|
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: 617.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 2 SFMLALPKISLHGAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYA 81
Cdd:TIGR02638 1 SNRLILNETSYFGAGAIEDIVDEVKRRGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 82 AYQAARCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYS--GVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVK 159
Cdd:TIGR02638 81 AFKASGADYLIAIGGGSPIDTAKAIGIISNNPEFADVRSleGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEENKRK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 160 EVIIDPNLIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAR 239
Cdd:TIGR02638 161 FVCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGGKDLEAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 240 EQMAFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAAS 319
Cdd:TIGR02638 241 EQMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAEFTGEKYREIAKAMGVKTEGMSDEEAR 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 914217994 320 MEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELY 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: 608.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 3 FMLALPKISLHGAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAA 82
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 83 YQAARCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVI 162
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 163 IDPNLIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQM 242
Cdd:cd08188 161 VDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKDLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 243 AFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAASMEA 322
Cdd:cd08188 241 AYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGENTEGLSDEEAAEAA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 914217994 323 INAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELY 378
Cdd:cd08188 321 IEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENALKDACGPTNPRQATKEDVIAIY 376
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-382 |
8.10e-174 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 489.25 E-value: 8.10e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 1 MSFMLALPKISLHGAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGY 80
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 81 AAYQAARCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKE 160
Cdd:COG1454 81 AAAREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 161 VIIDPNLIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQARE 240
Cdd:COG1454 161 GIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLEARE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 241 QMAFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTrGMSDEAASM 320
Cdd:COG1454 241 KMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARALGLDV-GLSDEEAAE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914217994 321 EAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELYLEAL 382
Cdd:COG1454 320 ALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
3-378 |
3.25e-165 |
|
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: 467.41 E-value: 3.25e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 3 FMLALPKISLHGAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAA 82
Cdd:cd08176 1 NRFVLNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 83 YQAARCDYLIAFGGGSPIDTAKAIKILTANPG-PSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEV 161
Cdd:cd08176 81 YKESGADGIIAVGGGSSIDTAKAIGIIVANPGaDVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKRKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 162 IIDPNLIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQ 241
Cdd:cd08176 161 CVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNVEAREN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 242 MAFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAASME 321
Cdd:cd08176 241 MALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDEEAAEA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 914217994 322 AINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELY 378
Cdd:cd08176 321 AVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDALNDVCTPGNPREATKEDIIALY 377
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
12-378 |
3.63e-158 |
|
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: 449.21 E-value: 3.63e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 12 LHGAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYL 91
Cdd:cd08551 5 VFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGADLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 92 IAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPDI 171
Cdd:cd08551 85 IAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLLPDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 172 AVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLAGM 251
Cdd:cd08551 165 AILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLASLLAGI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 252 AFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAASMEAINAIRALSK 331
Cdd:cd08551 245 AFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELLR 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 914217994 332 RVGIPQGFSQLGVSKADIEGWLDKALADPCAP-CNPRPASRDEVRELY 378
Cdd:cd08551 325 DLGIPTSLSELGVTEEDIPELAEDAMKSGRLLsNNPRPLTEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-374 |
3.08e-144 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 413.54 E-value: 3.08e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 8 PKISLHGAGAIGDMVKLVAGKQWgKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAAR 87
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGA-RALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 88 CDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNL 167
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 168 IPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQY 247
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLAST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 248 LAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDtrgmSDEAASMEAINAIR 327
Cdd:pfam00465 240 LAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGED----SDEEAAEEAIEALR 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 914217994 328 ALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEV 374
Cdd:pfam00465 316 ELLRELGLPTTLSELGVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
1-378 |
4.40e-143 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 411.31 E-value: 4.40e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 1 MSFMLALPKISLHGAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGY 80
Cdd:PRK10624 1 MANRMILNETAYFGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 81 AAYQAARCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYS--GVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQV 158
Cdd:PRK10624 81 EVFKASGADYLIAIGGGSPQDTCKAIGIISNNPEFADVRSleGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 159 KEVIIDPNLIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDghDLQA 238
Cdd:PRK10624 161 KFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAG--DKEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 239 REQMAFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAA 318
Cdd:PRK10624 239 GEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVKVEGMSLEEA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 319 SMEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELY 378
Cdd:PRK10624 319 RNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAFDDVCTGGNPREATLEDIVELY 378
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-381 |
4.77e-141 |
|
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: 405.76 E-value: 4.77e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 8 PKISLHGAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAAR 87
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 88 CDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNL 167
Cdd:cd08194 81 CDFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 168 IPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQY 247
Cdd:cd08194 161 LPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 248 LAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAASMEAINAIR 327
Cdd:cd08194 241 EAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 914217994 328 ALSKRVGIPQgFSQLGVSKADIEGWLDK----ALADPCAPCNPRPASRDEVRELYLEA 381
Cdd:cd08194 321 RLCADLEIPT-LREYGIDEEEFEAALDKmaedALASGSPANNPRVPTKEEIIELYREA 377
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-378 |
2.87e-137 |
|
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: 396.14 E-value: 2.87e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGA---IGDMVKLVAGKqwgKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDY 90
Cdd:cd17814 10 GVGArklAGRYAKNLGAR---KVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 91 LIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPD 170
Cdd:cd17814 87 IVAVGGGSPIDCAKGIGIVVSNGGHILDYEGVDKVRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 171 IAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLAG 250
Cdd:cd17814 167 VSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMMLASLQAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 251 MAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAASMEAINAIRALS 330
Cdd:cd17814 247 LAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLR 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 914217994 331 KRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELY 378
Cdd:cd17814 327 EDLGIPETLSELGVDEEDIPELAKRAMKDPCLVTNPRRPTREDIEEIY 374
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-380 |
2.44e-135 |
|
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: 391.45 E-value: 2.44e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 8 PKIsLHGAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAAR 87
Cdd:cd08189 6 PEL-FEGAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 88 CDYLIAFGGGSPIDTAKAIKILTANPGPS-TAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPN 166
Cdd:cd08189 85 CDAIIAIGGGSVIDCAKVIAARAANPKKSvRKLKGLLKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 167 LIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQ 246
Cdd:cd08189 165 LIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEARENMLLAS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 247 YLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAASMEAINAI 326
Cdd:cd08189 245 YYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGDSGESDSEKAEAFIAAI 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 914217994 327 RALSKRVGIPQGFSQLgvSKADIEGWLDKAL--ADPCAPCnPRPASRDEVRELYLE 380
Cdd:cd08189 325 RELNRRMGIPTTLEEL--KEEDIPEIAKRALkeANPLYPV-PRIMDRKDCEELLRK 377
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
14-382 |
4.39e-127 |
|
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: 370.30 E-value: 4.39e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYLIA 93
Cdd:cd14861 9 GAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDGIIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 94 FGGGSPIDTAKAIKILTANPGPSTAYS----GVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIP 169
Cdd:cd14861 89 LGGGSAIDAAKAIALMATHPGPLWDYEdgegGPAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSPKLLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 170 DIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLA 249
Cdd:cd14861 169 KVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDLEARGEMMMAALMG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 250 GMAFnSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGmsdeaaSMEAINAIRAL 329
Cdd:cd14861 249 AVAF-QKGLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALGLGLGG------FDDFIAWVEDL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 914217994 330 SKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELYLEAL 382
Cdd:cd14861 322 NERLGLPATLSELGVTEDDLDELAELALADPCHATNPRPVTAEDYRALLREAL 374
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-382 |
8.33e-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: 341487 [Multi-domain] Cd Length: 383 Bit Score: 369.95 E-value: 8.33e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 12 LHGAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYL 91
Cdd:cd14865 10 VSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAGADGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 92 IAFGGGSPIDTAKAIKILTANPGPSTA-YSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPD 170
Cdd:cd14865 90 IAVGGGSVIDTAKGVNILLSEGGDDLDdYGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVSPFLLPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 171 IAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLAG 250
Cdd:cd14865 170 VAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGKDLEARLALAIAATMAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 251 MAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAM--GVDTRGMSDEAASMEAINAIRA 328
Cdd:cd14865 250 IAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALayGVTPAGRRAEEAIEAAIDLVRR 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 914217994 329 LSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELYLEAL 382
Cdd:cd14865 330 LHELCGLPTRLRDVGVPEEQLEAIAELALNDGAILFNPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-377 |
8.34e-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: 341485 [Multi-domain] Cd Length: 380 Bit Score: 369.94 E-value: 8.34e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGA---IGDMVKLVAGKqwgKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDY 90
Cdd:cd14863 11 GAGAveqIGELLKELGCK---KVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 91 LIAFGGGSPIDTAKAIKILTANPGPSTAY-SGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIP 169
Cdd:cd14863 88 VIGIGGGSVLDTAKAIAVLLTNPGPIIDYaLAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 170 DIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLA 249
Cdd:cd14863 168 DLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENMLLASNLA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 250 GMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAASMEAINAIRAL 329
Cdd:cd14863 248 GIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREF 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 914217994 330 SKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVREL 377
Cdd:cd14863 328 MKELGIPSLFEDYGIDKEDLDKIAEAVLKDPFAMFNPRPITEEEVAEI 375
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
7-382 |
9.80e-123 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 359.65 E-value: 9.80e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 7 LPKISLHGAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAA 86
Cdd:PRK09860 8 IPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 87 RCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPN 166
Cdd:PRK09860 88 NCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 167 LIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQ 246
Cdd:PRK09860 168 VTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 247 YLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAASMEAINAI 326
Cdd:PRK09860 248 FLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINAI 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 914217994 327 RALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELYLEAL 382
Cdd:PRK09860 328 RELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAAM 383
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
13-381 |
1.13e-114 |
|
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: 338.78 E-value: 1.13e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 13 HGAGAIgDMVKLVAGKqwgKALIVTDGQ-LVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYL 91
Cdd:cd08179 10 FGEGAL-EYLKTLKGK---RAFIVTGGGsMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDWI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 92 IAFGGGSPIDTAKAIKILTANPGpstaYSGVGKVKNAGVP-------LVAINTTAGTAAEMTSNAVIIDSERQVKEVIID 164
Cdd:cd08179 86 IAIGGGSVIDAAKAMWVFYEYPE----LTFEDALVPFPLPelrkkarFIAIPSTSGTGSEVTRASVITDTEKGIKYPLAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 165 PNLIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAF 244
Cdd:cd08179 162 FEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKDLEAREKMHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 245 GQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAqamgvdtrgMSDEAASMEA-- 322
Cdd:cd08179 242 ASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAA---------LLIGLTDEELve 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914217994 323 --INAIRALSKRVGIPQGFSQLGVS----KADIEGWLDKALADPCAPCNPRPASRDEVRELYLEA 381
Cdd:cd08179 313 dlIEAIEELNKKLGIPLSFKEAGIDedefFAKLDEMAENAMNDACTGTNPRKPTVEEMKELLKAA 377
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
28-378 |
7.63e-111 |
|
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: 329.07 E-value: 7.63e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 28 KQWG-KALIVTD-GQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYLIAFGGGSPIDTAKA 105
Cdd:cd08185 22 LRPGkKALIVTGkGSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGCDFVIGLGGGSSMDAAKA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 106 IKILTANPGPSTAY----SGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPDIAVDDASVMLD 181
Cdd:cd08185 102 IAFMATNPGDIWDYifggTGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKKGIGHPALFPKVSIVDPELMLT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 182 IPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLAGMAFNSAGLGLV 261
Cdd:cd08185 182 VPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEAREKMAWASTLAGIVIANSGTTLP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 262 HALAHQPGA-THNLPHGVCNAILLPIIENFNRPNAVARFARVAQAmgvDTRGMSDEAASMEAINAIRALSKRVGIPQGFS 340
Cdd:cd08185 262 HGLEHPLSGyHPNIPHGAGLAALYPAYFEFTIEKAPEKFAFVARA---EASGLSDAKAAEDFIEALRKLLKDIGLDDLLS 338
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 914217994 341 QLGVSKADIEGWLDKAL--ADPCAPCNPRPASRDEVRELY 378
Cdd:cd08185 339 DLGVTEEDIPWLAENAMetMGGLFANNPVELTEEDIVEIY 378
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
8-379 |
9.82e-109 |
|
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: 322.14 E-value: 9.82e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 8 PKIsLHGAGAIgDMVKLVAGKqwgKALIVTDGQLVKLGLLDSLFSALDeQQMAYQLFDDVFPNPTEALVQQGYAAYQAAR 87
Cdd:cd08180 5 TKI-YSGEDSL-ERLKELKGK---RVFIVTDPFMVKSGMVDKVTDELD-KSNEVEIFSDVVPDPSIEVVAKGLAKILEFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 88 CDYLIAFGGGSPIDTAKAIKILTANpgpstaYSGVGKVKnagvPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNL 167
Cdd:cd08180 79 PDTIIALGGGSAIDAAKAIIYFALK------QKGNIKKP----LFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 168 IPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQY 247
Cdd:cd08180 149 LPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNASC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 248 LAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLP-IIENFnrpnavarfarvaqamgvdtrgmsdeaasmeaINAI 326
Cdd:cd08180 229 MAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPyVIEFL--------------------------------IAAI 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 914217994 327 RALSKRVGIPQGFSQLGVSKAD----IEGWLDKALADPCAPCNPRPASRDEVRELYL 379
Cdd:cd08180 277 RRLNKKLGIPSTLKELGIDEEEfekaIDEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
32-382 |
1.79e-103 |
|
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: 311.40 E-value: 1.79e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 32 KALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYLIAFGGGSPIDTAKAIKILTA 111
Cdd:cd08190 25 KVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVAVGGGSVIDTAKAANLYAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 112 NPGPSTAY----SGVGK-VKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPDIAVDDASVMLDIPPAV 186
Cdd:cd08190 105 HPGDFLDYvnapIGKGKpVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISSRYLRPTLAIVDPLLTLTLPPRV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 187 TAATGMDALTHAIEAF------------------VSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYL 248
Cdd:cd08190 185 TASSGFDVLCHALESYtarpynarprpanpderpAYQGSNPISDVWAEKAIELIGKYLRRAVNDGDDLEARSNMLLASTL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 249 AGMAFNSAGLGLVHALAH-------------QPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSD 315
Cdd:cd08190 265 AGIGFGNAGVHLPHAMAYpiaglvkdyrppgYPVDHPHVPHGLSVALTAPAVFRFTAPACPERHLEAAELLGADTSGASD 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914217994 316 EAASMEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALadpcaP------CNPRPASRDEVRELYLEAL 382
Cdd:cd08190 345 RDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTL-----PqqrllkLNPRPVTEEDLEEIFEDAL 412
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-377 |
1.83e-103 |
|
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: 310.20 E-value: 1.83e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGAIGDMVKLVAGKqWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDdVFPNPTEALVQQGYAAYQAARCDYLIA 93
Cdd:cd08183 7 GRGSLQELGELAAEL-GKRALLVTGRSSLRSGRLARLLEALEAAGIEVALFS-VSGEPTVETVDAAVALAREAGCDVVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 94 FGGGSPIDTAKAIKILTANPGPSTAY-SGVGK---VKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIP 169
Cdd:cd08183 85 IGGGSVIDAAKAIAALLTNEGSVLDYlEVVGKgrpLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLRSPSMLP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 170 DIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLA 249
Cdd:cd08183 165 DVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 250 GMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFAR----VAQAMGVDTRGMSDEAASMEAINA 325
Cdd:cd08183 245 GLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRALREREPDspalARYRELAGILTGDPDAAAEDGVEW 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 914217994 326 IRALSKRVGIPqGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVREL 377
Cdd:cd08183 325 LEELCEELGIP-RLSEYGLTEEDFPEIVEKARGSSSMKGNPIELSDEELLEI 375
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-382 |
4.73e-102 |
|
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: 307.23 E-value: 4.73e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGAIGDMVKLVAGKQWgKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYLIA 93
Cdd:cd08191 10 GPGARRALGRVAARLGS-RVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDPDVVIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 94 FGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPDIAV 173
Cdd:cd08191 89 LGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRPAVAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 174 DDASVMLDIPPAVTAATGMDALTHAIEAF---------------VSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQA 238
Cdd:cd08191 169 VDPELTLTCPPGVTADSGIDALTHAIESYtardfppfprldpdpVYVGKNPLTDLLALEAIRLIGRHLPRAVRDGDDLEA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 239 REQMAFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAA 318
Cdd:cd08191 249 RSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVTTAGTSEEAA 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 914217994 319 SmEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALA-DPCAPCNPRPASRDEVRELYLEAL 382
Cdd:cd08191 329 D-RAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSvTRLIANNPRPPTEEDLLRILRAAF 392
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
32-379 |
1.60e-100 |
|
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: 303.34 E-value: 1.60e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 32 KALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYLIAFGGGSPIDTAKAIKILTA 111
Cdd:cd08178 25 RAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFKPDVIIALGGGSAMDAAKIMWLFYE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 112 NP-----GPSTAYSGVGK--VKN----AGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPDIAVDDASVML 180
Cdd:cd08178 105 HPetkfeDLAQRFMDIRKrvYKFpklgKKAKLVAIPTTSGTGSEVTPFAVITDDKTGKKYPLADYALTPDMAIVDPELVM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 181 DIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLAGMAFNSAGLGL 260
Cdd:cd08178 185 TMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGNDIEAREKMHNAATIAGMAFANAFLGI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 261 VHALAHQPGATHNLPHGVCNAILLPIIENFN---------------RPNAVARFARVAQAMGVdtRGMSDEAASMEAINA 325
Cdd:cd08178 265 CHSLAHKLGAAFHIPHGRANAILLPHVIRYNatdpptkqaafpqykYYVAKERYAEIADLLGL--GGKTPEEKVESLIKA 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 914217994 326 IRALSKRVGIPQGFSQLGVSKADIEGWLDK----ALADPCAPCNPRPASRDEVRELYL 379
Cdd:cd08178 343 IEDLKKDLGIPTSIREAGIDEADFLAAVDKlaedAFDDQCTGANPRYPLISELKEILL 400
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
14-382 |
7.64e-98 |
|
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: 295.96 E-value: 7.64e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYLIA 93
Cdd:cd08193 10 GAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAGADGVIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 94 FGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSErQVKEVIIDPNLIPDIAV 173
Cdd:cd08193 90 FGGGSSMDVAKLVALLAGSDQPLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIVTTGE-TEKKGVVSPQLLPDVAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 174 DDASVMLDIPPAVTAATGMDALTHAIEAFVS-VGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLAGMA 252
Cdd:cd08193 169 LDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDALAREALRLLGANLRRAVEDGSDLEAREAMLLGSMLAGQA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 253 FNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAASMEAINAIRALSKR 332
Cdd:cd08193 249 FANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVEA 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 914217994 333 VGIPQGFSQLGVSKADIEgwldkALADPCA------PCNPRPASRDEVRELYLEAL 382
Cdd:cd08193 329 SGLPTRLRDVGVTEEDLP-----MLAEDAMkqtrllVNNPREVTEEDALAIYQAAL 379
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
32-378 |
4.51e-96 |
|
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: 291.05 E-value: 4.51e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 32 KALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYLIAFGGGSPIDTAKAIKILTA 111
Cdd:cd14862 26 RALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAKAAWVLYE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 112 NPGPS----TAYSGVGKVKNAgvPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPDIAVDDASVMLDIPPAVT 187
Cdd:cd14862 106 RPDLDpediSPLDLLGLRKKA--KLIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 188 AATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLAGMAFNSAGLGLVHALAHQ 267
Cdd:cd14862 184 AGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGDDLEAREKMHNAATIAGLAFGNSQAGLAHALGHS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 268 PGATHNLPHGVCNAILLPIIENFNRpNAVARFARVAQAMGVDTRgmSDEAASMEAINAIRALSKRVGIPQGFSQLGVSKA 347
Cdd:cd14862 264 LGAVFHVPHGIAVGLFLPYVIEFYA-KVTDERYDLLKLLGIEAR--DEEEALKKLVEAIRELYKEVGQPLSIKDLGISEE 340
|
330 340 350
....*....|....*....|....*....|....*
gi 914217994 348 DIEGWLDK----ALADPCAPCNPRPASRDEVRELY 378
Cdd:cd14862 341 EFEEKLDElveyAMEDSCTITSPRPPSEEDLKKLF 375
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
32-381 |
2.45e-95 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 302.87 E-value: 2.45e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 32 KALIVTDGQLVKLGLLDSLFSALD--EQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYLIAFGGGSPIDTAKAIKIL 109
Cdd:PRK13805 482 RAFIVTDRFMVELGYVDKVTDVLKkrENGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMWLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 110 TANPgpSTAYSGVG------------------KVKnagvpLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPDI 171
Cdd:PRK13805 562 YEHP--ETDFEDLAqkfmdirkriykfpklgkKAK-----LVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDV 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 172 AVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDG-HDLQAREQMAFGQYLAG 250
Cdd:PRK13805 635 AIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGaKDPEAREKMHNASTIAG 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 251 MAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLP-IIE-------------NFNRPNAVARFARVAQAMGVdtRGMSDE 316
Cdd:PRK13805 715 MAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPhVIRynatdppkqaafpQYEYPRADERYAEIARHLGL--PGSTTE 792
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914217994 317 AASMEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDK----ALADPCAPCNPRPASRDEVRELYLEA 381
Cdd:PRK13805 793 EKVESLIKAIEELKAELGIPMSIKEAGVDEADFLAKLDElaelAFDDQCTGANPRYPLISELKEILLDA 861
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-378 |
1.69e-88 |
|
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: 271.37 E-value: 1.69e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYqlFDDVFPNPTEALVQQGYAAYQAARCDYLIA 93
Cdd:cd08196 12 GEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVAV--FSDVEPNPTVENVDKCARLARENGADFVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 94 FGGGSPIDTAKAIKILTANPGPSTAY-SGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPDIA 172
Cdd:cd08196 90 IGGGSVLDTAKAAACLAKTDGSIEDYlEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLVSPGFYPDIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 173 VDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLAGMA 252
Cdd:cd08196 170 IVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPNDKEAREKMALASLLAGLA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 253 FNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGmsdeaasmEAINAIRALSKR 332
Cdd:cd08196 250 FSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQLGFKDAE--------ELADKIEELKKR 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 914217994 333 VGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELY 378
Cdd:cd08196 322 IGLRTRLSELGITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
5-381 |
4.54e-87 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 268.82 E-value: 4.54e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 5 LALPKISLHGAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQ 84
Cdd:PRK15454 24 FSVPPVTLCGPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 85 AARCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIID 164
Cdd:PRK15454 104 ESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 165 PNLIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAF 244
Cdd:PRK15454 184 ASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESMLL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 245 GQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMgvdtrgMSDEAASMEAIN 324
Cdd:PRK15454 264 ASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRAL------RTKKSDDRDAIN 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 914217994 325 AIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELYLEA 381
Cdd:PRK15454 338 AVSELIAEVGIGKRLGDVGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLYAAA 394
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
14-378 |
1.98e-78 |
|
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: 245.98 E-value: 1.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGLLDSLFSALDEQQMAYQlFDDVFPNPTEALVQQGYAAYQAARCDYLIA 93
Cdd:cd08182 7 GPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDALGGRIPVVV-FSDFSPNPDLEDLERGIELFRESGPDVIIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 94 FGGGSPIDTAKAIKILTANPGPSTAYS--GVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPDI 171
Cdd:cd08182 86 VGGGSVIDTAKAIAALLGSPGENLLLLrtGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPSLYPDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 172 AVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLAGM 251
Cdd:cd08182 166 AILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEASLLAGL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 252 AFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAasmEAINAIRALSK 331
Cdd:cd08182 246 AISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDECDDDPRGREILLALGASDPA---EAAERLRALLE 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 914217994 332 RVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELY 378
Cdd:cd08182 323 SLGLPTRLSEYGVTAEDLEALAASVNTPERLKNNPVRLSEEDLLRLL 369
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
32-378 |
8.78e-73 |
|
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: 230.94 E-value: 8.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 32 KALIVTdGQ--LVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYLIAFGGGSPIDTAKAIKIL 109
Cdd:cd08181 27 KALIVT-GKhsAKKNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELARKEGADFVIGIGGGSPLDAAKAIALL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 110 TANPGPSTAYSGVGKVKNAgVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPDIAVDDASVMLDIPPAVTAA 189
Cdd:cd08181 106 AANKDGDEDLFQNGKYNPP-LPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTID 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 190 TGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLAGMAFNSAGLGLVHALAHQPG 269
Cdd:cd08181 185 TAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 270 ATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGvdtrgmsdeaasMEAINAIRA-LSKRVGIPQgfsqlGVSKAD 348
Cdd:cd08181 265 YFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLG------------FGSIEEFQKfLNRLLGKKE-----ELSEEE 327
|
330 340 350
....*....|....*....|....*....|
gi 914217994 349 IEGWLDKALADPCAPCNPRPASRDEVRELY 378
Cdd:cd08181 328 LEKYADEAMKAKNKKNTPGNVTKEDILRIY 357
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
14-382 |
1.21e-67 |
|
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: 218.29 E-value: 1.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGAIGDMVKLVAGKQWGKALIVTDGQLVKL-GLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYLI 92
Cdd:cd08186 7 GVGAIAKIKDILKDLGIDKVIIVTGRSSYKKsGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 93 AFGGGSPIDTAKAIKILTANPGpSTA---YSGVGKVKNAgVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIP 169
Cdd:cd08186 87 AIGGGSPIDTAKSVAVLLAYGG-KTArdlYGFRFAPERA-LPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIYP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 170 DIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLA 249
Cdd:cd08186 165 LYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYASMIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 250 GMAFNSAGLGLVHALAHQ-PGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAAsmEAINAIRA 328
Cdd:cd08186 245 GIAIDNGLLHLTHALEHPlSGLKPELPHGLGLALLGPAVVKYIYKAVPETLADILRPIVPGLKGTPDEAE--KAARGVEE 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 914217994 329 LSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPC----NPRPASRDEVRELYLEAL 382
Cdd:cd08186 323 FLFSVGFTEKLSDYGFTEDDVDRLVELAFTTPSLDLllslAPVEVTEEVVREIYEESL 380
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
14-378 |
3.60e-64 |
|
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: 209.21 E-value: 3.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGAIGDMVKLVagKQWG-KALIVTDGQ-LVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYL 91
Cdd:cd08187 13 GKGAIEELGEEI--KKYGkKVLLVYGGGsIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVDFI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 92 IAFGGGSPIDTAKAIKILTANPG-PSTAYSGVGKVKNAgVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPD 170
Cdd:cd08187 91 LAVGGGSVIDAAKAIAAGAKYDGdVWDFFTGKAPPEKA-LPVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 171 IAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAH-PLTDANALEAIRLINLWLPKAVDDGHDLQAREQMafgQYLA 249
Cdd:cd08187 170 FSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDaPLQDRLAEGLLRTVIENGPKALKDPDDYEARANL---MWAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 250 GMAFN-SAGLGL-----VHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQA-MGVDTrGMSDEAASMEA 322
Cdd:cd08187 247 TLALNgLLGAGRggdwaTHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRvFGIDP-GGDDEETALEG 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 914217994 323 INAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRELY 378
Cdd:cd08187 326 IEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGFKPLTREDIEEIL 381
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
14-377 |
5.69e-62 |
|
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: 202.35 E-value: 5.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGAIGDMVKLVAGKQWGKALIVTDGQLVKLGllDSLFSALDEQQMAyqLFDDVFPNPTEALVQQGYAAYQAARCDYLIA 93
Cdd:cd08177 7 GAGTLAELAEELERLGARRALVLSTPRQRALA--ERVAALLGDRVAG--VFDGAVMHVPVEVAERALAAAREAGADGLVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 94 FGGGSPIDTAKAIKILTanpgpstaysgvgkvknaGVPLVAINTT-AGtaAEMTSnaVIIDSERQVKEVIIDPNLIPDIA 172
Cdd:cd08177 83 IGGGSAIGLAKAIALRT------------------GLPIVAVPTTyAG--SEMTP--IWGETEDGVKTTGRDPRVLPRTV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 173 VDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQYLAGMA 252
Cdd:cd08177 141 IYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 253 FNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTrgmsdeaasmeAINAIRALSKR 332
Cdd:cd08177 221 LGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGGGD-----------AAGGLYDLARR 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 914217994 333 VGIPQGFSQLGVSKADIEGWLDKALADPCApcNPRPASRDEVREL 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 |
2.22e-58 |
|
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: 194.06 E-value: 2.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 8 PKISLhGAGAIGDMVKLVagKQWG-KALIVTDGQLVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAA 86
Cdd:cd14864 5 PNIVF-GADSLERIGEEV--KEYGsRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 87 RCDYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPN 166
Cdd:cd14864 82 GADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKAQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 167 LIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQMAFGQ 246
Cdd:cd14864 162 GLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEELLAQAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 247 YLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGMSDEAASMEAINAI 326
Cdd:cd14864 242 CLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGV 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 914217994 327 RALSKRVGIPQGFSQLGVsKADIEGWLDKALADPCAPCNPRPASRDEVREL 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 |
6.61e-56 |
|
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: 187.82 E-value: 6.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 13 HGAGAIGDMVKLVAGKQWGKALIVTDGQLVKLG-LLDSLFSALDEQQMAyqLFDDVFPNPTEALVQQGYAAYQAARCDYL 91
Cdd:cd14866 10 SGRGALARLGRELDRLGARRALVVCGSSVGANPdLMDPVRAALGDRLAG--VFDGVRPHSPLETVEAAAEALREADADAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 92 IAFGGGSPIDTAKAIKILTANPGP----STAYSGVG-----KVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQvKEVI 162
Cdd:cd14866 88 VAVGGGSAIVTARAASILLAEDRDvrelCTRRAEDGlmvspRLDAPKLPIFVVPTTPTTADVKAGSAVTDPPAGQ-RLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 163 IDPNLIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGhDLQAREQM 242
Cdd:cd14866 167 FDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLADDD-DPAARADL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 243 AFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGmsDEAASMEA 322
Cdd:cd14866 246 VLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGVADAG--DEASAAAV 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 323 INAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRP-ASRDEVRELYLEA 381
Cdd:cd14866 324 VDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNNPRPvPTAEELEALLEAA 383
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
13-382 |
1.61e-54 |
|
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: 183.99 E-value: 1.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 13 HGAGAIGDMVKLVAgkQWG--KALIVTDGQL-VKLGLLDSLFSALDEqqMAYQLFDDVFPNPTEALVQQGYAAYQAARCD 89
Cdd:cd08192 6 YGPGAVEALLHELA--TLGasRVFIVTSKSLaTKTDVIKRLEEALGD--RHVGVFSGVRQHTPREDVLEAARAVREAGAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 90 YLIAFGGGSPIDTAKAIKILTAN--PGPSTAYS------GVGKVKNAGVPLVAINTTAgTAAEMTSNAVIIDSERQVKEV 161
Cdd:cd08192 82 LLVSLGGGSPIDAAKAVALALAEdvTDVDQLDAledgkrIDPNVTGPTLPHIAIPTTL-SGAEFTAGAGATDDDTGHKQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 162 IIDPNLIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKAVDDGHDLQAREQ 241
Cdd:cd08192 161 FAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADPEDLEARLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 242 MAFGQYLAGMAF-NSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGVDTRGmsDEAASM 320
Cdd:cd08192 241 CQLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALGLVTGG--LGREAA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 914217994 321 EAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRP-ASRDEVRELyLEAL 382
Cdd:cd08192 319 DAADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRPiTDKDDVLEI-LESA 380
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
14-382 |
4.55e-52 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 177.96 E-value: 4.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGAIGDMVKLVAgKQWGKALIVTDGQ-LVKLGLLDSLFSALDEQQMAYQLFDDVFPNPTEALVQQGYAAYQAARCDYLI 92
Cdd:COG1979 15 GKGQIAKLGEEIP-KYGKKVLLVYGGGsIKKNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDFIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 93 AFGGGSPIDTAKAIKILTANPG-PSTAYSGVGKVKNAgVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPNLIPDI 171
Cdd:COG1979 94 AVGGGSVIDGAKAIAAGAKYDGdPWDILTGKAPVEKA-LPLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFPKF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 172 AVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAH-PLTDANAlEAIrLINL--WLPKAVDDGHDLQAREQMafgQYL 248
Cdd:COG1979 173 SILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDaPLQDRFA-EGL-LRTLieEGPKALKDPEDYDARANL---MWA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 249 AGMAFN-SAGLGL-----VHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQ-AMGVDtrGMSDEAASME 321
Cdd:COG1979 248 ATLALNgLIGAGVpqdwaTHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAErVWGIT--EGDDEERALE 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 914217994 322 AINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPC-NPRPASRDEVRELYLEAL 382
Cdd:COG1979 326 GIEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMTALgEFKDLTPEDVREILELAL 387
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-357 |
1.93e-40 |
|
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: 144.04 E-value: 1.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 8 PKISLHGAGAIGDmVKLVAGKQWGKALIVTDGQLVKlGLLDSLFSALDEQqMAYQLFDDVFPNPTEALVQQGYAAYQAAR 87
Cdd:cd07766 1 PTRIVFGEGAIAK-LGEIKRRGFDRALVVSDEGVVK-GVGEKVADSLKKG-LAVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 88 CDYLIAFGGGSPIDTAKAIKILTanpgpstaysgvgkvkNAGVPLVAINTTAGTAAEMTSNAVIidSERQVKEVIIDPNL 167
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAALL----------------NRGIPFIIVPTTASTDSEVSPKSVI--TDKGGKNKQVGPHY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 168 IPDIAVDDASVMLDIPPAVTAATGMDALTHAIEafvsvgahpltdanaleairlinlwlpkavddghdlqaREQMAFGQY 247
Cdd:cd07766 140 NPDVVFVDTDITKGLPPRQVASGGVDALAHAVE--------------------------------------LEKVVEAAT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 248 LAGMA-FNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFNRpnavarfarvaqamgvDTRGMSDeaasmEAINAI 326
Cdd:cd07766 182 LAGMGlFESPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVAN----------------DMNPEPE-----AAIEAV 240
|
330 340 350
....*....|....*....|....*....|.
gi 914217994 327 RALSKRVGIPQGFSQLGVSKADIEGWLDKAL 357
Cdd:cd07766 241 FKFLEDLGLPTHLADLGVSKEDIPKLAEKAL 271
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
71-380 |
2.38e-32 |
|
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: 125.02 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 71 PTEALVQQGYAAYQAARCDYLIAFGGGSPIDTAKaikILT-ANPGPSTA-YSG---VGKVKnagvPLVAINTTAGTAAEM 145
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAK---LLAlKGISPVLDlFDGkipLIKEK----ELIIVPTTCGTGSEV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 146 TSNAVIIDSERQVKEVIIDPNLIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLW 225
Cdd:cd14860 135 TNISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 226 LPKAVDDGHDlqAREQMaFGQYL-----AGMAFNSAGLGLVHALAHQPGATHNLPHGVCN-AILLPIIENFNRPN---AV 296
Cdd:cd14860 215 YQEIAEKGEE--ARFPL-LGDFLiasnyAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANyAVFTGVLKNYQEKNpdgEI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 297 ARF-ARVAQAMGVdtrgmsDEAASMEAINAI--RALSKRvgipqGFSQLGVSKADIEGWLD-------KALADpcapcNP 366
Cdd:cd14860 292 KKLnEFLAKILGC------DEEDVYDELEELlnKILPKK-----PLHEYGMKEEEIDEFADsvmenqqRLLAN-----NY 355
|
330
....*....|....
gi 914217994 367 RPASRDEVRELYLE 380
Cdd:cd14860 356 VPLDREDVAEIYKE 369
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
14-316 |
6.24e-31 |
|
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: 120.45 E-value: 6.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGAIGDMVKLVAGKQW---GKALIVTDGQLVKLGLLDSLFSaldeQQMAYQLFDDVFPNPTEALVQQGYAAYQAARC-- 88
Cdd:cd08184 7 GRGSFDQLGELLAERRKsnnDYVVFFIDDVFKGKPLLDRLPL----QNGDLLIFVDTTDEPKTDQIDALRAQIRAENDkl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 89 -DYLIAFGGGSPIDTAKAIKILTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQV--------- 158
Cdd:cd08184 83 pAAVVGIGGGSTMDIAKAVSNMLTNPGSAADYQGWDLVKNPGIYKIGVPTLSGTGAEASRTAVLTGPEKKLginsdytvf 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 159 KEVIIDPNLIPDIAVDDASVmldippavtaaTGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWLPKavDDGHDLQA 238
Cdd:cd08184 163 DQVILDPELIATVPRDQYFY-----------TGMDCYIHCVESLNGTYRNAFGDAYAEKALELCRDVFLS--DDMMSPEN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 239 REQMAFGQYLAGMAFNSAGLGLVHALAHQPGATHNLPHGVCNAILLPIIENFnRPNAVARFARVAQAMGVD-----TRGM 313
Cdd:cd08184 230 REKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCIVFNVLEEF-YPEGVKEFREMLEKQNITlpkgiCKDL 308
|
...
gi 914217994 314 SDE 316
Cdd:cd08184 309 TDE 311
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
3-355 |
1.49e-20 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 92.16 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 3 FMLALPKISLHGAGAIGDMVKLVAgkQWGKALIVTDGQLVK-LGLLDSLFSALdeQQMAYQLFDDVFPNPTEALVQQGYA 81
Cdd:PRK15138 4 FNLHTPTRILFGKGAIAGLREQIP--ADARVLITYGGGSVKkTGVLDQVLDAL--KGMDVLEFGGIEPNPTYETLMKAVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 82 AYQAARCDYLIAFGGGSPIDTAKAIKI---LTANPGPSTAYSGVGKVKNAGVPLVAINTTAGTAAEMTSNAVIIDSERQV 158
Cdd:PRK15138 80 LVREEKITFLLAVGGGSVLDGTKFIAAaanYPENIDPWHILETGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 159 KEVIIDPNLIPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSVGAHPLTDANALEAIRLINLWL-PKAVDDGHDLQ 237
Cdd:PRK15138 160 KQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAKIQDRFAEGILLTLIEEgPKALKEPENYD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 238 AREQMafgQYLAGMAFNS-AGLGL-----VHALAHQPGATHNLPHGVCNAILLPIIENFNRPNAVARFARVAQAMGvDTR 311
Cdd:PRK15138 240 VRANV---MWAATQALNGlIGAGVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVW-NIT 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 914217994 312 GMSDEAASMEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDK 355
Cdd:PRK15138 316 EGSDDERIDAAIAATRNFFEQMGVPTRLSDYGLDGSSIPALLKK 359
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
7-350 |
1.24e-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: 74.43 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 7 LPKISLHGAGAIGDMVKLVAgKQWGKALIVTDGQLVKLgLLDSLFSALDEQQMAYQLFDdVFPNPTEALVQQGYAAYQAA 86
Cdd:COG0371 5 LPRRYVQGEGALDELGEYLA-DLGKRALIITGPTALKA-AGDRLEESLEDAGIEVEVEV-FGGECSEEEIERLAEEAKEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 87 RCDYLIAFGGGSPIDTAKAIkiltanpgpstAYsgvgkvkNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDPN 166
Cdd:COG0371 82 GADVIIGVGGGKALDTAKAV-----------AY-------RLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 167 LiPDIAVDDASVMLDIPPAVTAAtGM-DALTHAIEAFVSVGAH------PLTDA--------------NALEAIrlinlw 225
Cdd:COG0371 144 N-PDLVLVDTDIIAKAPVRLLAA-GIgDALAKWYEARDWSLAHrdlageYYTEAavalarlcaetlleYGEAAI------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 226 lpKAVDDGHDLQAREQMAFGQ-YLAGMAFN----SAGLGLVHALAHQ----PgATHNLPHGvcnaillpiienfnrpNAV 296
Cdd:COG0371 216 --KAVEAGVVTPALERVVEANlLLSGLAMGigssRPGSGAAHAIHNGltalP-ETHHALHG----------------EKV 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 914217994 297 ArFARVAQAMgvdTRGMSDEaasmeaINAIRALSKRVGIPQGFSQLGVSKADIE 350
Cdd:COG0371 277 A-FGTLVQLV---LEGRPEE------IEELLDFLRSVGLPTTLADLGLDDETEE 320
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
14-381 |
5.09e-11 |
|
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: 63.20 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 14 GAGAIGDMVKLVA--GKqwgKALIVTDGQLVKLgLLDSLFSALDEQQMAYQLfdDVFPNP-TEALVQQGYAAYQAARCDY 90
Cdd:cd08170 7 GPGALDRLGEYLAplGK---KALVIADPFVLDL-VGERLEESLEKAGLEVVF--EVFGGEcSREEIERLAAIARANGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 91 LIAFGGGSPIDTAKAIkiltanpgpstAYsgvgkvkNAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVIIDP-NliP 169
Cdd:cd08170 81 VIGIGGGKTIDTAKAV-----------AD-------YLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPrN--P 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 170 DIAVDDASVMLDIPPAVTAAtGM-DAL--------------------------------------THAIEAFVSVGAHPL 210
Cdd:cd08170 141 DLVLVDTEIIAKAPVRFLVA-GMgDALatyfearacarsgapnmaggrptlaalalaelcydtllEYGVAAKAAVEAGVV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 211 TDA--NALEAirliNLwlpkavddghdlqareqmafgqYLAGMAFNSAGLGLVHALAH---QPGATHNLPHGVCnaillp 285
Cdd:cd08170 220 TPAleAVIEA----NT----------------------LLSGLGFESGGLAAAHAIHNgltALPETHHLLHGEK------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 286 iienfnrpnaVArFARVAQAMgvdtrgMsdEAASMEAINAIRALSKRVGIPQGFSQLGVSKADIEGWL---DKALADPCA 362
Cdd:cd08170 268 ----------VA-FGTLVQLV------L--EGRPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRkvaEAACAPGET 328
|
410 420
....*....|....*....|
gi 914217994 363 PCN-PRPASRDEVRELYLEA 381
Cdd:cd08170 329 IHNmPFPVTPEDVVDAILAA 348
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
8-376 |
1.45e-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: 61.78 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 8 PKISLHGAGAIGDMVKLVAgkQWG-KALIVTDGQ-LVKLGllDSLFSALDEQQMAYQLFddVFP-NPTEALVQQgYAAY- 83
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIA--PLGkKALIIGGKTaLEAVG--EKLEKSLEEAGIDYEVE--VFGgECTEENIER-LAEKa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 84 QAARCDYLIAFGGGSPIDTAKAIkiltanpgpstAYSgvgkvknAGVPLVAINTTAGTAAEMTSNAVIIDSERQVKEVII 163
Cdd:cd08550 74 KEEGADVIIGIGGGKVLDTAKAV-----------ADR-------LGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 164 DPNLiPDIAVDDASVMLDIPPAVTAATGMDALTHAIEAFVSV--GAHPLTD----ANALEAIRLINLWLPKAVDD---GH 234
Cdd:cd08550 136 LKRS-PDLVLVDTDIIAAAPVRYLAAGIGDTLAKWYEARPSSrgGPDDLALqaavQLAKLAYDLLLEYGVQAVEDvrqGK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 235 DLQAREQMAFGQ-YLAGMAFNSAG----LGLVHA----LAHQPGaTHNLPHG----VCNAILLpIIENfnrpnavarfar 301
Cdd:cd08550 215 VTPALEDVVDAIiLLAGLVGSLGGggcrTAAAHAihngLTKLPE-THGTLHGekvaFGLLVQL-ALEG------------ 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914217994 302 vaqamgvdtrgmsdeaASMEAINAIRALSKRVGIPQGFSQLGV--SKADIEGWLDKALADP-CAPCNPRPASRDEVRE 376
Cdd:cd08550 281 ----------------RSEEEIEELIEFLRRLGLPVTLEDLGLelTEEELRKIAEYACDPPdMAHMLPFPVTPEMLAE 342
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
1-363 |
8.49e-07 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 50.58 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 1 MSFMLALPKISLHGAGAIGDMVKLVA--GKqwgKALIVTDGQLVKLgLLDSLFSALDEQQMayQLFDDVFP-NPTEALVQ 77
Cdd:PRK09423 1 MDRIFISPSKYVQGKGALARLGEYLKplGK---RALVIADEFVLGI-VGDRVEASLKEAGL--TVVFEVFNgECSDNEID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 78 QGYAAYQAARCDYLIAFGGGSPIDTAKAIkiltanpgpstAYsgvgkvkNAGVPLVAINTTAGTAAEMTSNAVIIDSERQ 157
Cdd:PRK09423 75 RLVAIAEENGCDVVIGIGGGKTLDTAKAV-----------AD-------YLGVPVVIVPTIASTDAPTSALSVIYTEEGE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 158 VKEVIIDP-NliPDIAVDDASVMLDIPPAVTAAtGM-DALTHAIEA--------FVSVGAHPLTDANAL----EAIRLIN 223
Cdd:PRK09423 137 FERYLFLPkN--PDLVLVDTAIIAKAPARFLAA-GIgDALATWFEAracsrsggTTMAGGKPTLAALALaelcYETLLED 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 224 LWLPK-AVDDGHDLQAREQMAFGQ-YLAGMAFNSAGLGLVHALaHQpG-----ATHNLPHGvcnaillpiienfnrpNAV 296
Cdd:PRK09423 214 GLKAKlAVEAKVVTPALENVIEANtLLSGLGFESGGLAAAHAI-HN-GltaleDTHHLTHG----------------EKV 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914217994 297 ArFARVAQamgvdtrgMSDEAASMEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALAdPCAP 363
Cdd:PRK09423 276 A-FGTLTQ--------LVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSDEELRKVAEA-ACAE 332
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
13-168 |
1.81e-05 |
|
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: 46.36 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 13 HGAGAIGDMVKLVAGKQWGKALIVTDGQlvklglldslfsaldeqqmAYQLFDDVFPNPTEALVQ----QGYAAY----- 83
Cdd:cd08172 6 CEEGALKELPELLSEFGIKRPLIIHGEK-------------------SWQAAKPYLPKLFEIEYPvlryDGECSYeeidr 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914217994 84 -----QAARCDYLIAFGGGSPIDTAKAikilTANpgpstaysgvgkvkNAGVPLVAINTTAGTAAEMTSNAVIIDSE--- 155
Cdd:cd08172 67 laeeaKEHQADVIIGIGGGKVLDTAKA----VAD--------------KLNIPLILIPTLASNCAAWTPLSVIYDEDgef 128
|
170 180
....*....|....*....|
gi 914217994 156 -------RQVKEVIIDPNLI 168
Cdd:cd08172 129 igydyfpRSAYLVLVDPRLL 148
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
320-376 |
5.98e-03 |
|
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: 341450 Cd Length: 345 Bit Score: 38.27 E-value: 5.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 914217994 320 MEAINAIRALSKRVGIPQGFSQLGVSKADIEGWLDKALADPCAPCNPRPASRDEVRE 376
Cdd:cd08171 284 FEELEKVYAFNKSIGLPTCLADLGLTVEDLEKVLDKALKTKDLRHSPYPITKEMFEE 340
|
|
| |
