401
|
410 420 430
....*....|....*....|....*....|
gi 564372361 474 LPFGGVGASGMGAYHGKYSFDTFSHQRPCL 503
Cdd:cd07137 402 LPFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
83-501 |
8.83e-174 |
|
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: 499.32 E-value: 8.83e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 83 QRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADlskselnaYSH---------EVITILGEIDFMLGNLP 153
Cdd:cd07133 5 ERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISAD--------FGHrsrhetllaEILPSIAGIKHARKHLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 154 ELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLD 233
Cdd:cd07133 77 KWMKPSRRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 234 QDLYMIVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMN 313
Cdd:cd07133 157 EDEVAVVTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 314 CGQTCIAPDYILCEASLQDQIVQKIKDTVKDFYGeNVKASPDYERIINLRHFKRIKSLLE-----GQKI---AFGGETDE 385
Cdd:cd07133 237 AGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEdarakGARVielNPAGEDFA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 386 ATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDV 465
Cdd:cd07133 316 ATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDT 395
|
410 420 430
....*....|....*....|....*....|....*.
gi 564372361 466 IMHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRP 501
Cdd:cd07133 396 LLHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
78-526 |
1.46e-153 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 449.56 E-value: 1.46e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 78 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELAS 157
Cdd:PLN02203 8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 158 ARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLY 237
Cdd:PLN02203 88 PKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 238 MIVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYID---RDCDLDVACRRITWGKYMNC 314
Cdd:PLN02203 168 KVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWGSC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 315 -GQTCIAPDYILCEASLQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLEGQKIA----FGGETDEATRY 389
Cdd:PLN02203 248 aGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAasivHGGSIDEKKLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 390 IAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHF 469
Cdd:PLN02203 328 IEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQY 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 564372361 470 TVNSLPFGGVGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESvnKLRYPPNSESKVS 526
Cdd:PLN02203 408 ACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEF--EFRYPPWNDFKLG 462
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
82-525 |
3.60e-129 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 387.09 E-value: 3.60e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 82 VQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPA 161
Cdd:PLN02174 16 VTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 162 KKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVN 241
Cdd:PLN02174 96 KTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 242 GGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKY-MNCGQTCIA 320
Cdd:PLN02174 176 GAVTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACIS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 321 PDYILCEASLQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLE----GQKIAFGGETDEATRYIAPTILT 396
Cdd:PLN02174 256 PDYILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 397 DVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPF 476
Cdd:PLN02174 336 DVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPF 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 564372361 477 GGVGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESVnkLRYPPNSESKV 525
Cdd:PLN02174 416 GGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSA--VRYPPYSRGKL 462
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
79-504 |
5.46e-127 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 379.63 E-value: 5.46e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAyshevitiLGEIDFMLGNL---PEL 155
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEA--------LGEVARAADTFryyAGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 156 ASARPAKKNLLTMMD-EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LD 233
Cdd:cd07078 73 ARRLHGEVIPSPDPGeLAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 234 QDLYMIVNGGVEETTELLR--QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKY 311
Cdd:cd07078 153 PGVLNVVTGDGDEVGAALAshPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 312 MNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDFYGEN-VKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETDE 385
Cdd:cd07078 233 GNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEdakaeGAKLLCGGKRLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 386 AT--RYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGN 463
Cdd:cd07078 313 GGkgYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 564372361 464 DVIMHFTVNsLPFGGVGASGMGAYHGKYSFDTFSHQRPCLL 504
Cdd:cd07078 393 DYSVGAEPS-APFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
86-504 |
7.89e-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: 315.32 E-value: 7.89e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 86 RQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVITILGEIDFmlgnLPELASARPAKKNL 165
Cdd:cd06534 4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRY----AAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 166 LTMMD-EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNG- 242
Cdd:cd06534 79 SPDPGgEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 243 GVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAP 321
Cdd:cd06534 159 GDEVGAALLSHpRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 322 DYILCEASLQDQIVQKIKdtvkdfygenvkaspdyeriinlrhfkriksllegqkiafggetdeatryiapTILTDVDPN 401
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV-----------------------------------------------------TVLVDVDPD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 402 SKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNsLPFGGVGA 481
Cdd:cd06534 266 MPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-APFGGVKN 344
|
410 420
....*....|....*....|...
gi 564372361 482 SGMGAYHGKYSFDTFSHQRPCLL 504
Cdd:cd06534 345 SGIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
60-500 |
3.85e-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: 301.66 E-value: 3.85e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 60 TGIVLLHLPRSafsSGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAyshevi 139
Cdd:COG1012 30 TGEVLARVPAA---TAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEA------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 140 tiLGEIDFMLGNL---PELASARPAKKNLLTMMD-EAYVQPEPLGVVLIIGAWNYPFVLTLQP------------Lvgai 203
Cdd:COG1012 101 --RGEVDRAADFLryyAGEARRLYGETIPSDAPGtRAYVRREPLGVVGAITPWNFPLALAAWKlapalaagntvvL---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 204 aagnaaivKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTP 280
Cdd:COG1012 175 --------KPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALvaHPDVDKISFTGSTAVGRRIAAAAAENLKR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 281 VTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERI 359
Cdd:COG1012 247 VTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 360 INLRHFKRIKSLL-----EGQKIAFGGE--TDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDR 432
Cdd:COG1012 327 ISEAQLERVLAYIedavaEGAELLTGGRrpDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDT 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564372361 433 EKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNsLPFGGVGASGMGAYHGKYSFDTFSHQR 500
Cdd:COG1012 407 EYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETK 473
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
60-500 |
2.57e-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: 270.25 E-value: 2.57e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 60 TGIVLLHLPrsaFSSGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSElNAYSHEVI 139
Cdd:cd07099 5 TGEVLGEVP---VTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPR-ADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 140 TILGEIDFMLGNLPELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSEN 219
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 220 TAKILAELLPQY-LDQDLYMIVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCD 298
Cdd:cd07099 161 VGELLAEAWAAAgPPQGVLQVVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 299 LDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF---YGENVKAspDYERIINLRHFKRIKSLLE-- 373
Cdd:cd07099 241 LERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALrpgADDIGDA--DIGPMTTARQLDIVRRHVDda 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 374 ---GQKIAFGGE-TDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIK 449
Cdd:cd07099 319 vakGAKALTGGArSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAE 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 564372361 450 RVIDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQR 500
Cdd:cd07099 399 AIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPK 449
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
60-500 |
1.51e-82 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 265.93 E-value: 1.51e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 60 TGIVLLHLPRSafsSGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYsHEVI 139
Cdd:pfam00171 16 TGEVIATVPAA---TAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR-GEVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 140 TILGEIDFMLGNLPELA-SARPAKKNLLtmmdeAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSE 218
Cdd:pfam00171 92 RAIDVLRYYAGLARRLDgETLPSDPGRL-----AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 219 NTAKILAELLPQY-LDQDLYMIVNGGVEETTELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDR 295
Cdd:pfam00171 167 LTALLLAELFEEAgLPAGVLNVVTGSGAEVGEALVEhpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 296 DCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-- 372
Cdd:pfam00171 247 DADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVed 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 373 ---EGQKIAFGGETDEAT-RYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLI 448
Cdd:pfam00171 327 akeEGAKLLTGGEAGLDNgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 564372361 449 KRVIDETSSGGVTGNDVIMhFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQR 500
Cdd:pfam00171 407 LRVARRLEAGMVWINDYTT-GDADGLPFGGFKQSGFGREGGPYGLEEYTEVK 457
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
60-490 |
2.32e-70 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 234.12 E-value: 2.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 60 TGIVLLHLPrsafSSGPA-MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEV 138
Cdd:cd07098 5 TGQHLGSVP----ADTPEdVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 139 ITILGEIDFMLGNLPELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSE 218
Cdd:cd07098 81 LVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 219 NTAKILAELLPQYL-----DQDLYMIVNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCY 292
Cdd:cd07098 161 WSSGFFLSIIRECLaacghDPDLVQLVTCLPETAEALTSHpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 293 IDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSL 371
Cdd:cd07098 241 VLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 372 L-----EGQKIAFGGE-----TDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIF 441
Cdd:cd07098 321 VadaveKGARLLAGGKryphpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVF 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 564372361 442 SHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMGAYHGK 490
Cdd:cd07098 401 GKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFGRFAGE 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
79-500 |
1.86e-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: 212.01 E-value: 1.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDIL-------------AAIAADLSKSELNAYSHEVITILGEI 145
Cdd:cd07104 3 DRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIAdwliresgstrpkAAFEVGAAIAILREAAGLPRRPEGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 146 dfmlgnlpeLASARPAKKNlltmmdeaYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENT----- 220
Cdd:cd07104 83 ---------LPSDVPGKES--------MVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgglli 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 221 AKILAEL-LPQyldqDLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDC 297
Cdd:cd07104 146 AEIFEEAgLPK----GVLNVVPGGGSEIGDALveHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 298 DLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLL 372
Cdd:cd07104 222 DLDLAVSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKalpvgDPRDPDTVIGP----LINERQVDRVHAIV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 373 E-----GQKIAFGGETDEatRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKL 447
Cdd:cd07104 298 EdavaaGARLLTGGTYEG--LFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLER 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 564372361 448 IKRVIDETSSGGVTGNDVimhfTVNS---LPFGGVGASGMGAYHGKYSFDTFSHQR 500
Cdd:cd07104 376 AMAFAERLETGMVHINDQ----TVNDephVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
78-454 |
1.17e-60 |
|
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: 208.27 E-value: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 78 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPE--- 154
Cdd:cd07088 37 ADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV-EVEFTADYIDYMAEWARRieg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 155 --LASARPAKKnlltmmdeAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY- 231
Cdd:cd07088 116 eiIPSDRPNEN--------IFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAg 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 232 LDQDLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWG 309
Cdd:cd07088 188 LPAGVLNIVTGRGSVVGDALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 310 KYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGET 383
Cdd:cd07088 268 RIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVkVGDPFDAATDMGPLVNEAALDKVEEMVEraveaGATLLTGGKR 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564372361 384 DEATR--YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDE 454
Cdd:cd07088 348 PEGEKgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNE 420
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
69-500 |
8.82e-60 |
|
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: 205.64 E-value: 8.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 69 RSAFSSGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYshevitilGEIDFM 148
Cdd:cd07150 14 RVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW--------FETTFT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 149 LGNLPELASA--RPAKKnllTMMDEA-----YVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTA 221
Cdd:cd07150 86 PELLRAAAGEcrRVRGE---TLPSDSpgtvsMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 222 KILAELLPQY-LDQDLYMIVNGGVEETTELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCD 298
Cdd:cd07150 163 LKIAEIMEEAgLPKGVFNVVTGGGAEVGDELVDdpRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 299 LDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKI-----KDTVKDFYGENVKASPdyerIINLRHFKRIKSLLE 373
Cdd:cd07150 243 LDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFvarasKLKVGDPRDPDTVIGP----LISPRQVERIKRQVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 374 -----GQKIAFGGETDeaTRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLI 448
Cdd:cd07150 319 davakGAKLLTGGKYD--GNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 564372361 449 KRVIDETSSGGVTGNDVIMHFTVNsLPFGGVGASGMGAYHGKYSFDTFSHQR 500
Cdd:cd07150 397 FKLAERLESGMVHINDPTILDEAH-VPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
60-500 |
3.47e-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: 203.95 E-value: 3.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 60 TGIVLLHLPRSafssGPA-MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEV 138
Cdd:cd07093 6 TGEVLAKVPEG----GAAeVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 139 ITILGEIDFmlgnLPELASARPAkkNLLTMMDEA--YVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSEL 216
Cdd:cd07093 82 PRAAANFRF----FADYILQLDG--ESYPQDGGAlnYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 217 SENTAKILAELLpqyLDQDL----YMIVNGGVEETTELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSP 290
Cdd:cd07093 156 TPLTAWLLAELA---NEAGLppgvVNVVHGFGPEAGAALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 291 CYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YG----ENVKASPdyerIINLRHF 365
Cdd:cd07093 233 NIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALkVGdpldPDTEVGP----LISKEHL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 366 KRIKSLL-----EGQKIAFGGETDEATR-----YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKP 435
Cdd:cd07093 309 EKVLGYVelaraEGATILTGGGRPELPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564372361 436 LALYIFSHNNKLIKRVIDETSSGGVTGNDvimhFTVNSL--PFGGVGASGMGAYHGKYSFDTFSHQR 500
Cdd:cd07093 389 LAAYVWTRDLGRAHRVARRLEAGTVWVNC----WLVRDLrtPFGGVKASGIGREGGDYSLEFYTELK 451
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
177-500 |
2.83e-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: 196.02 E-value: 2.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 177 EPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL--RQ 253
Cdd:cd07118 118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMteHP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 254 RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQ 333
Cdd:cd07118 198 DVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 334 IVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGETDE--ATRYIAPTILTDVDPNSKVM 405
Cdd:cd07118 278 FVAAVVARSRKVrVGDPLDPETKVGAIINEAQLAKITDYVdagraEGATLLLGGERLAsaAGLFYQPTIFTDVTPDMAIA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 406 QEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTvnSLPFGGVGASGMG 485
Cdd:cd07118 358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSGIG 435
|
330
....*....|....*
gi 564372361 486 AYHGKYSFDTFSHQR 500
Cdd:cd07118 436 RELGRYGVEEYTELK 450
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
60-496 |
3.54e-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: 195.73 E-value: 3.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 60 TGIVLLHLPrsafSSGPA-MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADL------SKSELN 132
Cdd:cd07103 6 TGEVIGEVP----DAGAAdADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQgkplaeARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 133 A-------YSHEVITILGEIdfmlgnLPelaSARPAKKNLltmmdeayVQPEPLGVVLIIGAWNYP-------------- 191
Cdd:cd07103 82 YaasflewFAEEARRIYGRT------IP---SPAPGKRIL--------VIKQPVGVVAAITPWNFPaamitrkiapalaa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 192 ---FVLtlqplvgaiaagnaaivKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL----RQRfdHILYTGN 263
Cdd:cd07103 145 gctVVL-----------------KPAEETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEALcaspRVR--KISFTGS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 264 TAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVK 343
Cdd:cd07103 206 TAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 344 DF-----YGENVKASPdyerIINLRHFKRIKSLLE-----GQKIAFGGETDEAT-RYIAPTILTDVDPNSKVMQEEIFGP 412
Cdd:cd07103 286 KLkvgngLDEGTDMGP----LINERAVEKVEALVEdavakGAKVLTGGKRLGLGgYFYEPTVLTDVTDDMLIMNEETFGP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 413 ILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMhfTVNSLPFGGVGASGMGAYHGKYS 492
Cdd:cd07103 362 VAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLI--SDAEAPFGGVKESGLGREGGKEG 439
|
....
gi 564372361 493 FDTF 496
Cdd:cd07103 440 LEEY 443
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
74-498 |
6.31e-55 |
|
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: 192.46 E-value: 6.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 74 SGPAMERQVQRLRQTFRSGRSRPLRFRLqqlEALRRMVqerekDILAAIAADLSKS-------ELNAYSHEVITILGEID 146
Cdd:cd07102 16 SLEAVRAALERARAAQKGWRAVPLEERK---AIVTRAV-----ELLAANTDEIAEEltwqmgrPIAQAGGEIRGMLERAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 147 FMLGNLPE-LASARPAKKNLLtmmdEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELS----ENTA 221
Cdd:cd07102 88 YMISIAEEaLADIRVPEKDGF----ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTplcgERFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 222 KILAE-LLPQyldqDLYMIVNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDL 299
Cdd:cd07102 164 AAFAEaGLPE----GVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 300 DVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE----- 373
Cdd:cd07102 240 DAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIAdaiak 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 374 GQKIAFGGET----DEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIK 449
Cdd:cd07102 320 GARALIDGALfpedKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 564372361 450 RVIDETSSGGVTGN--DvimhFTVNSLPFGGVGASGMGAYHGKYSFDTFSH 498
Cdd:cd07102 400 ALGEQLETGTVFMNrcD----YLDPALAWTGVKDSGRGVTLSRLGYDQLTR 446
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
113-496 |
2.23e-54 |
|
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: 191.85 E-value: 2.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 113 EREKDILAAI-AADLSKS-ELNAYSH--EVITIL----GEIDFMLGnlpELASARPAKknlltmmdEAYVQPEPLGVVLI 184
Cdd:cd07144 82 EKNRDLLAAIeALDSGKPyHSNALGDldEIIAVIryyaGWADKIQG---KTIPTSPNK--------LAYTLHEPYGVCGQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 185 IGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELLRQR--FDHILYT 261
Cdd:cd07144 151 IIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHpdVDKIAFT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 262 GNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDT 341
Cdd:cd07144 231 GSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEH 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 342 VK------DFYGENVKASPdyerIINLRHFKRIKSLLE-----GQKIAFGGE----TDEATRYIAPTILTDVDPNSKVMQ 406
Cdd:cd07144 311 VKqnykvgSPFDDDTVVGP----QVSKTQYDRVLSYIEkgkkeGAKLVYGGEkapeGLGKGYFIPPTIFTDVPQDMRIVK 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 407 EEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGV---TGNDviMHFTVnslPFGGVGASG 483
Cdd:cd07144 387 EEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVwinSSND--SDVGV---PFGGFKMSG 461
|
410
....*....|...
gi 564372361 484 MGAYHGKYSFDTF 496
Cdd:cd07144 462 IGRELGEYGLETY 474
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
172-497 |
4.41e-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: 190.14 E-value: 4.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 172 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNG-GVEETTE 249
Cdd:cd07109 111 VYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGlGAEAGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 250 LLRQR-FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEA 328
Cdd:cd07109 191 LVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 329 SLQDQIVQKIkdtVKDFYGENVKAS---PDYERIINLRHFKRIKSLLE-----GQKIAFGGETDEATR----YIAPTILT 396
Cdd:cd07109 271 SIYDEVLERL---VERFRALRVGPGledPDLGPLISAKQLDRVEGFVArararGARIVAGGRIAEGAPaggyFVAPTLLD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 397 DVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDvimHFTVN--SL 474
Cdd:cd07109 348 DVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAGQVFVNN---YGAGGgiEL 424
|
330 340
....*....|....*....|...
gi 564372361 475 PFGGVGASGMGAYHGKYSFDTFS 497
Cdd:cd07109 425 PFGGVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
60-497 |
3.39e-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: 187.92 E-value: 3.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 60 TGIVLLHLPrsafSSGPA-MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEV 138
Cdd:cd07092 6 TGEEIATVP----DASAAdVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 139 ITILGEIDFMLGnlpelaSAR----PAKKNLLTMMdEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPS 214
Cdd:cd07092 82 PGAVDNFRFFAG------AARtlegPAAGEYLPGH-TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 215 ELSENTAKILAELLPQYLDQDLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCY 292
Cdd:cd07092 155 ETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 293 IDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSL 371
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 372 LE----GQKIAFGGETDEATRY-IAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNK 446
Cdd:cd07092 315 VErapaHARVLTGGRRAEGPGYfYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 564372361 447 LIKRVIDETSSGGVTGNDvimHFT-VNSLPFGGVGASGMGAYHGKYSFDTFS 497
Cdd:cd07092 395 RAMRLSARLDFGTVWVNT---HIPlAAEMPHGGFKQSGYGKDLSIYALEDYT 443
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
177-496 |
4.92e-53 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 188.36 E-value: 4.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 177 EPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEE------TTE 249
Cdd:PLN02278 159 QPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAgIPPGVLNVVMGDAPEigdallASP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 250 LLRQrfdhILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEAS 329
Cdd:PLN02278 239 KVRK----ITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEG 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 330 LQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLL-----EGQKIAFGGE--TDEATRYiAPTILTD 397
Cdd:PLN02278 315 IYDKFAEAFSKAVQklvvgDGFEEGVTQGP----LINEAAVQKVESHVqdavsKGAKVLLGGKrhSLGGTFY-EPTVLGD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 398 VDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVnsLPFG 477
Cdd:PLN02278 390 VTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEV--APFG 467
|
330
....*....|....*....
gi 564372361 478 GVGASGMGAYHGKYSFDTF 496
Cdd:PLN02278 468 GVKQSGLGREGSKYGIDEY 486
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
177-497 |
5.43e-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: 186.63 E-value: 5.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 177 EPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyLDQDL----YMIVNGGVEETTELLR 252
Cdd:cd07105 97 EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVF---HEAGLpkgvLNVVTHSPEDAPEVVE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 253 QRFDH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCE 327
Cdd:cd07105 174 ALIAHpavrkVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVH 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 328 ASLQDQIVQKIKDTVKDFYGENVKASPdyerIINLRHFKRIKSLLE-----GQKIAFGGETD--EATRYIAPTILTDVDP 400
Cdd:cd07105 254 ESIADEFVEKLKAAAEKLFAGPVVLGS----LVSAAAADRVKELVDdalskGAKLVVGGLADesPSGTSMPPTILDNVTP 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 401 NSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHfTVNSLPFGGVG 480
Cdd:cd07105 330 DMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVH-DEPTLPHGGVK 408
|
330
....*....|....*..
gi 564372361 481 ASGMGAYHGKYSFDTFS 497
Cdd:cd07105 409 SSGYGRFNGKWGIDEFT 425
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
69-485 |
9.19e-53 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 186.65 E-value: 9.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 69 RSAFSSGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSelnaysheVITILGEIDFM 148
Cdd:cd07149 14 RVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKP--------IKDARKEVDRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 149 LGNLpELaSARPAKKNLLTM--MDE--------AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSE 218
Cdd:cd07149 86 IETL-RL-SAEEAKRLAGETipFDAspggegriGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 219 NTAKILAELLPQ-YLDQDLYMIVNGGVEET-TELLR-QRFDHILYTGNTAVGKIVMEAAAkhLTPVTLELGGKSPCYIDR 295
Cdd:cd07149 164 LSALKLAELLLEaGLPKGALNVVTGSGETVgDALVTdPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 296 DCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKS 370
Cdd:cd07149 242 DADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKklvvgDPLDEDTDVGP----MISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 371 LLE-----GQKIAFGGETDEAtrYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNN 445
Cdd:cd07149 318 WVEeavegGARLLTGGKRDGA--ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDL 395
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 564372361 446 KLIKRVIDETSSGGVTGNDvIMHFTVNSLPFGGVGASGMG 485
Cdd:cd07149 396 QKALKAARELEVGGVMIND-SSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
172-494 |
1.20e-52 |
|
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: 187.03 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 172 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQD-LYMIVNG-----GVE 245
Cdd:cd07091 135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPgVVNIVPGfgptaGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 246 ETTELlrqRFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYI 324
Cdd:cd07091 215 ISSHM---DVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 325 LCEASLQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLL-----EGQKIAFGGET-DEATRYIAPT 393
Cdd:cd07091 292 FVQESIYDEFVEKFKARAEkrvvgDPFDPDTFQGP----QVSKAQFDKILSYIesgkkEGATLLTGGERhGSKGYFIQPT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 394 ILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGN--DVIMHftv 471
Cdd:cd07091 368 VFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNtyNVFDA--- 444
|
330 340
....*....|....*....|...
gi 564372361 472 nSLPFGGVGASGMGAYHGKYSFD 494
Cdd:cd07091 445 -AVPFGGFKQSGFGRELGEEGLE 466
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
178-491 |
4.25e-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: 184.65 E-value: 4.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 178 PLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVNGGVEETTELLRQ-RFD 256
Cdd:cd07106 114 PLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGGDELGPALTSHpDIR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 257 HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQ 336
Cdd:cd07106 194 KISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCE 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 337 KIKDTVKDFY-GENVKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETDEATRY-IAPTILTDVDPNSKVMQEEI 409
Cdd:cd07106 274 ALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEdakakGAKVLAGGEPLDGPGYfIPPTIVDDPPEGSRIVDEEQ 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 410 FGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNdviMHFTVN-SLPFGGVGASGMGAYH 488
Cdd:cd07106 354 FGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN---THGALDpDAPFGGHKQSGIGVEF 430
|
...
gi 564372361 489 GKY 491
Cdd:cd07106 431 GIE 433
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
78-496 |
5.16e-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: 182.32 E-value: 5.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 78 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELAS 157
Cdd:cd07138 38 VDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 158 ARPAKKNLLTMmdeayvqpEPLGVVLIIGAWNYPF-----------------VLtlqplvgaiaagnaaivKPSELSENT 220
Cdd:cd07138 118 EERRGNSLVVR--------EPIGVCGLITPWNWPLnqivlkvapalaagctvVL-----------------KPSEVAPLS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 221 AKILAELLpqyLDQDL----YMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYID 294
Cdd:cd07138 173 AIILAEIL---DEAGLpagvFNLVNGDGPVVGEALsaHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIIL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 295 RDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKD-----TVKDFYGENVKASPdyerIINLRHFKRIK 369
Cdd:cd07138 250 DDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAaaeayVVGDPRDPATTLGP----LASAAQFDRVQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 370 SLL-----EGQKIAFGG----ETDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYI 440
Cdd:cd07138 326 GYIqkgieEGARLVAGGpgrpEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYV 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 564372361 441 FSHNNKLIKRVIDETSSGGVTGNDVIMHFtvnSLPFGGVGASGMGAYHGKYSFDTF 496
Cdd:cd07138 406 WSADPERARAVARRLRAGQVHINGAAFNP---GAPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
71-500 |
1.25e-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: 181.01 E-value: 1.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 71 AFSSGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEReKDILAAIAADLSKSELNAYSHEVITILGEIDFMlg 150
Cdd:cd07110 14 PAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRER-REELAELEARDNGKPLDEAAWDVDDVAGCFEYY-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 151 nlPELASARPAKKNL-LTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAE 226
Cdd:cd07110 91 --ADLAEQLDAKAERaVPLPSEdfkARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 227 ------LLPQYLDqdlymIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCD 298
Cdd:cd07110 169 iaaeagLPPGVLN-----VVTGTGDEAGAPLaaHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDAD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 299 LDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKD-----TVKDFYGENVKASP-----DYERIinLRHFKRI 368
Cdd:cd07110 244 LEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATaaeaiRVGDPLEEGVRLGPlvsqaQYEKV--LSFIARG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 369 KSllEGQKIAFGGETDEATR---YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNN 445
Cdd:cd07110 322 KE--EGARLLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 564372361 446 KLIKRVIDETSSGGVTGNDVIMHFTvnSLPFGGVGASGMGAYHGKYSFDTFSHQR 500
Cdd:cd07110 400 ERCDRVAEALEAGIVWINCSQPCFP--QAPWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
78-500 |
2.13e-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: 180.52 E-value: 2.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 78 MERQVQRLRQTF-RSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELA 156
Cdd:cd07089 21 VDAAIAAARRAFdTGDWSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSFP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 157 --SARPAKkNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLpqyLDQ 234
Cdd:cd07089 101 weFDLPVP-ALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEII---AET 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 235 DL----YMIVNGGVEETTELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITW 308
Cdd:cd07089 177 DLpagvVNVVTGSDNAVGEALTTdpRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 309 GKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YG----ENVKASPdyerIINLRHFKRIKSLL-----EGQKIA 378
Cdd:cd07089 257 VCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGdpadPGTVMGP----LISAAQRDRVEGYIargrdEGARLV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 379 FGGETDEATR---YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDET 455
Cdd:cd07089 333 TGGGRPAGLDkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRI 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 564372361 456 SSGGVTGNDViMHFTVNSlPFGGVGASGMGAYHGKYSFDTFSHQR 500
Cdd:cd07089 413 RTGSVGINGG-GGYGPDA-PFGGYKQSGLGRENGIEGLEEFLETK 455
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
172-500 |
2.20e-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: 180.44 E-value: 2.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 172 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAEL-----LPQYLDQdlymIVNGGVEE 246
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPPGVVN----VVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 247 TTELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYI 324
Cdd:cd07114 189 TGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 325 LCEASLQDQIVQKIKDTVKdfygeNVK-ASPDYER-----IINLRHFKRIKSLL-----EGQKIAFGGET-----DEATR 388
Cdd:cd07114 269 LVQRSIYDEFVERLVARAR-----AIRvGDPLDPEtqmgpLATERQLEKVERYVarareEGARVLTGGERpsgadLGAGY 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 389 YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDviMH 468
Cdd:cd07114 344 FFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YR 421
|
330 340 350
....*....|....*....|....*....|..
gi 564372361 469 FTVNSLPFGGVGASGMGAYHGKYSFDTFSHQR 500
Cdd:cd07114 422 ALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
67-485 |
2.47e-50 |
|
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: 180.25 E-value: 2.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 67 LPRSAFSSGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSHEVITILGEID 146
Cdd:cd07108 10 IGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAAVLADLFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 147 FMLGNLPEL-ASARPAKKNLLTmmdeaYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILA 225
Cdd:cd07108 90 YFGGLAGELkGETLPFGPDVLT-----YTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 226 ELLPQYLDQDLYMIVNGGVEETTELLRQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVAC 303
Cdd:cd07108 165 EILAQVLPAGVLNVITGYGEECGAALVDHpdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 304 RRITWG-KYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE------GQ 375
Cdd:cd07108 245 DGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDlglstsGA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 376 KIAFGGETDEATR-----YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKR 450
Cdd:cd07108 325 TVLRGGPLPGEGPladgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALR 404
|
410 420 430
....*....|....*....|....*....|....*
gi 564372361 451 VIDETSSGGVTGNDviMHFTVNSLPFGGVGASGMG 485
Cdd:cd07108 405 AAHALEAGWVQVNQ--GGGQQPGQSYGGFKQSGLG 437
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
178-500 |
4.87e-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: 179.03 E-value: 4.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 178 PLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENT-----AKILAEL-LPQYLDQdlymIVNGGVEETTELL 251
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSggvviARLFEEAgLPAGVLH----VLPGGADAGEALV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 252 R-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASL 330
Cdd:cd07152 186 EdPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 331 QDQIVQKIKD-----TVKDFYGENVKASPdyerIINLRHFKRIKSLLE-----GQKIAFGGETDEatRYIAPTILTDVDP 400
Cdd:cd07152 266 ADAYTAKLAAkakhlPVGDPATGQVALGP----LINARQLDRVHAIVDdsvaaGARLEAGGTYDG--LFYRPTVLSGVKP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 401 NSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVimhfTVNS---LPFG 477
Cdd:cd07152 340 GMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQ----TVNDephNPFG 415
|
330 340
....*....|....*....|....
gi 564372361 478 GVGASGMGAYHG-KYSFDTFSHQR 500
Cdd:cd07152 416 GMGASGNGSRFGgPANWEEFTQWQ 439
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
173-497 |
1.21e-49 |
|
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: 178.40 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 173 YVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL 251
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 252 RQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEAS 329
Cdd:cd07115 192 VEHpdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 330 LQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGETDEATR-YIAPTILTDVDPNS 402
Cdd:cd07115 272 IYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDRVLDYVdvgreEGARLLTGGKRPGARGfFVEPTIFAAVPPEM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 403 KVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNdvIMHFTVNSLPFGGVGAS 482
Cdd:cd07115 352 RIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQS 429
|
330
....*....|....*
gi 564372361 483 GMGAYHGKYSFDTFS 497
Cdd:cd07115 430 GFGREMGREALDEYT 444
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
172-498 |
3.10e-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: 177.11 E-value: 3.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 172 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGvEETTEL 250
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 251 LRQRFD--HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEA 328
Cdd:cd07090 189 LCEHPDvaKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 329 SLQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLL-----EGQKIAFGGE----TD--EATRYIAP 392
Cdd:cd07090 269 SIKDEFTERLVERTKkirigDPLDEDTQMGA----LISEEHLEKVLGYIesakqEGAKVLCGGErvvpEDglENGFYVSP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 393 TILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDvimhFTVN 472
Cdd:cd07090 345 CVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT----YNIS 420
|
330 340
....*....|....*....|....*...
gi 564372361 473 S--LPFGGVGASGMGAYHGKYSFDTFSH 498
Cdd:cd07090 421 PveVPFGGYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
79-498 |
1.89e-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: 172.92 E-value: 1.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSK--SELNAyshEVITILGEIDFMLGNLPEL- 155
Cdd:cd07131 40 DAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKplAEGRG---DVQEAIDMAQYAAGEGRRLf 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 156 ----ASARPAKknlltmmdEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY 231
Cdd:cd07131 117 getvPSELPNK--------DAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 232 -LDQDLYMIVNGGVEETTELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITW 308
Cdd:cd07131 189 gLPPGVVNVVHGRGEEVGEALVEhpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALW 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 309 GKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGE 382
Cdd:cd07131 269 SAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLNYNeigkeEGATLLLGGE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 383 -----TDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSS 457
Cdd:cd07131 349 rltggGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEA 428
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 564372361 458 GGVTGNDVIMHFTVNsLPFGGVGASGMGAYHGKYS-FDTFSH 498
Cdd:cd07131 429 GITYVNAPTIGAEVH-LPFGGVKKSGNGHREAGTTaLDAFTE 469
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
113-497 |
2.34e-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: 172.71 E-value: 2.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 113 EREKDILAAIAA-DLSKSELNAYSHEVITILGEIDFMLGnlpelasarPAKKNLLTMMDE-----AYVQPEPLGVVLIIG 186
Cdd:cd07143 82 ERNLDYLASIEAlDNGKTFGTAKRVDVQASADTFRYYGG---------WADKIHGQVIETdikklTYTRHEPIGVCGQII 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 187 AWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL--RQRFDHILYTGN 263
Cdd:cd07143 153 PWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAIssHMDIDKVAFTGS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 264 TAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTV 342
Cdd:cd07143 233 TLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 343 K-----DFYGENVKASPDYERIinlrHFKRIKSLLE-----GQKIAFGGETDEATRY-IAPTILTDVDPNSKVMQEEIFG 411
Cdd:cd07143 313 KklkvgDPFAEDTFQGPQVSQI----QYERIMSYIEsgkaeGATVETGGKRHGNEGYfIEPTIFTDVTEDMKIVKEEIFG 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 412 PILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDV-IMHFTVnslPFGGVGASGMGAYHGK 490
Cdd:cd07143 389 PVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYnLLHHQV---PFGGYKQSGIGRELGE 465
|
....*..
gi 564372361 491 YSFDTFS 497
Cdd:cd07143 466 YALENYT 472
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
171-497 |
4.87e-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: 171.73 E-value: 4.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 171 EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTE 249
Cdd:cd07119 127 ISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 250 LL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCE 327
Cdd:cd07119 207 ELaeSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 328 ASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGE--TDEATR---YIAPTILT 396
Cdd:cd07119 287 ESIHDKFVAALAERAKKIkLGNGLDADTEMGPLVSAEHREKVLSYIqlgkeEGARLVCGGKrpTGDELAkgyFVEPTIFD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 397 DVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDviMHFTVNSLPF 476
Cdd:cd07119 367 DVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEAPW 444
|
330 340
....*....|....*....|.
gi 564372361 477 GGVGASGMGAYHGKYSFDTFS 497
Cdd:cd07119 445 GGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
100-497 |
8.24e-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: 170.56 E-value: 8.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 100 RLQQLEALRRMVQEREKDILAAIAADLSKSELNAyshevitiLGEIDFMLGNLPELAS--ARPAKKNLLTMMD--EAYVQ 175
Cdd:cd07151 56 RAEILEKAAQILEERRDEIVEWLIRESGSTRIKA--------NIEWGAAMAITREAATfpLRMEGRILPSDVPgkENRVY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 176 PEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENT-----AKILAEL-LPQYLdqdLYMIVNGGVEETTE 249
Cdd:cd07151 128 REPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITgglllAKIFEEAgLPKGV---LNVVVGAGSEIGDA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 250 LLRQ---RFdhILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC 326
Cdd:cd07151 205 FVEHpvpRL--ISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 327 EASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETDEatRYIAPTILTDVDP 400
Cdd:cd07151 283 HEDVYDEFVEKFVERVKALpYGDPSDPDTVVGPLINESQVDGLLDKIEqaveeGATLLVGGEAEG--NVLEPTVLSDVTN 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 401 NSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVimhfTVNS---LPFG 477
Cdd:cd07151 361 DMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQ----PVNDephVPFG 436
|
410 420
....*....|....*....|
gi 564372361 478 GVGASGMGAYHGKYSFDTFS 497
Cdd:cd07151 437 GEKNSGLGRFNGEWALEEFT 456
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
60-496 |
3.03e-46 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 169.29 E-value: 3.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 60 TGIVLLHLPRSafssGPA-MERQVQRLRQTFRSG--RSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSH 136
Cdd:cd07139 23 TEEVVGRVPEA----TPAdVDAAVAAARRAFDNGpwPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSRRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 137 EVITILGEIDFMLgnlpELASARPAKKNLLTM-MDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSE 215
Cdd:cd07139 99 QGPGPAALLRYYA----ALARDFPFEERRPGSgGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 216 LSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYI 293
Cdd:cd07139 175 ETPLDAYLLAEAAEEAgLPPGVVNVVPADREVGEYLVRHpGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 294 DRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRI 368
Cdd:cd07139 255 LDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAalkvgDPLDPATQIGP----LASARQRERV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 369 -----KSLLEGQKIAFGGET-DEATR--YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYI 440
Cdd:cd07139 331 egyiaKGRAEGARLVTGGGRpAGLDRgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSV 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 564372361 441 FSHNNKLIKRVIDETSSGGVTGNDVIMHFtvnSLPFGGVGASGMGAYHGKYSFDTF 496
Cdd:cd07139 411 WTADVERGLAVARRIRTGTVGVNGFRLDF---GAPFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
172-485 |
6.53e-46 |
|
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: 167.91 E-value: 6.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 172 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEET-TE 249
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVgDE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 250 LLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEA 328
Cdd:cd07145 197 IVTNpKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 329 SLQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLL-----EGQKIAFGGETDEATrYIAPTILTDV 398
Cdd:cd07145 277 EVYDKFLKLLVEKVKklkvgDPLDESTDLGP----LISPEAVERMENLVndaveKGGKILYGGKRDEGS-FFPPTVLEND 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 399 DPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMhFTVNSLPFGG 478
Cdd:cd07145 352 TPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDSTR-FRWDNLPFGG 430
|
....*..
gi 564372361 479 VGASGMG 485
Cdd:cd07145 431 FKKSGIG 437
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
67-489 |
8.50e-46 |
|
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: 167.94 E-value: 8.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 67 LPRSAFSSGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDiLAAIAADLSKSELNAYSHEVITILGEID 146
Cdd:cd07107 10 LARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEE-LALIDALDCGNPVSAMLGDVMVAAALLD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 147 FMLGNLPELasarpaKKNLLTMMDEA--YVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKIL 224
Cdd:cd07107 89 YFAGLVTEL------KGETIPVGGRNlhYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 225 AELLPQYLDQDLYMIVNGGVEETTE-LLRQR-FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVA 302
Cdd:cd07107 163 AELAREVLPPGVFNILPGDGATAGAaLVRHPdVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 303 CRRITWGkyMN---CGQTCIAPDYILCEASLQDQIVQKIKDTVKDFY-GENVKASPDYERIINLRHFKRIKSLL-----E 373
Cdd:cd07107 243 ADAAVAG--MNftwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIdsakrE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 374 GQKIAFGG--ETDEATR---YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLI 448
Cdd:cd07107 321 GARLVTGGgrPEGPALEggfYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 564372361 449 KRVIDETSSGGVTGNDVIMHFTvnSLPFGGVGASGMGAYHG 489
Cdd:cd07107 401 HRTARRVEAGYVWINGSSRHFL--GAPFGGVKNSGIGREEC 439
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
172-497 |
1.61e-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: 167.01 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 172 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAEL-----LPQyldqDLYMIVNGGVEE 246
Cdd:cd07112 118 ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELaleagLPA----GVLNVVPGFGHT 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 247 TTELL--RQRFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDC-DLDVACRRITWGKYMNCGQTCIAPD 322
Cdd:cd07112 194 AGEALglHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 323 YILCEASLQDQIVQKIKDTVKDFY-GENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGETDEATR---YIAPT 393
Cdd:cd07112 274 RLLVHESIKDEFLEKVVAAAREWKpGDPLDPATRMGALVSEAHFDKVLGYIesgkaEGARLVAGGKRVLTETggfFVEPT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 394 ILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNdvimhfTVN- 472
Cdd:cd07112 354 VFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVN------CFDe 427
|
330 340
....*....|....*....|....*...
gi 564372361 473 ---SLPFGGVGASGMGAYHGKYSFDTFS 497
Cdd:cd07112 428 gdiTTPFGGFKQSGNGRDKSLHALDKYT 455
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
170-497 |
1.62e-45 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 167.29 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 170 DEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETT 248
Cdd:TIGR01804 125 SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 249 ELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC 326
Cdd:TIGR01804 205 PLLvnHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 327 EASLQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRIKSLL-----EGQKIAFGG------ETDEATrYI 390
Cdd:TIGR01804 285 HKKIKERFLARLVERTEriklgDPFDEATEMGP----LISAAHRDKVLSYIekgkaEGATLATGGgrpenvGLQNGF-FV 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 391 APTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDviMHFT 470
Cdd:TIGR01804 360 EPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLY 437
|
330 340
....*....|....*....|....*..
gi 564372361 471 VNSLPFGGVGASGMGAYHGKYSFDTFS 497
Cdd:TIGR01804 438 PAEAPFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
156-485 |
1.70e-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: 167.52 E-value: 1.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 156 ASARPAKKNLLTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL 232
Cdd:cd07559 111 AGVIRAQEGSLSEIDEdtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 233 DQDLYMIVNG-GVEETTELL-RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYI-----DRDCDLDVACRR 305
Cdd:cd07559 191 PKGVVNVVTGfGSEAGKPLAsHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 306 ITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVkdfygENVKA-SP-DYERII----NLRHFKRIKSLL-----EG 374
Cdd:cd07559 271 GQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERF-----EAIKVgNPlDPETMMgaqvSKDQLEKILSYVdigkeEG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 375 QKIAFGGE-----TDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIK 449
Cdd:cd07559 346 AEVLTGGErltlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRAL 425
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 564372361 450 RVIDETSSGGVTGNdvimhfTVNSLP----FGGVGASGMG 485
Cdd:cd07559 426 RVARGIQTGRVWVN------CYHQYPahapFGGYKKSGIG 459
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
59-490 |
5.07e-45 |
|
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: 165.56 E-value: 5.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 59 LTGIVLLHLPRSafssGPA-MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShE 137
Cdd:cd07101 4 FTGEPLGELPQS----TPAdVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFE-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 138 VITILGEIDFMLGNLPELASARPaKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELS 217
Cdd:cd07101 79 VLDVAIVARYYARRAERLLKPRR-RRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 218 ENTAKILAELLPQY-LDQDLYMIVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRD 296
Cdd:cd07101 158 ALTALWAVELLIEAgLPRDLWQVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 297 CDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVkdfygENVKASPDYE------RIINLRHFKRIKS 370
Cdd:cd07101 238 ADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVART-----RALRLGAALDygpdmgSLISQAQLDRVTA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 371 LLE-----GQKIAFGGET--DEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSH 443
Cdd:cd07101 313 HVDdavakGATVLAGGRArpDLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 564372361 444 NNKLIKRVIDETSSGGVTGNDvIMHFTVNSL--PFGGVGASGMGAYHGK 490
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNE-GYAAAWASIdaPMGGMKDSGLGRRHGA 440
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
78-496 |
1.18e-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: 161.09 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 78 MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEReKDILAAIAAD-----LSKSelnayshevitiLGEI------- 145
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRER-KDELARLITLemgkpIAEA------------RAEVekcawic 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 146 DFMLGNLPELASARPAKknllTMMDEAYVQPEPLGVVLIIGAWNYPF---------------VLTLqplvgaiaagnaai 210
Cdd:cd07100 68 RYYAENAEAFLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFwqvfrfaapnlmagnTVLL-------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 211 vKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELLR-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGK 288
Cdd:cd07100 130 -KHASNVPGCALAIEELFREAgFPEGVFQNLLIDSDQVEAIIAdPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 289 SPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVK-----DFYGENVKASP--------D 355
Cdd:cd07100 209 DPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAalkvgDPMDEDTDLGPlarkdlrdE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 356 YERIINlrhfkriKSLLEGQKIAFGGET-DEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREK 434
Cdd:cd07100 289 LHEQVE-------EAVAAGATLLLGGKRpDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPF 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564372361 435 PLALYIFSHNNKLIKRVIDETSSGGVTGNDVimhftVNS---LPFGGVGASGMGAYHGKYSFDTF 496
Cdd:cd07100 362 GLGGSVFTTDLERAERVARRLEAGMVFINGM-----VKSdprLPFGGVKRSGYGRELGRFGIREF 421
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
77-485 |
1.51e-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: 161.45 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 77 AMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAyshevitiLGEIDFMLGNLpELA 156
Cdd:cd07094 22 DAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDA--------RVEVDRAIDTL-RLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 157 SAR---------PAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAEL 227
Cdd:cd07094 93 AEEaerirgeeiPLDATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 228 L-PQYLDQDLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKhlTPVTLELGGKSPCYIDRDCDLDVACR 304
Cdd:cd07094 173 LvEAGVPEGVLQVVTGEREVLGDAFaaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 305 RITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRI-----KSLLEGQKIA 378
Cdd:cd07094 251 ALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLkVGDPLDEDTDVGPLISEEAAERVerwveEAVEAGARLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 379 FGGETDEATRYiaPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHN-NKLIKrVIDETSS 457
Cdd:cd07094 331 CGGERDGALFK--PTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDlNVAFK-AAEKLEV 407
|
410 420
....*....|....*....|....*...
gi 564372361 458 GGVTGNDViMHFTVNSLPFGGVGASGMG 485
Cdd:cd07094 408 GGVMVNDS-SAFRTDWMPFGGVKESGVG 434
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
173-458 |
2.05e-43 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 159.90 E-value: 2.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 173 YVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL 251
Cdd:PRK10090 66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 252 --RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEAS 329
Cdd:PRK10090 146 agNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 330 LQDQIVQKIKDTVKDF-YGENVKAS-PDYERIINLRHFKRIKSLL-----EGQKIAFGGETDEATRYI-APTILTDVDPN 401
Cdd:PRK10090 226 IYDQFVNRLGEAMQAVqFGNPAERNdIAMGPLINAAALERVEQKVaraveEGARVALGGKAVEGKGYYyPPTLLLDVRQE 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 564372361 402 SKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSG 458
Cdd:PRK10090 306 MSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFG 362
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
171-486 |
2.78e-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: 161.26 E-value: 2.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 171 EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNG-GVEETT 248
Cdd:cd07097 128 EVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGsGSEVGQ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 249 ELLR-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCE 327
Cdd:cd07097 208 ALVEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 328 ASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGET-DEATR--YIAPTILTDV 398
Cdd:cd07097 288 EGIHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIeiarsEGAKLVYGGERlKRPDEgyYLAPALFAGV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 399 DPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGN--DVIMHFTVnslPF 476
Cdd:cd07097 368 TNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlpTAGVDYHV---PF 444
|
330
....*....|
gi 564372361 477 GGVGASGMGA 486
Cdd:cd07097 445 GGRKGSSYGP 454
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
156-485 |
3.34e-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: 161.08 E-value: 3.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 156 ASARPAKKNLLTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL 232
Cdd:cd07117 111 AGVIRAEEGSANMIDEdtlSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 233 DQDLYMIVNGGVEETTELLRQR--FDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGK 310
Cdd:cd07117 191 PKGVVNIVTGKGSKSGEYLLNHpgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 311 YMNCGQTCIAPDYILCEASLQDQIVQKIKdtvKDFygENVKA----SPDYE--RIINLRHFKRIKSLL-----EGQKIAF 379
Cdd:cd07117 271 LFNQGQVCCAGSRIFVQEGIYDEFVAKLK---EKF--ENVKVgnplDPDTQmgAQVNKDQLDKILSYVdiakeEGAKILT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 380 GGE-----TDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDE 454
Cdd:cd07117 346 GGHrltenGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARA 425
|
330 340 350
....*....|....*....|....*....|....*
gi 564372361 455 TSSGGVTGNdvimhfTVNSLP----FGGVGASGMG 485
Cdd:cd07117 426 VETGRVWVN------TYNQIPagapFGGYKKSGIG 454
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
172-485 |
1.00e-42 |
|
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: 159.53 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 172 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGgveeTTEL 250
Cdd:cd07113 136 AFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNG----KGAV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 251 LRQRFDH-----ILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYIL 325
Cdd:cd07113 212 GAQLISHpdvakVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 326 CEASLQDQIVQKIKDTVKDFY-GENVKASPDYERIINLRHFKRIKSLL-----EGQKIAFGGET-DEATRYIAPTILTDV 398
Cdd:cd07113 292 VHRSKFDELVTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEAlAGEGYFVQPTLVLAR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 399 DPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNdviMHFTVN-SLPFG 477
Cdd:cd07113 372 SADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHTFLDpAVPFG 448
|
....*...
gi 564372361 478 GVGASGMG 485
Cdd:cd07113 449 GMKQSGIG 456
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
79-497 |
5.39e-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: 157.14 E-value: 5.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRSRPLRF-RLQQLEALRRMVQEREKDILAAIAADLSKS-------------ELNAYSHEVITILGE 144
Cdd:cd07146 20 EEALREALALAASYRSTLTRYqRSAILNKAAALLEARREEFARLITLESGLClkdtryevgraadVLRFAAAEALRDDGE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 145 -IDFmlgnlpELASARPAKKnlltmmdeAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKI 223
Cdd:cd07146 100 sFSC------DLTANGKARK--------IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 224 LAELLPQY-LDQDLYMIVNGGVEETTELLRQ--RFDHILYTGNTAVGKIVMEAAA-KHLTpvtLELGGKSPCYIDRDCDL 299
Cdd:cd07146 166 LADLLYEAgLPPDMLSVVTGEPGEIGDELIThpDVDLVTFTGGVAVGKAIAATAGyKRQL---LELGGNDPLIVMDDADL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 300 DVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIIN---LRHFKRI--KSLLE 373
Cdd:cd07146 243 ERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDeeaAIQIENRveEAIAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 374 GQKIAFGGETDEAtrYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVID 453
Cdd:cd07146 323 GARVLLGNQRQGA--LYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 564372361 454 ETSSGGVTGNDViMHFTVNSLPFGGVGASGMGAYHG-KYSFDTFS 497
Cdd:cd07146 401 RLDVGTVNVNEV-PGFRSELSPFGGVKDSGLGGKEGvREAMKEMT 444
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
172-496 |
2.22e-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: 156.11 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 172 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNG-GVEETTE 249
Cdd:cd07142 135 VYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGfGPTAGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 250 LLRQR-FDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCE 327
Cdd:cd07142 215 IASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVH 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 328 ASLQDQIVQKIKD-----TVKDFYGENVKASPDyeriINLRHFKRIKSLL-----EGQKIAFGGE-TDEATRYIAPTILT 396
Cdd:cd07142 295 ESIYDEFVEKAKAralkrVVGDPFRKGVEQGPQ----VDKEQFEKILSYIehgkeEGATLITGGDrIGSKGYYIQPTIFS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 397 DVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGN--DVimhFTVnSL 474
Cdd:cd07142 371 DVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNcyDV---FDA-SI 446
|
330 340
....*....|....*....|..
gi 564372361 475 PFGGVGASGMGAYHGKYSFDTF 496
Cdd:cd07142 447 PFGGYKMSGIGREKGIYALNNY 468
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
60-500 |
6.12e-41 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 155.42 E-value: 6.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 60 TGIVLLHLPrsafSSGPA-MERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEV 138
Cdd:PRK09407 41 TGEPLATVP----VSTAAdVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFE-EV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 139 ITILGEIDFMLGNLPE-LASARpaKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELS 217
Cdd:PRK09407 116 LDVALTARYYARRAPKlLAPRR--RAGALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 218 ENTAKILAELLPQY-LDQDLYMIVNGGVEETTELLRQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRD 296
Cdd:PRK09407 194 PLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALVDNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 297 CDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDFygeNVKASPDYE----RIINLRHFKRIKSLL 372
Cdd:PRK09407 274 ADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAM---RLGAGYDYSadmgSLISEAQLETVSAHV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 373 E-----GQKIAFGGET--DEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNN 445
Cdd:PRK09407 351 DdavakGATVLAGGKArpDLGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDT 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564372361 446 KLIKRVIDETSSGGVTGNDVIMH-FTVNSLPFGGVGASGMGAYHG-----KYS-FDTFSHQR 500
Cdd:PRK09407 431 ARGRAIAARIRAGTVNVNEGYAAaWGSVDAPMGGMKDSGLGRRHGaegllKYTeSQTIATQR 492
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
79-486 |
9.02e-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: 155.07 E-value: 9.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKS--ELNAYSHEVItilgeiDF-------ML 149
Cdd:cd07124 72 EAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNwaEADADVAEAI------DFleyyareML 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 150 GNLPELASARPAKKNLLTMmdeayvqpEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLP 229
Cdd:cd07124 146 RLRGFPVEMVPGEDNRYVY--------RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 230 QY-LDQDLYMIVNGGVEETTELLrqrFDH-----ILYTGNTAVGKIVMEAAAK------HLTPVTLELGGKSPCYIDRDC 297
Cdd:cd07124 218 EAgLPPGVVNFLPGPGEEVGDYL---VEHpdvrfIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 298 DLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE--- 373
Cdd:cd07124 295 DLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALkVGDPEDPEVYMGPVIDKGARDRIRRYIEigk 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 374 -GQKIAFGGETDE-ATR--YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIK 449
Cdd:cd07124 375 sEGRLLLGGEVLElAAEgyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLE 454
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 564372361 450 RVIDETSSG------GVTGNDVIMHftvnslPFGGVGASGMGA 486
Cdd:cd07124 455 RARREFEVGnlyanrKITGALVGRQ------PFGGFKMSGTGS 491
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
79-485 |
4.54e-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: 152.33 E-value: 4.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRS--RPLRFrlqqlEALRRMVQEREKDiLAAIAADLSKselnayshEVITIL----GEI------- 145
Cdd:cd07086 38 EAAVAAAREAFKEWRKvpAPRRG-----EIVRQIGEALRKK-KEALGRLVSL--------EMGKILpeglGEVqemidic 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 146 DFMLG-----NLPELASARPAKKnlltMMDeayvQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSE----L 216
Cdd:cd07086 104 DYAVGlsrmlYGLTIPSERPGHR----LME----QWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSEttplT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 217 SENTAKILAELLPQY-LDQDLYMIVNGGVEeTTELLR--QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYI 293
Cdd:cd07086 176 AIAVTKILAEVLEKNgLPPGVVNLVTGGGD-GGELLVhdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 294 DRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL 372
Cdd:cd07086 255 MDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNAI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 373 E-----GQKIAFGGET---DEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHN 444
Cdd:cd07086 335 EiaksqGGTVLTGGKRidgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTED 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 564372361 445 NKLIKRVIDETSS--------GGVTGNDVimhftvnSLPFGGVGASGMG 485
Cdd:cd07086 415 LREAFRWLGPKGSdcgivnvnIPTSGAEI-------GGAFGGEKETGGG 456
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
75-485 |
7.67e-40 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 151.24 E-value: 7.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 75 GPAM-ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAY-------------SHEVIT 140
Cdd:cd07147 19 GPDDiEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARgevaraidtfriaAEEATR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 141 ILGEIdfmlgnLPELASARPAKKnlltmmdEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENT 220
Cdd:cd07147 99 IYGEV------LPLDISARGEGR-------QGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 221 AKILAELL-PQYLDQDLYMIVNGGVEETTELLR-QRFDHILYTGNTAVG-KIVMEAAAKHltpVTLELGGKSPCYIDRDC 297
Cdd:cd07147 166 ALILGEVLaETGLPKGAFSVLPCSRDDADLLVTdERIKLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 298 DLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE--- 373
Cdd:cd07147 243 DLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALkTGDPKDDATDVGPMISESEAERVEGWVNeav 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 374 --GQKIAFGGETDEATryIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRV 451
Cdd:cd07147 323 daGAKLLTGGKRDGAL--LEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRA 400
|
410 420 430
....*....|....*....|....*....|....
gi 564372361 452 IDETSSGGVTGNDViMHFTVNSLPFGGVGASGMG 485
Cdd:cd07147 401 WDELEVGGVVINDV-PTFRVDHMPYGGVKDSGIG 433
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
169-500 |
1.83e-39 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 151.04 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 169 MDE--AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAE------LLPQYLDqdlymIV 240
Cdd:PLN02467 140 METfkGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADicrevgLPPGVLN-----VV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 241 NG-GVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTC 318
Cdd:PLN02467 215 TGlGTEAGAPLASHpGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQIC 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 319 IAPDYILCEASLQDQIVQKIKDTVKdfygeNVKASPDYER------IINLRHFKRIKSLL-----EGQKIAFGGETDEAT 387
Cdd:PLN02467 295 SATSRLLVHERIASEFLEKLVKWAK-----NIKISDPLEEgcrlgpVVSEGQYEKVLKFIstaksEGATILCGGKRPEHL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 388 R---YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGND 464
Cdd:PLN02467 370 KkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINC 449
|
330 340 350
....*....|....*....|....*....|....*.
gi 564372361 465 VIMHFTvnSLPFGGVGASGMGAYHGKYSFDTFSHQR 500
Cdd:PLN02467 450 SQPCFC--QAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
171-497 |
4.68e-39 |
|
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: 149.26 E-value: 4.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 171 EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVgaiaagnaaivkPSELSENT-----AK---ILAELLPQYLDQ-----DLY 237
Cdd:cd07082 134 IAQVRREPLGVVLAIGPFNYPLNLTVSKLI------------PALIMGNTvvfkpATqgvLLGIPLAEAFHDagfpkGVV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 238 MIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKhlTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCG 315
Cdd:cd07082 202 NVVTGRGREIGDPLvtHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSG 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 316 QTCIAPDYILCEASLQDQIVQKIKD-----TVKDFYGENV-------KASPDYeriinlrhfkrIKSLLE-----GQKIA 378
Cdd:cd07082 280 QRCTAIKRVLVHESVADELVELLKEevaklKVGMPWDNGVditplidPKSADF-----------VEGLIDdavakGATVL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 379 FGGETDEATrYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSG 458
Cdd:cd07082 349 NGGGREGGN-LIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVG 427
|
330 340 350
....*....|....*....|....*....|....*....
gi 564372361 459 GVTGNDVIMHfTVNSLPFGGVGASGMGAYHGKYSFDTFS 497
Cdd:cd07082 428 TVNINSKCQR-GPDHFPFLGRKDSGIGTQGIGDALRSMT 465
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
173-494 |
8.69e-39 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 148.52 E-value: 8.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 173 YVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVNGGVEETTELL- 251
Cdd:PRK13473 133 MIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALv 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 252 -RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASL 330
Cdd:PRK13473 213 gHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGI 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 331 QDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE------GQKIAFGGET-DEATRYIAPTILTDVDPNS 402
Cdd:PRK13473 293 YDDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFVErakalgHIRVVTGGEApDGKGYYYEPTLLAGARQDD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 403 KVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMhfTVNSLPFGGVGAS 482
Cdd:PRK13473 373 EIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM--LVSEMPHGGQKQS 450
|
330
....*....|....*.
gi 564372361 483 GmgayHGK----YSFD 494
Cdd:PRK13473 451 G----YGKdmslYGLE 462
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
177-483 |
1.35e-38 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 148.93 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 177 EPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL---- 251
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYLvdhp 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 252 RQRFdhILYTGNTAVGKIVMEAAAK------HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYIL 325
Cdd:PRK03137 250 KTRF--ITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 326 CEASLQDQIVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSLLE-GQ---KIAFGGETDEATRY-IAPTILTDVDP 400
Cdd:PRK03137 328 VHEDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEiGKeegRLVLGGEGDDSKGYfIQPTIFADVDP 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 401 NSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSG------GVTGNDVIMHftvnsl 474
Cdd:PRK03137 408 KARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGnlyfnrGCTGAIVGYH------ 481
|
....*....
gi 564372361 475 PFGGVGASG 483
Cdd:PRK03137 482 PFGGFNMSG 490
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
172-497 |
5.98e-38 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 146.34 E-value: 5.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 172 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAEL-------------LPQYLDQDLYM 238
Cdd:cd07141 139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLikeagfppgvvnvVPGYGPTAGAA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 239 IVNggveettellRQRFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQT 317
Cdd:cd07141 219 ISS----------HPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQC 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 318 CIAPDYILCEASLQDQIVQKI-----KDTVKDFYGENVKASPDyeriINLRHFKRIKSLL-----EGQKIAFGGET-DEA 386
Cdd:cd07141 289 CCAGSRTFVQESIYDEFVKRSverakKRVVGNPFDPKTEQGPQ----IDEEQFKKILELIesgkkEGAKLECGGKRhGDK 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 387 TRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNnklIKRVIdeTSSGGVTGNDVI 466
Cdd:cd07141 365 GYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD---IDKAI--TFSNALRAGTVW 439
|
330 340 350
....*....|....*....|....*....|....*
gi 564372361 467 M----HFTVNSlPFGGVGASGMGAYHGKYSFDTFS 497
Cdd:cd07141 440 VncynVVSPQA-PFGGYKMSGNGRELGEYGLQEYT 473
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
171-498 |
1.27e-37 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 145.73 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 171 EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVNGGVEETTEL 250
Cdd:PLN02766 151 QGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 251 L---RQRFDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC 326
Cdd:PLN02766 231 AiasHMDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 327 EASLQDQIVQKIKDTVKDF-----YGENVKASP-----DYERIIN-LRHFKRiksllEGQKIAFGGE-TDEATRYIAPTI 394
Cdd:PLN02766 311 QEGIYDEFVKKLVEKAKDWvvgdpFDPRARQGPqvdkqQFEKILSyIEHGKR-----EGATLLTGGKpCGDKGYYIEPTI 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 395 LTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNdviMHFTV-NS 473
Cdd:PLN02766 386 FTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYFAFdPD 462
|
330 340
....*....|....*....|....*
gi 564372361 474 LPFGGVGASGMGAYHGKYSFDTFSH 498
Cdd:PLN02766 463 CPFGGYKMSGFGRDQGMDALDKYLQ 487
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
73-497 |
3.12e-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: 143.64 E-value: 3.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 73 SSGPAMERQVQRLRQTFRSG---RSRPLRFRlqqleALRRMVQ--EREKDILAAIAA--------------DLSKSELNA 133
Cdd:cd07120 16 GGVAEAEAAIAAARRAFDETdwaHDPRLRAR-----VLLELADafEANAERLARLLAlengkilgearfeiSGAISELRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 134 YSHEVITILGeidfmlgnlpelASARPAKKNLLTMMDEayvqpePLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKP 213
Cdd:cd07120 91 YAGLARTEAG------------RMIEPEPGSFSLVLRE------PMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 214 SELSENTAKILAELLPQ--YLDQDLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKS 289
Cdd:cd07120 153 AGQTAQINAAIIRILAEipSLPAGVVNLFTESGSEGAAHLvaSPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 290 PCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDtvkdfYGENVKASPDYER------IINLR 363
Cdd:cd07120 233 PCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAA-----RLAAVKVGPGLDPasdmgpLIDRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 364 HFKRIKSLLE------GQKIAFGGETDEATR---YIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREK 434
Cdd:cd07120 308 NVDRVDRMVEraiaagAEVVLRGGPVTEGLAkgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDY 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564372361 435 PLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFtvNSLPFGGVGASGMGAYHGKYSFDTFS 497
Cdd:cd07120 388 GLAASVWTRDLARAMRVARAIRAGTVWINDWNKLF--AEAEEGGYRQSGLGRLHGVAALEDFI 448
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
60-496 |
4.24e-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: 141.12 E-value: 4.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 60 TGIVLLHLPrsaFSSGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVI 139
Cdd:cd07085 25 TGEVIARVP---LATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARG-DVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 140 TILGEIDFMLGnLPELASARPAKkNLLTMMDeAYVQPEPLGVVLIIGAWNYP-----------------FVLtlqplvga 202
Cdd:cd07085 101 RGLEVVEFACS-IPHLLKGEYLE-NVARGID-TYSYRQPLGVVAGITPFNFPamiplwmfpmaiacgntFVL-------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 203 iaagnaaivKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELLrqrfDH-----ILYTGNTAVGKIVMEAAAK 276
Cdd:cd07085 170 ---------KPSERVPGAAMRLAELLQEAgLPDGVLNVVHGGKEAVNALL----DHpdikaVSFVGSTPVGEYIYERAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 277 HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPD 355
Cdd:cd07085 237 NGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLkVGAGDDPGAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 356 YERIINLRHFKRIKSLL-----EGQKIAFGGETDEATRY-----IAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEA 425
Cdd:cd07085 317 MGPVISPAAKERIEGLIesgveEGAKLVLDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564372361 426 INFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVI-----MHftvnslPFGGVGASGMGAYH--GKYSFDTF 496
Cdd:cd07085 397 IAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIpvplaFF------SFGGWKGSFFGDLHfyGKDGVRFY 468
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
143-485 |
1.04e-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: 139.94 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 143 GEIDFMLGNLPELASARPaKKNLltmmdeAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAK 222
Cdd:cd07140 119 GWCDKIQGKTIPINQARP-NRNL------TLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 223 ILAEL-LPQYLDQDLYMIVNGgveeTTELLRQRF-DH-----ILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYID 294
Cdd:cd07140 192 KFAELtVKAGFPKGVINILPG----SGSLVGQRLsDHpdvrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIF 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 295 RDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRI----- 368
Cdd:cd07140 268 ADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLveyce 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 369 KSLLEGQKIAFGG-ETDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKN--VEEAINFINDREKPLALYIFSHNN 445
Cdd:cd07140 348 RGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDI 427
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 564372361 446 KLIKRVIDETSSGGVTGNdvIMHFTVNSLPFGGVGASGMG 485
Cdd:cd07140 428 NKALYVSDKLEAGTVFVN--TYNKTDVAAPFGGFKQSGFG 465
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
174-496 |
3.11e-35 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 138.50 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 174 VQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNG-----GVEET 247
Cdd:PRK11241 142 VIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGsagavGGELT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 248 TELLRQRFDhilYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCE 327
Cdd:PRK11241 222 SNPLVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 328 ASLQDQIVQKIKDTVKDFY-GENVKASPDYERIINLRHFKRIK-----SLLEGQKIAFGGETDE-ATRYIAPTILTDVDP 400
Cdd:PRK11241 299 DGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARVVCGGKAHElGGNFFQPTILVDVPA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 401 NSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVnsLPFGGVG 480
Cdd:PRK11241 379 NAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV--APFGGIK 456
|
330
....*....|....*.
gi 564372361 481 ASGMGAYHGKYSFDTF 496
Cdd:PRK11241 457 ASGLGREGSKYGIEDY 472
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
172-497 |
1.12e-34 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 137.33 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 172 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAEL-----LPqylDQDLYMIVNGGVEE 246
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLakeagLP---DGVLNVVTGFGHEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 247 TTEL-LRQRFDHILYTGNTAVGKIVM-EAAAKHLTPVTLELGGKSPCYIDRDC-DLDVACRRITWGKYMNCGQTCIAPDY 323
Cdd:PRK09847 228 GQALsRHNDIDAIAFTGSTRTGKQLLkDAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 324 ILCEASLQDQIVQKIKDTVKDFY-GENVKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETDEATrYIAPTILTD 397
Cdd:PRK09847 308 LLLEESIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIRegeskGQLLLDGRNAGLAA-AIGPTIFVD 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 398 VDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGV---TGNDVIMhftvnSL 474
Cdd:PRK09847 387 VDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVfvnNYNDGDM-----TV 461
|
330 340
....*....|....*....|...
gi 564372361 475 PFGGVGASGMGAYHGKYSFDTFS 497
Cdd:PRK09847 462 PFGGYKQSGNGRDKSLHALEKFT 484
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
177-496 |
1.05e-33 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 134.94 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 177 EPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNG-GVEETTELLRQR 254
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGfGPTAGAALASHM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 255 -FDHILYTGNTAVGKIVMEAAAK-HLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQD 332
Cdd:PLN02466 274 dVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 333 QIVQK-----IKDTVKDFYGENVKASPDyeriINLRHFKR----IKSLLE-GQKIAFGGETDEATRY-IAPTILTDVDPN 401
Cdd:PLN02466 354 EFVEKakaraLKRVVGDPFKKGVEQGPQ----IDSEQFEKilryIKSGVEsGATLECGGDRFGSKGYyIQPTVFSNVQDD 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 402 SKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGN--DVimhFTVnSLPFGGV 479
Cdd:PLN02466 430 MLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDV---FDA-AIPFGGY 505
|
330
....*....|....*..
gi 564372361 480 GASGMGAYHGKYSFDTF 496
Cdd:PLN02466 506 KMSGIGREKGIYSLNNY 522
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
60-485 |
5.71e-32 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 128.83 E-value: 5.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 60 TGIVLLHLPrsaFSSGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVI 139
Cdd:PRK13968 16 TGEQLSVLP---WAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-EVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 140 TILGEIDFMLGNLPELASARPAkknlLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSEN 219
Cdd:PRK13968 92 KSANLCDWYAEHGPAMLKAEPT----LVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 220 TAKILAELlpqYLDQDLYMIVNGGVEETTELLRQ-----RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYID 294
Cdd:PRK13968 168 CAQLIAQV---FKDAGIPQGVYGWLNADNDGVSQmindsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 295 RDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDFygeNVKASPDYERII------NLR---HF 365
Cdd:PRK13968 245 NDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAAL---KMGDPRDEENALgpmarfDLRdelHH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 366 KRIKSLLEGQKIAFGGETDE-ATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHN 444
Cdd:PRK13968 322 QVEATLAEGARLLLGGEKIAgAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTD 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 564372361 445 NKLIKRVIDETSSGGVtgndVIMHFTVNS--LPFGGVGASGMG 485
Cdd:PRK13968 402 ETQARQMAARLECGGV----FINGYCASDarVAFGGVKKSGFG 440
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
169-490 |
5.84e-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: 129.05 E-value: 5.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 169 MDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEET 247
Cdd:cd07111 138 LDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGSFG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 248 TELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC 326
Cdd:cd07111 218 SALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLV 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 327 EASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLEGQKiAFGGETDEATR-------YIAPTILTDV 398
Cdd:cd07111 298 QESVAEELIRKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADVFQPGAdlpskgpFYPPTLFTNV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 399 DPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMhFTVNSlPFGG 478
Cdd:cd07111 377 PPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNL-FDAAA-GFGG 454
|
330
....*....|..
gi 564372361 479 VGASGMGAYHGK 490
Cdd:cd07111 455 YRESGFGREGGK 466
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
71-489 |
1.83e-31 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 128.08 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 71 AFSSGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAySHEVITILGEIDFMLG 150
Cdd:cd07083 50 AKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEA-IDDVAEAIDFIRYYAR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 151 NLPELASARPAKKNLLTMMDEAYVQPepLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQ 230
Cdd:cd07083 129 AALRLRYPAVEVVPYPGEDNESFYVG--LGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 231 Y-LDQDLYMIVNGGVEETTELL--RQRFDHILYTGNTAVGKIVMEAAAKHLT------PVTLELGGKSPCYIDRDCDLDV 301
Cdd:cd07083 207 AgFPPGVVQFLPGVGEEVGAYLteHERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFEL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 302 ACRRITWGKYMNCGQTCIAPDYILCEASLQDQI---VQKIKDTVKdfYGENVKASPDYERIINLRHFKRIKSLLEGQK-- 376
Cdd:cd07083 287 VVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVlerLLKRAERLS--VGPPEENGTDLGPVIDAEQEAKVLSYIEHGKne 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 377 --IAFGGETDEATRY-IAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVE--EAINFINDREKPLALYIFSHNNKLIKRV 451
Cdd:cd07083 365 gqLVLGGKRLEGEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEA 444
|
410 420 430
....*....|....*....|....*....|....*...
gi 564372361 452 IDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMGAYHG 489
Cdd:cd07083 445 RREFHVGNLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
82-483 |
8.25e-30 |
|
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: 121.99 E-value: 8.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 82 VQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEReKDILA-AIAADLSKSELNAYShEVITILGEIDFMLGNLPElasaRP 160
Cdd:cd07095 6 VAAARAAFPGWAALSLEERAAILRRFAELLKAN-KEELArLISRETGKPLWEAQT-EVAAMAGKIDISIKAYHE----RT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 161 AKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELL-PQYLDQDLYMI 239
Cdd:cd07095 80 GERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPGVLNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 240 VNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHltP---VTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCG 315
Cdd:cd07095 160 VQGGRETGEALAAHeGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 316 QTC------IAPDYILCEASLqDQIVQKIK-------DTVKDFYGENV--KASPDYERIINLRHFKRIKSLLEGQKIafg 380
Cdd:cd07095 238 QRCtcarrlIVPDGAVGDAFL-ERLVEAAKrlrigapDAEPPFMGPLIiaAAAARYLLAQQDLLALGGEPLLAMERL--- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 381 getDEATRYIAPTILtDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGV 460
Cdd:cd07095 314 ---VAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIV 389
|
410 420
....*....|....*....|...
gi 564372361 461 TGNDVIMhFTVNSLPFGGVGASG 483
Cdd:cd07095 390 NWNRPTT-GASSTAPFGGVGLSG 411
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
170-485 |
1.93e-29 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 121.91 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 170 DEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGgVEETT 248
Cdd:PRK13252 134 SFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVVQG-DGRVG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 249 ELLRQ--RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC 326
Cdd:PRK13252 213 AWLTEhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 327 EASLQDQIVQKIKDTVK-----DFYGENVKASPdyerIINLRHFKRI-----KSLLEGQKIAFGGE--TDEATR---YIA 391
Cdd:PRK13252 293 QKSIKAAFEARLLERVEririgDPMDPATNFGP----LVSFAHRDKVlgyieKGKAEGARLLCGGErlTEGGFAngaFVA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 392 PTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVtgndvimhfTV 471
Cdd:PRK13252 369 PTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGIC---------WI 439
|
330 340
....*....|....*....|.
gi 564372361 472 NS-------LPFGGVGASGMG 485
Cdd:PRK13252 440 NTwgespaeMPVGGYKQSGIG 460
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
156-485 |
8.63e-28 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 116.78 E-value: 8.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 156 ASARPAKKNLLTMMDE---AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYL 232
Cdd:cd07116 111 AGCIRAQEGSISEIDEntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 233 DQDLYMIVNG-GVEETTELL-RQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSP-CYIDRDCDLDVA-CRRITW 308
Cdd:cd07116 191 PPGVVNVVNGfGLEAGKPLAsSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPnIFFADVMDADDAfFDKALE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 309 GKYM---NCGQTCIAPDYILCEASLQDQIVQKIKDTVKDFygenVKASP-DYERII----NLRHFKRIKSLL-----EGQ 375
Cdd:cd07116 271 GFVMfalNQGEVCTCPSRALIQESIYDRFMERALERVKAI----KQGNPlDTETMIgaqaSLEQLEKILSYIdigkeEGA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 376 KIAFGGE-----TDEATRYIAPTILTDVDpNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKR 450
Cdd:cd07116 347 EVLTGGErnelgGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYR 425
|
330 340 350
....*....|....*....|....*....|....*
gi 564372361 451 VIDETSSGGVTGNdvIMHFTVNSLPFGGVGASGMG 485
Cdd:cd07116 426 MGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIG 458
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
67-488 |
2.44e-27 |
|
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: 115.36 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 67 LPRSAFSSGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYSH-----EVITI 141
Cdd:TIGR01722 29 TTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIAELITAEHGKTHSDALGDvarglEVVEH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 142 LGEID-FMLGNLPElasarpakkNLLTMMDeAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENT 220
Cdd:TIGR01722 109 ACGVNsLLKGETST---------QVATRVD-VYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 221 AKILAELLPQY-LDQDLYMIVNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCD 298
Cdd:TIGR01722 179 AVKLAELFSEAgAPDGVLNVVHGDKEAVDRLLEHpDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 299 LDVACRRITWGKYMNCGQTCIAPDYILCEASLqDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLL----- 372
Cdd:TIGR01722 259 KDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIrIGPGDDPGAEMGPLITPQAKDRVASLIaggaa 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 373 EGQKIAFGG-----ETDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKL 447
Cdd:TIGR01722 338 EGAEVLLDGrgykvDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAA 417
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 564372361 448 IKRVIDETSSGGVtGNDVIMHFTVNSLPFGGVGASGMGAYH 488
Cdd:TIGR01722 418 ARRFQHEIEVGQV-GVNVPIPVPLPYFSFTGWKDSFFGDHH 457
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
74-493 |
2.83e-25 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 109.06 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 74 SGPAMERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSeLNAYSHEVITILGEIDFMLGNLP 153
Cdd:PRK09406 21 TDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKT-LASAKAEALKCAKGFRYYAEHAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 154 ELASARPAKKNLLTMmDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELL----- 228
Cdd:PRK09406 100 ALLADEPADAAAVGA-SRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFrragf 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 229 PQYLDQDLyMIVNGGVEEtteLLR-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIT 307
Cdd:PRK09406 179 PDGCFQTL-LVGSGAVEA---ILRdPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 308 WGKYMNCGQTCIAPDYILCEASLQDQIVQKIKD-----TVKDFYGENVKASP--------DYERIINlrhfkriKSLLEG 374
Cdd:PRK09406 255 TARVQNNGQSCIAAKRFIVHADVYDAFAEKFVArmaalRVGDPTDPDTDVGPlateqgrdEVEKQVD-------DAVAAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 375 QKIAFGGET-DEATRYIAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVID 453
Cdd:PRK09406 328 ATILCGGKRpDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFID 407
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 564372361 454 ETSSGGVTGNDviMHFTVNSLPFGGVGASGMG---AYHGKYSF 493
Cdd:PRK09406 408 DLEAGQVFING--MTVSYPELPFGGVKRSGYGrelSAHGIREF 448
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
79-444 |
1.86e-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: 103.83 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRSRPLRFR---LQQL-EALRRmvqerEKDILAAIAadlskselnaySHEVITI----LGEI----- 145
Cdd:cd07130 37 ESTIKAAQEAFKEWRDVPAPKRgeiVRQIgDALRK-----KKEALGKLV-----------SLEMGKIlpegLGEVqemid 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 146 --DFMLG-----NLPELASARPAKKnlltMMDeayvQPEPLGVVLIIGAWNYP-------FVLTLqplvgaiAAGNAAIV 211
Cdd:cd07130 101 icDFAVGlsrqlYGLTIPSERPGHR----MME----QWNPLGVVGVITAFNFPvavwgwnAAIAL-------VCGNVVVW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 212 KPSELSENTA----KILAELLPQY-LDQDLYMIVNGGVEETTELLR-QRFDHILYTGNTAVGKIVMEAAAKHLTPVTLEL 285
Cdd:cd07130 166 KPSPTTPLTAiavtKIVARVLEKNgLPGAIASLVCGGADVGEALVKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 286 GGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKD---TVK--DFYGENVKASP------ 354
Cdd:cd07130 246 GGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKaykQVRigDPLDDGTLVGPlhtkaa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 355 --DYERIINlrhfkRIKSllEGQKIAFGGE-TDEATRYIAPTILTdVDPNSKVMQEEIFGPILPIVSVKNVEEAINFIND 431
Cdd:cd07130 326 vdNYLAAIE-----EAKS--QGGTVLFGGKvIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNE 397
|
410
....*....|...
gi 564372361 432 REKPLALYIFSHN 444
Cdd:cd07130 398 VPQGLSSSIFTTD 410
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
172-485 |
4.51e-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: 99.42 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 172 AYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSE---LS-ENTAKILAEL-LPQYLDQDLYMIVNGGVEE 246
Cdd:cd07148 118 AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALatpLScLAFVDLLHEAgLPEGWCQAVPCENAVAEKL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 247 TTEllrQRFDHILYTGNTAVGKIVMEAAAKHlTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC 326
Cdd:cd07148 198 VTD---PRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 327 EASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLRHFKRIKSLLE-----GQKIAFGGETDEATRYiAPTILTDVDP 400
Cdd:cd07148 274 PAEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVEEWVNeavaaGARLLCGGKRLSDTTY-APTVLLDPPR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 401 NSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDvimH--FTVNSLPFGG 478
Cdd:cd07148 353 DAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND---HtaFRVDWMPFAG 429
|
....*..
gi 564372361 479 VGASGMG 485
Cdd:cd07148 430 RRQSGYG 436
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
105-486 |
1.10e-18 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 89.04 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 105 EALRRMVQEREKDilaAIAADLSKSELNAYS-HEVITILGEIDFMLGNlpelaSARPAKKNLLTMMDEAyvqpePLGVVL 183
Cdd:PLN00412 97 ECLVKEIAKPAKD---AVTEVVRSGDLISYTaEEGVRILGEGKFLVSD-----SFPGNERNKYCLTSKI-----PLGVVL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 184 IIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELLRQR--FDHILY 260
Cdd:PLN00412 164 AIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAgFPKGLISCVTGKGSEIGDFLTMHpgVNCISF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 261 TGNTAVGKIVMEAAakhLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKD 340
Cdd:PLN00412 244 TGGDTGIAISKKAG---MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 341 TVKDFYGENVKASPDYERIINLRHFKRIKSLLEG--QKIA-FGGETDEATRYIAPTILTDVDPNSKVMQEEIFGPILPIV 417
Cdd:PLN00412 321 KVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDakEKGAtFCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVI 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564372361 418 SVKNVEEAINFINDREKPLALYIFSHN-NKLIkRVIDETSSGGVTGNDVIM----HFtvnslPFGGVGASGMGA 486
Cdd:PLN00412 401 RINSVEEGIHHCNASNFGLQGCVFTRDiNKAI-LISDAMETGTVQINSAPArgpdHF-----PFQGLKDSGIGS 468
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
79-483 |
2.28e-18 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 88.09 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVITILGEIDFMLGNLPElasa 158
Cdd:PRK09457 40 DAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAAT-EVTAMINKIAISIQAYHE---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 159 RPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLY 237
Cdd:PRK09457 115 RTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 238 MIVNGGVEETTELLRQR-FDHILYTGNTAVGKIVMEAAAKHltP---VTLELGGKSPCYIDRDCDLDVACRRITWGKYMN 313
Cdd:PRK09457 195 NLVQGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFIS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 314 CGQTCIAPDYILCEASLQ-DQIVQKIKDTVK-----DFYGENvkaSPDYERIINLRHFKRiksLLEGQK--IAFGGET-- 383
Cdd:PRK09457 273 AGQRCTCARRLLVPQGAQgDAFLARLVAVAKrltvgRWDAEP---QPFMGAVISEQAAQG---LVAAQAqlLALGGKSll 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 384 -----DEATRYIAPTILtDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSG 458
Cdd:PRK09457 347 emtqlQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAG 425
|
410 420
....*....|....*....|....*
gi 564372361 459 GVTGNDVIMHFTvNSLPFGGVGASG 483
Cdd:PRK09457 426 IVNWNKPLTGAS-SAAPFGGVGASG 449
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
171-498 |
2.25e-16 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 82.49 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 171 EAYVQPEPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYMIVNGGVEETTEL 250
Cdd:PLN02419 242 DTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 251 LRQRFD--HILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILC-- 326
Cdd:PLN02419 322 ICDDEDirAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvg 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 327 -EASLQDQIVQKIKdTVKDFYGENVKAspDYERIINLRHFKRI------------KSLLEGQKIAFGGEtdEATRYIAPT 393
Cdd:PLN02419 402 dAKSWEDKLVERAK-ALKVTCGSEPDA--DLGPVISKQAKERIcrliqsgvddgaKLLLDGRDIVVPGY--EKGNFIGPT 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 394 ILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVtGNDVIMHFTVNS 473
Cdd:PLN02419 477 ILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQI-GINVPIPVPLPF 555
|
330 340
....*....|....*....|....*..
gi 564372361 474 LPFGGVGASGMG--AYHGKYSFDTFSH 498
Cdd:PLN02419 556 FSFTGNKASFAGdlNFYGKAGVDFFTQ 582
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
137-502 |
2.89e-16 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 81.80 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 137 EVITILGEIDFMLG-----NLPELASARPAKknlltMMDEAYvqpEPLGVVLIIGAWNYP-FVLTLQP-LVGAIAAGNAA 209
Cdd:PLN02315 116 EVQEIIDMCDFAVGlsrqlNGSIIPSERPNH-----MMMEVW---NPLGIVGVITAFNFPcAVLGWNAcIALVCGNCVVW 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 210 IVKPSE--LSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKHLTPVTLEL 285
Cdd:PLN02315 188 KGAPTTplITIAMTKLVAEVLEKNnLPGAIFTSFCGGAEIGEAIAKDtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLEL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 286 GGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKAS-------PDYE 357
Cdd:PLN02315 268 SGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVkIGDPLEKGtllgplhTPES 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 358 RIINLRHFKRIKSllEGQKIAFGGETDEAT-RYIAPTILtDVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPL 436
Cdd:PLN02315 348 KKNFEKGIEIIKS--QGGKILTGGSAIESEgNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGL 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564372361 437 ALYIFSHNNKLIKRVIdetssgGVTGND---VIMHFTVNSL----PFGGVGASGMGAYHGKYSFDTFSHQRPC 502
Cdd:PLN02315 425 SSSIFTRNPETIFKWI------GPLGSDcgiVNVNIPTNGAeiggAFGGEKATGGGREAGSDSWKQYMRRSTC 491
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
79-486 |
7.49e-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: 80.32 E-value: 7.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 79 ERQVQRLRQTFRSGRSRPLRFRLQQLEALRRMVQEREKDILAAIAADLSKSELNAYShEVitilGE-IDF-------MLG 150
Cdd:cd07125 72 DAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADA-EV----REaIDFcryyaaqARE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 151 NLPELASARP-AKKNLLTMmdeayvqpEPLGVVLIIGAWNYPF----------------VLTlqplvgaiaagnaaivKP 213
Cdd:cd07125 147 LFSDPELPGPtGELNGLEL--------HGRGVFVCISPWNFPLaiftgqiaaalaagntVIA----------------KP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 214 SELSENTAKILAELL-----PQYLdqdLYMIVNGGVEETTELLRQ-RFDHILYTGNTAVGKIVMEAAAKH---LTPVTLE 284
Cdd:cd07125 203 AEQTPLIAARAVELLheagvPRDV---LQLVPGDGEEIGEALVAHpRIDGVIFTGSTETAKLINRALAERdgpILPLIAE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 285 LGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINLR 363
Cdd:cd07125 280 TGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLkVGDPWDLSTDVGPLIDKP 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 364 HFKRIKS---LLEGQK--IAFGGETDEATRYIAPTILTDVdpNSKVMQEEIFGPILPIVSVK--NVEEAINFINDREKPL 436
Cdd:cd07125 360 AGKLLRAhteLMRGEAwlIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 564372361 437 ALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMGA 486
Cdd:cd07125 438 TLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWGLSGTGP 487
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
178-486 |
1.26e-15 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 79.20 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 178 PLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQ--YLDQDLYMIVNGGVEETTELLRQ-R 254
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGKTMQALLLHpN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 255 FDHILYTGNTAVGKIVmeAAAKHLTPVTLELGGKSPCYIDRDCD-LDVACRRITWGKYMNCGQTCIAPDYILCEASLQdq 333
Cdd:cd07084 180 PKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWS-- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 334 iVQKIKDTVKDFYGENVKASPDYERIINLRHFKRIKSL--LEGQKIAFGGETDEATRY-------IAPTILTDVDPN--- 401
Cdd:cd07084 256 -KTPLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMenLLGSVLLFSGKELKNHSIpsiygacVASALFVPIDEIlkt 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 402 SKVMQEEIFGPILPIVSVKNVEEA--INFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTV--NSLPFG 477
Cdd:cd07084 335 YELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAGRTYAILRGRTGVapNQNHGG 414
|
....*....
gi 564372361 478 GVGASGMGA 486
Cdd:cd07084 415 GPAADPRGA 423
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
284-483 |
6.87e-13 |
|
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: 71.08 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 284 ELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQKIKDTVKDF-YGENVKASPDYERIINL 362
Cdd:cd07123 284 ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIkMGDPDDFSNFMGAVIDE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 363 RHFKRIKSLLE------GQKIAFGGETDEATRY-IAPTILTDVDPNSKVMQEEIFGPILpIVSV---KNVEEAINFINDR 432
Cdd:cd07123 364 KAFDRIKGYIDhaksdpEAEIIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFGPVL-TVYVypdSDFEETLELVDTT 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564372361 433 EkPLALY--IFSHNNKLIKRV------------IDETSSGGVTGNDvimhftvnslPFGGVGASG 483
Cdd:cd07123 443 S-PYALTgaIFAQDRKAIREAtdalrnaagnfyINDKPTGAVVGQQ----------PFGGARASG 496
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
177-489 |
1.00e-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: 70.71 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 177 EPLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQY-LDQDLYMIVNGGVEETTELL--RQ 253
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAgFPAGTIQLLPGRGADVGAALtsDP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 254 RFDHILYTGNTAVGKIVMEAAAKHL---TPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDyILCeasL 330
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALR-VLC---V 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 331 QDQIVQKIKDTVKDFYGENVKASP-----DYERIIN-------LRHFKRIKSllEGQKIA-FGGETDEATR---YIAPTi 394
Cdd:TIGR01238 315 QEDVADRVLTMIQGAMQELKVGVPhllttDVGPVIDaeakqnlLAHIEHMSQ--TQKKIAqLTLDDSRACQhgtFVAPT- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 395 LTDVDpNSKVMQEEIFGPILPIVSVK--NVEEAINFINDREKPLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVN 472
Cdd:TIGR01238 392 LFELD-DIAELSEEVFGPVLHVVRYKarELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVG 470
|
330
....*....|....*..
gi 564372361 473 SLPFGGVGASGMGAYHG 489
Cdd:TIGR01238 471 VQPFGGQGLSGTGPKAG 487
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
362-485 |
3.17e-06 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 50.20 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 362 LRHFKRIKSllEGQKIA---FGGETDEATrYIAPTI--LTDVDpnskVMQEEIFGPILPIVSVK--NVEEAINFINDREK 434
Cdd:PRK11904 882 DAHIERMKR--EARLLAqlpLPAGTENGH-FVAPTAfeIDSIS----QLEREVFGPILHVIRYKasDLDKVIDAINATGY 954
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 564372361 435 PLALYIFSHNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMG 485
Cdd:PRK11904 955 GLTLGIHSRIEETADRIADRVRVGNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
178-485 |
2.24e-04 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 44.19 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 178 PLGVVLIIGAWNYPFVLTLQPLVGAIAAGNAAIVKPSELSENTA----KILAE---------LLPqyldqdlymivngGV 244
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAaqavRILLEagvpagvvqLLP-------------GR 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 245 EET--TELLR-QRFDHILYTGNTAVGKIVMEAAAKHL------TPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMNCG 315
Cdd:PRK11809 835 GETvgAALVAdARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAG 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 316 QTCIAPDyILCeasLQDQIVQKIKDTVKDFYGENVKASPDY-----------ERIINL-RHFKRIKSllEGQKI---AFG 380
Cdd:PRK11809 915 QRCSALR-VLC---LQDDVADRTLKMLRGAMAECRMGNPDRlstdigpvidaEAKANIeRHIQAMRA--KGRPVfqaARE 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 381 GETDEAT-RYIAPTI--LTDVDPnskvMQEEIFGPILPIVSVK--NVEEAINFINDREKPLALYIFSHNNKLIKRVIDET 455
Cdd:PRK11809 989 NSEDWQSgTFVPPTLieLDSFDE----LKREVFGPVLHVVRYNrnQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSA 1064
|
330 340 350
....*....|....*....|....*....|
gi 564372361 456 SSGGVTGNDVIMHFTVNSLPFGGVGASGMG 485
Cdd:PRK11809 1065 HVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
315-452 |
4.37e-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: 43.03 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 315 GQTCIAPDYILCEASLQDQIVQKIKD-----TVKDFYGENVKASPdyerIINLRHF----KRIKSLLEGQKIAFGGETDE 385
Cdd:cd07128 289 GQKCTAIRRAFVPEARVDAVIEALKArlakvVVGDPRLEGVRMGP----LVSREQRedvrAAVATLLAEAEVVFGGPDRF 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564372361 386 ATR--------YIAPTILT--DVDPNSKVMQEEIFGPILPIVSVKNVEEAINFINDREKPLALYIFSHNNKLIKRVI 452
Cdd:cd07128 365 EVVgadaekgaFFPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
171-426 |
7.06e-04 |
|
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: 42.21 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 171 EAYVQPEPLGVVLIIGAWNYPfVLTLQPLVGAIAAGNAAIVKPSELSENTAKILA----ELLPQYLDQDLYMIVN-GGVE 245
Cdd:cd07077 93 ETYVRAFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTNRALAllfqAADAAHGPKILVLYVPhPSDE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 246 ETTELLRQ-RFDHILYTGntavGKIVMEAAAKH--LTPVTLELGGKSPCYIDRDCDLDVACRRITWGKYMncgqtciapD 322
Cdd:cd07077 172 LAEELLSHpKIDLIVATG----GRDAVDAAVKHspHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFF---------D 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 323 YILCeASLQDQIVqkikdtVKDFYgenvkaSPDYERIInLRHFKRIKSLLEGQKIAFGGETDEATRYIaptiltdvdpns 402
Cdd:cd07077 239 QNAC-ASEQNLYV------VDDVL------DPLYEEFK-LKLVVEGLKVPQETKPLSKETTPSFDDEA------------ 292
|
250 260
....*....|....*....|....
gi 564372361 403 kvmqEEIFGPILPIVSVKNVEEAI 426
Cdd:cd07077 293 ----LESMTPLECQFRVLDVISAV 312
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
376-485 |
7.29e-04 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 42.54 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 376 KIAFGGETDEATrYIAPTILtDVDpNSKVMQEEIFGPILPIVSVK--NVEEAINFINDREKPLALYIFSHNNKLIKRVID 453
Cdd:PRK11905 889 QLPLPAETEKGT-FVAPTLI-EID-SISDLEREVFGPVLHVVRFKadELDRVIDDINATGYGLTFGLHSRIDETIAHVTS 965
|
90 100 110
....*....|....*....|....*....|..
gi 564372361 454 ETSSGGVTGNDVIMHFTVNSLPFGGVGASGMG 485
Cdd:PRK11905 966 RIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTG 997
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
238-450 |
1.39e-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: 41.32 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 238 MIVNGGVEETTELLRQR-FDHILYTGNTAVGKivmeAAAKHLTPVtleLG---GKSPCYIDRDCDLDVACRRITWGKYMN 313
Cdd:cd07122 161 WIEEPSIELTQELMKHPdVDLILATGGPGMVK----AAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 314 CGQTCIAPDYILCEASLQDQIVQKIKDT-------------VKDFYGENVKASPDyerIINlrhfkriKSlleGQKIA-- 378
Cdd:cd07122 234 NGTICASEQSVIVDDEIYDEVRAELKRRgayflneeekeklEKALFDDGGTLNPD---IVG-------KS---AQKIAel 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 379 FGGETDEATRYIAPTIlTDVDPNSKVMQEEIFgPILPIVSVKNVEEAInfindrEKPLALY----------IFSHNNKLI 448
Cdd:cd07122 301 AGIEVPEDTKVLVAEE-TGVGPEEPLSREKLS-PVLAFYRAEDFEEAL------EKARELLeyggaghtavIHSNDEEVI 372
|
..
gi 564372361 449 KR 450
Cdd:cd07122 373 EE 374
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
261-427 |
1.73e-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: 41.07 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 261 TGNTAVGKIVMEAAAKhltpvtlELG---GKSPCYIDRDCDLDVACRRITWGKYMNCGQTCIAPDYILCEASLQDQIVQK 337
Cdd:cd07121 187 TGGPAVVKAALSSGKK-------AIGagaGNPPVVVDETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 338 IKDtvkdfYGENVKASPDYERIINL----RHFKRIKSLLEGQ---KIA--FGGETDEATRyiapTILTDVDPNSKVMQEE 408
Cdd:cd07121 260 MQR-----NGAYVLNDEQAEQLLEVvlltNKGATPNKKWVGKdasKILkaAGIEVPADIR----LIIVETDKDHPFVVEE 330
|
170
....*....|....*....
gi 564372361 409 IFGPILPIVSVKNVEEAIN 427
Cdd:cd07121 331 QMMPILPVVRVKNFDEAIE 349
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
362-485 |
1.79e-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: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 362 LRHFKRIKSllEGQKIA---FGGETDEATrYIAPTI--LTDVDpnskVMQEEIFGPILPIVSVK--NVEEAINFINDREK 434
Cdd:COG4230 878 EAHIERMRA--EGRLVHqlpLPEECANGT-FVAPTLieIDSIS----DLEREVFGPVLHVVRYKadELDKVIDAINATGY 950
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 435 PLALYIFSHNNKLIKRVIDETSsggvTGNdvimhFTVN---------SLPFGGVGASGMG 485
Cdd:COG4230 951 GLTLGVHSRIDETIDRVAARAR----VGN-----VYVNrniigavvgVQPFGGEGLSGTG 1001
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
378-426 |
1.82e-03 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 41.04 E-value: 1.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 564372361 378 AFGGETDEATRyiapTILTDVDPNSKVMQEEIFGPILPIVSVKNVEEAI 426
Cdd:PRK15398 334 AAGINVPKDTR----LLIVETDANHPFVVTELMMPVLPVVRVKDVDEAI 378
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
178-486 |
5.07e-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: 39.79 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 178 PLGVVLIIGAWNYPFVLTLQPLVGAIAAGnaaiVKPSELSENTAKILAELLPQYL------DQDLYMIVNGGVEETTELL 251
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMG----NKPLLKVDSKVSVVMEQFLRLLhlcgmpATDVDLIHSDGPTMNKILL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 252 RQRFDHILYTGNTAV---------GKIVMEAAA---KHLTPVTLELGgkspcYIDRDCDLDVacrritwgkYMNCGQTCI 319
Cdd:cd07126 218 EANPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQDA---------YACSGQKCS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 320 APDYILCEASLQDQ-IVQKIKDTVKDFYGENVKASP----DYERIINlrHFKRIKSlLEGQKIAFGGEtdEATRYIAPTI 394
Cdd:cd07126 284 AQSILFAHENWVQAgILDKLKALAEQRKLEDLTIGPvltwTTERILD--HVDKLLA-IPGAKVLFGGK--PLTNHSIPSI 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372361 395 LTDVDP--------------NSKVMQEEIFGPILPIVSVKNVEEainfindrekPLALYIFSHnnklikrvIDETSSGGV 460
Cdd:cd07126 359 YGAYEPtavfvpleeiaieeNFELVTTEVFGPFQVVTEYKDEQL----------PLVLEALER--------MHAHLTAAV 420
|
330 340 350
....*....|....*....|....*....|.
gi 564372361 461 TGNDV-----IMHFTVNSLPFGGVGASGMGA 486
Cdd:cd07126 421 VSNDIrflqeVLANTVNGTTYAGIRARTTGA 451
|
|
| |
