|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
2-454 |
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: 767.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 2 NLIEKQfqesKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYATEIGILLKSIKTARKELKNW 81
Cdd:cd07136 2 SLVEKQ----RAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 82 AKTKQVDTPLFMFPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSD 161
Cdd:cd07136 78 MKPKRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 162 FVAVVEGGVEETQTLINLPFDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAG 241
Cdd:cd07136 158 YVAVVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 242 QTCVAPDYILVNRKVKNELIQSFKQSIEEFYGKNIQNSPDFGRIVNTKHFNRLSELLAIHrnEVIFGGHTDENEQYIEPT 321
Cdd:cd07136 238 QTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNG--KIVFGGNTDRETLYIEPT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 322 ILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLANPN 401
Cdd:cd07136 316 ILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPY 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1090914694 402 LPFGGVGASGIGEYHGKYSFDTFSHMKSYIFKSTRLDSSIIYPPYKGKFKYIR 454
Cdd:cd07136 396 LPFGGVGNSGMGSYHGKYSFDTFSHKKSILKKSTWFDLPLRYPPYKGKKKKLK 448
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
8-429 |
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: 670.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 8 FQESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYATEIGILLKSIKTARKELKNWAKTKQV 87
Cdd:cd07087 4 VARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 88 DTPLFMFPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVE 167
Cdd:cd07087 84 SVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 168 GGVEETQTLINLPFDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAP 247
Cdd:cd07087 164 GGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 248 DYILVNRKVKNELIQSFKQSIEEFYGKNIQNSPDFGRIVNTKHFNRLSELLAIHRneVIFGGHTDENEQYIEPTILDGIT 327
Cdd:cd07087 244 DYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGK--VVIGGQVDKEERYIAPTILDDVS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 328 PQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLANPNLPFGGV 407
Cdd:cd07087 322 PDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGGV 401
|
410 420
....*....|....*....|..
gi 1090914694 408 GASGIGEYHGKYSFDTFSHMKS 429
Cdd:cd07087 402 GNSGMGAYHGKAGFDTFSHLKS 423
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
26-430 |
0e+00 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 577.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 26 RKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYATEIGILLKSIKTARKELKNWAKTKQVDTPLFMFPSKSYIKPEPY 105
Cdd:cd07134 22 RIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPLLLFGTKSKIRYEPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 106 GTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEGGVEETQTLINLPFDYIF 185
Cdd:cd07134 102 GVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAEVAQALLELPFDHIF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 186 FTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNELIQSFK 265
Cdd:cd07134 182 FTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 266 QSIEEFYGKN--IQNSPDFGRIVNTKHFNRLSELL--AIHRN-EVIFGGHTDENEQYIEPTILDGITPQSKIMEEEIFGP 340
Cdd:cd07134 262 AEIEKFYGKDaaRKASPDLARIVNDRHFDRLKGLLddAVAKGaKVEFGGQFDAAQRYIAPTVLTNVTPDMKIMQEEIFGP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 341 LLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLANPNLPFGGVGASGIGEYHGKYS 420
Cdd:cd07134 342 VLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGSYHGVYG 421
|
410
....*....|
gi 1090914694 421 FDTFSHMKSY 430
Cdd:cd07134 422 FKAFSHERAV 431
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
4-459 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 576.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 4 IEKQFQESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYATEIGILLKSIKTARKELKNWAK 83
Cdd:PTZ00381 9 IPPIVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 84 TKQVDTPLFMFPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFV 163
Cdd:PTZ00381 89 PEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 164 AVVEGGVEETQTLINLPFDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQT 243
Cdd:PTZ00381 169 RVIEGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 244 CVAPDYILVNRKVKNELIQSFKQSIEEFYGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNEVIFGGHTDENEQYIEPTIL 323
Cdd:PTZ00381 249 CVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKDHGGKVVYGGEVDIENKYVAPTII 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 324 DGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLANPNLP 403
Cdd:PTZ00381 329 VNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLP 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1090914694 404 FGGVGASGIGEYHGKYSFDTFSHMKSYIFKST--RLDSSIIYPPY-KGKFKYIRTFFKN 459
Cdd:PTZ00381 409 FGGVGNSGMGAYHGKYGFDTFSHPKPVLNKSTgnSFDLSLRYPPYtSFKSWVLSFLLKL 467
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
15-446 |
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: 573.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 15 FKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYATEIGILLKSIKTARKELKNWAKTKQVDTPLFMF 94
Cdd:cd07132 11 FSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKPEPVKKNLATL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 95 PSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEGGVEETQ 174
Cdd:cd07132 91 LDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYPVVLGGVEETT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 175 TLINLPFDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNR 254
Cdd:cd07132 171 ELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 255 KVKNELIQSFKQSIEEFYGKNIQNSPDFGRIVNTKHFNRLSELLAihRNEVIFGGHTDENEQYIEPTILDGITPQSKIME 334
Cdd:cd07132 251 EVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLS--GGKVAIGGQTDEKERYIAPTVLTDVKPSDPVMQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 335 EEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLANPNLPFGGVGASGIGE 414
Cdd:cd07132 329 EEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGGVGNSGMGA 408
|
410 420 430
....*....|....*....|....*....|....
gi 1090914694 415 YHGKYSFDTFSHMKSYIFKSTRLDS--SIIYPPY 446
Cdd:cd07132 409 YHGKYSFDTFSHKRSCLVKSLNMEKlnSLRYPPY 442
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
4-431 |
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: 550.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 4 IEKQFQESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYATEIGILLKSIKTARKELKNWAK 83
Cdd:cd07135 7 IDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 84 TKQV-DTPLFMFPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDF 162
Cdd:cd07135 87 DEKVkDGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 163 VAVVEGGVEETQTLINLPFDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQ 242
Cdd:cd07135 167 FQVVQGGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 243 TCVAPDYILVNRKVKNELIQSFKQSIEEFYGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNEVIFGGHTDENEQYIEPTI 322
Cdd:cd07135 247 ICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTKGKVVIGGEMDEATRFIPPTI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 323 LDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLANPNL 402
Cdd:cd07135 327 VSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNA 406
|
410 420
....*....|....*....|....*....
gi 1090914694 403 PFGGVGASGIGEYHGKYSFDTFSHMKSYI 431
Cdd:cd07135 407 PFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
7-433 |
4.82e-176 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 500.09 E-value: 4.82e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 7 QFQESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYA-TEIGILLKSIKTARKELKNWAKTK 85
Cdd:cd07133 3 LLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGHRSRHETLlAEILPSIAGIKHARKHLKKWMKPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 86 QVDTPLFMFPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAV 165
Cdd:cd07133 83 RRHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 166 VEGGVEETQTLINLPFDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCV 245
Cdd:cd07133 163 VTGGADVAAAFSSLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 246 APDYILVNRKVKNELIQSFKQSIEEFYGkNIQNSPDFGRIVNTKHFNRLSELLA--------IHrnEVIFGGHTDENEQY 317
Cdd:cd07133 243 APDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEdarakgarVI--ELNPAGEDFAATRK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 318 IEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHL 397
Cdd:cd07133 320 LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHV 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 1090914694 398 ANPNLPFGGVGASGIGEYHGKYSFDTFSHMKSyIFK 433
Cdd:cd07133 400 AQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP-VFK 434
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
10-429 |
3.24e-166 |
|
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: 474.98 E-value: 3.24e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 10 ESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYATEIGILLKSIKTARKELKNWAKTKQVDT 89
Cdd:cd07137 7 ELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPEKVKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 90 PLFMFPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEGG 169
Cdd:cd07137 87 PLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 170 VEETQTLINLPFDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKF-TNAGQTCVAPD 248
Cdd:cd07137 167 VPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 249 YILVNRKVKNELIQSFKQSIEEFYGKNIQNSPDFGRIVNTKHFNRLSELL--AIHRNEVIFGGHTDENEQYIEPTILDGI 326
Cdd:cd07137 247 YVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLddPSVADKIVHGGERDEKNLYIEPTILLDP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 327 TPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLANPNLPFGG 406
Cdd:cd07137 327 PLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTLPFGG 406
|
410 420
....*....|....*....|...
gi 1090914694 407 VGASGIGEYHGKYSFDTFSHMKS 429
Cdd:cd07137 407 VGESGFGAYHGKFSFDAFSHKKA 429
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
4-458 |
3.88e-148 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 431.07 E-value: 3.88e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 4 IEKQFQESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYATEIGILLKSIKTARKELKNWAK 83
Cdd:PLN02203 8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKKWMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 84 TKQVDTPLFMFPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFV 163
Cdd:PLN02203 88 PKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 164 AVVEGGVEETQTLINLPFDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVD---ETANIKVASDRISFGKF-TN 239
Cdd:PLN02203 168 KVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKWgSC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 240 AGQTCVAPDYILVNRKVKNELIQSFKQSIEEFYGKNIQNSPDFGRIVNTKHFNRLSELLAIHR--NEVIFGGHTDENEQY 317
Cdd:PLN02203 248 AGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRvaASIVHGGSIDEKKLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 318 IEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHL 397
Cdd:PLN02203 328 IEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIQY 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1090914694 398 ANPNLPFGGVGASGIGEYHGKYSFDTFSHMKSYIFKSTRLDSSIIYPPYKG-KFKYIRTFFK 458
Cdd:PLN02203 408 ACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTEFEFRYPPWNDfKLGFLRLVYR 469
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
5-432 |
4.28e-125 |
|
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: 370.39 E-value: 4.28e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 5 EKQFQESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKgSVEAYATEIGILLKSIKTARKELKNWAKT 84
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGK-PIEEALGEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 85 KQVDTPLfmfPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFV 163
Cdd:cd07078 80 VIPSPDP---GELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 164 AVVEGGVEET-QTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAG 241
Cdd:cd07078 157 NVVTGDGDEVgAALASHPrVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 242 QTCVAPDYILVNRKVKNELIQSFKQSIEEFYGKN-IQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENE-- 315
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNpLDPDTDMGPLISAAQLDRVLAYIEDAKAEgakLLCGGKRLEGGkg 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 316 QYIEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLM 395
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 1090914694 396 HlANPNLPFGGVGASGIGEYHGKYSFDTFSHMKSYIF 432
Cdd:cd07078 397 G-AEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
10-456 |
4.37e-124 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 369.76 E-value: 4.37e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 10 ESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYATEIGILLKSIKTARKELKNWAKTKQVDT 89
Cdd:PLN02174 18 ELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 90 PLFMFPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEGG 169
Cdd:PLN02174 98 SLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 170 VEETQTLINLPFDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKF-TNAGQTCVAPD 248
Cdd:PLN02174 178 VTETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 249 YILVNRKVKNELIQSFKQSIEEFYGKNIQNSPDFGRIVNTKHFNRLSELLAIHR--NEVIFGGHTDENEQYIEPTILDGI 326
Cdd:PLN02174 258 YILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDEKEvsDKIVYGGEKDRENLKIAPTILLDV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 327 TPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLANPNLPFGG 406
Cdd:PLN02174 338 PLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGG 417
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1090914694 407 VGASGIGEYHGKYSFDTFSHMKSYIFKSTRLDSSIIYPPY-KGKFKYIRTF 456
Cdd:PLN02174 418 VGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSAVRYPPYsRGKLRLLKAL 468
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
11-432 |
3.81e-102 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 309.16 E-value: 3.81e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 11 SKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYAtEIGILLKSIKTARKELKNWAKTKQVDTP 90
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGPELPSPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 91 LfmfPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEG- 168
Cdd:cd06534 82 P---GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 169 GVEETQTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAP 247
Cdd:cd06534 159 GDEVGAALLSHPrVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 248 DYILVNRKVKNELIQSFKqsieefygkniqnspdfgrivntkhfnrlsellaihrnevifgghtdeneqyiepTILDGIT 327
Cdd:cd06534 239 SRLLVHESIYDEFVEKLV-------------------------------------------------------TVLVDVD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 328 PQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHlANPNLPFGGV 407
Cdd:cd06534 264 PDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIG-VGPEAPFGGV 342
|
410 420
....*....|....*....|....*
gi 1090914694 408 GASGIGEYHGKYSFDTFSHMKSYIF 432
Cdd:cd06534 343 KNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
98-429 |
1.53e-99 |
|
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: 306.28 E-value: 1.53e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIED------VFTsdfvaVVEGGVE 171
Cdd:COG1012 135 AYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEaglpagVLN-----VVTGDGS 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 172 ET-QTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDY 249
Cdd:COG1012 210 EVgAALVAHPdVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASR 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 250 ILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENEQ--YIEPTIL 323
Cdd:COG1012 290 LLVHESIYDEFVERLVAAAKALkVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEgaeLLTGGRRPDGEGgyFVEPTVL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 324 DGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHlANPNLP 403
Cdd:COG1012 370 ADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTG-AVPQAP 448
|
330 340
....*....|....*....|....*.
gi 1090914694 404 FGGVGASGIGEYHGKYSFDTFSHMKS 429
Cdd:COG1012 449 FGGVKQSGIGREGGREGLEEYTETKT 474
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
98-429 |
7.84e-89 |
|
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: 278.26 E-value: 7.84e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEET-QT 175
Cdd:pfam00171 120 AYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVgEA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 176 LINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNR 254
Cdd:pfam00171 200 LVEHPdVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 255 KVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTD-ENEQYIEPTILDGITPQ 329
Cdd:pfam00171 280 SIYDEFVEKLVEAAKKLkVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEgakLLTGGEAGlDNGYFVEPTVLANVTPD 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 330 SKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLAnPNLPFGGVGA 409
Cdd:pfam00171 360 MRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDA-DGLPFGGFKQ 438
|
330 340
....*....|....*....|
gi 1090914694 410 SGIGEYHGKYSFDTFSHMKS 429
Cdd:pfam00171 439 SGFGREGGPYGLEEYTEVKT 458
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
26-431 |
3.12e-82 |
|
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: 261.00 E-value: 3.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 26 RKQQLKLLSKSIKDHETELLESLKIDLGKgSVEAYATEIGILLKSIKTARKELKNWAKTKQVDTPLFMFPSKSYIKPEPY 105
Cdd:cd07099 42 RAQRLLRWKRALADHADELAELLHAETGK-PRADAGLEVLLALEAIDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 106 GTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEETQTLINLPFDYI 184
Cdd:cd07099 121 GVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAgPPQGVLQVVTGDGATGAALIDAGVDKV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 185 FFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNELIQSF 264
Cdd:cd07099 201 AFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 265 KQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELL--AIHRNEVIFGGHTDENEQ--YIEPTILDGITPQSKIMEEEIFG 339
Cdd:cd07099 281 VAKARALrPGADDIGDADIGPMTTARQLDIVRRHVddAVAKGAKALTGGARSNGGgpFYEPTVLTDVPHDMDVMREETFG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 340 PLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLANPNLPFGGVGASGIGEYHGKY 419
Cdd:cd07099 361 PVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGAE 440
|
410
....*....|..
gi 1090914694 420 SFDTFSHMKSYI 431
Cdd:cd07099 441 GLREFCRPKAIA 452
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
26-432 |
5.37e-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: 234.89 E-value: 5.37e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 26 RKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYATEIGILLKSIKTARKELKNWAKTKQVDTPLFMFPSKSYIKPEPY 105
Cdd:cd07098 42 RRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRPESRPGGLLMFYKRARVEYEPL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 106 GTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQ----VVRKVIEDVFTS-DFVAVVEGGVEETQTLINLP 180
Cdd:cd07098 122 GVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGfflsIIRECLAACGHDpDLVQLVTCLPETAEALTSHP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 181 -FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNE 259
Cdd:cd07098 202 vIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 260 LIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELL--AIHRN-EVIFGGH-----TDENEQYIEPTILDGITPQS 330
Cdd:cd07098 282 LLEILTDRVQALrQGPPLDGDVDVGAMISPARFDRLEELVadAVEKGaRLLAGGKryphpEYPQGHYFPPTLLVDVTPDM 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 331 KIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLANPNLPFGGVGAS 410
Cdd:cd07098 362 KIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGS 441
|
410 420
....*....|....*....|..
gi 1090914694 411 GIGEYHGKYSFDTFSHMKSYIF 432
Cdd:cd07098 442 GFGRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
103-429 |
2.57e-64 |
|
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: 213.59 E-value: 2.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIED----------VFTS--DFVAVVEggv 170
Cdd:cd07105 97 EPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEaglpkgvlnvVTHSpeDAPEVVE--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 171 eetqTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDY 249
Cdd:cd07105 174 ----ALIAHPaVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTER 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 250 ILVNRKVKNELIQSFKQSIEEFYGKniqnSPDFGRIVNTKHFNRLSELL--AIHRN-EVIFGGHTDENE--QYIEPTILD 324
Cdd:cd07105 250 IIVHESIADEFVEKLKAAAEKLFAG----PVVLGSLVSAAAADRVKELVddALSKGaKLVVGGLADESPsgTSMPPTILD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 325 GITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHlANPNLPF 404
Cdd:cd07105 326 NVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVH-DEPTLPH 404
|
330 340
....*....|....*....|....*
gi 1090914694 405 GGVGASGIGEYHGKYSFDTFSHMKS 429
Cdd:cd07105 405 GGVKSSGYGRFNGKWGIDEFTETKW 429
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
103-431 |
4.69e-63 |
|
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: 210.75 E-value: 4.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEE-TQTLINLP 180
Cdd:cd07103 116 QPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSALALAELAEEAgLPAGVLNVVTGSPAEiGEALCASP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 181 -FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNE 259
Cdd:cd07103 196 rVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 260 LIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELL--AIHRN-EVIFGGHTDENEQY-IEPTILDGITPQSKIME 334
Cdd:cd07103 276 FVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALVedAVAKGaKVLTGGKRLGLGGYfYEPTVLTDVTDDMLIMN 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 335 EEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMhlANPNLPFGGVGASGIGE 414
Cdd:cd07103 356 EETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLI--SDAEAPFGGVKESGLGR 433
|
330
....*....|....*..
gi 1090914694 415 YHGKYSFDTFSHMKsYI 431
Cdd:cd07103 434 EGGKEGLEEYLETK-YV 449
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
103-429 |
9.04e-62 |
|
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: 207.58 E-value: 9.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKV-IEDVFTSDFVAVVEG-GVEETQTLINLP 180
Cdd:cd07118 118 EPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELlIEAGLPAGVVNIVTGyGATVGQAMTEHP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 181 -FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNE 259
Cdd:cd07118 198 dVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 260 LIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENE--QYIEPTILDGITPQSKIM 333
Cdd:cd07118 278 FVAAVVARSRKVrVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEgatLLLGGERLASAagLFYQPTIFTDVTPDMAIA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 334 EEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMhlANPNLPFGGVGASGIG 413
Cdd:cd07118 358 REEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLD--GSPELPFGGFKQSGIG 435
|
330
....*....|....*.
gi 1090914694 414 EYHGKYSFDTFSHMKS 429
Cdd:cd07118 436 RELGRYGVEEYTELKT 451
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
98-429 |
1.05e-59 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 202.02 E-value: 1.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEET-QT 175
Cdd:cd07093 111 NYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAgLPPGVVNVVHGFGPEAgAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 176 LINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNR 254
Cdd:cd07093 191 LVAHPdVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 255 KVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDE-----NEQYIEPTILDG 325
Cdd:cd07093 271 SIYDEFLERFVERAKALkVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEgatILTGGGRPElpdleGGYFVEPTVITG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 326 ITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLM-HLanpNLPF 404
Cdd:cd07093 351 LDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEAGTVWVNCWLVrDL---RTPF 427
|
330 340
....*....|....*....|....*
gi 1090914694 405 GGVGASGIGEYHGKYSFDTFSHMKS 429
Cdd:cd07093 428 GGVKASGIGREGGDYSLEFYTELKN 452
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
98-428 |
3.46e-59 |
|
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: 200.06 E-value: 3.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVV-RKVIED------VFTsdfvaVVEGGV 170
Cdd:cd07104 92 SMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiAEIFEEaglpkgVLN-----VVPGGG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 171 EET-QTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPD 248
Cdd:cd07104 167 SEIgDALVEHPrVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 249 YILVNRKVKNELIQSFKQSIEEF-YGKniQNSPD--FGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENeqYIEPTI 322
Cdd:cd07104 247 RILVHESVYDEFVEKLVAKAKALpVGD--PRDPDtvIGPLINERQVDRVHAIVEDAVAAgarLLTGGTYEGL--FYQPTV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 323 LDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHlANPNL 402
Cdd:cd07104 323 LSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVN-DEPHV 401
|
330 340
....*....|....*....|....*.
gi 1090914694 403 PFGGVGASGIGEYHGKYSFDTFSHMK 428
Cdd:cd07104 402 PFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
61-432 |
3.04e-58 |
|
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: 198.20 E-value: 3.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 61 ATEIGillKSIKTARKELknwakTKQVDTPLF-----------MFP------SKS---YIKPEPYGTILIIGPFNYPVQL 120
Cdd:cd07149 68 ALEAG---KPIKDARKEV-----DRAIETLRLsaeeakrlageTIPfdaspgGEGrigFTIREPIGVVAAITPFNFPLNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 121 LFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEET-QTLINLP-FDYIFFTGSENVGRIVY 197
Cdd:cd07149 140 VAHKVGPAIAAGNAVVLKPASQTPLSALKLAELLLEAgLPKGALNVVTGSGETVgDALVTDPrVRMISFTGSPAVGEAIA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 198 EATSknLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNELIQSFKQSIEEF-YGKNI 276
Cdd:cd07149 220 RKAG--LKKVTLELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLvVGDPL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 277 QNSPDFGRIVNTKHFNRLSELL--AIHRN-EVIFGGHTDENeqYIEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEA 353
Cdd:cd07149 298 DEDTDVGPMISEAEAERIEEWVeeAVEGGaRLLTGGKRDGA--ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 354 IDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTlmhlanPN-----LPFGGVGASGIGEYHGKYSFDTFSHMK 428
Cdd:cd07149 376 IAMANDSPYGLQAGVFTNDLQKALKAARELEVGGVMINDS------STfrvdhMPYGGVKESGTGREGPRYAIEEMTEIK 449
|
....
gi 1090914694 429 SYIF 432
Cdd:cd07149 450 LVCF 453
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
26-424 |
3.82e-58 |
|
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: 198.26 E-value: 3.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 26 RKQQLKLLSKSIKDHETELleslkidlgkgsVEAYATEIGillKSIKTARKELK----------NWAKTKQVDtplfMFP 95
Cdd:cd07088 59 RAAYLRKLADLIRENADEL------------AKLIVEEQG---KTLSLARVEVEftadyidymaEWARRIEGE----IIP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 96 SKS-----YIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEG- 168
Cdd:cd07088 120 SDRpneniFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGr 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 169 GVEETQTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAP 247
Cdd:cd07088 200 GSVVGDALVAHPkVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 248 DYILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENE--QYIEPT 321
Cdd:cd07088 280 ERVYVHEDIYDEFMEKLVEKMKAVkVGDPFDAATDMGPLVNEAALDKVEEMVERAVEAgatLLTGGKRPEGEkgYFYEPT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 322 ILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTlmhlaNPN 401
Cdd:cd07088 360 VLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRE-----NFE 434
|
410 420
....*....|....*....|....*.
gi 1090914694 402 LPFG---GVGASGIGEYHGKYSFDTF 424
Cdd:cd07088 435 AMQGfhaGWKKSGLGGADGKHGLEEY 460
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
25-432 |
3.87e-57 |
|
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: 195.54 E-value: 3.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 25 FRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYATEIGILLKSIKTARKELKNWAKTKQV-DTPLFMFPSKSYIKPE 103
Cdd:cd07089 43 ERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQVDGPIGHLRYFADLADSFPWEFDLpVPALRGGPGRRVVRRE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVftsDF----VAVVEGGVEET-QTLIN 178
Cdd:cd07089 123 PVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEIIAET---DLpagvVNVVTGSDNAVgEALTT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 179 LP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVK 257
Cdd:cd07089 200 DPrVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRY 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 258 NELIQSFKQSIEEF-YGKniQNSPD--FGRIVNTKHFNRLSELLAIHRNE----VIFGGHTDENEQ--YIEPTILDGITP 328
Cdd:cd07089 280 DEVVEALAAAFEALpVGD--PADPGtvMGPLISAAQRDRVEGYIARGRDEgarlVTGGGRPAGLDKgfYVEPTLFADVDN 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 329 QSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTlmHLANPNLPFGGVG 408
Cdd:cd07089 358 DMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRVARRIRTGSVGINGG--GGYGPDAPFGGYK 435
|
410 420
....*....|....*....|....
gi 1090914694 409 ASGIGEYHGKYSFDTFSHMKSYIF 432
Cdd:cd07089 436 QSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
98-429 |
4.96e-57 |
|
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: 195.08 E-value: 4.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEET-QT 175
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAgFPPGVVNVVTGFGPETgEA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 176 LINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNR 254
Cdd:cd07114 193 LVEHPlVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQR 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 255 KVKNELIQSFKQSIeefygKNI------QNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENE-----QYIEP 320
Cdd:cd07114 273 SIYDEFVERLVARA-----RAIrvgdplDPETQMGPLATERQLEKVERYVARAREEgarVLTGGERPSGAdlgagYFFEP 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 321 TILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDtlMHLANP 400
Cdd:cd07114 348 TILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YRALSP 425
|
330 340
....*....|....*....|....*....
gi 1090914694 401 NLPFGGVGASGIGEYHGKYSFDTFSHMKS 429
Cdd:cd07114 426 SSPFGGFKDSGIGRENGIEAIREYTQTKS 454
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
103-429 |
1.13e-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: 1.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEG-GVEETQTLINLP 180
Cdd:cd07109 116 EPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAgLPAGALNVVTGlGAEAGAALVAHP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 181 -FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNE 259
Cdd:cd07109 196 gVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 260 LIQSFKQSIEEF-YGKNIQNsPDFGRIVNTKHFNRLSELLAIHR---NEVIFGGHTDENEQ----YIEPTILDGITPQSK 331
Cdd:cd07109 276 VLERLVERFRALrVGPGLED-PDLGPLISAKQLDRVEGFVARARargARIVAGGRIAEGAPaggyFVAPTLLDDVPPDSR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 332 IMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELS---------FGGGAIndtlmhlanpNL 402
Cdd:cd07109 355 LAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRagqvfvnnyGAGGGI----------EL 424
|
330 340
....*....|....*....|....*..
gi 1090914694 403 PFGGVGASGIGEYHGKYSFDTFSHMKS 429
Cdd:cd07109 425 PFGGVKKSGHGREKGLEALYNYTQTKT 451
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
26-431 |
1.45e-56 |
|
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: 193.72 E-value: 1.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 26 RKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYAtEIGILLKSIKTARKELKNW-AKTKQVDTPLFMFPSKSYIKPEP 104
Cdd:cd07145 45 RYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV-EVERTIRLFKLAAEEAKVLrGETIPVDAYEYNERRIAFTVREP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 105 YGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEET--QTLINLPF 181
Cdd:cd07145 124 IGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVgdEIVTNPKV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 182 DYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNELI 261
Cdd:cd07145 204 NMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 262 QSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENeQYIEPTILDGITPQSKIMEEEI 337
Cdd:cd07145 284 KLLVEKVKKLkVGDPLDESTDLGPLISPEAVERMENLVNDAVEKggkILYGGKRDEG-SFFPPTVLENDTPDMIVMKEEV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 338 FGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTlMHLANPNLPFGGVGASGIGEYHG 417
Cdd:cd07145 363 FGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDINRALKVARELEAGGVVINDS-TRFRWDNLPFGGFKKSGIGREGV 441
|
410
....*....|....
gi 1090914694 418 KYSFDTFSHMKSYI 431
Cdd:cd07145 442 RYTMLEMTEEKTIV 455
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
97-428 |
8.92e-56 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 191.77 E-value: 8.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 97 KSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEET-Q 174
Cdd:cd07150 112 VSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVgD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 175 TLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVN 253
Cdd:cd07150 192 ELVDDPrVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 254 RKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELL--AIHRN-EVIFGGHTDENeqYIEPTILDGITPQ 329
Cdd:cd07150 272 EPVYDEFVKKFVARASKLkVGDPRDPDTVIGPLISPRQVERIKRQVedAVAKGaKLLTGGKYDGN--FYQPTVLTDVTPD 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 330 SKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHlANPNLPFGGVGA 409
Cdd:cd07150 350 MRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTIL-DEAHVPFGGVKA 428
|
330
....*....|....*....
gi 1090914694 410 SGIGEYHGKYSFDTFSHMK 428
Cdd:cd07150 429 SGFGREGGEWSMEEFTELK 447
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
104-429 |
6.15e-55 |
|
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: 190.25 E-value: 6.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQ-VVRKVIEDVFTSDFVAVVEGGVEET-QTLINLP- 180
Cdd:cd07131 135 PIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALkLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPd 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 181 FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNEL 260
Cdd:cd07131 215 VDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEF 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 261 IQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGH--TDENEQ---YIEPTILDGITPQSK 331
Cdd:cd07131 295 LKRFVERAKRLrVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEgatLLLGGErlTGGGYEkgyFVEPTVFTDVTPDMR 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 332 IMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHlANPNLPFGGVGASG 411
Cdd:cd07131 375 IAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIG-AEVHLPFGGVKKSG 453
|
330
....*....|....*....
gi 1090914694 412 IGEYHGKYS-FDTFSHMKS 429
Cdd:cd07131 454 NGHREAGTTaLDAFTEWKA 472
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
31-429 |
7.27e-55 |
|
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: 189.73 E-value: 7.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 31 KLLSK---SIKDHETEL--LESLkiDLGKGSVEAYATEIGIllkSIKTARkELKNWA-----KTKQVDTPLFmfpskSYI 100
Cdd:cd07091 69 RLLNKladLIERDRDELaaLESL--DNGKPLEESAKGDVAL---SIKCLR-YYAGWAdkiqgKTIPIDGNFL-----AYT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 101 KPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEG-GVEETQTLIN 178
Cdd:cd07091 138 RREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGfGPTAGAAISS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 179 LP-FDYIFFTGSENVGRIVYEATSK-NLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKV 256
Cdd:cd07091 218 HMdVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 257 KNELIQSFKQSIEEFY-GKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENEQY-IEPTILDGITPQSK 331
Cdd:cd07091 298 YDEFVEKFKARAEKRVvGDPFDPDTFQGPQVSKAQFDKILSYIESGKKEgatLLTGGERHGSKGYfIQPTVFTDVKDDMK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 332 IMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDtlMHLANPNLPFGGVGASG 411
Cdd:cd07091 378 IAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNT--YNVFDAAVPFGGFKQSG 455
|
410
....*....|....*...
gi 1090914694 412 IGEYHGKYSFDTFSHMKS 429
Cdd:cd07091 456 FGRELGEEGLEEYTQVKA 473
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
99-429 |
3.11e-54 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 188.39 E-value: 3.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 99 YIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEG-GVEETQTL 176
Cdd:cd07144 139 YTLHEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGyGAVAGSAL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 177 INLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRK 255
Cdd:cd07144 219 AEHPdVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQES 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 256 VKNELIQSFKQSIEEFY--GKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGG--HTDENEQ--YIEPTILDGI 326
Cdd:cd07144 299 IYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEgakLVYGGekAPEGLGKgyFIPPTIFTDV 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 327 TPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTlmHLANPNLPFGG 406
Cdd:cd07144 379 PQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSS--NDSDVGVPFGG 456
|
330 340
....*....|....*....|...
gi 1090914694 407 VGASGIGEYHGKYSFDTFSHMKS 429
Cdd:cd07144 457 FKMSGIGRELGEYGLETYTQTKA 479
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
79-429 |
9.65e-54 |
|
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: 186.97 E-value: 9.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 79 KNWAKTKQVDTPLFmfpskSYIKPEPYGTILIIGPFNYPVqLLFEPLIG-AIAAGNNAIIKPSELTPHVAQVVRKVIEDV 157
Cdd:cd07143 124 KIHGQVIETDIKKL-----TYTRHEPIGVCGQIIPWNFPL-LMCAWKIApALAAGNTIVLKPSELTPLSALYMTKLIPEA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 158 -FTSDFVAVVEGGVEETQTLI--NLPFDYIFFTGSENVGRIVYEATSK-NLVPVTLELGGKSPVIVDETANIKVASDRIS 233
Cdd:cd07143 198 gFPPGVINVVSGYGRTCGNAIssHMDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 234 FGKFTNAGQTCVAPDYILVNRKVKNELIQSFKQSIEEF-----YGKNIQNSPDFGRIvntkHFNRLSELLAIHRNE---V 305
Cdd:cd07143 278 YGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLkvgdpFAEDTFQGPQVSQI----QYERIMSYIESGKAEgatV 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 306 IFGGHTDENEQY-IEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELS 384
Cdd:cd07143 354 ETGGKRHGNEGYfIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALK 433
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1090914694 385 FGGGAINDtlMHLANPNLPFGGVGASGIGEYHGKYSFDTFSHMKS 429
Cdd:cd07143 434 AGTVWVNC--YNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKA 476
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
15-429 |
4.32e-53 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 184.27 E-value: 4.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 15 FKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYAtEIGILLKSIK-TARKELKNwakTKQVDTPlfm 93
Cdd:cd07106 32 FPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-EVGGAVAWLRyTASLDLPD---EVIEDDD--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 94 fPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEGGVEET 173
Cdd:cd07106 105 -TRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEVLPPGVLNVVSGGDELG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 174 QTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILV 252
Cdd:cd07106 184 PALTSHPdIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 253 NRKVKNELIQSFKQSIEEFY-GKNIQNSPDFGRIVNTKHFNRLSELLA-IHRN--EVIFGGHTDENEQY-IEPTILDGIT 327
Cdd:cd07106 264 HESIYDEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEdAKAKgaKVLAGGEPLDGPGYfIPPTIVDDPP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 328 PQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINdtlMHLA-NPNLPFGG 406
Cdd:cd07106 344 EGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWIN---THGAlDPDAPFGG 420
|
410 420
....*....|....*....|...
gi 1090914694 407 VGASGIGEYHGKYSFDTFSHMKS 429
Cdd:cd07106 421 HKQSGIGVEFGIEGLKEYTQTQV 443
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
99-429 |
1.06e-52 |
|
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: 183.41 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 99 YIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEET-QTL 176
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAgAAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 177 INLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRK 255
Cdd:cd07115 192 VEHPdVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 256 VKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTD-ENEQYIEPTILDGITPQS 330
Cdd:cd07115 272 IYDEFLERFTSLARSLrPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEgarLLTGGKRPgARGFFVEPTIFAAVPPEM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 331 KIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINdtLMHLANPNLPFGGVGAS 410
Cdd:cd07115 352 RIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQS 429
|
330
....*....|....*....
gi 1090914694 411 GIGEYHGKYSFDTFSHMKS 429
Cdd:cd07115 430 GFGREMGREALDEYTEVKS 448
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
26-432 |
2.88e-52 |
|
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: 182.25 E-value: 2.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 26 RKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYAtEIGILLKSIKTARKELK-NWAKTKQVDTPLFMFPSKSYIKPEP 104
Cdd:cd07094 45 RMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV-EVDRAIDTLRLAAEEAErIRGEEIPLDATQGSDNRLAWTIREP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 105 YGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVI------EDVFTsdfVAVVEGGVEETQTLIN 178
Cdd:cd07094 124 VGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILveagvpEGVLQ---VVTGEREVLGDAFAAD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 179 LPFDYIFFTGSENVGRIVYEATSKNlvPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKN 258
Cdd:cd07094 201 ERVAMLSFTGSAAVGEALRANAGGK--RIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 259 ELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELL--AIHRNEVIFGGHTDENEQYiEPTILDGITPQSKIMEE 335
Cdd:cd07094 279 EFIEAFVAAVKKLkVGDPLDEDTDVGPLISEEAAERVERWVeeAVEAGARLLCGGERDGALF-KPTVLEDVPRDTKLSTE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 336 EIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTlMHLANPNLPFGGVGASGIGEY 415
Cdd:cd07094 358 ETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDS-SAFRTDWMPFGGVKESGVGRE 436
|
410
....*....|....*..
gi 1090914694 416 HGKYSFDTFSHMKSYIF 432
Cdd:cd07094 437 GVPYAMEEMTEEKTVVI 453
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
4-430 |
4.52e-52 |
|
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: 181.68 E-value: 4.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 4 IEKQFQESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGsVEAYATEIGILLKS----IKTARKELK 79
Cdd:cd07102 20 VRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP-IAQAGGEIRGMLERarymISIAEEALA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 80 NwakTKQVDTPLFmfpsKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTP----HVAQVVRK--V 153
Cdd:cd07102 99 D---IRVPEKDGF----ERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPlcgeRFAAAFAEagL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 154 IEDVFtsdfvAVVEGGVEETQTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRI 232
Cdd:cd07102 172 PEGVF-----QVLHLSHETSAALIADPrIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 233 SFGKFTNAGQTCVAPDYILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELL--AIHRNE--VIF 307
Cdd:cd07102 247 VDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAADFVRAQIadAIAKGAraLID 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 308 GGHTDENEQ---YIEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELS 384
Cdd:cd07102 327 GALFPEDKAggaYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLE 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1090914694 385 FGGGAIN--DTLmhlaNPNLPFGGVGASGIGEYHGKYSFDTFSHMKSY 430
Cdd:cd07102 407 TGTVFMNrcDYL----DPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
37-428 |
9.88e-52 |
|
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: 181.35 E-value: 9.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 37 IKDHETELLESLKIDLG----KGSVEAYATeIGILLKSIK-TARKElknwAKTKQVDTPlfmfPSKSYIKPEPYGTILII 111
Cdd:cd07151 67 LEERRDEIVEWLIRESGstriKANIEWGAA-MAITREAATfPLRME----GRILPSDVP----GKENRVYREPLGVVGVI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 112 GPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQV-VRKVIEDVFTSDFV--AVVEGGVEETQTLINLPF-DYIFFT 187
Cdd:cd07151 138 SPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLlLAKIFEEAGLPKGVlnVVVGAGSEIGDAFVEHPVpRLISFT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 188 GSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNELIQSFKQS 267
Cdd:cd07151 218 GSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVER 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 268 IEEF-YGKniQNSPD--FGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENeqYIEPTILDGITPQSKIMEEEIFGPL 341
Cdd:cd07151 298 VKALpYGD--PSDPDtvVGPLINESQVDGLLDKIEQAVEEgatLLVGGEAEGN--VLEPTVLSDVTNDMEIAREEIFGPV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 342 LPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHlANPNLPFGGVGASGIGEYHGKYSF 421
Cdd:cd07151 374 APIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVN-DEPHVPFGGEKNSGLGRFNGEWAL 452
|
....*..
gi 1090914694 422 DTFSHMK 428
Cdd:cd07151 453 EEFTTDK 459
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
98-429 |
2.65e-51 |
|
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: 179.86 E-value: 2.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEG-GVEETQTL 176
Cdd:cd07108 111 TYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGyGEECGAAL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 177 INLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFG-KFTNAGQTCVAPDYILVNR 254
Cdd:cd07108 191 VDHPdVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 255 KVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRN----EVIFGG-----HTDENEQYIEPTILD 324
Cdd:cd07108 271 DIYDAFLEKLVAKLSKLkIGDPLDEATDIGAIISEKQFAKVCGYIDLGLStsgaTVLRGGplpgeGPLADGFFVQPTIFS 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 325 GITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLanPNLPF 404
Cdd:cd07108 351 GVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQ--PGQSY 428
|
330 340
....*....|....*....|....*.
gi 1090914694 405 GGVGASGIG-EYHGKYSFDTFSHMKS 429
Cdd:cd07108 429 GGFKQSGLGrEASLEGMLEHFTQKKT 454
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
95-428 |
7.48e-51 |
|
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: 179.43 E-value: 7.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 95 PSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEET 173
Cdd:cd07119 125 HVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATV 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 174 QTLI--NLPFDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYIL 251
Cdd:cd07119 205 GAELaeSPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 252 VNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHT-DENE----QYIEPTI 322
Cdd:cd07119 285 VEESIHDKFVAALAERAKKIkLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEEgarLVCGGKRpTGDElakgYFVEPTI 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 323 LDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDtlMHLANPNL 402
Cdd:cd07119 365 FDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWIND--YHPYFAEA 442
|
330 340
....*....|....*....|....*.
gi 1090914694 403 PFGGVGASGIGEYHGKYSFDTFSHMK 428
Cdd:cd07119 443 PWGGYKQSGIGRELGPTGLEEYQETK 468
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
98-428 |
7.64e-51 |
|
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: 178.67 E-value: 7.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEGGVEET-QTL 176
Cdd:cd07092 112 SMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAgDAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 177 INLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRK 255
Cdd:cd07092 192 VAHPrVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 256 VKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRN--EVIFGGH-TDENEQYIEPTILDGITPQSK 331
Cdd:cd07092 272 VYDEFVAALVEAVSAIrVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAhaRVLTGGRrAEGPGYFYEPTVVAGVAQDDE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 332 IMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLAnpNLPFGGVGASG 411
Cdd:cd07092 352 IVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVWVNTHIPLAA--EMPHGGFKQSG 429
|
330
....*....|....*..
gi 1090914694 412 IGEYHGKYSFDTFSHMK 428
Cdd:cd07092 430 YGKDLSIYALEDYTRIK 446
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
103-432 |
2.76e-50 |
|
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: 177.31 E-value: 2.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIED------VFTsdfvaVVEG-GVEETQT 175
Cdd:cd07138 129 EPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEaglpagVFN-----LVNGdGPVVGEA 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 176 LINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNR 254
Cdd:cd07138 204 LSAHPdVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPR 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 255 KVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGG--HTDENEQ--YIEPTILDGI 326
Cdd:cd07138 284 SRYAEAEEIAAAAAEAYvVGDPRDPATTLGPLASAAQFDRVQGYIQKGIEEgarLVAGGpgRPEGLERgyFVKPTVFADV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 327 TPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTlmhLANPNLPFGG 406
Cdd:cd07138 364 TPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGA---AFNPGAPFGG 440
|
330 340
....*....|....*....|....*.
gi 1090914694 407 VGASGIGEYHGKYSFDTFSHMKSYIF 432
Cdd:cd07138 441 YKQSGNGREWGRYGLEEFLEVKSIQG 466
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
99-429 |
2.93e-50 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 177.11 E-value: 2.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 99 YIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFV-AVVEGGVEETQTLI 177
Cdd:cd07090 111 YTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAGLPDGVfNVVQGGGETGQLLC 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 178 NLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKV 256
Cdd:cd07090 191 EHPdVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 257 KNELIQSF-KQSIEEFYGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGG---HTD---ENEQYIEPTILDGI 326
Cdd:cd07090 271 KDEFTERLvERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQEgakVLCGGervVPEdglENGFYVSPCVLTDC 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 327 TPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDtlMHLANPNLPFGG 406
Cdd:cd07090 351 TDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVEVPFGG 428
|
330 340
....*....|....*....|...
gi 1090914694 407 VGASGIGEYHGKYSFDTFSHMKS 429
Cdd:cd07090 429 YKQSGFGRENGTAALEHYTQLKT 451
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
103-413 |
5.41e-50 |
|
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: 5.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEG-GVEETQTLINLP 180
Cdd:cd07124 165 RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPGpGEEVGDYLVEHP 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 181 -FDYIFFTGSENVGRIVYEATSK------NLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVN 253
Cdd:cd07124 245 dVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVH 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 254 RKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE--VIFGGHTDENEQ---YIEPTILDGIT 327
Cdd:cd07124 325 ESVYDEFLERLVERTKALkVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEgrLLLGGEVLELAAegyFVQPTIFADVP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 328 PQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGG--------GAINDtlMHlan 399
Cdd:cd07124 405 PDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNlyanrkitGALVG--RQ--- 479
|
330
....*....|....
gi 1090914694 400 pnlPFGGVGASGIG 413
Cdd:cd07124 480 ---PFGGFKMSGTG 490
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
98-428 |
8.46e-50 |
|
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: 176.38 E-value: 8.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEG-GVEETQTL 176
Cdd:cd07559 130 SYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGfGSEAGKPL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 177 INLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIV-----DETANIKVASDRISFGKFTNAGQTCVAPDYI 250
Cdd:cd07559 210 ASHPrIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFAFNQGEVCTCPSRA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 251 LVNRKVKNELIqsfKQSIEEFYGKNIQNSPD----FGRIVNTKHFNRLSELLAIHRNE---VIFGGH-----TDENEQYI 318
Cdd:cd07559 290 LVQESIYDEFI---ERAVERFEAIKVGNPLDpetmMGAQVSKDQLEKILSYVDIGKEEgaeVLTGGErltlgGLDKGYFY 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 319 EPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINdtLMHLA 398
Cdd:cd07559 367 EPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVN--CYHQY 444
|
330 340 350
....*....|....*....|....*....|.
gi 1090914694 399 NPNLPFGGVGASGIG-EYHgKYSFDTFSHMK 428
Cdd:cd07559 445 PAHAPFGGYKKSGIGrETH-KMMLDHYQQTK 474
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
26-429 |
1.56e-49 |
|
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: 175.10 E-value: 1.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 26 RKQQLKLLSKSIKDHETEL--LESLkiDLGKGSVEAYATEIGillKSIKTARkelknW---AKTKQVDTplfMFPSK--- 97
Cdd:cd07112 50 RKAVLLRLADLIEAHRDELalLETL--DMGKPISDALAVDVP---SAANTFR-----WyaeAIDKVYGE---VAPTGpda 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 -SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTP----HVAQVVRK--VIEDVFTsdfvaVVEGGV 170
Cdd:cd07112 117 lALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPltalRLAELALEagLPAGVLN-----VVPGFG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 171 EETQTLINL--PFDYIFFTGSENVGR--IVYEATSkNLVPVTLELGGKSPVIV-DETANIKVASDRISFGKFTNAGQTCV 245
Cdd:cd07112 192 HTAGEALGLhmDVDALAFTGSTEVGRrfLEYSGQS-NLKRVWLECGGKSPNIVfADAPDLDAAAEAAAAGIFWNQGEVCS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 246 APDYILVNRKVKNELIQSFKQSIEEFYGKNIQN-SPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENEQ---YI 318
Cdd:cd07112 271 AGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDpATRMGALVSEAHFDKVLGYIESGKAEgarLVAGGKRVLTETggfFV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 319 EPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAIN--DTlmh 396
Cdd:cd07112 351 EPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDLSRAHRVARRLRAGTVWVNcfDE--- 427
|
410 420 430
....*....|....*....|....*....|...
gi 1090914694 397 lANPNLPFGGVGASGIGEYHGKYSFDTFSHMKS 429
Cdd:cd07112 428 -GDITTPFGGFKQSGNGRDKSLHALDKYTELKT 459
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
93-429 |
3.56e-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: 3.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 93 MFPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVE 171
Cdd:cd07139 126 SGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPADRE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 172 ETQTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYI 250
Cdd:cd07139 206 VGEYLVRHPgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 251 LVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE----VIFGGHTDENEQ--YIEPTIL 323
Cdd:cd07139 286 LVPRSRYDEVVEALAAAVAALkVGDPLDPATQIGPLASARQRERVEGYIAKGRAEgarlVTGGGRPAGLDRgwFVEPTLF 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 324 DGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMhlaNPNLP 403
Cdd:cd07139 366 ADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRL---DFGAP 442
|
330 340
....*....|....*....|....*.
gi 1090914694 404 FGGVGASGIGEYHGKYSFDTFSHMKS 429
Cdd:cd07139 443 FGGFKQSGIGREGGPEGLDAYLETKS 468
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
4-430 |
8.99e-49 |
|
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: 172.26 E-value: 8.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 4 IEKQFQESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYAtEIGillKSIKTAR---KELKN 80
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVE---KCAWICRyyaENAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 81 WAKTKQVDTPLfmfpSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVvrkvIEDVFTs 160
Cdd:cd07100 77 FLADEPIETDA----GKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALA----IEELFR- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 161 dfvavvEGGVEEtQTLINLPFDY--------------IFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIK 226
Cdd:cd07100 148 ------EAGFPE-GVFQNLLIDSdqveaiiadprvrgVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 227 VASDRISFGKFTNAGQTCVAPDYILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELL--AI-HR 302
Cdd:cd07100 221 KAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALkVGDPMDEDTDLGPLARKDLRDELHEQVeeAVaAG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 303 NEVIFGGHT-DENEQYIEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLE 381
Cdd:cd07100 301 ATLLLGGKRpDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVAR 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1090914694 382 ELSFGGGAINDtlMHLANPNLPFGGVGASGIGEYHGKYSFDTFSHMKSY 430
Cdd:cd07100 381 RLEAGMVFING--MVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
4-433 |
1.99e-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: 172.92 E-value: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 4 IEKQFQESKQFFK---THQTKDIKFRKQQLKLLSKSIKDHETEL--LESLkiDLGKGSVEAYATEIGILLKSIKT-ARKE 77
Cdd:cd07141 46 VDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYLasLETL--DNGKPFSKSYLVDLPGAIKVLRYyAGWA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 78 LKNWAKTKQVDTPLFmfpskSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTP----HVAQVVRkv 153
Cdd:cd07141 124 DKIHGKTIPMDGDFF-----TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPltalYLASLIK-- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 154 iEDVFTSDFVAVVEG-GVEETQTLINLP-FDYIFFTGSENVGRIVYEATSK-NLVPVTLELGGKSPVIVDETANIKVASD 230
Cdd:cd07141 197 -EAGFPPGVVNVVPGyGPTAGAAISSHPdIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 231 RISFGKFTNAGQTCVAPDYILVNRKVKNELIqsfKQSIEEFYGKNIQN----SPDFGRIVNTKHFNRLSELLAIHRNE-- 304
Cdd:cd07141 276 QAHEALFFNMGQCCCAGSRTFVQESIYDEFV---KRSVERAKKRVVGNpfdpKTEQGPQIDEEQFKKILELIESGKKEga 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 305 --VIFGGHTDENEQYIEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEE 382
Cdd:cd07141 353 klECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNA 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1090914694 383 LSFGGGAINdTLMHLAnPNLPFGGVGASGIGEYHGKYSFDTFSHMKSYIFK 433
Cdd:cd07141 433 LRAGTVWVN-CYNVVS-PQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
93-417 |
5.09e-48 |
|
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: 170.94 E-value: 5.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 93 MFPSK----SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVrkvIEDVFT-----SDFV 163
Cdd:cd07152 95 ILPSApgrlSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVV---IARLFEeaglpAGVL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 164 AVVEGGVEETQTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQ 242
Cdd:cd07152 172 HVLPGGADAGEALVEDPnVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQ 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 243 TCVAPDYILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDenEQYI 318
Cdd:cd07152 252 ICMAAGRHLVHESVADAYTAKLAAKAKHLpVGDPATGQVALGPLINARQLDRVHAIVDDSVAAgarLEAGGTYD--GLFY 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 319 EPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAIND-TLMHl 397
Cdd:cd07152 330 RPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDqTVND- 408
|
330 340
....*....|....*....|
gi 1090914694 398 aNPNLPFGGVGASGIGEYHG 417
Cdd:cd07152 409 -EPHNPFGGMGASGNGSRFG 427
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
95-428 |
8.89e-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: 170.76 E-value: 8.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 95 PSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVA-VVEGGVEET 173
Cdd:TIGR01804 124 PSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFnVVQGDGAEV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 174 -QTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYIL 251
Cdd:TIGR01804 204 gPLLVNHPdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVF 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 252 VNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENEQ-----YIEPTI 322
Cdd:TIGR01804 284 VHKKIKERFLARLVERTERIkLGDPFDEATEMGPLISAAHRDKVLSYIEKGKAEgatLATGGGRPENVGlqngfFVEPTV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 323 LDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDtlMHLANPNL 402
Cdd:TIGR01804 364 FADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINT--YNLYPAEA 441
|
330 340
....*....|....*....|....*.
gi 1090914694 403 PFGGVGASGIGEYHGKYSFDTFSHMK 428
Cdd:TIGR01804 442 PFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
104-413 |
1.67e-47 |
|
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: 170.05 E-value: 1.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDF-----VAVVEGGVEETQTLIN 178
Cdd:cd07086 133 PLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNGlppgvVNLVTGGGDGGELLVH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 179 LP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVK 257
Cdd:cd07086 213 DPrVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVY 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 258 NELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENEQ---YIEPTILDGITPQS 330
Cdd:cd07086 293 DEFLERLVKAYKQVrIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQggtVLTGGKRIDGGEpgnYVEPTIVTGVTDDA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 331 KIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENttncvlEELSFGGGAINDTlmHLANPN--------- 401
Cdd:cd07086 373 RIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLR------EAFRWLGPKGSDC--GIVNVNiptsgaeig 444
|
330
....*....|..
gi 1090914694 402 LPFGGVGASGIG 413
Cdd:cd07086 445 GAFGGEKETGGG 456
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
103-432 |
2.80e-47 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 169.87 E-value: 2.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHV----------AQVVRKVIEdVFTSDFVAVVEGGVEE 172
Cdd:PLN02278 159 QPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTalaaaelalqAGIPPGVLN-VVMGDAPEIGDALLAS 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 173 TQTlinlpfDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILV 252
Cdd:PLN02278 238 PKV------RKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILV 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 253 NRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELL--AIHRN-EVIFGG--HTDENEQYiEPTILDGI 326
Cdd:PLN02278 312 QEGIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVESHVqdAVSKGaKVLLGGkrHSLGGTFY-EPTVLGDV 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 327 TPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLANPnlPFGG 406
Cdd:PLN02278 391 TEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVA--PFGG 468
|
330 340
....*....|....*....|....*.
gi 1090914694 407 VGASGIGEYHGKYSFDTFSHMKsYIF 432
Cdd:PLN02278 469 VKQSGLGREGSKYGIDEYLEIK-YVC 493
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
103-429 |
1.19e-46 |
|
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: 168.00 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTP-HVAQVVRKVIEDVFTSDFVAVVEGGVEETQTLINLP- 180
Cdd:cd07113 141 EPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPlTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISHPd 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 181 FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNEL 260
Cdd:cd07113 221 VAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDEL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 261 IQSFKQSIEEFY-GKNIQNSPDFGRIVNTKHFNRLSELLAIHR---NEVIFGGHTDENEQY-IEPTILDGITPQSKIMEE 335
Cdd:cd07113 301 VTKLKQALSSFQvGSPMDESVMFGPLANQPHFDKVCSYLDDARaegDEIVRGGEALAGEGYfVQPTLVLARSADSRLMRE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 336 EIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINdtlMH-LANPNLPFGGVGASGIGE 414
Cdd:cd07113 381 ETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN---MHtFLDPAVPFGGMKQSGIGR 457
|
330
....*....|....*
gi 1090914694 415 YHGKYSFDTFSHMKS 429
Cdd:cd07113 458 EFGSAFIDDYTELKS 472
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
103-417 |
2.04e-46 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 166.78 E-value: 2.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEGGVEET-QTLINLP- 180
Cdd:cd07107 115 EPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVFNILPGDGATAgAALVRHPd 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 181 FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFG-KFTNAGQTCVAPDYILVNRKVKNE 259
Cdd:cd07107 195 VKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 260 LIQSFKQSIEEFY-GKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENEQ-----YIEPTILDGITPQS 330
Cdd:cd07107 275 VLARVVERVAAIKvGDPTDPATTMGPLVSRQQYDRVMHYIDSAKREgarLVTGGGRPEGPAleggfYVEPTVFADVTPGM 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 331 KIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLAnpNLPFGGVGAS 410
Cdd:cd07107 355 RIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVWINGSSRHFL--GAPFGGVKNS 432
|
....*..
gi 1090914694 411 GIGEYHG 417
Cdd:cd07107 433 GIGREEC 439
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
97-428 |
1.06e-45 |
|
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: 164.83 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 97 KSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEET-Q 174
Cdd:cd07110 113 KARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAAEAgLPPGVLNVVTGTGDEAgA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 175 TLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVN 253
Cdd:cd07110 193 PLAAHPgIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVH 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 254 RKVKNELIQSFKQSIEefygkNIQNSPDF------GRIVNTKHFNRLSELLAIHRNE---VIFGG-HTDENEQ--YIEPT 321
Cdd:cd07110 273 ESIADAFLERLATAAE-----AIRVGDPLeegvrlGPLVSQAQYEKVLSFIARGKEEgarLLCGGrRPAHLEKgyFIAPT 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 322 ILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTlmHLANPN 401
Cdd:cd07110 348 VFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVWINCS--QPCFPQ 425
|
330 340
....*....|....*....|....*..
gi 1090914694 402 LPFGGVGASGIGEYHGKYSFDTFSHMK 428
Cdd:cd07110 426 APWGGYKRSGIGRELGEWGLDNYLEVK 452
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
97-430 |
1.55e-45 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 164.45 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 97 KSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVI-EDVFTSDFVAVVEGGVEE-TQ 174
Cdd:cd07146 113 KIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLyEAGLPPDMLSVVTGEPGEiGD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 175 TLI-NLPFDYIFFTGSENVGRIVyeATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVN 253
Cdd:cd07146 193 ELItHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVH 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 254 RKVKNELIQSF-KQSIEEFYGKNIQNSPDFGRIVN---TKHFNRLSElLAIHRNEVIFGGHTDENEQYiEPTILDGITPQ 329
Cdd:cd07146 271 ESVADEFVDLLvEKSAALVVGDPMDPATDMGTVIDeeaAIQIENRVE-EAIAQGARVLLGNQRQGALY-APTVLDHVPPD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 330 SKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDtLMHLANPNLPFGGVGA 409
Cdd:cd07146 349 AELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNE-VPGFRSELSPFGGVKD 427
|
330 340
....*....|....*....|..
gi 1090914694 410 SGIGEYHG-KYSFDTFSHMKSY 430
Cdd:cd07146 428 SGLGGKEGvREAMKEMTNVKTY 449
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
98-431 |
9.30e-45 |
|
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: 162.62 E-value: 9.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEG-GVEETQTL 176
Cdd:cd07117 130 SIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGkGSKSGEYL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 177 INLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRK 255
Cdd:cd07117 210 LNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 256 VKNELIqsfKQSIEEFYGKNIQNSPD----FGRIVNTKHFNRLSELLAIHRNE---VIFGGH-----TDENEQYIEPTIL 323
Cdd:cd07117 290 IYDEFV---AKLKEKFENVKVGNPLDpdtqMGAQVNKDQLDKILSYVDIAKEEgakILTGGHrltenGLDKGFFIEPTLI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 324 DGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINdtLMHLANPNLP 403
Cdd:cd07117 367 VNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVN--TYNQIPAGAP 444
|
330 340
....*....|....*....|....*....
gi 1090914694 404 FGGVGASGIGEYHGKYSFDTFSHMKS-YI 431
Cdd:cd07117 445 FGGYKKSGIGRETHKSMLDAYTQMKNiYI 473
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
20-433 |
1.82e-44 |
|
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: 161.97 E-value: 1.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 20 TKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAyATEIGILLKSIKTARKELKNwaktkqVDTPLFMFPSKSY 99
Cdd:cd07082 57 TMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDA-LKEVDRTIDYIRDTIEELKR------LDGDSLPGDWFPG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 100 -------IKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVE 171
Cdd:cd07082 130 tkgkiaqVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 172 ETQTLI--NLPFDYIFFTGSENVGRIVYEATSKnlVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDY 249
Cdd:cd07082 210 EIGDPLvtHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 250 ILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELL--AI-HRNEVIFGGHTdENEQYIEPTILDG 325
Cdd:cd07082 288 VLVHESVADELVELLKEEVAKLkVGMPWDNGVDITPLIDPKSADFVEGLIddAVaKGATVLNGGGR-EGGNLIYPTLLDP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 326 ITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHlaNP-NLPF 404
Cdd:cd07082 367 VTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQR--GPdHFPF 444
|
410 420
....*....|....*....|....*....
gi 1090914694 405 GGVGASGIGEYHGKYSFDTFSHMKSYIFK 433
Cdd:cd07082 445 LGRKDSGIGTQGIGDALRSMTRRKGIVIN 473
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
83-431 |
1.86e-44 |
|
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: 161.89 E-value: 1.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 83 KTKQVDTPLFMfpsksYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDF 162
Cdd:cd07142 125 MTLPADGPHHV-----YTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 163 VA-VVEGGVEETQTLI--NLPFDYIFFTGSENVGRIVYEATSK-NLVPVTLELGGKSPVIVDETANIKVASDRISFGKFT 238
Cdd:cd07142 200 VLnIVTGFGPTAGAAIasHMDVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFF 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 239 NAGQTCVAPDYILVNRKVKNELIQ-----SFKQSIEEFYGKNIQNSPDfgriVNTKHFNRLSELLAIHRNE----VIFGG 309
Cdd:cd07142 280 NQGQCCCAGSRTFVHESIYDEFVEkakarALKRVVGDPFRKGVEQGPQ----VDKEQFEKILSYIEHGKEEgatlITGGD 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 310 HTDENEQYIEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGA 389
Cdd:cd07142 356 RIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVW 435
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1090914694 390 INdtLMHLANPNLPFGGVGASGIGEYHGKYSFDTFSHMKSYI 431
Cdd:cd07142 436 VN--CYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
99-431 |
7.56e-44 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 160.11 E-value: 7.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 99 YIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSD--FVAVVEGGVEETQTL 176
Cdd:cd07097 130 ETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAgvFNLVMGSGSEVGQAL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 177 INLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNR- 254
Cdd:cd07097 210 VEHPdVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEg 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 255 ---KVKNELIQSFKqSIEefYGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENEQ---YIEPTILDG 325
Cdd:cd07097 290 ihdRFVEALVERTK-ALK--VGDALDEGVDIGPVVSERQLEKDLRYIEIARSEgakLVYGGERLKRPDegyYLAPALFAG 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 326 ITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLaNPNLPFG 405
Cdd:cd07097 367 VTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAGV-DYHVPFG 445
|
330 340
....*....|....*....|....*....
gi 1090914694 406 GVGASGIGeYH--GKYSFDTFSHMK-SYI 431
Cdd:cd07097 446 GRKGSSYG-PReqGEAALEFYTTIKtVYV 473
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
104-418 |
1.18e-43 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 159.40 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEG-GVEETQTLINlPF 181
Cdd:cd07101 118 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLPRDLWQVVTGpGSEVGGAIVD-NA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 182 DYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNELI 261
Cdd:cd07101 197 DYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFV 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 262 QSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRN---EVIFGGHT--DENEQYIEPTILDGITPQSKIMEE 335
Cdd:cd07101 277 RRFVARTRALrLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAkgaTVLAGGRArpDLGPYFYEPTVLTGVTEDMELFAE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 336 EIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLM-HLANPNLPFGGVGASGIGE 414
Cdd:cd07101 357 ETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNEGYAaAWASIDAPMGGMKDSGLGR 436
|
....
gi 1090914694 415 YHGK 418
Cdd:cd07101 437 RHGA 440
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
4-411 |
8.94e-43 |
|
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: 156.28 E-value: 8.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 4 IEKQFQESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAyATEIGILLKSIKTARKELKNWAK 83
Cdd:cd07095 2 VDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEA-QTEVAAMAGKIDISIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 84 TKQVDTPlfmfPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDF 162
Cdd:cd07095 81 ERATPMA----QGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAgLPPGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 163 VAVVEGGVEETQTLINLP-FDYIFFTGSENVGRIVYEATSKNL-VPVTLELGGKSPVIVDETANIKVASDRISFGKFTNA 240
Cdd:cd07095 157 LNLVQGGRETGEALAAHEgIDGLLFTGSAATGLLLHRQFAGRPgKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 241 GQTCV-APDYILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNT-------KHFNRLSEL--LAIHRNEVIfgg 309
Cdd:cd07095 237 GQRCTcARRLIVPDGAVGDAFLERLVEAAKRLrIGAPDAEPPFMGPLIIAaaaarylLAQQDLLALggEPLLAMERL--- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 310 htDENEQYIEPTILDgITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGA 389
Cdd:cd07095 314 --VAGTAFLSPGIID-VTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
|
410 420
....*....|....*....|..
gi 1090914694 390 INDTLMHlANPNLPFGGVGASG 411
Cdd:cd07095 391 WNRPTTG-ASSTAPFGGVGLSG 411
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
14-428 |
1.41e-42 |
|
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: 156.35 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 14 FFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAyATEIGillksikTARKELKNWAKTKQVDTPLFM 93
Cdd:cd07120 32 FDETDWAHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-RFEIS-------GAISELRYYAGLARTEAGRMI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 94 FPSK---SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVftSDFVA-----V 165
Cdd:cd07120 104 EPEPgsfSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEI--PSLPAgvvnlF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 166 VEGGVEETQTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTC 244
Cdd:cd07120 182 TESGSEGAAHLVASPdVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFC 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 245 VAPDYILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE----VIFGGHTDENEQ--- 316
Cdd:cd07120 262 MAGSRVLVQRSIADEVRDRLAARLAAVkVGPGLDPASDMGPLIDRANVDRVDRMVERAIAAgaevVLRGGPVTEGLAkga 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 317 YIEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDtlmH 396
Cdd:cd07120 342 FLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND---W 418
|
410 420 430
....*....|....*....|....*....|...
gi 1090914694 397 LAN-PNLPFGGVGASGIGEYHGKYSFDTFSHMK 428
Cdd:cd07120 419 NKLfAEAEEGGYRQSGLGRLHGVAALEDFIEYK 451
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
3-417 |
4.56e-42 |
|
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: 155.81 E-value: 4.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 3 LIEKQFQESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYAtEIGILLKSIK-TARKELKNW 81
Cdd:cd07083 56 EAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAID-DVAEAIDFIRyYARAALRLR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 82 AKTKQVDTPLfmfPSKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHV-AQVVRKVIEDVFTS 160
Cdd:cd07083 135 YPAVEVVPYP---GEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVgYKVFEIFHEAGFPP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 161 DFVAVVEG-GVEETQTLINLP-FDYIFFTGSENVGRIVYEATSKNL------VPVTLELGGKSPVIVDETANIKVASDRI 232
Cdd:cd07083 212 GVVQFLPGvGEEVGAYLTEHErIRGINFTGSLETGKKIYEAAARLApgqtwfKRLYVETGGKNAIIVDETADFELVVEGV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 233 SFGKFTNAGQTCVAPDYILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE--VIFGG 309
Cdd:cd07083 292 VVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLsVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEgqLVLGG 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 310 HTDENEQY-IEPTILDGITPQSKIMEEEIFGPLLPIIVY--DDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFG 386
Cdd:cd07083 372 KRLEGEGYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYkdDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVG 451
|
410 420 430
....*....|....*....|....*....|.
gi 1090914694 387 GGAINDTLMHLANPNLPFGGVGASGIGEYHG 417
Cdd:cd07083 452 NLYINRKITGALVGVQPFGGFKLSGTNAKTG 482
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
104-432 |
3.34e-41 |
|
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: 152.40 E-value: 3.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVI-EDVFTSDFVAVVEGGVEETQTLINLP-F 181
Cdd:cd07147 123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLaETGLPKGAFSVLPCSRDDADLLVTDErI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 182 DYIFFTGSENVGRIVYEATSKNlvPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNELI 261
Cdd:cd07147 203 KLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFK 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 262 QSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELL--AIHRN-EVIFGGHTDENeqYIEPTILDGITPQSKIMEEEI 337
Cdd:cd07147 281 SRLVARVKALkTGDPKDDATDVGPMISESEAERVEGWVneAVDAGaKLLTGGKRDGA--LLEPTILEDVPPDMEVNCEEV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 338 FGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTlmhlanP-----NLPFGGVGASGI 412
Cdd:cd07147 359 FGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINDV------PtfrvdHMPYGGVKDSGI 432
|
330 340
....*....|....*....|
gi 1090914694 413 GEYHGKYSFDTFSHMKSYIF 432
Cdd:cd07147 433 GREGVRYAIEEMTEPRLLVI 452
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
103-356 |
9.90e-41 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 152.40 E-value: 9.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEG-GVEETQTLINLP 180
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGsGSEVGDYLVDHP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 181 -FDYIFFTGSENVGRIVYEATSKN------LVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVN 253
Cdd:PRK03137 250 kTRFITFTGSREVGLRIYERAAKVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVH 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 254 RKVKNELIQSFKQSIEEFYGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE--VIFGGHTDENEQY-IEPTILDGITPQS 330
Cdd:PRK03137 330 EDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIEIGKEEgrLVLGGEGDDSKGYfIQPTIFADVDPKA 409
|
250 260
....*....|....*....|....*.
gi 1090914694 331 KIMEEEIFGPLLPIIVYDDFNEAIDI 356
Cdd:PRK03137 410 RIMQEEIFGPVVAFIKAKDFDHALEI 435
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
24-428 |
1.17e-40 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 152.19 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 24 KFRKQQLKLLSKSIKDHETELLESLKIDLGK-------------GSVEAYATeigiLLKSIKTARKElknwaktkQVDTP 90
Cdd:PLN02467 72 AVRAKYLRAIAAKITERKSELAKLETLDCGKpldeaawdmddvaGCFEYYAD----LAEALDAKQKA--------PVSLP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 91 LFMFpsKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEG- 168
Cdd:PLN02467 140 METF--KGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGVLNVVTGl 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 169 GVEETQTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAP 247
Cdd:PLN02467 218 GTEAGAPLASHPgVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSAT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 248 DYILVNRKVKNELIQSFKQsieefYGKNIQNSPDF------GRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENEQ-- 316
Cdd:PLN02467 298 SRLLVHERIASEFLEKLVK-----WAKNIKISDPLeegcrlGPVVSEGQYEKVLKFISTAKSEgatILCGGKRPEHLKkg 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 317 -YIEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINdtlm 395
Cdd:PLN02467 373 fFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWIN---- 448
|
410 420 430
....*....|....*....|....*....|....*.
gi 1090914694 396 hLANP---NLPFGGVGASGIGEYHGKYSFDTFSHMK 428
Cdd:PLN02467 449 -CSQPcfcQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
99-431 |
2.17e-40 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 151.13 E-value: 2.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 99 YIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEGGVEETQTLI- 177
Cdd:PLN02766 153 YTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAi 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 178 --NLPFDYIFFTGSENVGRIVYEATSK-NLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNR 254
Cdd:PLN02766 233 asHMDVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 255 KVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGH-TDENEQYIEPTILDGITPQ 329
Cdd:PLN02766 313 GIYDEFVKKLVEKAKDWvVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREgatLLTGGKpCGDKGYYIEPTIFTDVTED 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 330 SKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINdtlMHLA-NPNLPFGGVG 408
Cdd:PLN02766 393 MKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVN---CYFAfDPDCPFGGYK 469
|
330 340
....*....|....*....|...
gi 1090914694 409 ASGIGEYHGKYSFDTFSHMKSYI 431
Cdd:PLN02766 470 MSGFGRDQGMDALDKYLQVKSVV 492
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
104-391 |
7.22e-40 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 147.96 E-value: 7.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEG-GVEETQTLINLP- 180
Cdd:PRK10090 71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGrGETVGQELAGNPk 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 181 FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNEL 260
Cdd:PRK10090 151 VAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQF 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 261 IQSFKQSIEEF-YGKNIQNS-PDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTDENEQYI-EPTILDGITPQSKIME 334
Cdd:PRK10090 231 VNRLGEAMQAVqFGNPAERNdIAMGPLINAAALERVEQKVARAVEEgarVALGGKAVEGKGYYyPPTLLLDVRQEMSIMH 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1090914694 335 EEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAIN 391
Cdd:PRK10090 311 EETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN 367
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
98-422 |
1.04e-39 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 148.90 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEGGVEET-QTL 176
Cdd:PRK13473 132 SMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVgDAL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 177 INLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRK 255
Cdd:PRK13473 212 VGHPkVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRG 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 256 VKNELIqsfkQSIEEFYGKNIQNSP-----DFGRIVNTKHFNRLS----ELLAIHRNEVIFGGHT-DENEQYIEPTILDG 325
Cdd:PRK13473 292 IYDDLV----AKLAAAVATLKVGDPddedtELGPLISAAHRDRVAgfveRAKALGHIRVVTGGEApDGKGYYYEPTLLAG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 326 ITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMhLANpNLPFG 405
Cdd:PRK13473 368 ARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM-LVS-EMPHG 445
|
330
....*....|....*..
gi 1090914694 406 GVGASGIGEYHGKYSFD 422
Cdd:PRK13473 446 GQKQSGYGKDMSLYGLE 462
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
103-431 |
2.39e-38 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 146.11 E-value: 2.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVqLLFEPLIG-AIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEGGVEETQTLI---N 178
Cdd:PLN02466 194 EPIGVAGQIIPWNFPL-LMFAWKVGpALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAAlasH 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 179 LPFDYIFFTGSENVGRIVYEATSK-NLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVK 257
Cdd:PLN02466 273 MDVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 258 NELIQ-----SFKQSIEEFYGKNIQNSPDfgriVNTKHFNRLSELL--AIHRNEVIF--GGHTDENEQYIEPTILDGITP 328
Cdd:PLN02466 353 DEFVEkakarALKRVVGDPFKKGVEQGPQ----IDSEQFEKILRYIksGVESGATLEcgGDRFGSKGYYIQPTVFSNVQD 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 329 QSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINdtLMHLANPNLPFGGVG 408
Cdd:PLN02466 429 DMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVN--CFDVFDAAIPFGGYK 506
|
330 340
....*....|....*....|...
gi 1090914694 409 ASGIGEYHGKYSFDTFSHMKSYI 431
Cdd:PLN02466 507 MSGIGREKGIYSLNNYLQVKAVV 529
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
104-417 |
1.97e-37 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 143.48 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVA-QVVRKVIEDVFTSDFVAVVEG-GVEETQTLINLPf 181
Cdd:PRK09407 154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTAlAAVELLYEAGLPRDLWQVVTGpGPVVGTALVDNA- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 182 DYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNELI 261
Cdd:PRK09407 233 DYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFV 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 262 QSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSEllaiHRNE-------VIFGGHT--DENEQYIEPTILDGITPQSK 331
Cdd:PRK09407 313 RAFVAAVRAMrLGAGYDYSADMGSLISEAQLETVSA----HVDDavakgatVLAGGKArpDLGPLFYEPTVLTGVTPDME 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 332 IMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMH-LANPNLPFGGVGAS 410
Cdd:PRK09407 389 LAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAaWGSVDAPMGGMKDS 468
|
....*..
gi 1090914694 411 GIGEYHG 417
Cdd:PRK09407 469 GLGRRHG 475
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
103-428 |
1.40e-36 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 140.43 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEET--QTLINL 179
Cdd:PRK11241 145 QPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVggELTSNP 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 180 PFDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNE 259
Cdd:PRK11241 225 LVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 260 LIQSFKQSIEEFY-GKNIQNSPDFGRIVNTKHFNRLSELL--AIHRN-EVIFGGHTDENE-QYIEPTILDGITPQSKIME 334
Cdd:PRK11241 305 FAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEEHIadALEKGaRVVCGGKAHELGgNFFQPTILVDVPANAKVAK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 335 EEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLmhLANPNLPFGGVGASGIGE 414
Cdd:PRK11241 385 EETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGI--ISNEVAPFGGIKASGLGR 462
|
330
....*....|....
gi 1090914694 415 YHGKYSFDTFSHMK 428
Cdd:PRK11241 463 EGSKYGIEDYLEIK 476
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
37-411 |
1.14e-34 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 135.09 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 37 IKDHETELLESLKIDLGKGSVEAyATEIGILLK----SIKTARKelknwaKTKQVDTPlfMFPSKSYIKPEPYGTILIIG 112
Cdd:PRK09457 72 LEENKEELAEVIARETGKPLWEA-ATEVTAMINkiaiSIQAYHE------RTGEKRSE--MADGAAVLRHRPHGVVAVFG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 113 PFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVA-VVEGGVEETQTLINLP-FDYIFFTGSE 190
Cdd:PRK09457 143 PYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLnLVQGGRETGKALAAHPdIDGLLFTGSA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 191 NVGRIVYEATSKNlvP---VTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVK-NELIQSFKQ 266
Cdd:PRK09457 223 NTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 267 S-----IEEFygkNIQNSPDFGRIVNTKHFNRLselLAIHRNEVIFGG-------HTDENEQYIEPTILDgITPQSKIME 334
Cdd:PRK09457 301 VakrltVGRW---DAEPQPFMGAVISEQAAQGL---VAAQAQLLALGGksllemtQLQAGTGLLTPGIID-VTGVAELPD 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1090914694 335 EEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSfgGGAIN-DTLMHLANPNLPFGGVGASG 411
Cdd:PRK09457 374 EEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIR--AGIVNwNKPLTGASSAAPFGGVGASG 449
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
26-418 |
3.81e-34 |
|
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: 133.68 E-value: 3.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 26 RKQQLKLLSKSIKDHETEL--LESLkiDLGKGSVEAYATEIGILLKSIKtarkELKNWAKTKQVDTPlfmfpsksyiKPE 103
Cdd:cd07111 83 RARHLYRIARHIQKHQRLFavLESL--DNGKPIRESRDCDIPLVARHFY----HHAGWAQLLDTELA----------GWK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDV-FTSDFVAVVEGGVEETQTLINLP-F 181
Cdd:cd07111 147 PVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGSFGSALANHPgV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 182 DYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVKNELI 261
Cdd:cd07111 227 DKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 262 QSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNEvifGGHTDENEQ-------YIEPTILDGITPQSKIM 333
Cdd:cd07111 307 RKLKERMSHLrVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAE---GADVFQPGAdlpskgpFYPPTLFTNVPPASRIA 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 334 EEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTlmHLANPNLPFGGVGASGIG 413
Cdd:cd07111 384 QEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGH--NLFDAAAGFGGYRESGFG 461
|
....*
gi 1090914694 414 EYHGK 418
Cdd:cd07111 462 REGGK 466
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
99-429 |
4.41e-34 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 133.47 E-value: 4.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 99 YIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTP----HVAQVVRK--VIEDVFTsdfvaVVEGGVEE 172
Cdd:PRK13252 137 YTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPltalKLAEIYTEagLPDGVFN-----VVQGDGRV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 173 TQTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYIL 251
Cdd:PRK13252 212 GAWLTEHPdIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVF 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 252 VNRKVKNELIQSFKQSIEEFY-GKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGH--TDE---NEQYIEPTI 322
Cdd:PRK13252 292 VQKSIKAAFEARLLERVERIRiGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEgarLLCGGErlTEGgfaNGAFVAPTV 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 323 LDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDtlMHLANPNL 402
Cdd:PRK13252 372 FTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINT--WGESPAEM 449
|
330 340
....*....|....*....|....*..
gi 1090914694 403 PFGGVGASGIGEYHGKYSFDTFSHMKS 429
Cdd:PRK13252 450 PVGGYKQSGIGRENGIATLEHYTQIKS 476
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
98-428 |
6.29e-34 |
|
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: 132.96 E-value: 6.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEG-GVEETQTL 176
Cdd:cd07116 130 AYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGfGLEAGKPL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 177 INLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETAnikVASDRISFGK----FT----NAGQTCVAP 247
Cdd:cd07116 210 ASSKrIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNIFFADV---MDADDAFFDKalegFVmfalNQGEVCTCP 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 248 DYILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGH-----TDENEQYI 318
Cdd:cd07116 287 SRALIQESIYDRFMERALERVKAIkQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEgaeVLTGGErnelgGLLGGGYY 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 319 EPTILDGiTPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINdtLMHLA 398
Cdd:cd07116 367 VPTTFKG-GNKMRIFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTN--CYHLY 443
|
330 340 350
....*....|....*....|....*....|
gi 1090914694 399 NPNLPFGGVGASGIGEYHGKYSFDTFSHMK 428
Cdd:cd07116 444 PAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
23-359 |
8.14e-34 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 132.64 E-value: 8.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 23 IKFRKQQLkllsksIKDHETELLESLKIDLGKGSVEA------------YATEIGILLK--SIKTARKElknwaktkqVD 88
Cdd:cd07085 65 VMFKFRQL------LEENLDELARLITLEHGKTLADArgdvlrglevveFACSIPHLLKgeYLENVARG---------ID 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 89 TplfmfpsksYIKPEPYGTILIIGPFNYP--VQLLFEPLigAIAAGNNAIIKPSELTPHVAQVVRKVIED------VFTs 160
Cdd:cd07085 130 T---------YSYRQPLGVVAGITPFNFPamIPLWMFPM--AIACGNTFVLKPSERVPGAAMRLAELLQEaglpdgVLN- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 161 dfvaVVEGGVEETQTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTN 239
Cdd:cd07085 198 ----VVHGGKEAVNALLDHPdIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 240 AGQTCVAPDYILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHTD--- 312
Cdd:cd07085 274 AGQRCMALSVAVAVGDEADEWIPKLVERAKKLkVGAGDDPGADMGPVISPAAKERIEGLIESGVEEgakLVLDGRGVkvp 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1090914694 313 --ENEQYIEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQS 359
Cdd:cd07085 354 gyENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINA 402
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
104-372 |
3.99e-32 |
|
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: 127.71 E-value: 3.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFV-----AVVEGGVEETQTLIN 178
Cdd:cd07130 132 PLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLEKNGLpgaiaSLVCGGADVGEALVK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 179 LP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVK 257
Cdd:cd07130 212 DPrVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 258 NELIQSFKQSieefYGK-NIQNSPDFGRIV---NTKH-FNRLSELLAIHRN---EVIFGGHTDENE-QYIEPTILDGiTP 328
Cdd:cd07130 292 DEVLERLKKA----YKQvRIGDPLDDGTLVgplHTKAaVDNYLAAIEEAKSqggTVLFGGKVIDGPgNYVEPTIVEG-LS 366
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1090914694 329 QSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSED 372
Cdd:cd07130 367 DAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTD 410
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
100-429 |
1.98e-28 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 117.30 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 100 IKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVA-VVEG-GVEETQTLI 177
Cdd:PRK09847 153 IVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLnVVTGfGHEAGQALS 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 178 NLP-FDYIFFTGSENVGR-IVYEATSKNLVPVTLELGGKSPVIV-DETANIKVASDRISFGKFTNAGQTCVAPDYILVNR 254
Cdd:PRK09847 233 RHNdIDAIAFTGSTRTGKqLLKDAGDSNMKRVWLEAGGKSANIVfADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 255 KVKNELIQSFKQSIEEFY-GKNIQNSPDFGRIVNTKHFNRLSELL--AIHRNEVIFGGHTDENEQYIEPTILDGITPQSK 331
Cdd:PRK09847 313 SIADEFLALLKQQAQNWQpGHPLDPATTMGTLIDCAHADSVHSFIreGESKGQLLLDGRNAGLAAAIGPTIFVDVDPNAS 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 332 IMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDtlMHLANPNLPFGGVGASG 411
Cdd:PRK09847 393 LSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNN--YNDGDMTVPFGGYKQSG 470
|
330
....*....|....*...
gi 1090914694 412 IGEYHGKYSFDTFSHMKS 429
Cdd:PRK09847 471 NGRDKSLHALEKFTELKT 488
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
4-413 |
7.59e-28 |
|
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: 115.21 E-value: 7.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 4 IEKQFQESKQFFKT-------HQTKDIkfrkqqLKLLSKSIKDHETELLESLKIDLGKGSVEAyATEIGILLKSIKTARK 76
Cdd:cd07148 23 IDKALDTAHALFLDrnnwlpaHERIAI------LERLADLMEERADELALLIAREGGKPLVDA-KVEVTRAIDGVELAAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 77 ELKNWAKTkqvDTPLFMFPSKS----YIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQ-VVR 151
Cdd:cd07148 96 ELGQLGGR---EIPMGLTPASAgriaFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLaFVD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 152 KVIEDVFTSDFVAVVEGGVEETQTLINLP-FDYIFFTGSENVGrivYEATSKnLVPVT---LELGGKSPVIVDETANIKV 227
Cdd:cd07148 173 LLHEAGLPEGWCQAVPCENAVAEKLVTDPrVAFFSFIGSARVG---WMLRSK-LAPGTrcaLEHGGAAPVIVDRSADLDA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 228 ASDRISFGKFTNAGQTCVAPDYILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELL--AIHRNE 304
Cdd:cd07148 249 MIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLvVGDPTDPDTEVGPLIRPREVDRVEEWVneAVAAGA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 305 VIFGGHTDENEQYIEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDiiQSKSKPLSLY--LFSEDENTTNCVLEE 382
Cdd:cd07148 329 RLLCGGKRLSDTTYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIA--QANSLPVAFQaaVFTKDLDVALKAVRR 406
|
410 420 430
....*....|....*....|....*....|...
gi 1090914694 383 LSFGGGAINDtlmHLANPN--LPFGGVGASGIG 413
Cdd:cd07148 407 LDATAVMVND---HTAFRVdwMPFAGRRQSGYG 436
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
26-414 |
1.47e-27 |
|
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: 114.90 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 26 RKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYATEIGIllkSIKTARKeLKNWAKTKQVDT-PLFMF-PSK--SYIK 101
Cdd:cd07140 69 RGRLMYRLADLMEEHQEELATIESLDSGAVYTLALKTHVGM---SIQTFRY-FAGWCDKIQGKTiPINQArPNRnlTLTK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 102 PEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVA-QVVRKVIEDVFTSDFVAVVEG-GVEETQTLINL 179
Cdd:cd07140 145 REPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTAlKFAELTVKAGFPKGVINILPGsGSLVGQRLSDH 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 180 P-FDYIFFTGSENVGRIVYEATSK-NLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRKVK 257
Cdd:cd07140 225 PdVRKLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIH 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 258 NELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGG-HTDENEQYIEPTILDGITPQSKI 332
Cdd:cd07140 305 DEFVRRVVEEVKKMkIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEgatLVYGGkQVDRPGFFFEPTVFTDVEDHMFI 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 333 MEEEIFGPLLPIIVYDDfNEAIDIIQSKSKP---LSLYLFSEDENTTNCVLEELSFGGGAINdtLMHLANPNLPFGGVGA 409
Cdd:cd07140 385 AKEESFGPIMIISKFDD-GDVDGVLQRANDTeygLASGVFTKDINKALYVSDKLEAGTVFVN--TYNKTDVAAPFGGFKQ 461
|
....*
gi 1090914694 410 SGIGE 414
Cdd:cd07140 462 SGFGK 466
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
96-421 |
3.84e-26 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 110.21 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 96 SKSYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVI------EDVFTSdfVAVVEGG 169
Cdd:PRK09406 115 SRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFrragfpDGCFQT--LLVGSGA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 170 VEE--------TQTLinlpfdyiffTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAG 241
Cdd:PRK09406 193 VEAilrdprvaAATL----------TGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 242 QTCVAPDYILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELL--AIHRNEVIF-GGHT-DENEQ 316
Cdd:PRK09406 263 QSCIAAKRFIVHADVYDAFAEKFVARMAALrVGDPTDPDTDVGPLATEQGRDEVEKQVddAVAAGATILcGGKRpDGPGW 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 317 YIEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDtlMH 396
Cdd:PRK09406 343 FYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING--MT 420
|
330 340
....*....|....*....|....*...
gi 1090914694 397 LANPNLPFGGVGASGIGEY---HGKYSF 421
Cdd:PRK09406 421 VSYPELPFGGVKRSGYGRElsaHGIREF 448
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
19-416 |
2.85e-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: 108.04 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 19 QTKDIKFRKQQLkllsksIKDHETELLESLKIDLGK------GSVeAYATEIGILLKSIKTARKELKNWAKTKQVDTplf 92
Cdd:TIGR01722 61 QRTSVLLRYQAL------LKEHRDEIAELITAEHGKthsdalGDV-ARGLEVVEHACGVNSLLKGETSTQVATRVDV--- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 93 mfpsksYIKPEPYGTILIIGPFNYP--VQLLFEPLigAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFV-AVVEGG 169
Cdd:TIGR01722 131 ------YSIRQPLGVCAGITPFNFPamIPLWMFPI--AIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVlNVVHGD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 170 VEETQTLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPD 248
Cdd:TIGR01722 203 KEAVDRLLEHPdVKAVSFVGSTPIGRYIHTTGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 249 YILVNRKVKnELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFNRLSELLAIHRNE---VIFGGHT-----DENEQYIE 319
Cdd:TIGR01722 283 AAVLVGAAD-EWVPEIRERAEKIrIGPGDDPGAEMGPLITPQAKDRVASLIAGGAAEgaeVLLDGRGykvdgYEEGNWVG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 320 PTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINdTLMHLAN 399
Cdd:TIGR01722 362 PTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN-VPIPVPL 440
|
410
....*....|....*..
gi 1090914694 400 PNLPFGGVGASGIGEYH 416
Cdd:TIGR01722 441 PYFSFTGWKDSFFGDHH 457
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
4-413 |
6.70e-25 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 106.87 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 4 IEKQFQESKQFFKTHQTKDIKFRKQQLKLLSKSIKDHETELLESLKIDLGKGSVEAYAtEIGillksiKTArkELKNW-- 81
Cdd:PRK13968 31 IENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-EVA------KSA--NLCDWya 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 82 --AKTKQVDTPLFMFPSKSYIKPEPYGTILIIGPFNYPvqlLFEPLIGAIA---AGNNAIIKPSeltPHV---AQVVRKV 153
Cdd:PRK13968 102 ehGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFP---LWQVMRGAVPillAGNGYLLKHA---PNVmgcAQLIAQV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 154 IEDvftSDFVAVVEGGVEETQ----TLINLP-FDYIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVA 228
Cdd:PRK13968 176 FKD---AGIPQGVYGWLNADNdgvsQMINDSrIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 229 SDRISFGKFTNAGQTCVAPDYILVNRKVKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVntkHFNRLSELlaiHRN---- 303
Cdd:PRK13968 253 VKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALkMGDPRDEENALGPMA---RFDLRDEL---HHQveat 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 304 -----EVIFGGHTDENE-QYIEPTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTN 377
Cdd:PRK13968 327 laegaRLLLGGEKIAGAgNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQAR 406
|
410 420 430
....*....|....*....|....*....|....*.
gi 1090914694 378 CVLEELSFGGGAINDtlMHLANPNLPFGGVGASGIG 413
Cdd:PRK13968 407 QMAARLECGGVFING--YCASDARVAFGGVKKSGFG 440
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
103-413 |
2.38e-24 |
|
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: 105.74 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVA-QVVRK-----VIEDVftsdfVAVVEG-GVEETQT 175
Cdd:cd07125 166 HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAaRAVELlheagVPRDV-----LQLVPGdGEEIGEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 176 LINLP-FDYIFFTGSENVGRIVYEATSKN---LVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYIL 251
Cdd:cd07125 241 LVAHPrIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLY 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 252 VNRKVKNELIQSFKQSIEEF---YGKNIQNspDFGRIVNTKHFNRLSELLAIHRNE--VIFGGHTDE-NEQYIEPTILDG 325
Cdd:cd07125 321 LQEEIAERFIEMLKGAMASLkvgDPWDLST--DVGPLIDKPAGKLLRAHTELMRGEawLIAPAPLDDgNGYFVAPGIIEI 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 326 ITpqSKIMEEEIFGPLLPIIVYD--DFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGG--------GAIndTLM 395
Cdd:cd07125 399 VG--IFDLTTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNlyinrnitGAI--VGR 474
|
330
....*....|....*...
gi 1090914694 396 HlanpnlPFGGVGASGIG 413
Cdd:cd07125 475 Q------PFGGWGLSGTG 486
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
103-413 |
1.13e-23 |
|
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: 103.45 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 103 EPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVA-QVVRKVIEDVFTSDFVAVVEG-GVEETQTLINLP 180
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAyRAVELMQEAGFPAGTIQLLPGrGADVGAALTSDP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 181 -FDYIFFTGSENVGRIVYEATSKNL---VPVTLELGGKSPVIVDETA-NIKVASDRISfGKFTNAGQTCVAPDYILVNRK 255
Cdd:TIGR01238 239 rIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVDSTAlPEQVVRDVLR-SAFDSAGQRCSALRVLCVQED 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 256 VKNELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTK-------HFNRLSELLAIHRNEVIFGGHTDENEQYIEPTI--LDG 325
Cdd:TIGR01238 318 VADRVLTMIQGAMQELkVGVPHLLTTDVGPVIDAEakqnllaHIEHMSQTQKKIAQLTLDDSRACQHGTFVAPTLfeLDD 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 326 ITPqskiMEEEIFGPLLPIIVY--DDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINDTLMHLANPNLP 403
Cdd:TIGR01238 398 IAE----LSEEVFGPVLHVVRYkaRELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQP 473
|
330
....*....|
gi 1090914694 404 FGGVGASGIG 413
Cdd:TIGR01238 474 FGGQGLSGTG 483
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
104-413 |
5.89e-23 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 101.37 E-value: 5.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKP------SELtpHVAQVVRKViedVFTSDFVAVVEG-GVEETQTL 176
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPptqgavAAL--HMVHCFHLA---GFPKGLISCVTGkGSEIGDFL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 177 INLP-FDYIFFTGSENVGRIVYEAtskNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRK 255
Cdd:PLN00412 233 TMHPgVNCISFTGGDTGIAISKKA---GMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMES 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 256 VKNELIQSFKQSIEEFYGKNIQNSPDFGRIVNTKHFNRLSELL--AIHRNEViFGGHTDENEQYIEPTILDGITPQSKIM 333
Cdd:PLN00412 310 VADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVmdAKEKGAT-FCQEWKREGNLIWPLLLDNVRPDMRIA 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 334 EEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINdtlmhlANP-----NLPFGGVG 408
Cdd:PLN00412 389 WEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN------SAPargpdHFPFQGLK 462
|
....*
gi 1090914694 409 ASGIG 413
Cdd:PLN00412 463 DSGIG 467
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
106-411 |
1.00e-22 |
|
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: 100.74 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 106 GTILIIGPFNYPvqllfepligAIAA---------GNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVA--VVEGGVEETQ 174
Cdd:cd07123 172 GFVYAVSPFNFT----------AIGGnlagapalmGNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVInfVPGDGPVVGD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 175 TLINLP-FDYIFFTGSENVGRIVYEATSKNLV-----P-VTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVA- 246
Cdd:cd07123 242 TVLASPhLAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAa 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 247 -----PDYILvnRKVKNELIQSFKQ----SIEEFygkniqnSPDFGRIVNTKHFNRLSELLAIHRN----EVIFGGHTDE 313
Cdd:cd07123 322 srayvPESLW--PEVKERLLEELKEikmgDPDDF-------SNFMGAVIDEKAFDRIKGYIDHAKSdpeaEIIAGGKCDD 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 314 NEQY-IEPTILDGITPQSKIMEEEIFGPLLPIIVYDD--FNEAIDIIQSKSkPLSLY--LFSEDENTTNCVLEELSFGGG 388
Cdd:cd07123 393 SVGYfVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDsdFEETLELVDTTS-PYALTgaIFAQDRKAIREATDALRNAAG 471
|
330 340 350
....*....|....*....|....*....|.
gi 1090914694 389 A--INDtlmhlaNPN------LPFGGVGASG 411
Cdd:cd07123 472 NfyIND------KPTgavvgqQPFGGARASG 496
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
104-435 |
1.27e-21 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 97.21 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSD------FVAVVeGGVEETQTL- 176
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNnlpgaiFTSFC-GGAEIGEAIa 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 177 --INLPFdyIFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVN- 253
Cdd:PLN02315 233 kdTRIPL--VSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHe 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 254 ---RKVKNELIQSFKQSieefygkNIQNSPDFGRIVNTKH-------FNRLSELLAIHRNEVIFGGHTDENE-QYIEPTI 322
Cdd:PLN02315 311 siyDDVLEQLLTVYKQV-------KIGDPLEKGTLLGPLHtpeskknFEKGIEIIKSQGGKILTGGSAIESEgNFVQPTI 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 323 LDgITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTncvleeLSFGGGAINDTlmHLANPNL 402
Cdd:PLN02315 384 VE-ISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPETI------FKWIGPLGSDC--GIVNVNI 454
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1090914694 403 P---------FGGVGASGIGEYHGKYSFdtfshmKSYIFKST 435
Cdd:PLN02315 455 PtngaeiggaFGGEKATGGGREAGSDSW------KQYMRRST 490
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
98-429 |
4.36e-21 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 95.97 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 98 SYIKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSDFVAVVEGGVEETQTLI 177
Cdd:PLN02419 243 TYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 178 NLPFDY--IFFTGSENVGRIVYEATSKNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNAGQTCVAPDYILVNRK 255
Cdd:PLN02419 323 CDDEDIraVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGD 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 256 VK---NELIQSFKqSIEEFYGKniQNSPDFGRIVNTKHFNRLSEL----------LAIHRNEVIFGGHtdENEQYIEPTI 322
Cdd:PLN02419 403 AKsweDKLVERAK-ALKVTCGS--EPDADLGPVISKQAKERICRLiqsgvddgakLLLDGRDIVVPGY--EKGNFIGPTI 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 323 LDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLEELSFGGGAINdTLMHLANPNL 402
Cdd:PLN02419 478 LSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN-VPIPVPLPFF 556
|
330 340
....*....|....*....|....*....
gi 1090914694 403 PFGGVGASGIGE--YHGKYSFDTFSHMKS 429
Cdd:PLN02419 557 SFTGNKASFAGDlnFYGKAGVDFFTQIKL 585
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
104-353 |
2.11e-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: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSD--FVAVVEGGVEETQTLINLP- 180
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPpeDVTLINGDGKTMQALLLHPn 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 181 FDYIFFTGSENVGRIVyeATSKNLVPVTLELGGKSPVIVDETAN-IKVASDRISFGKFTNAGQTCVAPDYILV-NRKVKN 258
Cdd:cd07084 180 PKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVpENWSKT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 259 ELIQSFKQSIEefygKNIQNSPDFGRIVNTKHFNRLSELLAIHRNEVIFGG------HTDENEQYIEPTIL----DGITP 328
Cdd:cd07084 258 PLVEKLKALLA----RRKLEDLLLGPVQTFTTLAMIAHMENLLGSVLLFSGkelknhSIPSIYGACVASALfvpiDEILK 333
|
250 260
....*....|....*....|....*
gi 1090914694 329 QSKIMEEEIFGPLLPIIVYDDFNEA 353
Cdd:cd07084 334 TYELVTEEIFGPFAIVVEYKKDQLA 358
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
39-381 |
1.28e-12 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 69.17 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 39 DHETELLESLKIDLGKGSVEAYATEIGILL-------KSIKTARKELKNWAKTKQVDTPLFMfpsKSYIKPEPYGTILII 111
Cdd:cd07077 31 DTRQRLASEAVSERGAYIRSLIANWIAMMGcsesklyKNIDTERGITASVGHIQDVLLPDNG---ETYVRAFPIGVTMHI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 112 GPFNYPVQLLFEPLIGaIAAGNNAIIKPSELTPHVAQVVRKVIEDVFT----SDFVAVV-EGGVEETQTLINLP-FDYIF 185
Cdd:cd07077 108 LPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALALLFQAADAahgpKILVLYVpHPSDELAEELLSHPkIDLIV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 186 FTGSENVGRIVYEATskNLVPVTLELGGKSPVIVDETANIKVASDRISFGKFTNaGQTCVAPDYILVNRKVKNELIQSFK 265
Cdd:cd07077 187 ATGGRDAVDAAVKHS--PHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYVVDDVLDPLYEEFK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 266 QSIEEfygkniqnspdfgrivntkhfnrlsELLAIHRNEVIFGGHTdeneqyieptildgiTPQSKIMEEEIFGPLLPII 345
Cdd:cd07077 264 LKLVV-------------------------EGLKVPQETKPLSKET---------------TPSFDDEALESMTPLECQF 303
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1090914694 346 ----VYDDFNEAIDIIQSKSKPLSLYLFSEDENTTNCVLE 381
Cdd:cd07077 304 rvldVISAVENAWMIIESGGGPHTRCVYTHKINKVDDFVQ 343
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
81-373 |
1.93e-12 |
|
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: 69.04 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 81 WAKTKQVDTPLFMfpSKSYiKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELT----PHVAQVVRKVI-E 155
Cdd:cd07127 173 WEKPQGKHDPLAM--EKTF-TVVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAilplAITVQVAREVLaE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 156 DVFTSDFVAVVEGGVEE--TQTLINLP-FDYIFFTGSENVGRIVyEATSKNLVPVTlELGGKSPVIVDETANIKVASDRI 232
Cdd:cd07127 250 AGFDPNLVTLAADTPEEpiAQTLATRPeVRIIDFTGSNAFGDWL-EANARQAQVYT-EKAGVNTVVVDSTDDLKAMLRNL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 233 SFGKFTNAGQTCVAPDYILVNR---------KVKNELIQSFKQSIEEFYGKNIQNSPDFGRIVNTKHFNRLSELLAIHrn 303
Cdd:cd07127 328 AFSLSLYSGQMCTTPQNIYVPRdgiqtddgrKSFDEVAADLAAAIDGLLADPARAAALLGAIQSPDTLARIAEARQLG-- 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1090914694 304 EVIFGGHTDENEQYIE-----PTILDGITPQSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSK---PLSLYLFSEDE 373
Cdd:cd07127 406 EVLLASEAVAHPEFPDarvrtPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVRehgAMTVGVYSTDP 483
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
16-356 |
7.75e-10 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 60.74 E-value: 7.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 16 KTHQTKDIKFRKQQLKLLSKSIK----DHETELLESLKIDLGKGSVEAyateigillKSIKTARKELKNWAKTKQVDTPL 91
Cdd:cd07081 9 KVAQQGLSCKSQEMVDLIFRAAAeaaeDARIDLAKLAVSETGMGRVED---------KVIKNHFAAEYIYNVYKDEKTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 92 FMFPSKSY---IKPEPYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSD------F 162
Cdd:cd07081 80 VLTGDENGgtlIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAVAAgapenlI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 163 VAVVEGGVEETQTLINLP-FDYIFFTGSENVGRIVYEATsKNLVPVTlelGGKSPVIVDETANIKVASDRISFGKFTNAG 241
Cdd:cd07081 160 GWIDNPSIELAQRLMKFPgIGLLLATGGPAVVKAAYSSG-KPAIGVG---AGNTPVVIDETADIKRAVQSIVKSKTFDNG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 242 QTCVAPDYILVNRKVKNELIQSFK------------QSIEEFYGKNIQNSPDfgrIVNTKHFnRLSELLAI---HRNEVI 306
Cdd:cd07081 236 VICASEQSVIVVDSVYDEVMRLFEgqgaykltaeelQQVQPVILKNGDVNRD---IVGQDAY-KIAAAAGLkvpQETRIL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1090914694 307 FGghtdeneqyiEPTILDgitpQSKIMEEEIFGPLLPIIVYDDFNEAIDI 356
Cdd:cd07081 312 IG----------EVTSLA----EHEPFAHEKLSPVLAMYRAANFADADAK 347
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
104-359 |
1.36e-09 |
|
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: 59.86 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPvqLLFEPLIG----AIAAGNNAIIKP-------SELtphVAQVVRKVIED------VFtsdfvAVV 166
Cdd:cd07129 105 PLGPVAVFGASNFP--LAFSVAGGdtasALAAGCPVVVKAhpahpgtSEL---VARAIRAALRAtglpagVF-----SLL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 167 EGGVEET-QTLINLP-FDYIFFTGSENVGRIVYEATSKNL--VPVTLELGGKSPVIVDETAnIKVASDRI--SF-GKFT- 238
Cdd:cd07129 175 QGGGREVgVALVKHPaIKAVGFTGSRRGGRALFDAAAARPepIPFYAELGSVNPVFILPGA-LAERGEAIaqGFvGSLTl 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 239 NAGQTCVAPDYILVnrkVKNELIQSFKQSIeefyGKNIQNSPDF----GRIVntKHFNR-LSELLAIHRNEVIFGGHTDE 313
Cdd:cd07129 254 GAGQFCTNPGLVLV---PAGPAGDAFIAAL----AEALAAAPAQtmltPGIA--EAYRQgVEALAAAPGVRVLAGGAAAE 324
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1090914694 314 NEQYIEPTIL--DG---ITPQSkiMEEEIFGPLLPIIVYDDFNEAIDIIQS 359
Cdd:cd07129 325 GGNQAAPTLFkvDAaafLADPA--LQEEVFGPASLVVRYDDAAELLAVAEA 373
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
111-414 |
2.37e-09 |
|
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: 59.21 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 111 IGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIED--VFTSDFVAVVEGGVEETQTLINlPFDYIFFTG 188
Cdd:cd07128 151 INAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVEsgLLPEGALQLICGSVGDLLDHLG-EQDVVAFTG 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 189 SENVGRI--VYEATSKNLVPVTLELGGKSPVIVDETAnikvASDRISFGKF---------TNAGQTCVAPDYILVNRKVK 257
Cdd:cd07128 230 SAATAAKlrAHPNIVARSIRFNAEADSLNAAILGPDA----TPGTPEFDLFvkevaremtVKAGQKCTAIRRAFVPEARV 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 258 NELIQSFKQSIEEF-YGKNIQNSPDFGRIVNTKHFN----RLSELLAihRNEVIFGGHTDENEQ--------YIEPTILD 324
Cdd:cd07128 306 DAVIEALKARLAKVvVGDPRLEGVRMGPLVSREQREdvraAVATLLA--EAEVVFGGPDRFEVVgadaekgaFFPPTLLL 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 325 GITP--QSKIMEEEIFGPLLPIIVYDDFNEAIDIIQSKSKPLSLYLFSEDenttNCVLEELSFGGGAINDTLmHLAN--- 399
Cdd:cd07128 384 CDDPdaATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND----PAFARELVLGAAPYHGRL-LVLNrds 458
|
330 340
....*....|....*....|....*.
gi 1090914694 400 -----------PNLPFGGVGASGIGE 414
Cdd:cd07128 459 akestghgsplPQLVHGGPGRAGGGE 484
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
104-246 |
6.33e-09 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 58.45 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVA-QVVRKVIEDVFTSDFVAVVEG-GveET--QTLINL 179
Cdd:PRK11809 768 PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAaQAVRILLEAGVPAGVVQLLPGrG--ETvgAALVAD 845
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1090914694 180 P-FDYIFFTGSENVGRIVYEATSKNL------VPVTLELGGKSPVIVDETA-NIKVASDRISfGKFTNAGQTCVA 246
Cdd:PRK11809 846 ArVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSAlTEQVVADVLA-SAFDSAGQRCSA 919
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
104-355 |
4.99e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 54.94 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSD------FVAVVEGGVEETQTLI 177
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAggpdnlVVTVEEPTIETTNELM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 178 NLP-FDYIFFTGSENVGRIVYEATSKNLVPvtlelG-GKSPVIVDETANI-KVASDRISFGKFTNaGQTCVAPDYILVNR 254
Cdd:cd07121 177 AHPdINLLVVTGGPAVVKAALSSGKKAIGA-----GaGNPPVVVDETADIeKAARDIVQGASFDN-NLPCIAEKEVIAVD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 255 KVKNELIQSFK---------QSIEEFYGKNIQNSPdfGRIVNTKHFNR-LSELLAihrnevIFGGHTDENeqyIEPTILD 324
Cdd:cd07121 251 SVADYLIAAMQrngayvlndEQAEQLLEVVLLTNK--GATPNKKWVGKdASKILK------AAGIEVPAD---IRLIIVE 319
|
250 260 270
....*....|....*....|....*....|.
gi 1090914694 325 GITPQSKIMEEEIFgPLLPIIVYDDFNEAID 355
Cdd:cd07121 320 TDKDHPFVVEEQMM-PILPVVRVKNFDEAIE 349
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
104-380 |
1.76e-07 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 53.27 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIK-PSELTPHVAQVVRKVI------EDVftsDFVAvvEGGVEETQTL 176
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKvDSKVSVVMEQFLRLLHlcgmpaTDV---DLIH--SDGPTMNKIL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 177 INLPFDYIFFTGSENVG-RIVYEATSKnlvpVTLELGGKSPVI----VDETANIKVASDRISFGkftNAGQTCVAPDYIL 251
Cdd:cd07126 217 LEANPRMTLFTGSSKVAeRLALELHGK----VKLEDAGFDWKIlgpdVSDVDYVAWQCDQDAYA---CSGQKCSAQSILF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 252 VNrkvKNELIQSFKQSIEEFYGKNIQNSPDFGRIV---NTKHFNRLSELLAIHRNEVIFGGH--TDEN--EQY--IEPTI 322
Cdd:cd07126 290 AH---ENWVQAGILDKLKALAEQRKLEDLTIGPVLtwtTERILDHVDKLLAIPGAKVLFGGKplTNHSipSIYgaYEPTA 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1090914694 323 L------DGITPQSKIMEEEIFGPLLPIIVYDDFNE--AIDIIQSKSKPLSLYLFSEDENTTNCVL 380
Cdd:cd07126 367 VfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEVL 432
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
102-266 |
1.32e-05 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 47.49 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 102 PEPYGTILIIGPFNYPVQ-LLFEPLIgAIAAGNnAIIkpseLTPH---------VAQVVRKVIEDV-FTSDFVAVVEG-G 169
Cdd:cd07122 93 AEPVGVIAALIPSTNPTStAIFKALI-ALKTRN-AII----FSPHprakkcsieAAKIMREAAVAAgAPEGLIQWIEEpS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 170 VEETQTLINLP-FDYIFFTGSENVGRIVYeaTSKNlvPVtleLG---GKSPVIVDETANIKVASDRISFGK-FTNaGQTC 244
Cdd:cd07122 167 IELTQELMKHPdVDLILATGGPGMVKAAY--SSGK--PA---IGvgpGNVPAYIDETADIKRAVKDIILSKtFDN-GTIC 238
|
170 180
....*....|....*....|..
gi 1090914694 245 VAPDYILVNRKVKNELIQSFKQ 266
Cdd:cd07122 239 ASEQSVIVDDEIYDEVRAELKR 260
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
104-266 |
3.84e-05 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 46.05 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 104 PYGTILIIGPFNYPVQLLFEPLIGAIAAGNNAIIKPSELTPHVAQVVRKVIEDVFTSD------FVAVVEGGVEETQTLI 177
Cdd:PRK15398 129 PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAAggpenlVVTVAEPTIETAQRLM 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090914694 178 NLP-FDYIFFTGSENVGRIVYEaTSKNLVpvtlelG---GKSPVIVDETANI-KVASDRISFGKFTNaGQTCVAPDYILV 252
Cdd:PRK15398 209 KHPgIALLVVTGGPAVVKAAMK-SGKKAI------GagaGNPPVVVDETADIeKAARDIVKGASFDN-NLPCIAEKEVIV 280
|
170
....*....|....
gi 1090914694 253 NRKVKNELIQSFKQ 266
Cdd:PRK15398 281 VDSVADELMRLMEK 294
|
|
| |
