|
Name |
Accession |
Description |
Interval |
E-value |
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
2-378 |
0e+00 |
|
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase (pfam00465) proteins is generally found in apparent operons for the catabolism of rhamnose or fucose. Catabolism of both of these monosaccharides results in lactaldehyde which is reduced by this enzyme to 1,2 propanediol. This protein is alternatively known by the name 1,2 propanediol oxidoreductase. This enzyme is active under anaerobic conditions in E. coli while being inactivated by reactive oxygen species under aerobic conditions. Under aerobic conditions the lactaldehyde product of rhamnose and fucose catabolism is believed to be oxidized to lactate by a separate enzyme, lactaldehyde dehydrogenase. [Energy metabolism, Sugars]
Pssm-ID: 131686 [Multi-domain] Cd Length: 379 Bit Score: 592.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 2 SFMLALPKISLHGAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYA 81
Cdd:TIGR02638 1 SNRLILNETSYFGAGAIEDIVDEVKRRGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 82 AYREAGCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYS--GVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVK 159
Cdd:TIGR02638 81 AFKASGADYLIAIGGGSPIDTAKAIGIISNNPEFADVRSleGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEENKRK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 160 EVIIDPNIIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAR 239
Cdd:TIGR02638 161 FVCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGGKDLEAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 240 EQMAFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAAS 319
Cdd:TIGR02638 241 EQMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAEFTGEKYREIAKAMGVKTEGMSDEEAR 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 490994235 320 MEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELY 378
Cdd:TIGR02638 321 DAAVEAVKTLSKRVGIPEGLSELGVKEEDIPALAEAALADVCTGGNPRETTVEEIEELY 379
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
3-378 |
0e+00 |
|
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.
Pssm-ID: 341467 [Multi-domain] Cd Length: 377 Bit Score: 578.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 3 FMLALPKISLHGAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAA 82
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 83 YREAGCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVI 162
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 163 IDPNIIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQM 242
Cdd:cd08188 161 VDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKDLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 243 AFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAASMEA 322
Cdd:cd08188 241 AYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGENTEGLSDEEAAEAA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490994235 323 INAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELY 378
Cdd:cd08188 321 IEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENALKDACGPTNPRQATKEDVIAIY 376
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-382 |
1.55e-164 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 465.75 E-value: 1.55e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 1 MSFMLALPKISLHGAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGY 80
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 81 AAYREAGCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKE 160
Cdd:COG1454 81 AAAREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 161 VIIDPNIIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEARE 240
Cdd:COG1454 161 GIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLEARE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 241 QMAFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTrGMSDEAASM 320
Cdd:COG1454 241 KMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARALGLDV-GLSDEEAAE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994235 321 EAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELYLEAL 382
Cdd:COG1454 320 ALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
3-378 |
7.44e-159 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 451.23 E-value: 7.44e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 3 FMLALPKISLHGAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAA 82
Cdd:cd08176 1 NRFVLNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 83 YREAGCDYLIAFGGGSPIDTAKAIKILTANPG-PSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEV 161
Cdd:cd08176 81 YKESGADGIIAVGGGSSIDTAKAIGIIVANPGaDVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKRKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 162 IIDPNIIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQ 241
Cdd:cd08176 161 CVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNVEAREN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 242 MAFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAASME 321
Cdd:cd08176 241 MALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDEEAAEA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994235 322 AINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELY 378
Cdd:cd08176 321 AVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDALNDVCTPGNPREATKEDIIALY 377
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
12-378 |
1.92e-150 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 429.56 E-value: 1.92e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 12 LHGAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYL 91
Cdd:cd08551 5 VFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGADLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 92 IAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPDI 171
Cdd:cd08551 85 IAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLLPDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 172 AVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLAGM 251
Cdd:cd08551 165 AILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLASLLAGI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 252 AFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAASMEAINAIRALSK 331
Cdd:cd08551 245 AFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELLR 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 490994235 332 RVGIPQGFSQLGVSKADIEGWLDKALADPCAP-CNPRTASRDEVRELY 378
Cdd:cd08551 325 DLGIPTSLSELGVTEEDIPELAEDAMKSGRLLsNNPRPLTEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-374 |
2.92e-136 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 393.12 E-value: 2.92e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 8 PKISLHGAGAIGDMVKLVAGKRWgKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAG 87
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGA-RALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 88 CDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNI 167
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 168 IPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQY 247
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLAST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 248 LAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDtrgmSDEAASMEAINAIR 327
Cdd:pfam00465 240 LAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGED----SDEEAAEEAIEALR 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 490994235 328 ALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEV 374
Cdd:pfam00465 316 ELLRELGLPTTLSELGVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
1-378 |
2.08e-134 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 389.36 E-value: 2.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 1 MSFMLALPKISLHGAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGY 80
Cdd:PRK10624 1 MANRMILNETAYFGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 81 AAYREAGCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYS--GVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQV 158
Cdd:PRK10624 81 EVFKASGADYLIAIGGGSPQDTCKAIGIISNNPEFADVRSleGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 159 KEVIIDPNIIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGhhLEA 238
Cdd:PRK10624 161 KFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAGD--KEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 239 REQMAFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAA 318
Cdd:PRK10624 239 GEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVKVEGMSLEEA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 319 SMEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELY 378
Cdd:PRK10624 319 RNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAFDDVCTGGNPREATLEDIVELY 378
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-381 |
1.87e-133 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 386.50 E-value: 1.87e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 8 PKISLHGAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAG 87
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 88 CDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNI 167
Cdd:cd08194 81 CDFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 168 IPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQY 247
Cdd:cd08194 161 LPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 248 LAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAASMEAINAIR 327
Cdd:cd08194 241 EAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 490994235 328 ALSKRVGIPQgFSQLGVSKADIEGWLDK----ALADPCAPCNPRTASRDEVRELYLEA 381
Cdd:cd08194 321 RLCADLEIPT-LREYGIDEEEFEAALDKmaedALASGSPANNPRVPTKEEIIELYREA 377
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-380 |
1.14e-127 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341468 [Multi-domain] Cd Length: 378 Bit Score: 371.80 E-value: 1.14e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 8 PKIsLHGAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAG 87
Cdd:cd08189 6 PEL-FEGAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 88 CDYLIAFGGGSPIDTAKAIKILTANPGPS-TAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPN 166
Cdd:cd08189 85 CDAIIAIGGGSVIDCAKVIAARAANPKKSvRKLKGLLKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 167 IIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQ 246
Cdd:cd08189 165 LIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEARENMLLAS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 247 YLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAASMEAINAI 326
Cdd:cd08189 245 YYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGDSGESDSEKAEAFIAAI 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490994235 327 RALSKRVGIPQGFSQLgvSKADIEGWLDKAL--ADPCAPCnPRTASRDEVRELYLE 380
Cdd:cd08189 325 RELNRRMGIPTTLEEL--KEEDIPEIAKRALkeANPLYPV-PRIMDRKDCEELLRK 377
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-378 |
1.21e-127 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 371.49 E-value: 1.21e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGA---IGDMVKLVAGKrwgKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDY 90
Cdd:cd17814 10 GVGArklAGRYAKNLGAR---KVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 91 LIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPD 170
Cdd:cd17814 87 IVAVGGGSPIDCAKGIGIVVSNGGHILDYEGVDKVRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 171 IAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLAG 250
Cdd:cd17814 167 VSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMMLASLQAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 251 MAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAASMEAINAIRALS 330
Cdd:cd17814 247 LAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLR 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 490994235 331 KRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELY 378
Cdd:cd17814 327 EDLGIPETLSELGVDEEDIPELAKRAMKDPCLVTNPRRPTREDIEEIY 374
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-377 |
2.17e-121 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 356.07 E-value: 2.17e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLIA 93
Cdd:cd14863 11 GAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 94 FGGGSPIDTAKAIKILTANPGPSTAY-SGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPDIA 172
Cdd:cd14863 91 IGGGSVLDTAKAIAVLLTNPGPIIDYaLAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVPDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 173 VDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLAGMA 252
Cdd:cd14863 171 ILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENMLLASNLAGIA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 253 FNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAASMEAINAIRALSKR 332
Cdd:cd14863 251 FNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREFMKE 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 490994235 333 VGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVREL 377
Cdd:cd14863 331 LGIPSLFEDYGIDKEDLDKIAEAVLKDPFAMFNPRPITEEEVAEI 375
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
14-382 |
3.77e-120 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 352.58 E-value: 3.77e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLIA 93
Cdd:cd14861 9 GAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDGIIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 94 FGGGSPIDTAKAIKILTANPGPSTAYS----GVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIP 169
Cdd:cd14861 89 LGGGSAIDAAKAIALMATHPGPLWDYEdgegGPAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSPKLLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 170 DIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLA 249
Cdd:cd14861 169 KVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDLEARGEMMMAALMG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 250 GMAFnSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGmsdeaaSMEAINAIRAL 329
Cdd:cd14861 249 AVAF-QKGLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALGLGLGG------FDDFIAWVEDL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 490994235 330 SKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELYLEAL 382
Cdd:cd14861 322 NERLGLPATLSELGVTEDDLDELAELALADPCHATNPRPVTAEDYRALLREAL 374
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
7-382 |
4.18e-119 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 350.41 E-value: 4.18e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 7 LPKISLHGAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREA 86
Cdd:PRK09860 8 IPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 87 GCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPN 166
Cdd:PRK09860 88 NCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 167 IIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQ 246
Cdd:PRK09860 168 VTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 247 YLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAASMEAINAI 326
Cdd:PRK09860 248 FLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINAI 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490994235 327 RALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELYLEAL 382
Cdd:PRK09860 328 RELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAAM 383
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-382 |
9.02e-118 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 346.84 E-value: 9.02e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 12 LHGAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYL 91
Cdd:cd14865 10 VSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAGADGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 92 IAFGGGSPIDTAKAIKILTANPGPSTA-YSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPD 170
Cdd:cd14865 90 IAVGGGSVIDTAKGVNILLSEGGDDLDdYGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVSPFLLPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 171 IAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLAG 250
Cdd:cd14865 170 VAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGKDLEARLALAIAATMAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 251 MAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAM--GVDTRGMSDEAASMEAINAIRA 328
Cdd:cd14865 250 IAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALayGVTPAGRRAEEAIEAAIDLVRR 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 490994235 329 LSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELYLEAL 382
Cdd:cd14865 330 LHELCGLPTRLRDVGVPEEQLEAIAELALNDGAILFNPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
28-378 |
2.01e-107 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 320.21 E-value: 2.01e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 28 KRWG-KALIVTD-GQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLIAFGGGSPIDTAKA 105
Cdd:cd08185 22 LRPGkKALIVTGkGSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGCDFVIGLGGGSSMDAAKA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 106 IKILTANPGPSTAY----SGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPDIAVDDASVMLD 181
Cdd:cd08185 102 IAFMATNPGDIWDYifggTGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKKGIGHPALFPKVSIVDPELMLT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 182 IPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLAGMAFNSAGLGLV 261
Cdd:cd08185 182 VPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEAREKMAWASTLAGIVIANSGTTLP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 262 HALAHQPGA-THNLPHGVCNAILLPIIENFNRPHAVARFARVAQAmgvDTRGMSDEAASMEAINAIRALSKRVGIPQGFS 340
Cdd:cd08185 262 HGLEHPLSGyHPNIPHGAGLAALYPAYFEFTIEKAPEKFAFVARA---EASGLSDAKAAEDFIEALRKLLKDIGLDDLLS 338
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 490994235 341 QLGVSKADIEGWLDKAL--ADPCAPCNPRTASRDEVRELY 378
Cdd:cd08185 339 DLGVTEEDIPWLAENAMetMGGLFANNPVELTEEDIVEIY 378
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
13-381 |
3.65e-105 |
|
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341458 [Multi-domain] Cd Length: 379 Bit Score: 314.51 E-value: 3.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 13 HGAGAIgDMVKLVAGKRwgkALIVTDGQ-LVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYL 91
Cdd:cd08179 10 FGEGAL-EYLKTLKGKR---AFIVTGGGsMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDWI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 92 IAFGGGSPIDTAKAIKILTANPGpstaYSGVGKVKNAGVP-------LVAINTTAGTAAEMTSNAVIIDAERQVKEVIID 164
Cdd:cd08179 86 IAIGGGSVIDAAKAMWVFYEYPE----LTFEDALVPFPLPelrkkarFIAIPSTSGTGSEVTRASVITDTEKGIKYPLAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 165 PNIIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAF 244
Cdd:cd08179 162 FEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKDLEAREKMHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 245 GQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAqamgvdtrgMSDEAASMEA-- 322
Cdd:cd08179 242 ASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAA---------LLIGLTDEELve 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490994235 323 --INAIRALSKRVGIPQGFSQLGVS----KADIEGWLDKALADPCAPCNPRTASRDEVRELYLEA 381
Cdd:cd08179 313 dlIEAIEELNKKLGIPLSFKEAGIDedefFAKLDEMAENAMNDACTGTNPRKPTVEEMKELLKAA 377
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
8-379 |
3.05e-98 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 295.17 E-value: 3.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 8 PKIsLHGAGAIgDMVKLVAGKRwgkALIVTDGQLVKLGLLDSLFTALDeQQMSYHLFDEVFPNPTEALVQKGYAAYREAG 87
Cdd:cd08180 5 TKI-YSGEDSL-ERLKELKGKR---VFIVTDPFMVKSGMVDKVTDELD-KSNEVEIFSDVVPDPSIEVVAKGLAKILEFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 88 CDYLIAFGGGSPIDTAKAIKILTANpgpstaYSGVGKVKnagvPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNI 167
Cdd:cd08180 79 PDTIIALGGGSAIDAAKAIIYFALK------QKGNIKKP----LFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 168 IPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQY 247
Cdd:cd08180 149 LPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNASC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 248 LAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLP-IIENFnrphavarfarvaqamgvdtrgmsdeaasmeaINAI 326
Cdd:cd08180 229 MAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPyVIEFL--------------------------------IAAI 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994235 327 RALSKRVGIPQGFSQLGVSKAD----IEGWLDKALADPCAPCNPRTASRDEVRELYL 379
Cdd:cd08180 277 RRLNKKLGIPSTLKELGIDEEEfekaIDEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-377 |
3.63e-95 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 289.02 E-value: 3.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVAGkRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVfPNPTEALVQKGYAAYREAGCDYLIA 93
Cdd:cd08183 7 GRGSLQELGELAAE-LGKRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVS-GEPTVETVDAAVALAREAGCDVVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 94 FGGGSPIDTAKAIKILTANPGPSTAY-SGVGK---VKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIP 169
Cdd:cd08183 85 IGGGSVIDAAKAIAALLTNEGSVLDYlEVVGKgrpLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLRSPSMLP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 170 DIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLA 249
Cdd:cd08183 165 DVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 250 GMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRP---------HAVARFARVAQAmgvdtRGMSDEAASM 320
Cdd:cd08183 245 GLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRalrerepdsPALARYRELAGI-----LTGDPDAAAE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994235 321 EAINAIRALSKRVGIPqGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVREL 377
Cdd:cd08183 320 DGVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEKARGSSSMKGNPIELSDEELLEI 375
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
28-382 |
2.37e-94 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 287.90 E-value: 2.37e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 28 KRWG--KALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLIAFGGGSPIDTAKA 105
Cdd:cd08190 19 KRLGakKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVAVGGGSVIDTAKA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 106 IKILTANPGPSTAY----SGVGK-VKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPDIAVDDASVML 180
Cdd:cd08190 99 ANLYATHPGDFLDYvnapIGKGKpVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISSRYLRPTLAIVDPLLTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 181 DIPPSITAATGMDALTHAIEAF------------------VSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQM 242
Cdd:cd08190 179 TLPPRVTASSGFDVLCHALESYtarpynarprpanpderpAYQGSNPISDVWAEKAIELIGKYLRRAVNDGDDLEARSNM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 243 AFGQYLAGMAFNSAGLGLVHALAH-------------QPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVD 309
Cdd:cd08190 259 LLASTLAGIGFGNAGVHLPHAMAYpiaglvkdyrppgYPVDHPHVPHGLSVALTAPAVFRFTAPACPERHLEAAELLGAD 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994235 310 TRGMSDEAASMEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALadpcaP------CNPRTASRDEVRELYLEAL 382
Cdd:cd08190 339 TSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTL-----PqqrllkLNPRPVTEEDLEEIFEDAL 412
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
32-379 |
9.95e-94 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 286.01 E-value: 9.95e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 32 KALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLIAFGGGSPIDTAKAIKILTA 111
Cdd:cd08178 25 RAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFKPDVIIALGGGSAMDAAKIMWLFYE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 112 NP-----GPSTAYSGVGK--VKN----AGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPDIAVDDASVML 180
Cdd:cd08178 105 HPetkfeDLAQRFMDIRKrvYKFpklgKKAKLVAIPTTSGTGSEVTPFAVITDDKTGKKYPLADYALTPDMAIVDPELVM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 181 DIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLAGMAFNSAGLGL 260
Cdd:cd08178 185 TMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGNDIEAREKMHNAATIAGMAFANAFLGI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 261 VHALAHQPGATHNLPHGVCNAILLPIIENFN---------------RPHAVARFARVAQAMGVdtRGMSDEAASMEAINA 325
Cdd:cd08178 265 CHSLAHKLGAAFHIPHGRANAILLPHVIRYNatdpptkqaafpqykYYVAKERYAEIADLLGL--GGKTPEEKVESLIKA 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 490994235 326 IRALSKRVGIPQGFSQLGVSKADIEGWLDK----ALADPCAPCNPRTASRDEVRELYL 379
Cdd:cd08178 343 IEDLKKDLGIPTSIREAGIDEADFLAAVDKlaedAFDDQCTGANPRYPLISELKEILL 400
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-382 |
3.45e-92 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 281.81 E-value: 3.45e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVAGKRWgKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLIA 93
Cdd:cd08191 10 GPGARRALGRVAARLGS-RVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDPDVVIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 94 FGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPDIAV 173
Cdd:cd08191 89 LGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRPAVAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 174 DDASVMLDIPPSITAATGMDALTHAIEAF---------------VSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEA 238
Cdd:cd08191 169 VDPELTLTCPPGVTADSGIDALTHAIESYtardfppfprldpdpVYVGKNPLTDLLALEAIRLIGRHLPRAVRDGDDLEA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 239 REQMAFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAA 318
Cdd:cd08191 249 RSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVTTAGTSEEAA 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490994235 319 SmEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALA-DPCAPCNPRTASRDEVRELYLEAL 382
Cdd:cd08191 329 D-RAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSvTRLIANNPRPPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
32-378 |
8.71e-89 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 272.56 E-value: 8.71e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 32 KALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLIAFGGGSPIDTAKAIKILTA 111
Cdd:cd14862 26 RALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAKAAWVLYE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 112 NPGPS----TAYSGVGKVKNAgvPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPDIAVDDASVMLDIPPSIT 187
Cdd:cd14862 106 RPDLDpediSPLDLLGLRKKA--KLIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 188 AATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLAGMAFNSAGLGLVHALAHQ 267
Cdd:cd14862 184 AGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGDDLEAREKMHNAATIAGLAFGNSQAGLAHALGHS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 268 PGATHNLPHGVCNAILLPIIENFNRPHAVARFARvAQAMGVDTRgmSDEAASMEAINAIRALSKRVGIPQGFSQLGVSKA 347
Cdd:cd14862 264 LGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDL-LKLLGIEAR--DEEEALKKLVEAIRELYKEVGQPLSIKDLGISEE 340
|
330 340 350
....*....|....*....|....*....|....*
gi 490994235 348 DIEGWLDK----ALADPCAPCNPRTASRDEVRELY 378
Cdd:cd14862 341 EFEEKLDElveyAMEDSCTITSPRPPSEEDLKKLF 375
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
14-382 |
1.34e-88 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 272.08 E-value: 1.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLIA 93
Cdd:cd08193 10 GAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAGADGVIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 94 FGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAErQVKEVIIDPNIIPDIAV 173
Cdd:cd08193 90 FGGGSSMDVAKLVALLAGSDQPLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIVTTGE-TEKKGVVSPQLLPDVAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 174 DDASVMLDIPPSITAATGMDALTHAIEAFVS-VGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLAGMA 252
Cdd:cd08193 169 LDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDALAREALRLLGANLRRAVEDGSDLEAREAMLLGSMLAGQA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 253 FNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAASMEAINAIRALSKR 332
Cdd:cd08193 249 FANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVEA 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490994235 333 VGIPQGFSQLGVSKADIEgwldkALADPCA------PCNPRTASRDEVRELYLEAL 382
Cdd:cd08193 329 SGLPTRLRDVGVTEEDLP-----MLAEDAMkqtrllVNNPREVTEEDALAIYQAAL 379
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
32-381 |
1.42e-88 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 285.16 E-value: 1.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 32 KALIVTDGQLVKLGLLDSLFTALD--EQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLIAFGGGSPIDTAKAIKIL 109
Cdd:PRK13805 482 RAFIVTDRFMVELGYVDKVTDVLKkrENGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMWLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 110 TANPgpSTAYSGVG------------------KVKnagvpLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPDI 171
Cdd:PRK13805 562 YEHP--ETDFEDLAqkfmdirkriykfpklgkKAK-----LVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDV 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 172 AVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDG-HHLEAREQMAFGQYLAG 250
Cdd:PRK13805 635 AIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGaKDPEAREKMHNASTIAG 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 251 MAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLP-IIE-------------NFNRPHAVARFARVAQAMGVdtRGMSDE 316
Cdd:PRK13805 715 MAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPhVIRynatdppkqaafpQYEYPRADERYAEIARHLGL--PGSTTE 792
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994235 317 AASMEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDK----ALADPCAPCNPRTASRDEVRELYLEA 381
Cdd:PRK13805 793 EKVESLIKAIEELKAELGIPMSIKEAGVDEADFLAKLDElaelAFDDQCTGANPRYPLISELKEILLDA 861
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
5-381 |
9.37e-83 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 258.03 E-value: 9.37e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 5 LALPKISLHGAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYR 84
Cdd:PRK15454 24 FSVPPVTLCGPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 85 EAGCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIID 164
Cdd:PRK15454 104 ESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 165 PNIIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAF 244
Cdd:PRK15454 184 ASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESMLL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 245 GQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMgvdtrgMSDEAASMEAIN 324
Cdd:PRK15454 264 ASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRAL------RTKKSDDRDAIN 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994235 325 AIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELYLEA 381
Cdd:PRK15454 338 AVSELIAEVGIGKRLGDVGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLYAAA 394
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-378 |
4.82e-81 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 252.50 E-value: 4.82e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQQMSYhlFDEVFPNPTEALVQKGYAAYREAGCDYLIA 93
Cdd:cd08196 12 GEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVAV--FSDVEPNPTVENVDKCARLARENGADFVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 94 FGGGSPIDTAKAIKILTANPGPSTAY-SGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPDIA 172
Cdd:cd08196 90 IGGGSVLDTAKAAACLAKTDGSIEDYlEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLVSPGFYPDIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 173 VDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLAGMA 252
Cdd:cd08196 170 IVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPNDKEAREKMALASLLAGLA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 253 FNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGmsdeaasmEAINAIRALSKR 332
Cdd:cd08196 250 FSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQLGFKDAE--------ELADKIEELKKR 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 490994235 333 VGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELY 378
Cdd:cd08196 322 IGLRTRLSELGITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
14-378 |
4.74e-71 |
|
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.
Pssm-ID: 341461 [Multi-domain] Cd Length: 370 Bit Score: 226.72 E-value: 4.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGLLDSLFTALDEQqMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLIA 93
Cdd:cd08182 7 GPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDALGGR-IPVVVFSDFSPNPDLEDLERGIELFRESGPDVIIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 94 FGGGSPIDTAKAIKILTANPGPSTAYS--GVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPDI 171
Cdd:cd08182 86 VGGGSVIDTAKAIAALLGSPGENLLLLrtGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPSLYPDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 172 AVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLAGM 251
Cdd:cd08182 166 AILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEASLLAGL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 252 AFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAasmEAINAIRALSK 331
Cdd:cd08182 246 AISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDECDDDPRGREILLALGASDPA---EAAERLRALLE 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 490994235 332 RVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELY 378
Cdd:cd08182 323 SLGLPTRLSEYGVTAEDLEALAASVNTPERLKNNPVRLSEEDLLRLL 369
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
32-378 |
8.31e-68 |
|
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.
Pssm-ID: 341460 [Multi-domain] Cd Length: 358 Bit Score: 217.84 E-value: 8.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 32 KALIVTdGQ--LVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLIAFGGGSPIDTAKAIKIL 109
Cdd:cd08181 27 KALIVT-GKhsAKKNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELARKEGADFVIGIGGGSPLDAAKAIALL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 110 TANPGPSTAYSGVGKVKNAgVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPDIAVDDASVMLDIPPSITAA 189
Cdd:cd08181 106 AANKDGDEDLFQNGKYNPP-LPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTID 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 190 TGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLAGMAFNSAGLGLVHALAHQPG 269
Cdd:cd08181 185 TAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 270 ATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGvdtrgmsdeaasMEAINAIRA-LSKRVGIPQgfsqlGVSKAD 348
Cdd:cd08181 265 YFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLG------------FGSIEEFQKfLNRLLGKKE-----ELSEEE 327
|
330 340 350
....*....|....*....|....*....|
gi 490994235 349 IEGWLDKALADPCAPCNPRTASRDEVRELY 378
Cdd:cd08181 328 LEKYADEAMKAKNKKNTPGNVTKEDILRIY 357
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
14-382 |
6.93e-65 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 210.97 E-value: 6.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVAGKRWGKALIVTDGQLVKL-GLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLI 92
Cdd:cd08186 7 GVGAIAKIKDILKDLGIDKVIIVTGRSSYKKsGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 93 AFGGGSPIDTAKAIKILTANPGpSTA---YSGVGKVKNAgVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIP 169
Cdd:cd08186 87 AIGGGSPIDTAKSVAVLLAYGG-KTArdlYGFRFAPERA-LPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 170 DIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLA 249
Cdd:cd08186 165 LYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYASMIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 250 GMAFNSAGLGLVHALAHQ-PGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAAsmEAINAIRA 328
Cdd:cd08186 245 GIAIDNGLLHLTHALEHPlSGLKPELPHGLGLALLGPAVVKYIYKAVPETLADILRPIVPGLKGTPDEAE--KAARGVEE 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 490994235 329 LSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPC----NPRTASRDEVRELYLEAL 382
Cdd:cd08186 323 FLFSVGFTEKLSDYGFTEDDVDRLVELAFTTPSLDLllslAPVEVTEEVVREIYEESL 380
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
14-378 |
1.64e-60 |
|
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process; The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.
Pssm-ID: 341466 [Multi-domain] Cd Length: 382 Bit Score: 199.97 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVagKRWG-KALIVTDGQ-LVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYL 91
Cdd:cd08187 13 GKGAIEELGEEI--KKYGkKVLLVYGGGsIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVDFI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 92 IAFGGGSPIDTAKAIKILTANPG-PSTAYSGVGKVKNAgVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPD 170
Cdd:cd08187 91 LAVGGGSVIDAAKAIAAGAKYDGdVWDFFTGKAPPEKA-LPVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 171 IAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAH-PLTDANALEAIRLINLWLPQAVDDGHHLEAREQMafgQYLA 249
Cdd:cd08187 170 FSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDaPLQDRLAEGLLRTVIENGPKALKDPDDYEARANL---MWAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 250 GMAFN-SAGLGL-----VHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQA-MGVDTrGMSDEAASMEA 322
Cdd:cd08187 247 TLALNgLLGAGRggdwaTHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRvFGIDP-GGDDEETALEG 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490994235 323 INAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRTASRDEVRELY 378
Cdd:cd08187 326 IEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGFKPLTREDIEEIL 381
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
14-377 |
2.68e-55 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341456 [Multi-domain] Cd Length: 337 Bit Score: 185.02 E-value: 2.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVAGKRWGKALIVTDGQLVKLGllDSLFTALDEQQMsyHLFDEVFPNPTEALVQKGYAAYREAGCDYLIA 93
Cdd:cd08177 7 GAGTLAELAEELERLGARRALVLSTPRQRALA--ERVAALLGDRVA--GVFDGAVMHVPVEVAERALAAAREAGADGLVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 94 FGGGSPIDTAKAIKILTanpgpstaysgvgkvknaGVPLVAINTT-AGtaAEMTSNAVIIDAERqvKEVIIDPNIIPDIA 172
Cdd:cd08177 83 IGGGSAIGLAKAIALRT------------------GLPIVAVPTTyAG--SEMTPIWGETEDGV--KTTGRDPRVLPRTV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 173 VDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQYLAGMA 252
Cdd:cd08177 141 IYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 253 FNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTrgmsdeaasmeAINAIRALSKR 332
Cdd:cd08177 221 LGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGGGD-----------AAGGLYDLARR 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 490994235 333 VGIPQGFSQLGVSKADIEGWLDKALADPCApcNPRTASRDEVREL 377
Cdd:cd08177 290 LGAPTSLRDLGMPEDDIDRAADLALANPYP--NPRPVERDALRAL 332
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-377 |
3.79e-55 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 185.58 E-value: 3.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 8 PKISLhGAGAIGDMVKLVagKRWG-KALIVTDGQLVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREA 86
Cdd:cd14864 5 PNIVF-GADSLERIGEEV--KEYGsRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 87 GCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPN 166
Cdd:cd14864 82 GADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKAQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 167 IIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQMAFGQ 246
Cdd:cd14864 162 GLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEELLAQAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 247 YLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGMSDEAASMEAINAI 326
Cdd:cd14864 242 CLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGV 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 490994235 327 RALSKRVGIPQGFSQLGVsKADIEGWLDKALADPCAPCNPRTASRDEVREL 377
Cdd:cd14864 322 RRLIAQLNLPTRLKDLDL-ASSLEQLAAIAEDAPKLNGLPRSMSSDDIFDI 371
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-381 |
5.91e-52 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 177.42 E-value: 5.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 13 HGAGAIGDMVKLVAGKRWGKALIVTDGQLVKLG-LLDSLFTALDEQQMsyHLFDEVFPNPTEALVQKGYAAYREAGCDYL 91
Cdd:cd14866 10 SGRGALARLGRELDRLGARRALVVCGSSVGANPdLMDPVRAALGDRLA--GVFDGVRPHSPLETVEAAAEALREADADAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 92 IAFGGGSPIDTAKAIKILTANPGP----STAYSGVG-----KVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERQvKEVI 162
Cdd:cd14866 88 VAVGGGSAIVTARAASILLAEDRDvrelCTRRAEDGlmvspRLDAPKLPIFVVPTTPTTADVKAGSAVTDPPAGQ-RLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 163 IDPNIIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHlEAREQM 242
Cdd:cd14866 167 FDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLADDDDP-AARADL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 243 AFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGmsDEAASMEA 322
Cdd:cd14866 246 VLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGVADAG--DEASAAAV 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 323 INAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPR-TASRDEVRELYLEA 381
Cdd:cd14866 324 VDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNNPRpVPTAEELEALLEAA 383
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
14-382 |
3.94e-49 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 170.25 E-value: 3.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVAgKRWGKALIVTDGQ-LVKLGLLDSLFTALDEQQMSYHLFDEVFPNPTEALVQKGYAAYREAGCDYLI 92
Cdd:COG1979 15 GKGQIAKLGEEIP-KYGKKVLLVYGGGsIKKNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDFIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 93 AFGGGSPIDTAKAIKILTANPG-PSTAYSGVGKVKNAgVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPDI 171
Cdd:COG1979 94 AVGGGSVIDGAKAIAAGAKYDGdPWDILTGKAPVEKA-LPLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFPKF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 172 AVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAH-PLTDANAlEAIrLINL--WLPQAVDDGHHLEAREQMafgQYL 248
Cdd:COG1979 173 SILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDaPLQDRFA-EGL-LRTLieEGPKALKDPEDYDARANL---MWA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 249 AGMAFN-SAGLGL-----VHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQ-AMGVDtrGMSDEAASME 321
Cdd:COG1979 248 ATLALNgLIGAGVpqdwaTHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAErVWGIT--EGDDEERALE 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994235 322 AINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPC-NPRTASRDEVRELYLEAL 382
Cdd:COG1979 326 GIEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMTALgEFKDLTPEDVREILELAL 387
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
13-382 |
1.02e-48 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 168.97 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 13 HGAGAIGDMVKLVAgkRWG--KALIVTDGQL-VKLGLLDSLFTALDEqqMSYHLFDEVFPNPTEALVQKGYAAYREAGCD 89
Cdd:cd08192 6 YGPGAVEALLHELA--TLGasRVFIVTSKSLaTKTDVIKRLEEALGD--RHVGVFSGVRQHTPREDVLEAARAVREAGAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 90 YLIAFGGGSPIDTAKAIKILTAN--PGPSTAYS------GVGKVKNAGVPLVAINTTAgTAAEMTSNAVIIDAERQVKEV 161
Cdd:cd08192 82 LLVSLGGGSPIDAAKAVALALAEdvTDVDQLDAledgkrIDPNVTGPTLPHIAIPTTL-SGAEFTAGAGATDDDTGHKQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 162 IIDPNIIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQAVDDGHHLEAREQ 241
Cdd:cd08192 161 FAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADPEDLEARLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 242 MAFGQYLAGMAF-NSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGVDTRGmsDEAASM 320
Cdd:cd08192 241 CQLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALGLVTGG--LGREAA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490994235 321 EAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRT-ASRDEVRELyLEAL 382
Cdd:cd08192 319 DAADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRPiTDKDDVLEI-LESA 380
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-357 |
1.82e-37 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 136.34 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 8 PKISLHGAGAIGDM--VKLVAGKRwgkALIVTDGQLVKlGLLDSLFTALDEQqMSYHLFDEVFPNPTEALVQKGYAAYRE 85
Cdd:cd07766 1 PTRIVFGEGAIAKLgeIKRRGFDR---ALVVSDEGVVK-GVGEKVADSLKKG-LAVAIFDFVGENPTFEEVKNAVERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 86 AGCDYLIAFGGGSPIDTAKAIKILTanpgpstaysgvgkvkNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEViiDP 165
Cdd:cd07766 76 AEADAVIAVGGGSTLDTAKAVAALL----------------NRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQV--GP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 166 NIIPDIAVDDASVMLDIPPSITAATGMDALTHAIEafvsvgahpltdanaleairlinlwlpqavddghhleaREQMAFG 245
Cdd:cd07766 138 HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE--------------------------------------LEKVVEA 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 246 QYLAGMA-FNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRphavarfarvaqamgvDTRGMSDeaasmEAIN 324
Cdd:cd07766 180 ATLAGMGlFESPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVAN----------------DMNPEPE-----AAIE 238
|
330 340 350
....*....|....*....|....*....|...
gi 490994235 325 AIRALSKRVGIPQGFSQLGVSKADIEGWLDKAL 357
Cdd:cd07766 239 AVFKFLEDLGLPTHLADLGVSKEDIPKLAEKAL 271
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
71-380 |
2.36e-27 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 111.15 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 71 PTEALVQKGYAAYREAGCDYLIAFGGGSPIDTAKaikILT-ANPGPSTA-YSG---VGKVKnagvPLVAINTTAGTAAEM 145
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAK---LLAlKGISPVLDlFDGkipLIKEK----ELIIVPTTCGTGSEV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 146 TSNAVIIDAERQVKeviidpniiPDIAVD----DASVML-----DIPPSITAATGMDALTHAIEAFVSVGAHPLTDANAL 216
Cdd:cd14860 135 TNISIVELTSLGTK---------KGLAVDelyaDKAVLIpellkGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 217 EAIRLINLWLPQAVDDGHhlEAREQMaFGQYL-----AGMAFNSAGLGLVHALAHQPGATHNLPHGVCN-AILLPIIENF 290
Cdd:cd14860 206 KAIEMILEGYQEIAEKGE--EARFPL-LGDFLiasnyAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANyAVFTGVLKNY 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 291 ---NRPHAVARF-ARVAQAMGVdtrgmsDEAASMEAINAI--RALSKRvgipqGFSQLGVSKADIEGWLD-------KAL 357
Cdd:cd14860 283 qekNPDGEIKKLnEFLAKILGC------DEEDVYDELEELlnKILPKK-----PLHEYGMKEEEIDEFADsvmenqqRLL 351
|
330 340
....*....|....*....|...
gi 490994235 358 ADpcapcNPRTASRDEVRELYLE 380
Cdd:cd14860 352 AN-----NYVPLDREDVAEIYKE 369
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
14-316 |
7.54e-27 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 109.28 E-value: 7.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVAGKRW---GKALIVTDGQLVKLGLLDSLFTaldeQQMSYHLFDEVFPNPTEALVQKGYAAYREAGC-- 88
Cdd:cd08184 7 GRGSFDQLGELLAERRKsnnDYVVFFIDDVFKGKPLLDRLPL----QNGDLLIFVDTTDEPKTDQIDALRAQIRAENDkl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 89 -DYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAERqvKEVIIDPNI 167
Cdd:cd08184 83 pAAVVGIGGGSTMDIAKAVSNMLTNPGSAADYQGWDLVKNPGIYKIGVPTLSGTGAEASRTAVLTGPEK--KLGINSDYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 168 IPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPQavDDGHHLEAREQMAFGQY 247
Cdd:cd08184 161 VFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELCRDVFLS--DDMMSPENREKLMVASY 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994235 248 LAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFnRPHAVARFARVAQAMGVD-----TRGMSDE 316
Cdd:cd08184 239 LGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCIVFNVLEEF-YPEGVKEFREMLEKQNITlpkgiCKDLTDE 311
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
3-355 |
1.79e-18 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 86.00 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 3 FMLALPKISLHGAGAIGDMVKLV-AGKRwgkaLIVT--DGQLVKLGLLDSLFTALdeQQMSYHLFDEVFPNPTEALVQKG 79
Cdd:PRK15138 4 FNLHTPTRILFGKGAIAGLREQIpADAR----VLITygGGSVKKTGVLDQVLDAL--KGMDVLEFGGIEPNPTYETLMKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 80 YAAYREAGCDYLIAFGGGSPIDTAKAIKI---LTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDAER 156
Cdd:PRK15138 78 VKLVREEKITFLLAVGGGSVLDGTKFIAAaanYPENIDPWHILETGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 157 QVKEVIIDPNIIPDIAVDDASVMLDIPPSITAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWL-PQAVDDGHH 235
Cdd:PRK15138 158 GDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAKIQDRFAEGILLTLIEEgPKALKEPEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 236 LEAREQMafgQYLAGMAFNS-AGLGL-----VHALAHQPGATHNLPHGVCNAILLPIIENFNRPHAVARFARVAQAMGvD 309
Cdd:PRK15138 238 YDVRANV---MWAATQALNGlIGAGVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVW-N 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 490994235 310 TRGMSDEAASMEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDK 355
Cdd:PRK15138 314 ITEGSDDERIDAAIAATRNFFEQMGVPTRLSDYGLDGSSIPALLKK 359
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
7-350 |
3.12e-14 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 73.28 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 7 LPKISLHGAGAIGDMVKLVAgKRWGKALIVTDGQLVKLgLLDSLFTALDEQQMSYHLFdEVFPNPTEALVQKGYAAYREA 86
Cdd:COG0371 5 LPRRYVQGEGALDELGEYLA-DLGKRALIITGPTALKA-AGDRLEESLEDAGIEVEVE-VFGGECSEEEIERLAEEAKEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 87 GCDYLIAFGGGSPIDTAKAIkiltanpgpstAYsgvgkvkNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPN 166
Cdd:COG0371 82 GADVIIGVGGGKALDTAKAV-----------AY-------RLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 167 IIPDIAVdDASVMLDIPPSITAAtGM-DALTHAIEAFVSVGAH------PLTDA--------------NALEAIrlinlw 225
Cdd:COG0371 144 NPDLVLV-DTDIIAKAPVRLLAA-GIgDALAKWYEARDWSLAHrdlageYYTEAavalarlcaetlleYGEAAI------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 226 lpQAVDDGHHLEAREQMAFGQ-YLAGMAFN----SAGLGLVHALAHQ----PgATHNLPHGvcnaillpiienfnrpHAV 296
Cdd:COG0371 216 --KAVEAGVVTPALERVVEANlLLSGLAMGigssRPGSGAAHAIHNGltalP-ETHHALHG----------------EKV 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 490994235 297 ArFARVAQAMgvdTRGMSDEaasmeaINAIRALSKRVGIPQGFSQLGVSKADIE 350
Cdd:COG0371 277 A-FGTLVQLV---LEGRPEE------IEELLDFLRSVGLPTTLADLGLDDETEE 320
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
8-376 |
1.11e-10 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 62.17 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 8 PKISLHGAGAIGDMVKLVAgkRWG-KALIVTDGQ-LVKLGllDSLFTALDEQQMSYHLfdEVFP-NPTEALVQKgYAAY- 83
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIA--PLGkKALIIGGKTaLEAVG--EKLEKSLEEAGIDYEV--EVFGgECTEENIER-LAEKa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 84 REAGCDYLIAFGGGSPIDTAKAIkiltanpgpstAYSgvgkvknAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVII 163
Cdd:cd08550 74 KEEGADVIIGIGGGKVLDTAKAV-----------ADR-------LGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 164 DPNIIPDIAVdDASVMLDIPPSITAATGMDALTHAIEAFVSV--GAHPLTD----ANALEAIRLINLWLPQAVDD---GH 234
Cdd:cd08550 136 LKRSPDLVLV-DTDIIAAAPVRYLAAGIGDTLAKWYEARPSSrgGPDDLALqaavQLAKLAYDLLLEYGVQAVEDvrqGK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 235 HLEAREQMAFGQ-YLAGMAFNSAG----LGLVHA----LAHQPGaTHNLPHG----VCNAILLpIIENfnrphavarfar 301
Cdd:cd08550 215 VTPALEDVVDAIiLLAGLVGSLGGggcrTAAAHAihngLTKLPE-THGTLHGekvaFGLLVQL-ALEG------------ 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994235 302 vaqamgvdtrgmsdeaASMEAINAIRALSKRVGIPQGFSQLGV--SKADIEGWLDKALADP-CAPCNPRTASRDEVRE 376
Cdd:cd08550 281 ----------------RSEEEIEELIEFLRRLGLPVTLEDLGLelTEEELRKIAEYACDPPdMAHMLPFPVTPEMLAE 342
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
14-381 |
1.87e-10 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 61.66 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 14 GAGAIGDMVKLVA--GKrwgKALIVTDGQLVKLgLLDSLFTALDEQQMSYHLfdEVFPNP-TEALVQKGYAAYREAGCDY 90
Cdd:cd08170 7 GPGALDRLGEYLAplGK---KALVIADPFVLDL-VGERLEESLEKAGLEVVF--EVFGGEcSREEIERLAAIARANGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 91 LIAFGGGSPIDTAKAIkiltanpgpstAYsgvgkvkNAGVPLVAINTTAGTAAEMTSNAVIIDAERQVKEVIIDPNIIPD 170
Cdd:cd08170 81 VIGIGGGKTIDTAKAV-----------AD-------YLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 171 IAVDDAsVMLDIPPSITAAtGM-DAL--------------------------------------THAIEAFVSVGAHPLT 211
Cdd:cd08170 143 VLVDTE-IIAKAPVRFLVA-GMgDALatyfearacarsgapnmaggrptlaalalaelcydtllEYGVAAKAAVEAGVVT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 212 DanALEAIrlinlwlpqavddghhLEAReqmafgQYLAGMAFNSAGLGLVHALAH---QPGATHNLPHGVCnaillpiie 288
Cdd:cd08170 221 P--ALEAV----------------IEAN------TLLSGLGFESGGLAAAHAIHNgltALPETHHLLHGEK--------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 289 nfnrphaVArFARVAQAMgvdtrgMsdEAASMEAINAIRALSKRVGIPQGFSQLGVSKADIEGWL---DKALADPCAPCN 365
Cdd:cd08170 268 -------VA-FGTLVQLV------L--EGRPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRkvaEAACAPGETIHN 331
|
410
....*....|....*..
gi 490994235 366 -PRTASRDEVRELYLEA 381
Cdd:cd08170 332 mPFPVTPEDVVDAILAA 348
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
1-363 |
3.31e-06 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 48.66 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 1 MSFMLALPKISLHGAGAIGDMVKLVA--GKRwgkALIVTDGQLVKLgLLDSLFTALDEQQMSYHLfdEVFP-NPTEALVQ 77
Cdd:PRK09423 1 MDRIFISPSKYVQGKGALARLGEYLKplGKR---ALVIADEFVLGI-VGDRVEASLKEAGLTVVF--EVFNgECSDNEID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 78 KGYAAYREAGCDYLIAFGGGSPIDTAKAIkiltanpgpstAYsgvgkvkNAGVPLVAINTTAGTAAEMTSNAVIIDAERQ 157
Cdd:PRK09423 75 RLVAIAEENGCDVVIGIGGGKTLDTAKAV-----------AD-------YLGVPVVIVPTIASTDAPTSALSVIYTEEGE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 158 VKEVIIDPNIIPDIAVD--------------------------------DASVMLDIPPSITAATGMDA-----LTHAIE 200
Cdd:PRK09423 137 FERYLFLPKNPDLVLVDtaiiakaparflaagigdalatwfearacsrsGGTTMAGGKPTLAALALAELcyetlLEDGLK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 201 AFVSVGAHPLTDanALEAIrlinlwlpqavddghhLEAReqmafgQYLAGMAFNSAGLGLVHALaHQpG-----ATHNLP 275
Cdd:PRK09423 217 AKLAVEAKVVTP--ALENV----------------IEAN------TLLSGLGFESGGLAAAHAI-HN-GltaleDTHHLT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 276 HGvcnaillpiienfnrpHAVArFARVAQamgvdtrgMSDEAASMEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDK 355
Cdd:PRK09423 271 HG----------------EKVA-FGTLTQ--------LVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSDEELRKV 325
|
....*...
gi 490994235 356 ALAdPCAP 363
Cdd:PRK09423 326 AEA-ACAE 332
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
13-161 |
1.23e-04 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 43.66 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 13 HGAGAIGDMVKLVAGKRWGKALIVTDGQlvklglldslftaldeqqmSYHLFDEVFPNPTEALVQ----KGYAAYREA-- 86
Cdd:cd08172 6 CEEGALKELPELLSEFGIKRPLIIHGEK-------------------SWQAAKPYLPKLFEIEYPvlryDGECSYEEIdr 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 87 --------GCDYLIAFGGGSPIDTAKAikilTANpgpstaysgvgkvkNAGVPLVAINTTAGTAAEMTSNAVIIDAERQV 158
Cdd:cd08172 67 laeeakehQADVIIGIGGGKVLDTAKA----VAD--------------KLNIPLILIPTLASNCAAWTPLSVIYDEDGEF 128
|
...
gi 490994235 159 KEV 161
Cdd:cd08172 129 IGY 131
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
7-104 |
6.24e-03 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 38.34 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994235 7 LPKISLHGAGAIGDMVKLVAG-KRWGKALIVTDGQLVKLG---LLDSLftaldEQQMSYHLFdeVFPNPTEALVQKGYAA 82
Cdd:PRK00843 10 LPRDVVVGHGVLDDIGDVCSDlKLTGRALIVTGPTTKKIAgdrVEENL-----EDAGDVEVV--IVDEATMEEVEKVEEK 82
|
90 100
....*....|....*....|..
gi 490994235 83 YREAGCDYLIAFGGGSPIDTAK 104
Cdd:PRK00843 83 AKDVNAGFLIGVGGGKVIDVAK 104
|
|
| |
