|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
8-455 |
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: 789.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 8 EKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITELEFVKNDIKYQLDHIHQYVKP 87
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 88 QRVARPAANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYP 167
Cdd:cd07132 81 EPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 168 VVTGGADVANQLLQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVegQLEVAAKRVLWGKLTNSGQ 247
Cdd:cd07132 161 VVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSC--DIDVAARRIAWGKFINAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 248 TCVAPDYVLCSPSVQDRFVEASKKVLKDFYG-DPAKSDSFARIVNDRNFDRLEKLLSAtkGKVVVGGQTAKGERYIAPTL 326
Cdd:cd07132 239 TCIAPDYVLCTPEVQEKFVEALKKTLKEFYGeDPKESPDYGRIINDRHFQRLKKLLSG--GKVAIGGQTDEKERYIAPTV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 327 VANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHSL 406
Cdd:cd07132 317 LTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSL 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 26334245 407 PFGGIGNSGIGKYHGTYSFETFSHSKSVLAKDYNplIEYFASSRYPPYT 455
Cdd:cd07132 397 PFGGVGNSGMGAYHGKYSFDTFSHKRSCLVKSLN--MEKLNSLRYPPYS 443
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
15-435 |
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: 657.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 15 REAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITELEFVKNDIKYQLDHIHQYVKPQRVARPA 94
Cdd:cd07087 8 RETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRVSVPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 95 ANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYPVVTGGAD 174
Cdd:cd07087 88 LLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVEGGVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 175 VANQLLQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVegQLEVAAKRVLWGKLTNSGQTCVAPDY 254
Cdd:cd07087 168 VATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDA--NLEVAARRIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 255 VLCSPSVQDRFVEASKKVLKDFYG-DPAKSDSFARIVNDRNFDRLEKLLSAtkGKVVVGGQTAKGERYIAPTLVANVTGN 333
Cdd:cd07087 246 VLVHESIKDELIEELKKAIKEFYGeDPKESPDYGRIINERHFDRLASLLDD--GKVVIGGQVDKEERYIAPTILDDVSPD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 334 DSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHSLPFGGIGN 413
Cdd:cd07087 324 SPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGVGN 403
|
410 420
....*....|....*....|..
gi 26334245 414 SGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07087 404 SGMGAYHGKAGFDTFSHLKSVL 425
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
8-463 |
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: 604.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 8 EKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITELEFVKNDIKYQLDHIHQYVKP 87
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 88 QRVARPAANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYP 167
Cdd:cd07136 81 KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 168 VVTGGADVANQLLQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSveGQLEVAAKRVLWGKLTNSGQ 247
Cdd:cd07136 161 VVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDED--ANLKLAAKRIVWGKFLNAGQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 248 TCVAPDYVLCSPSVQDRFVEASKKVLKDFYG-DPAKSDSFARIVNDRNFDRLEKLLSatKGKVVVGGQTAKGERYIAPTL 326
Cdd:cd07136 239 TCVAPDYVLVHESVKEKFIKELKEEIKKFYGeDPLESPDYGRIINEKHFDRLAGLLD--NGKIVFGGNTDRETLYIEPTI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 327 VANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHSL 406
Cdd:cd07136 317 LDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYL 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26334245 407 PFGGIGNSGIGKYHGTYSFETFSHSKSVLAK----DyNPLieyfassRYPPYTDGKMKLLK 463
Cdd:cd07136 397 PFGGVGNSGMGSYHGKYSFDTFSHKKSILKKstwfD-LPL-------RYPPYKGKKKKLKK 449
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
3-468 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 595.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 3 SPVLIEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITELEFVKNDIKYQLDHIH 82
Cdd:PTZ00381 5 NPEIIPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 83 QYVKPQRVARPAANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLD 162
Cdd:PTZ00381 85 EYLKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 163 KECYPVVTGGADVANQLLQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKL 242
Cdd:PTZ00381 165 PSYVRVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCN--LKVAARRIAWGKF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 243 TNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDFYG-DPAKSDSFARIVNDRNFDRLEKLLSATKGKVVVGGQTAKGERY 321
Cdd:PTZ00381 243 LNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGeDPKKSEDYSRIVNEFHTKRLAELIKDHGGKVVYGGEVDIENKY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 322 IAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQM 401
Cdd:PTZ00381 323 VAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26334245 402 VLHSLPFGGIGNSGIGKYHGTYSFETFSHSKSVLAKdyNPLIEYFASSRYPPYTDGKMKLLKVLAGP 468
Cdd:PTZ00381 403 LNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVLNK--STGNSFDLSLRYPPYTSFKSWVLSFLLKL 467
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
7-435 |
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: 590.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITELEFVKNDIKYQLDHIHQYVK 86
Cdd:cd07135 7 IDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 87 PQRVAR-PAANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKEC 165
Cdd:cd07135 87 DEKVKDgPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 166 YPVVTGGADVANQLLQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVegQLEVAAKRVLWGKLTNS 245
Cdd:cd07135 167 FQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNA--DLELAAKRILWGKFGNA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 246 GQTCVAPDYVLCSPSVQDRFVEASKKVLKDFY-GDPAKSDSFARIVNDRNFDRLEKLLSATKGKVVVGGQTAKGERYIAP 324
Cdd:cd07135 245 GQICVAPDYVLVDPSVYDEFVEELKKVLDEFYpGGANASPDYTRIVNPRHFNRLKSLLDTTKGKVVIGGEMDEATRFIPP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 325 TLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLH 404
Cdd:cd07135 325 TIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVD 404
|
410 420 430
....*....|....*....|....*....|.
gi 26334245 405 SLPFGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07135 405 NAPFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
15-435 |
1.16e-179 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 511.00 E-value: 1.16e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 15 REAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITELEFVKNDIKYQLDHIHQYVKPQRVARPA 94
Cdd:cd07134 8 QAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 95 ANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYPVVTGGAD 174
Cdd:cd07134 88 LLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 175 VANQLLQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDY 254
Cdd:cd07134 168 VAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETAD--LKKAAKKIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 255 VLCSPSVQDRFVEASKKVLKDFYGD---PAKSDSFARIVNDRNFDRLEKLL--SATKG-KVVVGGQTAKGERYIAPTLVA 328
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIEKFYGKdaaRKASPDLARIVNDRHFDRLKGLLddAVAKGaKVEFGGQFDAAQRYIAPTVLT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 329 NVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHSLPF 408
Cdd:cd07134 326 NVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPF 405
|
410 420
....*....|....*....|....*..
gi 26334245 409 GGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07134 406 GGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
15-435 |
1.63e-165 |
|
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: 475.05 E-value: 1.63e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 15 REAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDF-RKPKFESVITELEFVKNDIKYQLDHIHQYVKPQRVA-- 91
Cdd:cd07133 8 KAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMKPSRRHvg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 92 ---RPAAnilddAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYPV 168
Cdd:cd07133 88 llfLPAK-----AEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 169 VTGGADVANQLLQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQT 248
Cdd:cd07133 163 VTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDAD--LAKAAERIAFGKLLNAGQT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 249 CVAPDYVLCSPSVQDRFVEASKKVLKDFYGDPAKSDSFARIVNDRNFDRLEKLLS--ATKGKVVV----GGQTAKGERYI 322
Cdd:cd07133 241 CVAPDYVLVPEDKLEEFVAAAKAAVAKMYPTLADNPDYTSIINERHYARLQGLLEdaRAKGARVIelnpAGEDFAATRKL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 323 APTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMV 402
Cdd:cd07133 321 PPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHVA 400
|
410 420 430
....*....|....*....|....*....|...
gi 26334245 403 LHSLPFGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07133 401 QDDLPFGGVGASGMGAYHGKEGFLTFSHAKPVF 433
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
15-435 |
1.41e-158 |
|
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: 457.26 E-value: 1.41e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 15 REAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITELEFVKNDIKYQLDHIHQYVKPQRVARPA 94
Cdd:cd07137 9 RETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPEKVKTPL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 95 ANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYPVVTGGAD 174
Cdd:cd07137 89 TTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEGGVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 175 VANQLLQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKL-TNSGQTCVAPD 253
Cdd:cd07137 169 ETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVD--LKVAVRRIAGGKWgCNNGQACIAPD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 254 YVLCSPSVQDRFVEASKKVLKDFYG-DPAKSDSFARIVNDRNFDRLEKLLSATK--GKVVVGGQTAKGERYIAPTLVANV 330
Cdd:cd07137 247 YVLVEESFAPTLIDALKNTLEKFFGeNPKESKDLSRIVNSHHFQRLSRLLDDPSvaDKIVHGGERDEKNLYIEPTILLDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 331 TGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHSLPFGG 410
Cdd:cd07137 327 PLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGG 406
|
410 420
....*....|....*....|....*
gi 26334245 411 IGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07137 407 VGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
7-465 |
2.50e-144 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 422.98 E-value: 2.50e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITELEFVKNDIKYQLDHIHQYVK 86
Cdd:PLN02203 8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 87 PQRVARPAANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECY 166
Cdd:PLN02203 88 PKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 167 PVVTGGADVANQLLQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDD-SVEGQLEVAAKRVLWGKL-TN 244
Cdd:PLN02203 168 KVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDSlSSSRDTKVAVNRIVGGKWgSC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 245 SGQTCVAPDYVLcspsVQDRF----VEASKKVLKDFYGD-PAKSDSFARIVNDRNFDRLEKLLS--ATKGKVVVGGQTAK 317
Cdd:PLN02203 248 AGQACIAIDYVL----VEERFapilIELLKSTIKKFFGEnPRESKSMARILNKKHFQRLSNLLKdpRVAASIVHGGSIDE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 318 GERYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDT 397
Cdd:PLN02203 324 KKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26334245 398 LMQMVLHSLPFGGIGNSGIGKYHGTYSFETFSHSKSVLAKDYnpLIEYFAssRYPPYTDGKMKLLKVL 465
Cdd:PLN02203 404 IIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSL--LTEFEF--RYPPWNDFKLGFLRLV 467
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
8-436 |
1.27e-126 |
|
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: 375.78 E-value: 1.27e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 8 EKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESViTELEFVKNDIKYQLDHIHQYVKP 87
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 88 QRVARPAANildDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECY 166
Cdd:cd07078 80 VIPSPDPGE---LAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 167 PVVTGGADVANQLL--QERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVegQLEVAAKRVLWGKLTN 244
Cdd:cd07078 157 NVVTGDGDEVGAALasHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDA--DLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 245 SGQTCVAPDYVLCSPSVQDRFVEASKKVLKDFY-GDPAKSDSFA-RIVNDRNFDRLEKLLSATK---GKVVVGGQTAKGE 319
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKvGNPLDPDTDMgPLISAAQLDRVLAYIEDAKaegAKLLCGGKRLEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 320 --RYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDT 397
Cdd:cd07078 315 kgYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDY 394
|
410 420 430
....*....|....*....|....*....|....*....
gi 26334245 398 LMQMVLHsLPFGGIGNSGIGKYHGTYSFETFSHSKSVLA 436
Cdd:cd07078 395 SVGAEPS-APFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
15-472 |
1.46e-117 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 354.35 E-value: 1.46e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 15 REAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITELEFVKNDIKYQLDHIHQYVKPQRVARPA 94
Cdd:PLN02174 20 RRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 95 ANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYPVVTGGAD 174
Cdd:PLN02174 100 TTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 175 VANQLLQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKL-TNSGQTCVAPD 253
Cdd:PLN02174 180 ETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTD--LKVTVRRIIAGKWgCNNGQACISPD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 254 YVLCSPSVQDRFVEASKKVLKDFYG-DPAKSDSFARIVNDRNFDRLEKLLSATK--GKVVVGGQTAKGERYIAPTLVANV 330
Cdd:PLN02174 258 YILTTKEYAPKVIDAMKKELETFYGkNPMESKDMSRIVNSTHFDRLSKLLDEKEvsDKIVYGGEKDRENLKIAPTILLDV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 331 TGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHSLPFGG 410
Cdd:PLN02174 338 PLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGG 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26334245 411 IGNSGIGKYHGTYSFETFSHSKSVLakdYNPLieyFASS--RYPPYTDGKMKLLKVLAGPTPLD 472
Cdd:PLN02174 418 VGESGMGAYHGKFSFDAFSHKKAVL---YRSL---FGDSavRYPPYSRGKLRLLKALVDSNIFD 475
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-434 |
1.04e-103 |
|
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: 318.61 E-value: 1.04e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 1 MSSPVLIEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESvitelefvKNDIKYQLDH 80
Cdd:COG1012 39 AATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEA--------RGEVDRAADF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 81 IHQYVK-PQRV---ARPAANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASL 156
Cdd:COG1012 111 LRYYAGeARRLygeTIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 157 LPKY-LDKECYPVVTG-GADVANQLLQ-ERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVA 233
Cdd:COG1012 191 LEEAgLPAGVLNVVTGdGSEVGAALVAhPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDAD--LDAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 234 AKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSDSF-ARIVNDRNFDRLEKLLSATK---GK 308
Cdd:COG1012 269 VEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALkVGDPLDPGTDmGPLISEAQLERVLAYIEDAVaegAE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 309 VVVGGQTAKGER--YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQ 386
Cdd:COG1012 349 LLTGGRRPDGEGgyFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARR 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 26334245 387 TSCGSVCVNDTLMQMVLHsLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:COG1012 429 LEAGMVWINDGTTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETKTV 475
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
14-436 |
1.20e-99 |
|
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: 304.15 E-value: 1.20e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 14 AREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKfESVITELEFVKNDIKYqldHIHQYVKPQRVARP 93
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPI-EEALGEVARAIDTFRY---AAGLADKLGGPELP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 94 AANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGG 172
Cdd:cd06534 79 SPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 173 ADVANQLL--QERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCV 250
Cdd:cd06534 159 GDEVGAALlsHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDAD--LDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 251 APDYVLCSPSVQDRFVEASKkvlkdfygdpaksdsfarivndrnfdrlekllsatkgkvvvggqtakgeryiapTLVANV 330
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV------------------------------------------------------TVLVDV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 331 TGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHsLPFGG 410
Cdd:cd06534 263 DPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPE-APFGG 341
|
410 420
....*....|....*....|....*.
gi 26334245 411 IGNSGIGKYHGTYSFETFSHSKSVLA 436
Cdd:cd06534 342 VKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
7-434 |
1.74e-96 |
|
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: 299.45 E-value: 1.74e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFA--RNVTRSVdfRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESViTELEFVKNDIKY---QLDHI 81
Cdd:pfam00171 31 VDAAIAAARAAFPawRKTPAAE--RAAILRKAADLLEERKDELAELETLENGKPLAEAR-GEVDRAIDVLRYyagLARRL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 82 HQYVKPQRVARpaanildDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY- 160
Cdd:pfam00171 108 DGETLPSDPGR-------LAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAg 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 161 LDKECYPVVTG-GADVANQLLQ-ERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVL 238
Cdd:pfam00171 181 LPAGVLNVVTGsGAEVGEALVEhPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDAD--LDAAVEAAV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 239 WGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSDSF-ARIVNDRNFDRLEKLLSATK---GKVVVGG 313
Cdd:pfam00171 259 FGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLkVGDPLDPDTDmGPLISKAQLERVLKYVEDAKeegAKLLTGG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 314 QTAKGE-RYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSV 392
Cdd:pfam00171 339 EAGLDNgYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMV 418
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 26334245 393 CVNDTLMQMVLHsLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:pfam00171 419 WINDYTTGDADG-LPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
1-436 |
9.00e-91 |
|
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: 284.50 E-value: 9.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 1 MSSPVLIEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVItELEFVkndikyqLDH 80
Cdd:cd07099 14 VTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL-EVLLA-------LEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 81 IHQYVK-------PQRVARPAANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVM 153
Cdd:cd07099 86 IDWAARnaprvlaPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 154 ASLLPKY-LDKECYPVVTGGADVANQLLQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEV 232
Cdd:cd07099 166 AEAWAAAgPPQGVLQVVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADAD--LER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 233 AAKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSD---------SFARIVNDRNFDRLEKll 302
Cdd:cd07099 244 AAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALrPGADDIGDadigpmttaRQLDIVRRHVDDAVAK-- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 303 satKGKVVVGGQTA-KGERYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVN 381
Cdd:cd07099 322 ---GAKALTGGARSnGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAE 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 26334245 382 KFLDQTSCGSVCVNDTLMQMVLHSLPFGGIGNSGIGKYHGTYSFETFSHSKSVLA 436
Cdd:cd07099 399 AIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
2-435 |
8.85e-72 |
|
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: 235.27 E-value: 8.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 2 SSPVLIEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITELEFVKNDIKYQLDHI 81
Cdd:cd07098 15 DTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 82 HQYVKPQRVARPAANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYL 161
Cdd:cd07098 95 EKALRPESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 162 -----DKECYPVVTGGADVANQLLQE-RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAK 235
Cdd:cd07098 175 aacghDPDLVQLVTCLPETAEALTSHpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDAD--LDQIAS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 236 RVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEA-SKKVLKDFYGDPAKS--DSFARIVNDRnFDRLEKLL--SATKG-KV 309
Cdd:cd07098 253 IIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEIlTDRVQALRQGPPLDGdvDVGAMISPAR-FDRLEELVadAVEKGaRL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 310 VVGGQTAKGER-----YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFL 384
Cdd:cd07098 332 LAGGKRYPHPEypqghYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIA 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 26334245 385 DQTSCGSVCVND-TLMQMVLhSLPFGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07098 412 SQLETGMVAINDfGVNYYVQ-QLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
107-434 |
1.25e-68 |
|
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: 226.54 E-value: 1.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVqLMLA-PLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTG-GADVANQLLQ-E 182
Cdd:cd07103 117 PVGVVAAITPWNFPA-AMITrKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPAGVLNVVTGsPAEIGEALCAsP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 183 RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYVLCSPSVQ 262
Cdd:cd07103 196 RVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD--LDKAVDGAIASKFRNAGQTCVCANRIYVHESIY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 263 DRFVEA-SKKVLKDFYGDPAKSDS-FARIVNDRNFDRLEKLLSA--TKG-KVVVGGQ-TAKGERYIAPTLVANVTGNDSL 336
Cdd:cd07103 274 DEFVEKlVERVKKLKVGNGLDEGTdMGPLINERAVEKVEALVEDavAKGaKVLTGGKrLGLGGYFYEPTVLTDVTDDMLI 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 337 MSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLmqMVLHSLPFGGIGNSGI 416
Cdd:cd07103 354 MNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGL--ISDAEAPFGGVKESGL 431
|
330
....*....|....*...
gi 26334245 417 GKYHGTYSFETFSHSKSV 434
Cdd:cd07103 432 GREGGKEGLEEYLETKYV 449
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
107-432 |
9.89e-68 |
|
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: 223.56 E-value: 9.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSE---VAGSTanVMASL-----LPKYLdkecYPVVTGGADVANQ 178
Cdd:cd07104 98 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSrtpVTGGL--LIAEIfeeagLPKGV----LNVVPGGGSEIGD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 179 LLQE--RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYI-DDSvegQLEVAAKRVLWGKLTNSGQTCVAPDYV 255
Cdd:cd07104 172 ALVEhpRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVlDDA---DLDLAVSAAAFGAFLHQGQICMAAGRI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 256 LCSPSVQDRFVEA-SKKVLKDFYGDPAKSDSF-ARIVNDRNFDRLEKLLSAT--KGKVVVGGQTAKGeRYIAPTLVANVT 331
Cdd:cd07104 249 LVHESVYDEFVEKlVAKAKALPVGDPRDPDTViGPLINERQVDRVHAIVEDAvaAGARLLTGGTYEG-LFYQPTVLSDVT 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 332 GNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDtlmQMVLHS--LPFG 409
Cdd:cd07104 328 PDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND---QTVNDEphVPFG 404
|
330 340
....*....|....*....|...
gi 26334245 410 GIGNSGIGKYHGTYSFETFSHSK 432
Cdd:cd07104 405 GVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
7-434 |
4.71e-65 |
|
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: 217.50 E-value: 4.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNV-TRSVDFRIRQLKQLRACIDDNYDQFL-------GALRedfrkpkfesVITELEFVKN---DIK 75
Cdd:cd07089 21 VDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRallvaevGAPV----------MTARAMQVDGpigHLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 76 YQLDHIHQYvkPQRVARPAANILDDAYIKW---DPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANV 152
Cdd:cd07089 91 YFADLADSF--PWEFDLPVPALRGGPGRRVvrrEPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 153 MASL-----LPKYLdkecYPVVTGGADVANQLL--QERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSP-LYIDD 224
Cdd:cd07089 169 LGEIiaetdLPAGV----VNVVTGSDNAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSAnIVLDD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 225 SVEGQLEVAAKRVLwgkLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSDS-FARIVNDRNFDRLEKLL 302
Cdd:cd07089 245 ADLAAAAPAAVGVC---MHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALpVGDPADPGTvMGPLISAAQRDRVEGYI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 303 SATK---GKVVVGG-QTAKGER--YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNK 376
Cdd:cd07089 322 ARGRdegARLVTGGgRPAGLDKgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSAD 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 26334245 377 QPTVNKFLDQTSCGSVCVNDTLMQMvlHSLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07089 402 VDRAYRVARRIRTGSVGINGGGGYG--PDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
2-435 |
8.11e-64 |
|
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: 214.11 E-value: 8.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 2 SSPVLIEKALIKAREAFA--RNVTRSVdfRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITELEFVkndikyqLD 79
Cdd:cd07092 16 ASAADVDAAVAAAHAAFPswRRTTPAE--RSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGA-------VD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 80 HIHQYVKPQRV--ARPAANILDD--AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMAS 155
Cdd:cd07092 87 NFRFFAGAARTleGPAAGEYLPGhtSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 156 LLPKYLDKECYPVVTGGADVANQLL--QERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVA 233
Cdd:cd07092 167 LAAEVLPPGVVNVVCGGGASAGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDAD--LDAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 234 AKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEA-SKKVLKDFYGDPAKSDS-FARIVNDRNFDRLEKLLSATKG--KV 309
Cdd:cd07092 245 VAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAAlVEAVSAIRVGDPDDEDTeMGPLNSAAQRERVAGFVERAPAhaRV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 310 VVGGQTAKGERY-IAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTS 388
Cdd:cd07092 325 LTGGRRAEGPGYfYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLD 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 26334245 389 CGSVCVNDTLmqMVLHSLPFGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07092 405 FGTVWVNTHI--PLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVM 449
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
107-434 |
1.40e-62 |
|
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: 210.65 E-value: 1.40e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASL-----LPKYLdkecYPVVTG-GADVANQLL 180
Cdd:cd07150 119 PLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEImeeagLPKGV----FNVVTGgGAEVGDELV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 181 Q-ERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYVLCSP 259
Cdd:cd07150 195 DdPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD--LDYAVRAAAFGAFMHQGQICMSASRIIVEE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 260 SVQDRFVEA-SKKVLKDFYGDPAKSDSF-ARIVNDRNFDRLEKLL--SATKGKVVVGGQTAKGERYiAPTLVANVTGNDS 335
Cdd:cd07150 273 PVYDEFVKKfVARASKLKVGDPRDPDTViGPLISPRQVERIKRQVedAVAKGAKLLTGGKYDGNFY-QPTVLTDVTPDMR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 336 LMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHsLPFGGIGNSG 415
Cdd:cd07150 352 IFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTILDEAH-VPFGGVKASG 430
|
330
....*....|....*....
gi 26334245 416 IGKYHGTYSFETFSHSKSV 434
Cdd:cd07150 431 FGREGGEWSMEEFTELKWI 449
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
66-434 |
5.10e-61 |
|
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: 206.71 E-value: 5.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 66 ELEFVKNDIKYQLDHIHQYVKPQRVARPAANildDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEV 145
Cdd:cd07102 78 EIRGMLERARYMISIAEEALADIRVPEKDGF---ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 146 AGSTANVMASLLPKY-LDKECYPVVTGGADVANQLLQE-RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYID 223
Cdd:cd07102 155 TPLCGERFAAAFAEAgLPEGVFQVLHLSHETSAALIADpRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 224 DSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDP-AKSDSFARIVNDRNFDRLEKL 301
Cdd:cd07102 235 PDAD--LDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPlDPSTTLGPVVSARAADFVRAQ 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 302 L--SATKG-KVVVGGQT----AKGERYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFS 374
Cdd:cd07102 313 IadAIAKGaRALIDGALfpedKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWT 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26334245 375 NKQPTVNKFLDQTSCGSVCVN--DTLMQmvlhSLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07102 393 KDIARAEALGEQLETGTVFMNrcDYLDP----ALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
101-434 |
4.93e-60 |
|
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: 204.32 E-value: 4.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASL-----LPKYLdkecYPVVTGGADV 175
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPPGV----VNVVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 176 ANQLLQE--RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPD 253
Cdd:cd07114 189 TGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDAD--LDAAVNGVVAGIFAAAGQTCVAGS 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 254 YVLCSPSVQDRFVEA-SKKVLKDFYGDPAKSDS-FARIVNDRNFDRLEKLLSATK---GKVVVGGQTAKGER-----YIA 323
Cdd:cd07114 267 RLLVQRSIYDEFVERlVARARAIRVGDPLDPETqMGPLATERQLEKVERYVARAReegARVLTGGERPSGADlgagyFFE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 324 PTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDtlMQMVL 403
Cdd:cd07114 347 PTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YRALS 424
|
330 340 350
....*....|....*....|....*....|.
gi 26334245 404 HSLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07114 425 PSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
7-434 |
6.18e-60 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 203.95 E-value: 6.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPkfesvITELefvkndikyqldhihqyvK 86
Cdd:cd07093 21 VDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKP-----ITLA------------------R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 87 PQRVARPAANI-----------------LDDA--YIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAG 147
Cdd:cd07093 78 TRDIPRAAANFrffadyilqldgesypqDGGAlnYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 148 STANVMASL-----LPKYLdkecYPVVTGGADVANQLLQE--RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPL 220
Cdd:cd07093 158 LTAWLLAELaneagLPPGV----VNVVHGFGPEAGAALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 221 YI-DDSvegQLEVAAKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASK---KVLKdfYGDPAKSDSF--ARIvndrN 294
Cdd:cd07093 234 IVfADA---DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVeraKALK--VGDPLDPDTEvgPLI----S 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 295 FDRLEKLLS------ATKGKVVVGGQTAKGER-----YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINR 363
Cdd:cd07093 305 KEHLEKVLGyvelarAEGATILTGGGRPELPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELAND 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26334245 364 GEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDtlmQMVLH-SLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07093 385 TPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNC---WLVRDlRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
101-435 |
1.89e-58 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 199.89 E-value: 1.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYPVVTGGADVANQLL 180
Cdd:cd07108 111 TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGYGEECGAAL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 181 QERFDL--VFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYI------DDSVEGQleVAAKRVlwgklTNSGQTCVAP 252
Cdd:cd07108 191 VDHPDVdkVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVfpdadlDDAVDGA--IAGMRF-----TRQGQSCTAG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 253 DYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSDS-FARIVNDRNFDR----LEKLLSATKGKVVVGGQTAKGER-----Y 321
Cdd:cd07108 264 SRLFVHEDIYDAFLEKLVAKLSKLkIGDPLDEATdIGAIISEKQFAKvcgyIDLGLSTSGATVLRGGPLPGEGPladgfF 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 322 IAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQM 401
Cdd:cd07108 344 VQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQ 423
|
330 340 350
....*....|....*....|....*....|....*...
gi 26334245 402 VlhSLPFGGIGNSGIGKyhgTYSFET----FSHSKSVL 435
Cdd:cd07108 424 P--GQSYGGFKQSGLGR---EASLEGmlehFTQKKTVN 456
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
101-434 |
2.22e-58 |
|
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: 200.13 E-value: 2.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLpkyldKEC-YP-----VVTGGAD 174
Cdd:cd07091 135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELI-----KEAgFPpgvvnIVPGFGP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 175 VANQLLQE--RFDLVFFTGSPNIGKLVYQAASK-HMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVA 251
Cdd:cd07091 210 TAGAAISShmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDAD--LDKAVEWAAFGIFFNQGQCCCA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 252 PDYVLCSPSVQDRFVEASKKVLKDFY-GDPAKSDSF-ARIVNDRNFDRLEKLLsaTKGK-----VVVGGQTAKGERY-IA 323
Cdd:cd07091 288 GSRIFVQESIYDEFVEKFKARAEKRVvGDPFDPDTFqGPQVSKAQFDKILSYI--ESGKkegatLLTGGERHGSKGYfIQ 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 324 PTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDtlMQMVL 403
Cdd:cd07091 366 PTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNT--YNVFD 443
|
330 340 350
....*....|....*....|....*....|.
gi 26334245 404 HSLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07091 444 AAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
7-435 |
2.45e-58 |
|
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: 200.26 E-value: 2.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITelefvknDIKYQLDHIHQYVK 86
Cdd:cd07559 40 VDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIRETLAA-------DIPLAIDHFRYFAG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 87 PQRVARPAANILDD---AYIKWDPLGVVLIFSAWNYPVqLMLA-PLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLD 162
Cdd:cd07559 113 VIRAQEGSLSEIDEdtlSYHFHEPLGVVGQIIPWNFPL-LMAAwKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 163 KECYPVVTG-GADVANQLL-QERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSP-LYIDD--SVEGQLEVAAKRV 237
Cdd:cd07559 192 KGVVNVVTGfGSEAGKPLAsHPRIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPnIFFDDamDADDDFDDKAEEG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 238 LWGKLTNSGQTCVAPDYVLCSPSVQDRFVE-ASKKVLKDFYGDPAKSDSF--ARIvndrNFDRLEKLLSATK------GK 308
Cdd:cd07559 272 QLGFAFNQGEVCTCPSRALVQESIYDEFIErAVERFEAIKVGNPLDPETMmgAQV----SKDQLEKILSYVDigkeegAE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 309 VVVGGQTAK-----GERYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKF 383
Cdd:cd07559 348 VLTGGERLTlggldKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRV 427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 26334245 384 LDQTSCGSVCVNdTLMQMVLHSlPFGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07559 428 ARGIQTGRVWVN-CYHQYPAHA-PFGGYKKSGIGRETHKMMLDHYQQTKNIL 477
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
92-434 |
5.33e-57 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 196.33 E-value: 5.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 92 RPAANIlddaYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVT 170
Cdd:cd07088 122 RPNENI----FIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVT 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 171 G-GADVANQLLQ-ERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDsvEGQLEVAAKRVLWGKLTNSGQT 248
Cdd:cd07088 198 GrGSVVGDALVAhPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMK--DADLDLAVKAIVDSRIINCGQV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 249 CVAPDYVLCSPSVQD----RFVEASKKVLkdfYGDPAKSDSF-ARIVNDRNFDRLEKLLSATK---GKVVVGGQTAKGER 320
Cdd:cd07088 276 CTCAERVYVHEDIYDefmeKLVEKMKAVK---VGDPFDAATDmGPLVNEAALDKVEEMVERAVeagATLLTGGKRPEGEK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 321 --YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDT- 397
Cdd:cd07088 353 gyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINREn 432
|
330 340 350
....*....|....*....|....*....|....*....
gi 26334245 398 --LMQMvLHSlpfgGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07088 433 feAMQG-FHA----GWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
101-434 |
1.21e-56 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 195.70 E-value: 1.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLpkyldKEC-YP-----VVTGGAD 174
Cdd:cd07144 138 AYTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLV-----KEAgFPpgvvnIIPGYGA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 175 VANQLLQERFDL--VFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAP 252
Cdd:cd07144 213 VAGSALAEHPDVdkIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDAD--LDQAVKWAAAGIMYNSGQNCTAT 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 253 DYVLCSPSVQDRFVEASKKVLKDFY--GDPAKSDSF-ARIVNDRNFDRLEKLLSATK--GKVVVGGQTAKGER-----YI 322
Cdd:cd07144 291 SRIYVQESIYDKFVEKFVEHVKQNYkvGSPFDDDTVvGPQVSKTQYDRVLSYIEKGKkeGAKLVYGGEKAPEGlgkgyFI 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 323 APTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMV 402
Cdd:cd07144 371 PPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDV 450
|
330 340 350
....*....|....*....|....*....|..
gi 26334245 403 lhSLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07144 451 --GVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
7-434 |
1.44e-56 |
|
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: 194.67 E-value: 1.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVItELEFvkndIKYQLDHIHQYVK 86
Cdd:cd07106 21 LDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-EVGG----AVAWLRYTASLDL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 87 PQRVARpaanilDDA----YIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLD 162
Cdd:cd07106 96 PDEVIE------DDDtrrvELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 163 KECYPVVTGGADVaNQLLQE--RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWG 240
Cdd:cd07106 170 PGVLNVVSGGDEL-GPALTShpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVD--IDAVAPKLFWG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 241 KLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDFY-GDPAKSDS-FARIVNDRNFDRLEKLLSATK---GKVVVGGQT 315
Cdd:cd07106 247 AFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVvGDGLDPGTtLGPVQNKMQYDKVKELVEDAKakgAKVLAGGEP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 316 AKGERY-IAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCV 394
Cdd:cd07106 327 LDGPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWI 406
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 26334245 395 NDtlMQMVLHSLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07106 407 NT--HGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
106-434 |
2.88e-56 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 194.09 E-value: 2.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 106 DPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGADVANQLLQE-- 182
Cdd:cd07118 118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATVGQAMTEhp 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 183 RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIddSVEGQLEVAAKRVLWGKLTNSGQTCVAPDYVLCSPSVQ 262
Cdd:cd07118 198 DVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIV--FADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIA 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 263 DRFVEASKKVLKDF-YGDPAKSDS-FARIVNDRNFDRLEKLLSATKG---KVVVGGQTAKGE--RYIAPTLVANVTGNDS 335
Cdd:cd07118 276 DAFVAAVVARSRKVrVGDPLDPETkVGAIINEAQLAKITDYVDAGRAegaTLLLGGERLASAagLFYQPTIFTDVTPDMA 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 336 LMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVlhSLPFGGIGNSG 415
Cdd:cd07118 356 IAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSP--ELPFGGFKQSG 433
|
330
....*....|....*....
gi 26334245 416 IGKYHGTYSFETFSHSKSV 434
Cdd:cd07118 434 IGRELGRYGVEEYTELKTV 452
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
107-432 |
3.33e-56 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 193.66 E-value: 3.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKP---SEVAGSTanVMASL-----LPKYLdkecYPVVTGGADVANQ 178
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPdprTPVSGGV--VIARLfeeagLPAGV----LHVLPGGADAGEA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 179 LLQE-RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYI-DDSvegQLEVAAKRVLWGKLTNSGQTCVAPDYVL 256
Cdd:cd07152 184 LVEDpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVlDDA---DLDLAASNGAWGAFLHQGQICMAAGRHL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 257 CSPSVQDRFVEA-SKKVLKDFYGDPAKSD-SFARIVNDRNFDRLEKLLSAT--KGKVVVGGQTAKGeRYIAPTLVANVTG 332
Cdd:cd07152 261 VHESVADAYTAKlAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIVDDSvaAGARLEAGGTYDG-LFYRPTVLSGVKP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 333 NDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDtlmQMVLHS--LPFGG 410
Cdd:cd07152 340 GMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHIND---QTVNDEphNPFGG 416
|
330 340
....*....|....*....|...
gi 26334245 411 IGNSGIGKYHG-TYSFETFSHSK 432
Cdd:cd07152 417 MGASGNGSRFGgPANWEEFTQWQ 439
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
7-434 |
3.58e-56 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 193.99 E-value: 3.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDF-RIRQLKQLRACIDDNYDQFLGALREDFRKP------KFESVITELEFVKNdikyQLD 79
Cdd:cd07109 21 VDRAVQAARRAFESGWLRLSPAeRGRLLLRIARLIREHADELARLESLDTGKPltqaraDVEAAARYFEYYGG----AAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 80 HIHQYVKPqrvarPAANILDdaYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPK 159
Cdd:cd07109 97 KLHGETIP-----LGPGYFV--YTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 160 Y-LDKECYPVVTG-GADVANQLLQER-FDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYI-DDSvegQLEVAAK 235
Cdd:cd07109 170 AgLPAGALNVVTGlGAEAGAALVAHPgVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVfADA---DLEAALP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 236 RVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDFYGDPAKSD-SFARIVNDRNFDRLEKLLS---ATKGKVVV 311
Cdd:cd07109 247 VVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDpDLGPLISAKQLDRVEGFVArarARGARIVA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 312 GGQTAKGER----YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQT 387
Cdd:cd07109 327 GGRIAEGAPaggyFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRL 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 26334245 388 SCGSVCVNDTL----MQmvlhsLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07109 407 RAGQVFVNNYGagggIE-----LPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
8-435 |
4.12e-56 |
|
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: 193.87 E-value: 4.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 8 EKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPkfesvitelefVKNDIKYQLDHihqyvkP 87
Cdd:cd07138 39 DRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAP-----------ITLARAAQVGL------G 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 88 QRVARPAANILDD---------AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLlp 158
Cdd:cd07138 102 IGHLRAAADALKDfefeerrgnSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEI-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 159 kyLDKECYP-----VVTG-GADVANQLL-QERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLE 231
Cdd:cd07138 180 --LDEAGLPagvfnLVNGdGPVVGEALSaHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDAD--LE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 232 VAAKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSDSF-ARIVNDRNFDRLEKLLSatKG-- 307
Cdd:cd07138 256 KAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYvVGDPRDPATTlGPLASAAQFDRVQGYIQ--KGie 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 308 ---KVVVGGqTAKGER-----YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPT 379
Cdd:cd07138 334 egaRLVAGG-PGRPEGlergyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPER 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 26334245 380 VNKFLDQTSCGSVCVNDTLMQMvlhSLPFGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07138 413 ARAVARRLRAGQVHINGAAFNP---GAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
107-434 |
5.17e-56 |
|
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: 192.79 E-value: 5.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVT----GGADVANQLLQ 181
Cdd:cd07105 98 PVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLNVVThspeDAPEVVEALIA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 182 E---RFdlVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYVLCS 258
Cdd:cd07105 178 HpavRK--VNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDAD--LDAAANAALFGAFLNSGQICMSTERIIVH 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 259 PSVQDRFVEASKKVLKDFYGDPAKSDSfarIVNDRNFDRLEKLLSA--TKG-KVVVGGQTAKGER--YIAPTLVANVTGN 333
Cdd:cd07105 254 ESIADEFVEKLKAAAEKLFAGPVVLGS---LVSAAAADRVKELVDDalSKGaKLVVGGLADESPSgtSMPPTILDNVTPD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 334 DSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKqptVNKFL---DQTSCGSVCVNdtlmQMVLH---SLP 407
Cdd:cd07105 331 MDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRD---LARALavaKRIESGAVHIN----GMTVHdepTLP 403
|
330 340
....*....|....*....|....*..
gi 26334245 408 FGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07105 404 HGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
7-435 |
1.14e-55 |
|
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: 192.57 E-value: 1.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFES------VITELEFVKnDIKYQLDh 80
Cdd:cd07110 21 VDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAawdvddVAGCFEYYA-DLAEQLD- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 81 ihQYvKPQRVARPAANIldDAYIKWDPLGVVLIFSAWNYPVqLMLA-PLAGAIAAGNCVVIKPSEVAGSTANVMASLlpk 159
Cdd:cd07110 99 --AK-AERAVPLPSEDF--KARVRREPVGVVGLITPWNFPL-LMAAwKVAPALAAGCTVVLKPSELTSLTELELAEI--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 160 yLDKECYP-----VVTGGADVANQLLQE--RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEV 232
Cdd:cd07110 170 -AAEAGLPpgvlnVVTGTGDEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDAD--LEK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 233 AAKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDP-AKSDSFARIVNDRNFDRLEKLLS---ATKG 307
Cdd:cd07110 247 AVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIrVGDPlEEGVRLGPLVSQAQYEKVLSFIArgkEEGA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 308 KVVVGGQTAKGER---YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFL 384
Cdd:cd07110 327 RLLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVA 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 26334245 385 DQTSCGSVCVNDTlmQMVLHSLPFGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07110 407 EALEAGIVWINCS--QPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
102-434 |
3.29e-54 |
|
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: 188.80 E-value: 3.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 102 YIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGADVANQLL 180
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 181 QERFDL--VFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDsvEGQLEVAAKRVLWGKLTNSGQTCVAPDYVLCS 258
Cdd:cd07115 192 VEHPDVdkITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFA--DADLDAAVRAAATGIFYNQGQMCTAGSRLLVH 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 259 PSVQDRFVEASKKVLKDF-YGDPA-KSDSFARIVNDRNFDRLEKL--LSATKGKVVVGGQTAKGER--YIAPTLVANVTG 332
Cdd:cd07115 270 ESIYDEFLERFTSLARSLrPGDPLdPKTQMGPLVSQAQFDRVLDYvdVGREEGARLLTGGKRPGARgfFVEPTIFAAVPP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 333 NDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNdtLMQMVLHSLPFGGIG 412
Cdd:cd07115 350 EMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYK 427
|
330 340
....*....|....*....|..
gi 26334245 413 NSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07115 428 QSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
101-434 |
5.60e-54 |
|
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: 187.95 E-value: 5.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGG-ADVANQ 178
Cdd:cd07146 114 IFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEpGEIGDE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 179 LLQ-ERFDLVFFTGSPNIGKLVyqAASKHMTPVVLELGGKSPLYIDDsvEGQLEVAAKRVLWGKLTNSGQTCVAPDYVLC 257
Cdd:cd07146 194 LIThPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMD--DADLERAATLAVAGSYANSGQRCTAVKRILV 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 258 SPSVQDRF----VEASKKVLkdfYGDPAKSDSF-ARIVNDRNFDRLEKLLS---ATKGKVVVGGQTaKGERYiAPTLVAN 329
Cdd:cd07146 270 HESVADEFvdllVEKSAALV---VGDPMDPATDmGTVIDEEAAIQIENRVEeaiAQGARVLLGNQR-QGALY-APTVLDH 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 330 VTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDtLMQMVLHSLPFG 409
Cdd:cd07146 345 VPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNE-VPGFRSELSPFG 423
|
330 340
....*....|....*....|....*.
gi 26334245 410 GIGNSGIGKYHG-TYSFETFSHSKSV 434
Cdd:cd07146 424 GVKDSGLGGKEGvREAMKEMTNVKTY 449
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
101-432 |
7.05e-54 |
|
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: 187.94 E-value: 7.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGAD-VANQ 178
Cdd:cd07145 117 AFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSeVGDE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 179 LLQ-ERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYI-DDSvegQLEVAAKRVLWGKLTNSGQTCVAPDYVL 256
Cdd:cd07145 197 IVTnPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVlKDA---DLERAVSIAVRGRFENAGQVCNAVKRIL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 257 CSPSVQDRFVEA-SKKVLKDFYGDPAKSDS-FARIVNDRNFDRLEKLL--SATKG-KVVVGGQTAKGErYIAPTLVANVT 331
Cdd:cd07145 274 VEEEVYDKFLKLlVEKVKKLKVGDPLDESTdLGPLISPEAVERMENLVndAVEKGgKILYGGKRDEGS-FFPPTVLENDT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 332 GNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTlMQMVLHSLPFGGI 411
Cdd:cd07145 353 PDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDS-TRFRWDNLPFGGF 431
|
330 340
....*....|....*....|.
gi 26334245 412 GNSGIGKYHGTYSFETFSHSK 432
Cdd:cd07145 432 KKSGIGREGVRYTMLEMTEEK 452
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
100-434 |
1.02e-53 |
|
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: 187.77 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 100 DAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYP-----VVTGGAD 174
Cdd:cd07086 126 RLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGLPpgvvnLVTGGGD 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 175 VANQLLQ-ERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPD 253
Cdd:cd07086 206 GGELLVHdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDAD--LDLAVRAVLFAAVGTAGQRCTTTR 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 254 YVLCSPSVQDRFVEAskkvLKDFY-----GDPAKSDSFA-RIVNDRNFDRLEKLLSATK---GKVVVGGQTAKGER---Y 321
Cdd:cd07086 284 RLIVHESVYDEFLER----LVKAYkqvriGDPLDEGTLVgPLINQAAVEKYLNAIEIAKsqgGTVLTGGKRIDGGEpgnY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 322 IAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQT--SCGSVCVNDTLM 399
Cdd:cd07086 360 VEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVNIPTS 439
|
330 340 350
....*....|....*....|....*....|....*
gi 26334245 400 QMVLHsLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07086 440 GAEIG-GAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
106-434 |
1.07e-53 |
|
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: 187.51 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 106 DPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPsevAGSTANVMASLLPKYLDKECYP------VVTGGADVANQL 179
Cdd:cd07151 129 EPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKP---ASDTPITGGLLLAKIFEEAGLPkgvlnvVVGAGSEIGDAF 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 180 LQERF-DLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYI-DDSvegQLEVAAKRVLWGKLTNSGQTCVAPDYVLC 257
Cdd:cd07151 206 VEHPVpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVlEDA---DIDAAVNAAVFGKFLHQGQICMAINRIIV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 258 SPSVQDRFVEA-SKKVLKDFYGDPAKSDS-FARIVNDRNFDRLEKLLSATK--GKVVVGGQTAKGeRYIAPTLVANVTGN 333
Cdd:cd07151 283 HEDVYDEFVEKfVERVKALPYGDPSDPDTvVGPLINESQVDGLLDKIEQAVeeGATLLVGGEAEG-NVLEPTVLSDVTND 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 334 DSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHsLPFGGIGN 413
Cdd:cd07151 362 MEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPH-VPFGGEKN 440
|
330 340
....*....|....*....|.
gi 26334245 414 SGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07151 441 SGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
7-434 |
1.23e-53 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 187.42 E-value: 1.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVD--FRIRQLKQLRACIDDNYDQFlgALRE--DFRKPKFESVITELEFVKNDIKYQ---LD 79
Cdd:cd07112 26 VDRAVAAARRAFESGVWSRLSpaERKAVLLRLADLIEAHRDEL--ALLEtlDMGKPISDALAVDVPSAANTFRWYaeaID 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 80 HIHQYVKPQrvarpAANILddAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASL--- 156
Cdd:cd07112 104 KVYGEVAPT-----GPDAL--ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELale 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 157 --LPKYLdkecYPVVTGGADVANQLL--QERFDLVFFTGSPNIGK--LVYQAASkHMTPVVLELGGKSPLYIDDSVEgQL 230
Cdd:cd07112 177 agLPAGV----LNVVPGFGHTAGEALglHMDVDALAFTGSTEVGRrfLEYSGQS-NLKRVWLECGGKSPNIVFADAP-DL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 231 EVAAKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDFY-GDPAKSDSFA-RIVNDRNFDRLEKLLS---AT 305
Cdd:cd07112 251 DAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKpGDPLDPATRMgALVSEAHFDKVLGYIEsgkAE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 306 KGKVVVGGQTAKGER---YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNK 382
Cdd:cd07112 331 GARLVAGGKRVLTETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHR 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 26334245 383 FLDQTSCGSVCVN--DTLMQMVlhslPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07112 411 VARRLRAGTVWVNcfDEGDITT----PFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
7-434 |
1.26e-53 |
|
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: 186.51 E-value: 1.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESvITELEFVKNDIKYQLDHIHQYVK 86
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYAENAEAFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 87 PQRVARPAANilddAYIKWDPLGVVLIFSAWNYPV-QLM--LAPlagAIAAGNCVVIKPSE-VAGStANVMASLLPKY-L 161
Cdd:cd07100 80 DEPIETDAGK----AYVRYEPLGVVLGIMPWNFPFwQVFrfAAP---NLMAGNTVLLKHASnVPGC-ALAIEELFREAgF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 162 DKECYPVVTGGADVANQLLQ-ERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPlYI--DDSvegQLEVAAKRVL 238
Cdd:cd07100 152 PEGVFQNLLIDSDQVEAIIAdPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDP-FIvlDDA---DLDKAVKTAV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 239 WGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSDSF--------ARivndrnfDRLEKLLSAT--KG 307
Cdd:cd07100 228 KGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALkVGDPMDEDTDlgplarkdLR-------DELHEQVEEAvaAG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 308 -KVVVGGQTAKGER-YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLD 385
Cdd:cd07100 301 aTLLLGGKRPDGPGaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVAR 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 26334245 386 QTSCGSVCVNdtlmQMVLHS--LPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07100 381 RLEAGMVFIN----GMVKSDprLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
7-418 |
5.94e-53 |
|
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: 185.74 E-value: 5.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFlgALRE--DFRKPkfesvITELEFVknDIKYQLDHIHQY 84
Cdd:cd07117 40 VDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL--AMVEtlDNGKP-----IRETRAV--DIPLAADHFRYF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 85 VKPQRVARPAANILDD---AYIKWDPLGVVLIFSAWNYPVqLMLA-PLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY 160
Cdd:cd07117 111 AGVIRAEEGSANMIDEdtlSIVLREPIGVVGQIIPWNFPF-LMAAwKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 161 LDKECYPVVTG-GADVANQLLQER-FDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSP--LYIDDSVEGQLEVAAKR 236
Cdd:cd07117 190 LPKGVVNIVTGkGSKSGEYLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSAniIFDDANWDKALEGAQLG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 237 VLWgkltNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSDS-FARIVNDRNFDRLEKLLSATK---GKVVV 311
Cdd:cd07117 270 ILF----NQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVkVGNPLDPDTqMGAQVNKDQLDKILSYVDIAKeegAKILT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 312 GGQ------TAKGErYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKqptVNKFLD 385
Cdd:cd07117 346 GGHrltengLDKGF-FIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKD---INRALR 421
|
410 420 430
....*....|....*....|....*....|....*.
gi 26334245 386 ---QTSCGSVCVNdTLMQMVLHSlPFGGIGNSGIGK 418
Cdd:cd07117 422 varAVETGRVWVN-TYNQIPAGA-PFGGYKKSGIGR 455
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
101-434 |
2.19e-52 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 183.57 E-value: 2.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPK-YLDKECYPVVTGGAD-VANQ 178
Cdd:cd07149 117 GFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEaGLPKGALNVVTGSGEtVGDA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 179 LLQ-ERFDLVFFTGSPNIGKLVYQAASkhMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYVLC 257
Cdd:cd07149 197 LVTdPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADAD--LEKAVERCVSGAFANAGQVCISVQRIFV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 258 SPSVQD----RFVEASKKvLKdfYGDPAKSDSF-ARIVNDRNFDRLEKLLS-ATKG--KVVVGGQtaKGERYIAPTLVAN 329
Cdd:cd07149 273 HEDIYDefleRFVAATKK-LV--VGDPLDEDTDvGPMISEAEAERIEEWVEeAVEGgaRLLTGGK--RDGAILEPTVLTD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 330 VTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHsLPFG 409
Cdd:cd07149 348 VPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDSSTFRVDH-MPYG 426
|
330 340
....*....|....*....|....*
gi 26334245 410 GIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07149 427 GVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
101-434 |
2.37e-52 |
|
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: 184.27 E-value: 2.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVqLMLA-PLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGADVANQ 178
Cdd:cd07143 138 TYTRHEPIGVCGQIIPWNFPL-LMCAwKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGN 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 179 LLQERFDL--VFFTGSPNIGKLVYQAASK-HMTPVVLELGGKSPLYIDDsvEGQLEVAAKRVLWGKLTNSGQTCVAPDYV 255
Cdd:cd07143 217 AISSHMDIdkVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFD--DADLESAVVWTAYGIFFNHGQVCCAGSRI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 256 LCSPSVQDRFVEASK-KVLKDFYGDPAKSDSF-ARIVNDRNFDRLEKLLSATK---GKVVVGGQTAKGERY-IAPTLVAN 329
Cdd:cd07143 295 YVQEGIYDKFVKRFKeKAKKLKVGDPFAEDTFqGPQVSQIQYERIMSYIESGKaegATVETGGKRHGNEGYfIEPTIFTD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 330 VTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDtlMQMVLHSLPFG 409
Cdd:cd07143 375 VTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNC--YNLLHHQVPFG 452
|
330 340
....*....|....*....|....*
gi 26334245 410 GIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07143 453 GYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
101-434 |
2.54e-52 |
|
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: 183.66 E-value: 2.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGADVAnQL 179
Cdd:cd07090 110 AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGGGETG-QL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 180 LQERFDL--VFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYI-DDSvegQLEVAAKRVLWGKLTNSGQTCVAPDYVL 256
Cdd:cd07090 189 LCEHPDVakVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIfDDA---DLENAVNGAMMANFLSQGQVCSNGTRVF 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 257 CSPSVQDRFVEA-SKKVLKDFYGDPAKSDS-FARIVNDRNFDRLEKLLSATK---GKVVVGGQTAKGER------YIAPT 325
Cdd:cd07090 266 VQRSIKDEFTERlVERTKKIRIGDPLDEDTqMGALISEEHLEKVLGYIESAKqegAKVLCGGERVVPEDglengfYVSPC 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 326 LVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLhs 405
Cdd:cd07090 346 VLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVE-- 423
|
330 340
....*....|....*....|....*....
gi 26334245 406 LPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07090 424 VPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
92-434 |
1.59e-51 |
|
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: 182.06 E-value: 1.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 92 RPAANIlddaYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVT 170
Cdd:cd07097 124 RPGVEV----ETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVM 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 171 G-GADVANQLLQ-ERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSveGQLEVAAKRVLWGKLTNSGQT 248
Cdd:cd07097 200 GsGSEVGQALVEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDD--ADLDLAVECAVQGAFFSTGQR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 249 CVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSDS-FARIVNDRNFDRLEKLLSATK---GKVVVGGQTAKGER--- 320
Cdd:cd07097 278 CTASSRLIVTEGIHDRFVEALVERTKALkVGDALDEGVdIGPVVSERQLEKDLRYIEIARsegAKLVYGGERLKRPDegy 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 321 YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQ 400
Cdd:cd07097 358 YLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAG 437
|
330 340 350
....*....|....*....|....*....|....*
gi 26334245 401 MVLHsLPFGGIGNSGIG-KYHGTYSFETFSHSKSV 434
Cdd:cd07097 438 VDYH-VPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
102-437 |
2.81e-51 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 181.26 E-value: 2.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 102 YIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLpkyldKECYP-----VVTG-GADV 175
Cdd:PRK13473 133 MIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELA-----ADILPpgvlnVVTGrGATV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 176 ANQLL-QERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDY 254
Cdd:PRK13473 208 GDALVgHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDAD--LDAVVEGIRTFGYYNAGQDCTAACR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 255 VLCSPSVQDRFVEA-SKKVLKDFYGDPAKSDS-FARIVNDRNFDRLEKLLSATKG----KVVVGGQTAKGE-RYIAPTLV 327
Cdd:PRK13473 286 IYAQRGIYDDLVAKlAAAVATLKVGDPDDEDTeLGPLISAAHRDRVAGFVERAKAlghiRVVTGGEAPDGKgYYYEPTLL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 328 ANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSN---KQPTVNKFLDqtsCGSVCVNDTLmqMVLH 404
Cdd:PRK13473 366 AGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRdvgRAHRVSARLQ---YGCTWVNTHF--MLVS 440
|
330 340 350
....*....|....*....|....*....|...
gi 26334245 405 SLPFGGIGNSGIGKYHGTYSFETFSHSKSVLAK 437
Cdd:PRK13473 441 EMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVK 473
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
100-434 |
4.16e-51 |
|
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: 181.01 E-value: 4.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 100 DAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGADVANQ 178
Cdd:cd07131 128 DAMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 179 LLQE--RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDsvEGQLEVAAKRVLWGKLTNSGQTCVAPDYVL 256
Cdd:cd07131 208 ALVEhpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMD--DADLDLALEGALWSAFGTTGQRCTATSRLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 257 CSPSVQD----RFVEASKKVLkdfYGDPAKSDSFA----------RIVNDRNFDRLEKLLSATKGKVVVGGQTAKGeRYI 322
Cdd:cd07131 286 VHESVYDeflkRFVERAKRLR---VGDGLDEETDMgplineaqleKVLNYNEIGKEEGATLLLGGERLTGGGYEKG-YFV 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 323 APTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMV 402
Cdd:cd07131 362 EPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIGAE 441
|
330 340 350
....*....|....*....|....*....|...
gi 26334245 403 LHsLPFGGIGNSGIG-KYHGTYSFETFSHSKSV 434
Cdd:cd07131 442 VH-LPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
107-434 |
6.93e-51 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 180.66 E-value: 6.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLpkyLDKECYP----VVTGGA-DVANQLLQ 181
Cdd:PLN02278 160 PVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELA---LQAGIPPgvlnVVMGDApEIGDALLA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 182 ErfDLV---FFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYI-DDSvegQLEVAAKRVLWGKLTNSGQTCVAPDYVLC 257
Cdd:PLN02278 237 S--PKVrkiTFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVfDDA---DLDVAVKGALASKFRNSGQTCVCANRILV 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 258 SPSVQDRFVEA-SKKVLKDFYGDPAKSD-SFARIVNDRNFDRLEKLL--SATKG-KVVVGGQTAK-GERYIAPTLVANVT 331
Cdd:PLN02278 312 QEGIYDKFAEAfSKAVQKLVVGDGFEEGvTQGPLINEAAVQKVESHVqdAVSKGaKVLLGGKRHSlGGTFYEPTVLGDVT 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 332 GNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVlhSLPFGGI 411
Cdd:PLN02278 392 EDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTE--VAPFGGV 469
|
330 340
....*....|....*....|...
gi 26334245 412 GNSGIGKYHGTYSFETFSHSKSV 434
Cdd:PLN02278 470 KQSGLGREGSKYGIDEYLEIKYV 492
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
7-434 |
8.56e-50 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 178.00 E-value: 8.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTR-----SVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESViTELEFVKNDIKYQLDHI 81
Cdd:PLN02467 47 VDAAVEAARKAFKRNKGKdwartTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAA-WDMDDVAGCFEYYADLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 82 HQYVKPQR--VARPAANIldDAYIKWDPLGVVLIFSAWNYPVqLMLA-PLAGAIAAGNCVVIKPSEVAGSTANVMAS--- 155
Cdd:PLN02467 126 EALDAKQKapVSLPMETF--KGYVLKEPLGVVGLITPWNYPL-LMATwKVAPALAAGCTAVLKPSELASVTCLELADicr 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 156 ---LLPKYLDkecypVVTG-----GADVANqllQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVE 227
Cdd:PLN02467 203 evgLPPGVLN-----VVTGlgteaGAPLAS---HPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 228 gqLEVAAKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSD-SFARIVNDRNFDRLEKLLSAT 305
Cdd:PLN02467 275 --LDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIkISDPLEEGcRLGPVVSEGQYEKVLKFISTA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 306 KGK---VVVGGQTAKGER---YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPT 379
Cdd:PLN02467 353 KSEgatILCGGKRPEHLKkgfFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLER 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 26334245 380 VNKFLDQTSCGSVCVNDTlmQMVLHSLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:PLN02467 433 CERVSEAFQAGIVWINCS--QPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
1-434 |
1.06e-49 |
|
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: 177.80 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 1 MSSPVLIEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDnydqflgalredfRKPKFESVITeLEFVKN------DI 74
Cdd:cd07124 65 KATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRR-------------RRFELAAWMV-LEVGKNwaeadaDV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 75 KYQLDHIHQYV------KPQRVARPAANilDDAYIkWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAG- 147
Cdd:cd07124 131 AEAIDFLEYYAremlrlRGFPVEMVPGE--DNRYV-YRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPv 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 148 STANVMASLLPKYLDKECYPVVTG-GADVANQLLQE-RFDLVFFTGSPNIGKLVYQAASK------HMTPVVLELGGKSP 219
Cdd:cd07124 208 IAAKLVEILEEAGLPPGVVNFLPGpGEEVGDYLVEHpDVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 220 LYIDDsvEGQLEVAAKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSDSF-ARIVNDRNFDR 297
Cdd:cd07124 288 IIVDE--DADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALkVGDPEDPEVYmGPVIDKGARDR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 298 LEKLLSATK--GKVVVGGQTAKGER---YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYI 372
Cdd:cd07124 366 IRRYIEIGKseGRLLLGGEVLELAAegyFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGV 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26334245 373 FSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHSLPFGGIGNSGIG-KYHGTYSFETFSHSKSV 434
Cdd:cd07124 446 FSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGFKMSGTGsKAGGPDYLLQFMQPKTV 508
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
101-435 |
1.58e-49 |
|
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: 176.73 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVqLMLA-PLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGADVANQ 178
Cdd:cd07119 128 SRTVREPVGVCGLITPWNYPL-LQAAwKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 179 LLQE--RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYVL 256
Cdd:cd07119 207 ELAEspDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADAD--FETAVDQALNGVFFNAGQVCSAGSRLL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 257 CSPSVQDRFVEA-SKKVLKDFYGDPAKSDS-FARIVNDRNFDRLEKLLSATKG---KVVVGGQT------AKGeRYIAPT 325
Cdd:cd07119 285 VEESIHDKFVAAlAERAKKIKLGNGLDADTeMGPLVSAEHREKVLSYIQLGKEegaRLVCGGKRptgdelAKG-YFVEPT 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 326 LVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDtlMQMVLHS 405
Cdd:cd07119 364 IFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAE 441
|
330 340 350
....*....|....*....|....*....|
gi 26334245 406 LPFGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07119 442 APWGGYKQSGIGRELGPTGLEEYQETKHIN 471
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
92-435 |
6.52e-49 |
|
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: 174.69 E-value: 6.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 92 RPAANiLDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASL-----LPKYLdkecY 166
Cdd:cd07139 123 RPGSG-GGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAaeeagLPPGV----V 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 167 PVVTGGADVANQL-LQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNS 245
Cdd:cd07139 198 NVVPADREVGEYLvRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDAD--LDAAVPGLVPASLMNN 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 246 GQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSDSF-ARIVNDRNFDRLEKLLSATK---GKVVVGGQTAKG-E 319
Cdd:cd07139 276 GQVCVALTRILVPRSRYDEVVEALAAAVAALkVGDPLDPATQiGPLASARQRERVEGYIAKGRaegARLVTGGGRPAGlD 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 320 R--YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDT 397
Cdd:cd07139 356 RgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF 435
|
330 340 350
....*....|....*....|....*....|....*...
gi 26334245 398 LMQMvlhSLPFGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07139 436 RLDF---GAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
92-434 |
1.18e-48 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 172.61 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 92 RPAANILddayIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVT 170
Cdd:PRK10090 60 RPGENIL----LFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 171 G-GADVANQLL-QERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSP-LYIDDSvegQLEVAAKRVLWGKLTNSGQ 247
Cdd:PRK10090 136 GrGETVGQELAgNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPaIVMDDA---DLDLAVKAIVDSRVINSGQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 248 TCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAKSDSFAR--IVNDRNFDRLEKLL-SATK--GKVVVGGQTAKGERY 321
Cdd:PRK10090 213 VCNCAERVYVQKGIYDQFVNRLGEAMQAVqFGNPAERNDIAMgpLINAAALERVEQKVaRAVEegARVALGGKAVEGKGY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 322 I-APTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVND---T 397
Cdd:PRK10090 293 YyPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRenfE 372
|
330 340 350
....*....|....*....|....*....|....*..
gi 26334245 398 LMQMvLHSlpfgGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:PRK10090 373 AMQG-FHA----GWRKSGIGGADGKHGLHEYLQTQVV 404
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
7-437 |
1.37e-48 |
|
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: 174.07 E-value: 1.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFAR-NVTRSVDF--RIRQLKQLRACIDDNYdQFLGALRE-DFRKPKFESVITELEFVKNDIKY---QLD 79
Cdd:cd07141 46 VDKAVKAARAAFKLgSPWRTMDAseRGRLLNKLADLIERDR-AYLASLETlDNGKPFSKSYLVDLPGAIKVLRYyagWAD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 80 HIHQYVKPqrvarpaaniLDD---AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASL 156
Cdd:cd07141 125 KIHGKTIP----------MDGdffTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 157 LpkyldKEC-YP-----VVTGGADVANQLLQERFDL--VFFTGSPNIGKLVYQAASK-HMTPVVLELGGKSPLYIDDSVE 227
Cdd:cd07141 195 I-----KEAgFPpgvvnVVPGYGPTAGAAISSHPDIdkVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADAD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 228 gqLEVAAKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVE-----ASKKVLkdfyGDPAKSDS-FARIVNDRNFDRLEKL 301
Cdd:cd07141 270 --LDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKrsverAKKRVV----GNPFDPKTeQGPQIDEEQFKKILEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 302 LSATK---GKVVVGGQtAKGER--YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNK 376
Cdd:cd07141 344 IESGKkegAKLECGGK-RHGDKgyFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKD 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26334245 377 QPTVNKFLDQTSCGSVCVNdtLMQMVLHSLPFGGIGNSGIGKYHGTYSFETFSHSKSVLAK 437
Cdd:cd07141 423 IDKAITFSNALRAGTVWVN--CYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
7-437 |
1.71e-48 |
|
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: 173.53 E-value: 1.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAF-ARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESViTElefVKNDIKYQLDHIHQYV 85
Cdd:cd07082 40 ILEAAETAYDAGrGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL-KE---VDRTIDYIRDTIEELK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 86 KPQRVARP------AANILddAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSeVAGStanVMASLLPK 159
Cdd:cd07082 116 RLDGDSLPgdwfpgTKGKI--AQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPA-TQGV---LLGIPLAE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 160 YLDKECYP-----VVTG-GADVANQLLQ-ERFDLVFFTGSPNIGKLVYQAASkhMTPVVLELGGKSP-LYIDDSvegQLE 231
Cdd:cd07082 190 AFHDAGFPkgvvnVVTGrGREIGDPLVThGRIDVISFTGSTEVGNRLKKQHP--MKRLVLELGGKDPaIVLPDA---DLE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 232 VAAKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEA-SKKVLKDFYGDPakSDSFARI---VNDRNFDRLEKLL--SAT 305
Cdd:cd07082 265 LAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELlKEEVAKLKVGMP--WDNGVDItplIDPKSADFVEGLIddAVA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 306 KGKVVVGGQTAKGERYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLD 385
Cdd:cd07082 343 KGATVLNGGGREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLAD 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 26334245 386 QTSCGSVCVNDTlMQMVLHSLPFGGIGNSGIGKYHGTYSFETFSHSKSVLAK 437
Cdd:cd07082 423 ALEVGTVNINSK-CQRGPDHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
101-435 |
2.71e-48 |
|
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: 173.40 E-value: 2.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLpkyldKEC-YP-----VVTGGAD 174
Cdd:cd07113 136 AFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELA-----KEAgIPdgvlnVVNGKGA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 175 VANQLLQE-RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSP------LYIDDSVEGQLEvaakrvlwGKLTNSGQ 247
Cdd:cd07113 211 VGAQLISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAaaflkdADIDWVVEGLLT--------AGFLHQGQ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 248 TCVAPDYVLCSPSVQDRFVEASKKVLKDFYGDPAKSDS--FARIVNDRNFDRLEKLLS---ATKGKVVVGGQTAKGERY- 321
Cdd:cd07113 283 VCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESvmFGPLANQPHFDKVCSYLDdarAEGDEIVRGGEALAGEGYf 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 322 IAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNdtlMQM 401
Cdd:cd07113 363 VQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHT 439
|
330 340 350
....*....|....*....|....*....|....*
gi 26334245 402 VLH-SLPFGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07113 440 FLDpAVPFGGMKQSGIGREFGSAFIDDYTELKSVM 474
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
97-432 |
8.37e-48 |
|
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: 171.92 E-value: 8.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 97 ILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTG-GAD 174
Cdd:TIGR01804 123 GPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGdGAE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 175 VANQLLQER-FDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDsvEGQLEVAAKRVLWGKLTNSGQTCVAPD 253
Cdd:TIGR01804 203 VGPLLVNHPdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFD--DADLESAVDGAMLGNFFSAGQVCSNGT 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 254 YVLCSPSVQDRFVEASKKVLKDF-YGDPAKSDS-FARIVNDRNFDRLEKLLSATK---GKVVVGGQTAKGER-----YIA 323
Cdd:TIGR01804 281 RVFVHKKIKERFLARLVERTERIkLGDPFDEATeMGPLISAAHRDKVLSYIEKGKaegATLATGGGRPENVGlqngfFVE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 324 PTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVl 403
Cdd:TIGR01804 361 PTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPA- 439
|
330 340
....*....|....*....|....*....
gi 26334245 404 hSLPFGGIGNSGIGKYHGTYSFETFSHSK 432
Cdd:TIGR01804 440 -EAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
2-434 |
1.04e-47 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 171.34 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 2 SSPVLIEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDF---RKPKFESVITelefVKNDIKYQL 78
Cdd:cd07101 15 STPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETgkaRRHAFEEVLD----VAIVARYYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 79 DHIHQYVKPQRvARPAANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLP 158
Cdd:cd07101 91 RRAERLLKPRR-RRGAIPVLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 159 KY-LDKECYPVVTGGADVANQLLQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRV 237
Cdd:cd07101 170 EAgLPRDLWQVVTGPGSEVGGAIVDNADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDAD--LDKAAAGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 238 LWGKLTNSGQTCVAPDYVLCSPSVQDRFVE---ASKKVLK-----DFYGDpaksdsFARIVNDRNFDRLEKLL--SATKG 307
Cdd:cd07101 248 VRACFSNAGQLCVSIERIYVHESVYDEFVRrfvARTRALRlgaalDYGPD------MGSLISQAQLDRVTAHVddAVAKG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 308 KVVVGGQTAK---GERYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFL 384
Cdd:cd07101 322 ATVLAGGRARpdlGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 26334245 385 DQTSCGSVCVNDTLMQmVLHSL--PFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07101 402 ARLRAGTVNVNEGYAA-AWASIdaPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
101-435 |
2.51e-46 |
|
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: 168.06 E-value: 2.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVqLMLA-PLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGADVANQ 178
Cdd:cd07142 135 VYTLHEPIGVVGQIIPWNFPL-LMFAwKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 179 LLQERFDL--VFFTGSPNIGKLVYQAASK-HMTPVVLELGGKSPLYI--DDSVEGQLEVAakrvLWGKLTNSGQTCVAPD 253
Cdd:cd07142 214 AIASHMDVdkVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVceDADVDKAVELA----HFALFFNQGQCCCAGS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 254 YVLCSPSVQDRFVEASK-KVLKDFYGDPAKSD-SFARIVNDRNFDRLEKLLSATK---GKVVVGGQT--AKGeRYIAPTL 326
Cdd:cd07142 290 RTFVHESIYDEFVEKAKaRALKRVVGDPFRKGvEQGPQVDKEQFEKILSYIEHGKeegATLITGGDRigSKG-YYIQPTI 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 327 VANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNdtLMQMVLHSL 406
Cdd:cd07142 369 FSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVN--CYDVFDASI 446
|
330 340
....*....|....*....|....*....
gi 26334245 407 PFGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07142 447 PFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
101-434 |
1.07e-44 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 162.99 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLL-PKYLDKECYPVVTG-GADVANQ 178
Cdd:cd07094 117 AWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEGVLQVVTGeREVLGDA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 179 LL-QERFDLVFFTGSPNIGKLVYQAASKhmTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYVLC 257
Cdd:cd07094 197 FAaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDAD--LDAAIEALAKGGFYHAGQVCISVQRIYV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 258 SPSVQDRFVE---ASKKVLKdfYGDPAKSDSF-ARIVNDRNFDRLEKLL--SATKGKVVVGGQTAKGeRYIAPTLVANVT 331
Cdd:cd07094 273 HEELYDEFIEafvAAVKKLK--VGDPLDEDTDvGPLISEEAAERVERWVeeAVEAGARLLCGGERDG-ALFKPTVLEDVP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 332 GNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKqptVNKFLDQTS---CGSVCVNDTLMQMVLHsLPF 408
Cdd:cd07094 350 RDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRD---LNVAFKAAEkleVGGVMVNDSSAFRTDW-MPF 425
|
330 340
....*....|....*....|....*.
gi 26334245 409 GGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07094 426 GGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
101-418 |
1.64e-43 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 159.72 E-value: 1.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGADVANQL 179
Cdd:cd07147 117 GLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETgLPKGAFSVLPCSRDDADLL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 180 LQ-ERFDLVFFTGSPNIG-KLVYQAASKHmtpVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYVLC 257
Cdd:cd07147 197 VTdERIKLLSFTGSPAVGwDLKARAGKKK---VVLELGGNAAVIVDSDAD--LDFAAQRIIFGAFYQAGQSCISVQRVLV 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 258 SPSVQDRF----VEASKKvLKdfYGDPAKSDSF-ARIVNDRNFDRLEKLLS---ATKGKVVVGGQTAkgERYIAPTLVAN 329
Cdd:cd07147 272 HRSVYDEFksrlVARVKA-LK--TGDPKDDATDvGPMISESEAERVEGWVNeavDAGAKLLTGGKRD--GALLEPTILED 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 330 VTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHsLPFG 409
Cdd:cd07147 347 VPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDVPTFRVDH-MPYG 425
|
....*....
gi 26334245 410 GIGNSGIGK 418
Cdd:cd07147 426 GVKDSGIGR 434
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
102-440 |
9.07e-42 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 155.75 E-value: 9.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 102 YIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEvagstANVMASLLPKYLDKEC-YP-----VVTG---- 171
Cdd:PLN02766 153 YTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAE-----QTPLSALFYAHLAKLAgVPdgvinVVTGfgpt 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 172 -GADVANQLlqeRFDLVFFTGSPNIGKLVYQAASK-HMTPVVLELGGKSPLYIDDsvEGQLEVAAKRVLWGKLTNSGQTC 249
Cdd:PLN02766 228 aGAAIASHM---DVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFD--DADVDMAVDLALLGIFYNKGEIC 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 250 VAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAksDSFARI---VNDRNFDRLEKLLSATK--GKVVVGGQTAKGER--Y 321
Cdd:PLN02766 303 VASSRVYVQEGIYDEFVKKLVEKAKDWvVGDPF--DPRARQgpqVDKQQFEKILSYIEHGKreGATLLTGGKPCGDKgyY 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 322 IAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLmqM 401
Cdd:PLN02766 381 IEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYF--A 458
|
330 340 350
....*....|....*....|....*....|....*....
gi 26334245 402 VLHSLPFGGIGNSGIGKYHGTYSFETFSHSKSVLAKDYN 440
Cdd:PLN02766 459 FDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSVVTPLYN 497
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
7-421 |
2.54e-41 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 155.04 E-value: 2.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLgalreDF--------RKPKFEsvitELEFVKNDIKYQL 78
Cdd:PRK09407 56 VEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELL-----DLvqletgkaRRHAFE----EVLDVALTARYYA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 79 DHIHQYVKPQRVaRPAANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLp 158
Cdd:PRK09407 127 RRAPKLLAPRRR-AGALPVLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELL- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 159 kY---LDKECYPVVTG-GADVANQLLqERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYI-DDSvegQLEVA 233
Cdd:PRK09407 205 -YeagLPRDLWQVVTGpGPVVGTALV-DNADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVlDDA---DLDKA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 234 AKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEA-----SKKVLKDFYGDPAKSDSfarIVNDRNFDRLEKLL-SAT-K 306
Cdd:PRK09407 280 AAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAfvaavRAMRLGAGYDYSADMGS---LISEAQLETVSAHVdDAVaK 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 307 GKVVVGGQTAK---GERYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKF 383
Cdd:PRK09407 357 GATVLAGGKARpdlGPLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAI 436
|
410 420 430
....*....|....*....|....*....|....*....
gi 26334245 384 LDQTSCGSVCVNDTLMQM-VLHSLPFGGIGNSGIGKYHG 421
Cdd:PRK09407 437 AARIRAGTVNVNEGYAAAwGSVDAPMGGMKDSGLGRRHG 475
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
107-421 |
4.82e-41 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 154.25 E-value: 4.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTG-GADVANQLLQE-R 183
Cdd:TIGR01237 167 PTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAgLPKGVVQFVPGsGSEVGDYLVDHpK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 184 FDLVFFTGSPNIGKLVYQAASK------HMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYVLC 257
Cdd:TIGR01237 247 TSLITFTGSREVGTRIFERAAKvqpgqkHLKRVIAEMGGKDTVIVDEDAD--IELAAQSAFTSAFGFAGQKCSAGSRAVV 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 258 SPSVQD----RFVEA--SKKVlkdfyGDPAKSDSF-ARIVNDRNFDRLEKLLSATK--GKVVVGGQTAKGERY-IAPTLV 327
Cdd:TIGR01237 325 HEKVYDevveRFVEIteSLKV-----GPPDSADVYvGPVIDQKSFNKIMEYIEIGKaeGRLVSGGCGDDSKGYfIGPTIF 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 328 ANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHSLP 407
Cdd:TIGR01237 400 ADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQP 479
|
330
....*....|....
gi 26334245 408 FGGIGNSGIGKYHG 421
Cdd:TIGR01237 480 FGGFKMSGTDSKAG 493
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
106-434 |
5.48e-41 |
|
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: 152.91 E-value: 5.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 106 DPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYPVVTGGADVANQLLQERFD 185
Cdd:cd07107 115 EPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALVRHPD 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 186 L--VFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWG-KLTNSGQTCVAPDYVLCSPSVQ 262
Cdd:cd07107 195 VkrIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD--PEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 263 DRFVEASKKVLKDFY-GDPAKSDSFARIVNDRN-FDRLEKLLSATK---GKVVVGGQTAKGER-----YIAPTLVANVTG 332
Cdd:cd07107 273 DEVLARVVERVAAIKvGDPTDPATTMGPLVSRQqYDRVMHYIDSAKregARLVTGGGRPEGPAleggfYVEPTVFADVTP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 333 NDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVlhSLPFGGIG 412
Cdd:cd07107 353 GMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFL--GAPFGGVK 430
|
330 340
....*....|....*....|..
gi 26334245 413 NSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07107 431 NSGIGREECLEELLSYTQEKNV 452
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
103-437 |
1.75e-40 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 151.69 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 103 IKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYPVVTG-GADVANQLL- 180
Cdd:TIGR03374 133 IRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVNILFGrGKTVGDPLTg 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 181 QERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDsvEGQLEVAAKRVLWGKLTNSGQTCVAPDYVLCSPS 260
Cdd:TIGR03374 213 HEKVRMVSLTGSIATGEHILSHTAPSIKRTHMELGGKAPVIVFD--DADIDAVVEGVRTFGFYNAGQDCTAACRIYAQRG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 261 VQDRFVEASKKVLKDF-YGDPA-KSDSFARIVNDRNFDRLEKLLSATKG----KVVVGGQTAKGE-RYIAPTLVANVTGN 333
Cdd:TIGR03374 291 IYDTLVEKLGAAVATLkSGAPDdESTELGPLSSLAHLERVMKAVEEAKAlghiKVITGGEKRKGNgYYFAPTLLAGAKQD 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 334 DSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLmqMVLHSLPFGGIGN 413
Cdd:TIGR03374 371 DAIVQKEVFGPVVSITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHF--MLVSEMPHGGQKL 448
|
330 340
....*....|....*....|....
gi 26334245 414 SGIGKYHGTYSFETFSHSKSVLAK 437
Cdd:TIGR03374 449 SGYGKDMSLYGLEDYTVVRHIMVK 472
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
7-441 |
2.63e-40 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 152.65 E-value: 2.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLR-ACIDDNYDQFLGALRE-DFRKPKFESVITELEFVKNDIKYQ---LDHI 81
Cdd:PLN02466 97 VNRAVAAARKAFDEGPWPKMTAYERSRILLRfADLLEKHNDELAALETwDNGKPYEQSAKAELPMFARLFRYYagwADKI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 82 HQYVKPqrvarpaANILDDAYIKWDPLGVVLIFSAWNYPVqLMLA-PLAGAIAAGNCVVIKPSEVAGSTANVMASLL--- 157
Cdd:PLN02466 177 HGLTVP-------ADGPHHVQTLHEPIGVAGQIIPWNFPL-LMFAwKVGPALACGNTIVLKTAEQTPLSALYAAKLLhea 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 158 ---PKYLDkecypVVTGGADVANQLLQERFDL--VFFTGSPNIGKLVYQAASK-HMTPVVLELGGKSPLYI--DDSVEGQ 229
Cdd:PLN02466 249 glpPGVLN-----VVSGFGPTAGAALASHMDVdkLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVceDADVDKA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 230 LEVAAKRVLWgkltNSGQTCVAPDYVLCSPSVQDRFVEASK-KVLKDFYGDPAKS--------DSfarivndrnfDRLEK 300
Cdd:PLN02466 324 VELAHFALFF----NQGQCCCAGSRTFVHERVYDEFVEKAKaRALKRVVGDPFKKgveqgpqiDS----------EQFEK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 301 LLSATKGKVVVGGQ-TAKGER------YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIF 373
Cdd:PLN02466 390 ILRYIKSGVESGATlECGGDRfgskgyYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVF 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26334245 374 SNKQPTVNKFLDQTSCGSVCVNdtLMQMVLHSLPFGGIGNSGIGKYHGTYSFETFSHSKSVLAKDYNP 441
Cdd:PLN02466 470 TQNLDTANTLSRALRVGTVWVN--CFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTPLKNP 535
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
101-435 |
4.46e-40 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 150.80 E-value: 4.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASL-----LPKYLdkecYPVVTGGADV 175
Cdd:PRK13252 136 VYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIyteagLPDGV----FNVVQGDGRV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 176 ANQLLQ-ERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYI-DDSvegQLEVAAKRVLWGKLTNSGQTCVAPD 253
Cdd:PRK13252 212 GAWLTEhPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVfDDA---DLDRAADIAMLANFYSSGQVCTNGT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 254 YVLCSPSVQDRFVEASK-KVLKDFYGDPAKSDS-FARIVndrNFDRLEKLLSA-TKGK-----VVVGGQTAKGER----- 320
Cdd:PRK13252 289 RVFVQKSIKAAFEARLLeRVERIRIGDPMDPATnFGPLV---SFAHRDKVLGYiEKGKaegarLLCGGERLTEGGfanga 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 321 YIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVN---DT 397
Cdd:PRK13252 366 FVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINtwgES 445
|
330 340 350
....*....|....*....|....*....|....*...
gi 26334245 398 LMQMvlhslPFGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:PRK13252 446 PAEM-----PVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
8-434 |
4.93e-40 |
|
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: 150.19 E-value: 4.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 8 EKALIKAREAFaRNVTRSVDFRIRQ--LKQLRACIDDNYDQFLGALREDFRKPKFESVItELEFVKNDIKYQLDHIhqYV 85
Cdd:cd07120 22 EAAIAAARRAF-DETDWAHDPRLRArvLLELADAFEANAERLARLLALENGKILGEARF-EISGAISELRYYAGLA--RT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 86 KPQRVARPAANILddAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPsevAGSTANVMASLLP-----KY 160
Cdd:cd07120 98 EAGRMIEPEPGSF--SLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKP---AGQTAQINAAIIRilaeiPS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 161 LDKECYPVVTG-GADVANQLLQE-RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYI-DDSvegQLEVAAKRV 237
Cdd:cd07120 173 LPAGVVNLFTEsGSEGAAHLVASpDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVfDDA---DLDAALPKL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 238 LWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDFYGDPA---KSDSFARIvnDR-NFDRLEKLLS---ATKGKVV 310
Cdd:cd07120 250 ERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGldpASDMGPLI--DRaNVDRVDRMVEraiAAGAEVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 311 VGGQT-----AKGERYiAPTLVAnVTGNDS-LMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFL 384
Cdd:cd07120 328 LRGGPvteglAKGAFL-RPTLLE-VDDPDAdIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVA 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 26334245 385 DQTSCGSVCVNDtlmQMVLHS-LPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07120 406 RAIRAGTVWIND---WNKLFAeAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
7-415 |
2.65e-39 |
|
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: 147.80 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESViTELEFVKNDIKYQLDHIHQYVK 86
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQ-TEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 87 PQRVARPAANilddAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLL-PKYLDKEC 165
Cdd:cd07095 81 ERATPMAQGR----AVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 166 YPVVTGGADVANQLL-QERFDLVFFTGSPNIGKLVYQAASKHmtPVV---LELGGKSPLYIDDSveGQLEVAAKRVLWGK 241
Cdd:cd07095 157 LNLVQGGRETGEALAaHEGIDGLLFTGSAATGLLLHRQFAGR--PGKilaLEMGGNNPLVVWDV--ADIDAAAYLIVQSA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 242 LTNSGQTCVAPDYVLCSPSVQ-----DRFVEASKK-VLKDFYGDPAKsdsFARIVNDrnfDRLEKLLSATKGKVVVGGQT 315
Cdd:cd07095 233 FLTAGQRCTCARRLIVPDGAVgdaflERLVEAAKRlRIGAPDAEPPF---MGPLIIA---AAAARYLLAQQDLLALGGEP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 316 -AKGER------YIAPTLVaNVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTS 388
Cdd:cd07095 307 lLAMERlvagtaFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420
....*....|....*....|....*..
gi 26334245 389 CGSVCVNDTLMQMVlHSLPFGGIGNSG 415
Cdd:cd07095 386 AGIVNWNRPTTGAS-STAPFGGVGLSG 411
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
7-435 |
4.78e-39 |
|
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: 147.98 E-value: 4.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESVITelefvknDIKYQLDHIHQYVK 86
Cdd:cd07116 40 IELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVRETLAA-------DIPLAIDHFRYFAG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 87 PQRVARPAANILDD---AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDK 163
Cdd:cd07116 113 CIRAQEGSISEIDEntvAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 164 ECYPVVTG-GADVANQLL-QERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSP------------LYIDDSVEGQ 229
Cdd:cd07116 193 GVVNVVNGfGLEAGKPLAsSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniffadvmdaddAFFDKALEGF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 230 LEVAakrvlwgklTNSGQTCVAPDYVLCSPSVQDRFVE-ASKKVLKDFYGDPAksDSFARIVNDRNFDRLEKLLSATK-G 307
Cdd:cd07116 273 VMFA---------LNQGEVCTCPSRALIQESIYDRFMErALERVKAIKQGNPL--DTETMIGAQASLEQLEKILSYIDiG 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 308 K-----VVVGGQTAK-----GERYIAPTLVAnvTGND-SLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNK 376
Cdd:cd07116 342 KeegaeVLTGGERNElggllGGGYYVPTTFK--GGNKmRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRD 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26334245 377 QPTVNKFLDQTSCGSVCVNdtlmqmVLHSLP----FGGIGNSGIGKYHGTYSFETFSHSKSVL 435
Cdd:cd07116 420 GNTAYRMGRGIQAGRVWTN------CYHLYPahaaFGGYKQSGIGRENHKMMLDHYQQTKNLL 476
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
100-422 |
6.09e-38 |
|
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: 144.97 E-value: 6.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 100 DAYIKWDPLGVVLIFSAWNYP--VQLMLAPLAgaIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGADVA 176
Cdd:cd07085 129 DTYSYRQPLGVVAGITPFNFPamIPLWMFPMA--IACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHGGKEAV 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 177 NQLLQE-RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYI-DDSvegQLEVAAKRVLWGKLTNSGQTCVAPDY 254
Cdd:cd07085 207 NALLDHpDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVmPDA---DLEQTANALVGAAFGAAGQRCMALSV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 255 VLCSPSVQDRFVEASK---KVLKDFYGDPAKSDsFARIVNDRNFDRLEKLL-SATK--GKVVVGGQTAKGERY-----IA 323
Cdd:cd07085 284 AVAVGDEADEWIPKLVeraKKLKVGAGDDPGAD-MGPVISPAAKERIEGLIeSGVEegAKLVLDGRGVKVPGYengnfVG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 324 PTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNdtlmqmV- 402
Cdd:cd07085 363 PTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN------Vp 436
|
330 340
....*....|....*....|....
gi 26334245 403 ----LHSLPFGGIGNSGIGKYHGT 422
Cdd:cd07085 437 ipvpLAFFSFGGWKGSFFGDLHFY 460
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
105-395 |
1.04e-37 |
|
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: 144.27 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 105 WDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYP-----VVTGGADVANQL 179
Cdd:cd07130 130 WNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLPgaiasLVCGGADVGEAL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 180 LQ-ERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYVLCS 258
Cdd:cd07130 210 VKdPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDAD--LDLAVRAVLFAAVGTAGQRCTTTRRLIVH 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 259 PSVQDRFVEASKKVLKDF-YGDPAKSDS-FARIVNDRNFDRLEKLLSATK---GKVVVGGQTAKGE-RYIAPTLVAnVTG 332
Cdd:cd07130 288 ESIYDEVLERLKKAYKQVrIGDPLDDGTlVGPLHTKAAVDNYLAAIEEAKsqgGTVLFGGKVIDGPgNYVEPTIVE-GLS 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26334245 333 NDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTS--CGSVCVN 395
Cdd:cd07130 367 DAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLGPKGsdCGIVNVN 431
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
107-415 |
3.23e-37 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 143.54 E-value: 3.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTG-GADVANQLLQE-- 182
Cdd:PRK03137 171 PLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGsGSEVGDYLVDHpk 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 183 -RFdlVFFTGSPNIGKLVYQAASK------HMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYV 255
Cdd:PRK03137 251 tRF--ITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDAD--LDLAAESIVASAFGFSGQKCSACSRA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 256 LCSPSVQDRFVEASKKVLKDF-YGDPAKSDSFARIVNDRNFDRLEKLLSATK--GKVVVGGQTAKGERY-IAPTLVANVT 331
Cdd:PRK03137 327 IVHEDVYDEVLEKVVELTKELtVGNPEDNAYMGPVINQASFDKIMSYIEIGKeeGRLVLGGEGDDSKGYfIQPTIFADVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 332 GNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHSLPFGGI 411
Cdd:PRK03137 407 PKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNRGCTGAIVGYHPFGGF 486
|
....
gi 26334245 412 GNSG 415
Cdd:PRK03137 487 NMSG 490
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
101-434 |
4.46e-36 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 140.03 E-value: 4.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGADVANQL 179
Cdd:PRK09847 151 AMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 180 L--QERFDLVFFTGSPNIGK-LVYQAASKHMTPVVLELGGKSP--LYIDDSvegQLEVAAKRVLWGKLTNSGQTCVAPDY 254
Cdd:PRK09847 231 LsrHNDIDAIAFTGSTRTGKqLLKDAGDSNMKRVWLEAGGKSAniVFADCP---DLQQAASATAAGIFYNQGQVCIAGTR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 255 VLCSPSVQDRFVEASKKVLKDFY-GDPAKSDS-FARIVNDRNFDRLEKLL--SATKGKVVVGGQTAKGERYIAPTLVANV 330
Cdd:PRK09847 308 LLLEESIADEFLALLKQQAQNWQpGHPLDPATtMGTLIDCAHADSVHSFIreGESKGQLLLDGRNAGLAAAIGPTIFVDV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 331 TGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCV---NDTLMqmvlhSLP 407
Cdd:PRK09847 388 DPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVnnyNDGDM-----TVP 462
|
330 340
....*....|....*....|....*..
gi 26334245 408 FGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:PRK09847 463 FGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
79-434 |
9.15e-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: 136.09 E-value: 9.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 79 DHIHQYVKPQRVARPAANIlddAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLP 158
Cdd:cd07140 122 DKIQGKTIPINQARPNRNL---TLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 159 KY-LDKECYPVVTGGADVANQLLQERFDL--VFFTGSPNIGKLVYQ-AASKHMTPVVLELGGKSPLYIDDSVEgqLEVAA 234
Cdd:cd07140 199 KAgFPKGVINILPGSGSLVGQRLSDHPDVrkLGFTGSTPIGKHIMKsCAVSNLKKVSLELGGKSPLIIFADCD--MDKAV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 235 KRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVeasKKVLKDF----YGDPAKSDSFARIVNDRNfdRLEKLLSATK---- 306
Cdd:cd07140 277 RMGMSSVFFNKGENCIAAGRLFVEESIHDEFV---RRVVEEVkkmkIGDPLDRSTDHGPQNHKA--HLDKLVEYCErgvk 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 307 --GKVVVGG-QTAKGERYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSE--EEAIQFINRGEKPLAMYIFSNKQPTVN 381
Cdd:cd07140 352 egATLVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGdvDGVLQRANDTEYGLASGVFTKDINKAL 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 26334245 382 KFLDQTSCGSVCVNDTLMQMVlhSLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:cd07140 432 YVSDKLEAGTVFVNTYNKTDV--AAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
107-428 |
1.04e-34 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 135.80 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGA-DVANQLLQERF 184
Cdd:PRK11241 146 PIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAgAVGGELTSNPL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 185 -DLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDsvEGQLEVAAKRVLWGKLTNSGQTCVAPDYVLCSPSVQD 263
Cdd:PRK11241 226 vRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFD--DADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYD 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 264 RFVEASKK-VLKDFYGDPAKSD-SFARIVNDRNFDRLEKLL--SATKG-KVVVGGQT-AKGERYIAPTLVANVTGNDSLM 337
Cdd:PRK11241 304 RFAEKLQQaVSKLHIGDGLEKGvTIGPLIDEKAVAKVEEHIadALEKGaRVVCGGKAhELGGNFFQPTILVDVPANAKVA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 338 SEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLhsLPFGGIGNSGIG 417
Cdd:PRK11241 384 KEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEV--APFGGIKASGLG 461
|
330
....*....|.
gi 26334245 418 KYHGTYSFETF 428
Cdd:PRK11241 462 REGSKYGIEDY 472
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
107-433 |
1.61e-32 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 129.88 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASL-----LPKYLdkecYPVVTG-GADVANQLL 180
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCfhlagFPKGL----ISCVTGkGSEIGDFLT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 181 QER-FDLVFFTGSpNIGKLVYQAASkhMTPVVLELGGKSPLYIDDsvEGQLEVAAKRVLWGKLTNSGQTCVAPDYVLCSP 259
Cdd:PLN00412 234 MHPgVNCISFTGG-DTGIAISKKAG--MVPLQMELGGKDACIVLE--DADLDLAAANIIKGGFSYSGQRCTAVKVVLVME 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 260 SVQDRFVEASK-KVLKDFYGDPAKSDSFARIVNDRNFDRLEKLLSATKGKVVVGGQTAKGE-RYIAPTLVANVTGNDSLM 337
Cdd:PLN00412 309 SVADALVEKVNaKVAKLTVGPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREgNLIWPLLLDNVRPDMRIA 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 338 SEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKqptVNK---FLDQTSCGSVCVNDTLMQMVLHsLPFGGIGNS 414
Cdd:PLN00412 389 WEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRD---INKailISDAMETGTVQINSAPARGPDH-FPFQGLKDS 464
|
330
....*....|....*....
gi 26334245 415 GIGKYHGTYSFETFSHSKS 433
Cdd:PLN00412 465 GIGSQGITNSINMMTKVKS 483
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
95-425 |
2.93e-32 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 128.67 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 95 ANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASL-----LPKYLdkecYPVV 169
Cdd:cd07111 135 AQLLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEIcaeagLPPGV----LNIV 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 170 TGGADVANQL-LQERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLY------IDDSVEGQLEVAakrvlWgkl 242
Cdd:cd07111 211 TGNGSFGSALaNHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIvfddadLDSAVEGIVDAI-----W--- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 243 TNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPA-KSDSFARIVNDRNFDRLEKLLSATK--GKVV--VGGQTA 316
Cdd:cd07111 283 FNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLrVGDPLdKAIDMGAIVDPAQLKRIRELVEEGRaeGADVfqPGADLP 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 317 KGERYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVND 396
Cdd:cd07111 363 SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWING 442
|
330 340 350
....*....|....*....|....*....|..
gi 26334245 397 TlmQMVLHSLPFGGIGNSGIGKY---HGTYSF 425
Cdd:cd07111 443 H--NLFDAAAGFGGYRESGFGREggkEGLYEY 472
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
6-417 |
8.17e-32 |
|
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: 127.70 E-value: 8.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 6 LIEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKpkfeSVITELEFVKNDI---KYQLDHIH 82
Cdd:cd07083 56 EAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGK----NWVEAIDDVAEAIdfiRYYARAAL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 83 QYVKPQRVARPAANILDDAYIKwdPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEvagsTANVMASLLPKYLD 162
Cdd:cd07083 132 RLRYPAVEVVPYPGEDNESFYV--GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAE----DAVVVGYKVFEIFH 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 163 KECYP------VVTGGADVANQLLQ-ERFDLVFFTGSPNIGKLVYQAASKHMT------PVVLELGGKSPLYIDDSveGQ 229
Cdd:cd07083 206 EAGFPpgvvqfLPGVGEEVGAYLTEhERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDET--AD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 230 LEVAAKRVLWGKLTNSGQTCVAPDYVLCS----PSVQDRFVEASKKVLkdfYGDPAKSDS-FARIVNDRNFDRLEKLLSA 304
Cdd:cd07083 284 FELVVEGVVVSAFGFQGQKCSAASRLILTqgayEPVLERLLKRAERLS---VGPPEENGTdLGPVIDAEQEAKVLSYIEH 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 305 TK--GKVVVGGQTAKGERY-IAPTLVANVTGNDSLMSEELFGPILPIVPVKSEE--EAIQFINRGEKPLAMYIFSNKQPT 379
Cdd:cd07083 361 GKneGQLVLGGKRLEGEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREH 440
|
410 420 430
....*....|....*....|....*....|....*...
gi 26334245 380 VNKFLDQTSCGSVCVNDTLMQMVLHSLPFGGIGNSGIG 417
Cdd:cd07083 441 LEEARREFHVGNLYINRKITGALVGVQPFGGFKLSGTN 478
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
101-425 |
1.88e-30 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 123.31 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 101 AYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKECYPVVTGGADVANQL 179
Cdd:PRK09406 117 AYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAgFPDGCFQTLLVGSGAVEAI 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 180 LQE-RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYVLCS 258
Cdd:PRK09406 197 LRDpRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSAD--LDRAAETAVTARVQNNGQSCIAAKRFIVH 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 259 PSVQDRFVE---ASKKVLKdfYGDPAKSDS-FARIVNDRNFDRLEKLL--SATKGKVVVGGqtakGER------YIAPTL 326
Cdd:PRK09406 275 ADVYDAFAEkfvARMAALR--VGDPTDPDTdVGPLATEQGRDEVEKQVddAVAAGATILCG----GKRpdgpgwFYPPTV 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 327 VANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDtlMQMVLHSL 406
Cdd:PRK09406 349 ITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING--MTVSYPEL 426
|
330 340
....*....|....*....|..
gi 26334245 407 PFGGIGNSGIGKY---HGTYSF 425
Cdd:PRK09406 427 PFGGVKRSGYGRElsaHGIREF 448
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
105-430 |
2.17e-30 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 123.79 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 105 WDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIK--PSE--VAGSTANVMASLLPKY-LDKECYPVVTGGADVANQL 179
Cdd:PLN02315 152 WNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKgaPTTplITIAMTKLVAEVLEKNnLPGAIFTSFCGGAEIGEAI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 180 LQE-RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDSVEGQLevAAKRVLWGKLTNSGQTCVAPDYVLCS 258
Cdd:PLN02315 232 AKDtRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQL--AVRSVLFAAVGTAGQRCTTCRRLLLH 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 259 PSVQDRFVEASKKVLKDF-YGDPAKSDSFARIVNDR----NFDRLEKLLSATKGKVVVGGQTAKGE-RYIAPTLVaNVTG 332
Cdd:PLN02315 310 ESIYDDVLEQLLTVYKQVkIGDPLEKGTLLGPLHTPeskkNFEKGIEIIKSQGGKILTGGSAIESEgNFVQPTIV-EISP 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 333 NDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQT--SCGSVCVNdtlmqmvlhsLP--- 407
Cdd:PLN02315 389 DADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWIGPLgsDCGIVNVN----------IPtng 458
|
330 340
....*....|....*....|....*....
gi 26334245 408 ------FGGIGNSGIGKYHGTYSFETFSH 430
Cdd:PLN02315 459 aeiggaFGGEKATGGGREAGSDSWKQYMR 487
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
7-434 |
3.24e-29 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 119.97 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESViTELEFVKNDIKYQLDHIHQYVK 86
Cdd:PRK13968 31 IENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVAKSANLCDWYAEHGPAMLK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 87 PQrvarPAANILDDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPS-EVAGSTANVMASLLPKYLDKEC 165
Cdd:PRK13968 110 AE----PTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHApNVMGCAQLIAQVFKDAGIPQGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 166 YPVVTGGADVANQLLQE-RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIDDsvEGQLEVAAKRVLWGKLTN 244
Cdd:PRK13968 186 YGWLNADNDGVSQMINDsRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLN--DADLELAVKAAVAGRYQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 245 SGQTCVAPDYVLCSPSVQDRFVE---ASKKVLKdfYGDPAKSDSF----ARI-VNDRNFDRLEKLLsATKGKVVVGGQTA 316
Cdd:PRK13968 264 TGQVCAAAKRFIIEEGIASAFTErfvAAAAALK--MGDPRDEENAlgpmARFdLRDELHHQVEATL-AEGARLLLGGEKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 317 KGE-RYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSV--- 392
Cdd:PRK13968 341 AGAgNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGGVfin 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 26334245 393 --CVNDTlmqmvlhSLPFGGIGNSGIGKYHGTYSFETFSHSKSV 434
Cdd:PRK13968 421 gyCASDA-------RVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
103-417 |
1.35e-28 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 118.84 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 103 IKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLL-----PKYLdkeCYPVVTGGADVAN 177
Cdd:cd07125 163 LELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLheagvPRDV---LQLVPGDGEEIGE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 178 QLLQ-ERFDLVFFTGSPNIGKLVYQAASKHM---TPVVLELGGKSPLYIDDSveGQLEVAAKRVLWGKLTNSGQTCVAPD 253
Cdd:cd07125 240 ALVAhPRIDGVIFTGSTETAKLINRALAERDgpiLPLIAETGGKNAMIVDST--ALPEQAVKDVVQSAFGSAGQRCSALR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 254 YVLCSPSVQDRFVE------ASKKVlkdfyGDPAKSDSF----ARIVNDRNFDRLEKLLSAtKGKVVVGGQT-AKGERYI 322
Cdd:cd07125 318 LLYLQEEIAERFIEmlkgamASLKV-----GDPWDLSTDvgplIDKPAGKLLRAHTELMRG-EAWLIAPAPLdDGNGYFV 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 323 APTLVANVtgNDSLMSEELFGPILPIVPVKSE--EEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNDTLMQ 400
Cdd:cd07125 392 APGIIEIV--GIFDLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITG 469
|
330
....*....|....*..
gi 26334245 401 MVLHSLPFGGIGNSGIG 417
Cdd:cd07125 470 AIVGRQPFGGWGLSGTG 486
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
7-415 |
3.53e-28 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 116.98 E-value: 3.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQFLGALREDFRKPKFESViTELEFVKNDIKYQLDHIHQYVK 86
Cdd:PRK09457 39 VDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAA-TEVTAMINKIAISIQAYHERTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 87 PQRVARPAANilddAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPKY-LDKEC 165
Cdd:PRK09457 118 EKRSEMADGA----AVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 166 YPVVTGGADVANQLLQER-FDLVFFTGSPNIGKLVYQAASKHMTPVV-LELGGKSPLYIDDSveGQLEVAAKRVLWGKLT 243
Cdd:PRK09457 194 LNLVQGGRETGKALAAHPdIDGLLFTGSANTGYLLHRQFAGQPEKILaLEMGGNNPLVIDEV--ADIDAAVHLIIQSAFI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 244 NSGQTCVAPDYVLCSPSVQ-----DRFVEASKKVLKD-FYGDPAK------SDSFArivndrnfdrlEKLLSATKGKVVV 311
Cdd:PRK09457 272 SAGQRCTCARRLLVPQGAQgdaflARLVAVAKRLTVGrWDAEPQPfmgaviSEQAA-----------QGLVAAQAQLLAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 312 GG-------QTAKGERYIAPTLVaNVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFL 384
Cdd:PRK09457 341 GGksllemtQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFL 419
|
410 420 430
....*....|....*....|....*....|.
gi 26334245 385 DQTSCGSVCVNDTLMQMVlHSLPFGGIGNSG 415
Cdd:PRK09457 420 LEIRAGIVNWNKPLTGAS-SAAPFGGVGASG 449
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
7-437 |
7.36e-25 |
|
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: 107.27 E-value: 7.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFARNVTRSVDFRIRQLKQLRACIDDNYDQF-------LGALREDFRKpkfeSVITELEFVkndikyqlD 79
Cdd:TIGR01722 40 VDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEIaelitaeHGKTHSDALG----DVARGLEVV--------E 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 80 H---IHQYVKPQRVARPAANIldDAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASL 156
Cdd:TIGR01722 108 HacgVNSLLKGETSTQVATRV--DVYSIRQPLGVCAGITPFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 157 LPKY-LDKECYPVVTGGADVANQLLQE-RFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKSPLYIddSVEGQLEVAA 234
Cdd:TIGR01722 186 FSEAgAPDGVLNVVHGDKEAVDRLLEHpDVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVV--MPDADKDAAA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 235 KRVLWGKLTNSGQTCVAPDYVLCSPSVQD---RFVEASKKVLKDFYGDPakSDSFARIVNDRNFDRLEKLL-SATK--GK 308
Cdd:TIGR01722 264 DALVGAAYGAAGQRCMAISAAVLVGAADEwvpEIRERAEKIRIGPGDDP--GAEMGPLITPQAKDRVASLIaGGAAegAE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 309 VVVGGQTAKGERY-----IAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKF 383
Cdd:TIGR01722 342 VLLDGRGYKVDGYeegnwVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRF 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 26334245 384 LDQTSCGSVCVNDTL-MQMVLHSlpFGGIGNSGIGKYH--GTYSFETFSHSKSVLAK 437
Cdd:TIGR01722 422 QHEIEVGQVGVNVPIpVPLPYFS--FTGWKDSFFGDHHiyGKQGTHFYTRGKTVTTR 476
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
7-417 |
2.56e-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: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 7 IEKALIKAREAFA-RNVTRSVDFRIRQLKQLRACIDDNYDQF-LGALREDfRKPKFESVItELEFVKNDIKYQLDHIHQY 84
Cdd:cd07148 23 IDKALDTAHALFLdRNNWLPAHERIAILERLADLMEERADELaLLIAREG-GKPLVDAKV-EVTRAIDGVELAADELGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 85 VK---PQRVARPAANILddAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKP-SEVAGSTANVMASLLPKY 160
Cdd:cd07148 101 GGreiPMGLTPASAGRI--AFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPaLATPLSCLAFVDLLHEAG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 161 LDKECYPVVTGGADVANQLLQE-RFDLVFFTGSPNIG-KLVYQAASKhmTPVVLELGGKSPLYIDDSVEgqLEVAAKRVL 238
Cdd:cd07148 179 LPEGWCQAVPCENAVAEKLVTDpRVAFFSFIGSARVGwMLRSKLAPG--TRCALEHGGAAPVIVDRSAD--LDAMIPPLV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 239 WGKLTNSGQTCVapdyvlcspSVQDRFVEASK----------KVLKDFYGDPAKSDS-FARIVNDRNFDRLEKLL--SAT 305
Cdd:cd07148 255 KGGFYHAGQVCV---------SVQRVFVPAEIaddfaqrlaaAAEKLVVGDPTDPDTeVGPLIRPREVDRVEEWVneAVA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 306 KGKVVVGGQTAKGERYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLD 385
Cdd:cd07148 326 AGARLLCGGKRLSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVR 405
|
410 420 430
....*....|....*....|....*....|....*...
gi 26334245 386 QTSCGSVCVNDtlmqmvlHS------LPFGGIGNSGIG 417
Cdd:cd07148 406 RLDATAVMVND-------HTafrvdwMPFAGRRQSGYG 436
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
73-421 |
2.49e-20 |
|
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: 93.82 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 73 DIKYQLDHIHQYvkpqrvARPAANILDDAYIKwdPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSE----VAGS 148
Cdd:TIGR01238 134 EVREAVDFCRYY------AKQVRDVLGEFSVE--SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEqtslIAYR 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 149 TANVM--ASLLPKYLDkecypVVTG-GADVANQLL-QERFDLVFFTGSPNIGKLVYQAASKHM---TPVVLELGGKSPLY 221
Cdd:TIGR01238 206 AVELMqeAGFPAGTIQ-----LLPGrGADVGAALTsDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 222 IDDSVEGQLEVAakRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKVLKDF-YGDPAK-SDSFARIVNDRNFDRLE 299
Cdd:TIGR01238 281 VDSTALPEQVVR--DVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELkVGVPHLlTTDVGPVIDAEAKQNLL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 300 KLLSATKGK-------VVVGGQTAKGERYIAPTLVAnvTGNDSLMSEELFGPILPIVPVKSEE--EAIQFINRGEKPLAM 370
Cdd:TIGR01238 359 AHIEHMSQTqkkiaqlTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTM 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 26334245 371 YIFSNKQPTVNKFLDQTSCGSVCVNDTLMQMVLHSLPFGGIGNSGIGKYHG 421
Cdd:TIGR01238 437 GVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
107-414 |
2.07e-19 |
|
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: 90.37 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASLLPK--YLDKECYPVVTGGADVANQLLQE-R 183
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGKTMQALLLHpN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 184 FDLVFFTGSPNIGKLVyqAASKHMTPVVLELGGKSPLYIDDSVEgQLEVAAKRVLWGKLTNSGQTCVAPDYVLC------ 257
Cdd:cd07084 180 PKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQ-AVDYVAWQCVQDMTACSGQKCTAQSMLFVpenwsk 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 258 SPSVQDRFVEASKKVLKDFYGDPAKSDSF-ARIVNDRNFDRLeKLLSATKGKVVVGGQTAKGERYIAPTLVANVTGNDS- 335
Cdd:cd07084 257 TPLVEKLKALLARRKLEDLLLGPVQTFTTlAMIAHMENLLGS-VLLFSGKELKNHSIPSIYGACVASALFVPIDEILKTy 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 336 -LMSEELFGPILPIVPVKSEEEA--IQFINRGEKPLAMYIFSNKQPTVNKFLDQT-SCGSVCVND----TLMQMVLHSLP 407
Cdd:cd07084 336 eLVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLwVAGRTYAILrgrtGVAPNQNHGGG 415
|
....*....
gi 26334245 408 F--GGIGNS 414
Cdd:cd07084 416 PaaDPRGAG 424
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
100-434 |
8.68e-18 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 86.34 E-value: 8.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 100 DAYIKWDPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEVAGSTANVMASL-LPKYLDKECYPVVTGGADVANQ 178
Cdd:PLN02419 242 DTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELaMEAGLPDGVLNIVHGTNDTVNA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 179 LLQ-ERFDLVFFTGSPNIGKLVYQAASKHMTPVVLELGGKS-PLYIDDSvegQLEVAAKRVLWGKLTNSGQTCVAPDYVL 256
Cdd:PLN02419 322 ICDdEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNhGLVLPDA---NIDATLNALLAAGFGAAGQRCMALSTVV 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 257 C---SPSVQDRFVEASKkVLKDFYGDPAKSDsFARIVNDRNFDRLEKLLSA---------TKGKVVVGGQTAKGErYIAP 324
Cdd:PLN02419 399 FvgdAKSWEDKLVERAK-ALKVTCGSEPDAD-LGPVISKQAKERICRLIQSgvddgakllLDGRDIVVPGYEKGN-FIGP 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 325 TLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSCGSVCVNdTLMQMVLH 404
Cdd:PLN02419 476 TILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN-VPIPVPLP 554
|
330 340 350
....*....|....*....|....*....|..
gi 26334245 405 SLPFGGIGNSGIG--KYHGTYSFETFSHSKSV 434
Cdd:PLN02419 555 FFSFTGNKASFAGdlNFYGKAGVDFFTQIKLV 586
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
94-417 |
1.73e-16 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 82.61 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 94 AANILDDAYIKwdPLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSEV--------------AGSTANVMAsLLPk 159
Cdd:PRK11905 665 ARRLLNGPGHK--PLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQtpliaaravrllheAGVPKDALQ-LLP- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 160 yldkecypvvtG-GADVANQLLQ-ERFDLVFFTGSPNIGKLVYQAASKHM---TPVVLELGGKSPLYIDDSVEGQLEVAA 234
Cdd:PRK11905 741 -----------GdGRTVGAALVAdPRIAGVMFTGSTEVARLIQRTLAKRSgppVPLIAETGGQNAMIVDSSALPEQVVAD 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 235 krVLWGKLTNSGQTCVAPDyVLCspsVQ----DRFVEASKKVLKDFY-GDPAKS--------DSFARIVNDRNFDRLEKl 301
Cdd:PRK11905 810 --VIASAFDSAGQRCSALR-VLC---LQedvaDRVLTMLKGAMDELRiGDPWRLstdvgpviDAEAQANIEAHIEAMRA- 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 302 lsatKGKVV----VGGQTAKGeRYIAPTLVAnvTGNDSLMSEELFGPILPIVPVKSEE--EAIQFINRGEKPLAMYIFSN 375
Cdd:PRK11905 883 ----AGRLVhqlpLPAETEKG-TFVAPTLIE--IDSISDLEREVFGPVLHVVRFKADEldRVIDDINATGYGLTFGLHSR 955
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 26334245 376 KQPTVNKFLDQTSCGSVCVNDTLMQMVLHSLPFGGIGNSGIG 417
Cdd:PRK11905 956 IDETIAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLSGTG 997
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
107-417 |
2.92e-15 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 78.86 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSE----VAGSTANVM---------ASLLPkyldkecypvvtG-G 172
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEqtplIAAQAVRILleagvpagvVQLLP------------GrG 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 173 ADVANQLLQ-ERFDLVFFTGSPNIGKLVYQAASK------HMTPVVLELGGKSPLYIDDSVEGQLEVAakRVLWGKLTNS 245
Cdd:PRK11809 836 ETVGAALVAdARVRGVMFTGSTEVARLLQRNLAGrldpqgRPIPLIAETGGQNAMIVDSSALTEQVVA--DVLASAFDSA 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 246 GQTCVAPDyVLCspsVQDRFVEASKKVLKDFY-----GDPAKS--------DSFARIVNDRNFDRLEkllsaTKGKVVVg 312
Cdd:PRK11809 914 GQRCSALR-VLC---LQDDVADRTLKMLRGAMaecrmGNPDRLstdigpviDAEAKANIERHIQAMR-----AKGRPVF- 983
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 313 gQTAKGE-------RYIAPTLVAnvTGNDSLMSEELFGPILPIVPVKSEE--EAIQFINRGEKPLAMYIFSNKQPTVNKF 383
Cdd:PRK11809 984 -QAARENsedwqsgTFVPPTLIE--LDSFDELKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQV 1060
|
330 340 350
....*....|....*....|....*....|....
gi 26334245 384 LDQTSCGSVCVNDTLMQMVLHSLPFGGIGNSGIG 417
Cdd:PRK11809 1061 TGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
107-363 |
1.23e-14 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 76.04 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPvqlmLA-PLAG-----AIAAGNCVVIK--PSEVAgsTANVMASLLPKYLDKECYP------VVTGG 172
Cdd:cd07129 105 PLGPVAVFGASNFP----LAfSVAGgdtasALAAGCPVVVKahPAHPG--TSELVARAIRAALRATGLPagvfslLQGGG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 173 ADVANQLLQE-RFDLVFFTGSPNIGKLVYQAASKHMT--PVVLELGGKSPLYI-DDSVEGQLEVAAKrVLWGKLT-NSGQ 247
Cdd:cd07129 179 REVGVALVKHpAIKAVGFTGSRRGGRALFDAAAARPEpiPFYAELGSVNPVFIlPGALAERGEAIAQ-GFVGSLTlGAGQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 248 TCVAPDYVLCSPSVQ-DRFVEASKKVLKDFYG----DPAKSDSFArivndrnfDRLEKLLSATKGKVVVGGQTAKGERYI 322
Cdd:cd07129 258 FCTNPGLVLVPAGPAgDAFIAALAEALAAAPAqtmlTPGIAEAYR--------QGVEALAAAPGVRVLAGGAAAEGGNQA 329
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 26334245 323 APTLVAnVTG----NDSLMSEELFGPILPIVPVKSEEEAIQFINR 363
Cdd:cd07129 330 APTLFK-VDAaaflADPALQEEVFGPASLVVRYDDAAELLAVAEA 373
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
109-417 |
8.05e-14 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 74.08 E-value: 8.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 109 GVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSE---------V-----AGSTANVMAsLLPkyldkecypvvtG-GA 173
Cdd:PRK11904 686 GVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEqtpliaaeaVkllheAGIPKDVLQ-LLP------------GdGA 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 174 DVANQLL-QERFDLVFFTGSPNIGKLVYQA-ASKHMTPVVL--ELGGKSPLYIDDSveGQLEVAAKRVLWGKLTNSGQTC 249
Cdd:PRK11904 753 TVGAALTaDPRIAGVAFTGSTETARIINRTlAARDGPIVPLiaETGGQNAMIVDST--ALPEQVVDDVVTSAFRSAGQRC 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 250 VAPDyVLCspsVQ----DRFVEASKKVLKDF-YGDPAK----------SDSFARIvnDRNFDRLE---KLLSATKgkvvV 311
Cdd:PRK11904 831 SALR-VLF---VQediaDRVIEMLKGAMAELkVGDPRLlstdvgpvidAEAKANL--DAHIERMKreaRLLAQLP----L 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 312 GGQTAKGErYIAPTLVAnvTGNDSLMSEELFGPILPIVPVKSEE--EAIQFINRGEKPLAMYIFSNKQPTVNKFLDQTSC 389
Cdd:PRK11904 901 PAGTENGH-FVAPTAFE--IDSISQLEREVFGPILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRV 977
|
330 340
....*....|....*....|....*...
gi 26334245 390 GSVCVNDTLMQMVLHSLPFGGIGNSGIG 417
Cdd:PRK11904 978 GNVYVNRNQIGAVVGVQPFGGQGLSGTG 1005
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
128-415 |
1.19e-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: 73.00 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 128 LAGAIA-AGNCVVIKPSevagSTANVMASLLPKYLDKECYP------VVTGGADVANQLLQ-ERFDLVFFTGSPNIGKLV 199
Cdd:cd07123 189 LAGAPAlMGNVVLWKPS----DTAVLSNYLVYKILEEAGLPpgvinfVPGDGPVVGDTVLAsPHLAGLHFTGSTPTFKSL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 200 YQAASKHMT-----P-VVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPD--YVLCS--PSVQDRFVEAS 269
Cdd:cd07123 265 WKQIGENLDryrtyPrIVGETGGKNFHLVHPSAD--VDSLVTATVRGAFEYQGQKCSAASraYVPESlwPEVKERLLEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 270 KKVLkdfYGDPAKSDSFARIVNDRN-FDRLEKLLSATKG----KVVVGGQTAKGERY-IAPTLVANVTGNDSLMSEELFG 343
Cdd:cd07123 343 KEIK---MGDPDDFSNFMGAVIDEKaFDRIKGYIDHAKSdpeaEIIAGGKCDDSVGYfVEPTVIETTDPKHKLMTEEIFG 419
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26334245 344 PILPI--VPVKSEEEAIQFINR-GEKPLAMYIFSNKQPTVNKFLD--QTSCGSVCVNDTLMQMVLHSLPFGGIGNSG 415
Cdd:cd07123 420 PVLTVyvYPDSDFEETLELVDTtSPYALTGAIFAQDRKAIREATDalRNAAGNFYINDKPTGAVVGQQPFGGARASG 496
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
109-375 |
4.01e-11 |
|
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: 64.98 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 109 GVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPsevAGSTANVM---------ASLLPKyldkECYPVVTGGA-DVANQ 178
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKP---ATATAYLTeavvkdiveSGLLPE----GALQLICGSVgDLLDH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 179 LlqERFDLVFFTGSPNIG-KL-VYQAASKHMTPVVLE--------LGgksplyiDDSVEGQLEVAA--KRVLWGKLTNSG 246
Cdd:cd07128 219 L--GEQDVVAFTGSAATAaKLrAHPNIVARSIRFNAEadslnaaiLG-------PDATPGTPEFDLfvKEVAREMTVKAG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 247 QTCVAPDYVLCSPSVQDRFVEASKKVL-KDFYGDPAKSD-SFARIVNDRNF----DRLEKLLSATK-------GKVVVGG 313
Cdd:cd07128 290 QKCTAIRRAFVPEARVDAVIEALKARLaKVVVGDPRLEGvRMGPLVSREQRedvrAAVATLLAEAEvvfggpdRFEVVGA 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26334245 314 QTAKGErYIAPTLV--ANVTGNDSLMSEELFGPILPIVPVKSEEEAIQFINRGEKPLAMYIFSN 375
Cdd:cd07128 370 DAEKGA-FFPPTLLlcDDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTN 432
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
107-417 |
1.19e-10 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 64.19 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 107 PLGVVLIFSAWNYPVQLMLAPLAGAIAAGNCVVIKPSE---------V-----AGSTANVMAsLLPkyldkecypvvtG- 171
Cdd:COG4230 680 GRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEqtpliaaraVrllheAGVPADVLQ-LLP------------Gd 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 172 GADVANQLL-QERFDLVFFTGSPNIGKLVYQA-ASKHMTPVVL--ELGGKSPLYIDDSVegQLEVAAKRVLWGKLTNSGQ 247
Cdd:COG4230 747 GETVGAALVaDPRIAGVAFTGSTETARLINRTlAARDGPIVPLiaETGGQNAMIVDSSA--LPEQVVDDVLASAFDSAGQ 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 248 TCVAPDyVLCspsVQ----DRFVEASK------KVlkdfyGDPAK----------SDSFARIvnDRNFDRLEKllsatKG 307
Cdd:COG4230 825 RCSALR-VLC---VQediaDRVLEMLKgamaelRV-----GDPADlstdvgpvidAEARANL--EAHIERMRA-----EG 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 308 KVV----VGGQTAKGeRYIAPTL--VANVtgndSLMSEELFGPILPIVPVKSEE--EAIQFINR---GekpLAMYIFSNK 376
Cdd:COG4230 889 RLVhqlpLPEECANG-TFVAPTLieIDSI----SDLEREVFGPVLHVVRYKADEldKVIDAINAtgyG---LTLGVHSRI 960
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 26334245 377 QPTVNKFLDQTSCGSVCVNDTLMQMVLHSLPFGGIGNSGIG 417
Cdd:COG4230 961 DETIDRVAARARVGNVYVNRNIIGAVVGVQPFGGEGLSGTG 1001
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
84-359 |
9.41e-07 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 51.33 E-value: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 84 YVKPQRVARPAAniLDDAYiKWDPLGVVLI-----FSAWN-YPvqlmlaPLAGAIAAGNCVVIKPSEVA----GSTANVM 153
Cdd:cd07127 173 WEKPQGKHDPLA--MEKTF-TVVPRGVALVigcstFPTWNgYP------GLFASLATGNPVIVKPHPAAilplAITVQVA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 154 ASLLPKY-LDKECYPVV--TGGADVANQL-LQERFDLVFFTGSPNIGKLVYQAASKHMtpVVLELGGKSPLYIDdSVEgQ 229
Cdd:cd07127 244 REVLAEAgFDPNLVTLAadTPEEPIAQTLaTRPEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVD-STD-D 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 230 LEVAAKRVLWGKLTNSGQTCVAPDYVLC-SPSVQ--------DRFVEASKKVLKDFYGDPAKSDS-FARIVNDRNFDRLE 299
Cdd:cd07127 320 LKAMLRNLAFSLSLYSGQMCTTPQNIYVpRDGIQtddgrksfDEVAADLAAAIDGLLADPARAAAlLGAIQSPDTLARIA 399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26334245 300 KllSATKGKVVVGGQTAK-----GERYIAPTLVANVTGNDSLMSEELFGPILPIVPVKSEEEAIQ 359
Cdd:cd07127 400 E--ARQLGEVLLASEAVAhpefpDARVRTPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIE 462
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
130-358 |
9.21e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 44.89 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 130 GAIAAGNCVVIKPSEVAGSTANVMASLLPKYLDKECYP---VVTGGA---DVANQLLQ-ERFDLVFFTGSPNIGKLVYQA 202
Cdd:PRK15398 152 SMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAAGGPenlVVTVAEptiETAQRLMKhPGIALLVVTGGPAVVKAAMKS 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 203 ASKhmtpVVLELGGKSPLYIDDSVEgqLEVAAKRVLWGKLTNSGQTCVAPDYVLCSPSVQDRFVEASKKvlkdfYGdpak 282
Cdd:PRK15398 232 GKK----AIGAGAGNPPVVVDETAD--IEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEK-----NG---- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26334245 283 sdsfARIVNDRNFDRLEKLLSATKG---KVVVGGQTAK-----GERYIAPT--LVANVTGNDSLMSEELFGPILPIVPVK 352
Cdd:PRK15398 297 ----AVLLTAEQAEKLQKVVLKNGGtvnKKWVGKDAAKileaaGINVPKDTrlLIVETDANHPFVVTELMMPVLPVVRVK 372
|
....*.
gi 26334245 353 SEEEAI 358
Cdd:PRK15398 373 DVDEAI 378
|
|
| |
