|
Name |
Accession |
Description |
Interval |
E-value |
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
3-377 |
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: 603.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 3 YRIPAVNLVGRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLK 82
Cdd:cd08188 3 FYIPPVNLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 83 KENCDFIVSIGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVD 162
Cdd:cd08188 83 ENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 163 RNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCY 242
Cdd:cd08188 163 WNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKDLEARENMAY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 243 ACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEECMDFVIG 322
Cdd:cd08188 243 AQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGENTEGLSDEEAAEAAIE 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 496558464 323 KIKELSERVGIPKTLSELGVENPDFETLAENSMKDACAGANPVFFDKELLIKLFK 377
Cdd:cd08188 323 AIRKLSRRVGIPSGLKELGVKEEDFPLLAENALKDACGPTNPRQATKEDVIAIYR 377
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-379 |
9.05e-180 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 504.27 E-value: 9.05e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 1 MVYRIPAVNLVGRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEV 80
Cdd:COG1454 3 FTFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 81 LKKENCDFIVSIGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIM 160
Cdd:COG1454 83 AREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVKKGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 161 VDRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQM 240
Cdd:COG1454 163 ADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLEAREKM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 241 CYACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVeGKTDEECMDFV 320
Cdd:COG1454 243 ALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARALGLDV-GLSDEEAAEAL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 496558464 321 IGKIKELSERVGIPKTLSELGVENPDFETLAENSMKDACAGANPVFFDKELLIKLFKKI 379
Cdd:COG1454 322 IEAIRELLRDLGIPTRLSELGVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAA 380
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
12-377 |
1.11e-163 |
|
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: 463.17 E-value: 1.11e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFIVS 91
Cdd:cd08176 12 GWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKESGADGIIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 92 IGGGSPQDCGKAISVLATNGGKITDY-EGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLASIT 170
Cdd:cd08176 92 VGGGSSIDTAKAIGIIVANPGADVRSlEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKRKFVCVDPHDIPTVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 171 VNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLNGIA 250
Cdd:cd08176 172 IVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNVEARENMALAQYIAGMA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 251 FSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEECMDFVIGKIKELSER 330
Cdd:cd08176 252 FSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKD 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 496558464 331 VGIPKTLSELGVENPDFETLAENSMKDACAGANPVFFDKELLIKLFK 377
Cdd:cd08176 332 VGIPQKLSELGVKEEDIEALAEDALNDVCTPGNPREATKEDIIALYK 378
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
12-376 |
7.22e-159 |
|
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: 450.75 E-value: 7.22e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFIVS 91
Cdd:cd08551 7 GAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGADLVIA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 92 IGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLASITV 171
Cdd:cd08551 87 VGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLLPDVAI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 172 NDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLNGIAF 251
Cdd:cd08551 167 LDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLASLLAGIAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 252 SNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEECMDFVIGKIKELSERV 331
Cdd:cd08551 247 GNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELLRDL 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 496558464 332 GIPKTLSELGVENPDFETLAENSMKDACAGAN-PVFFDKELLIKLF 376
Cdd:cd08551 327 GIPTSLSELGVTEEDIPELAEDAMKSGRLLSNnPRPLTEEDIREIY 372
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
5-364 |
9.44e-149 |
|
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: 425.31 E-value: 9.44e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 5 IPAVNLVGRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKE 84
Cdd:TIGR02638 6 LNETSYFGAGAIEDIVDEVKRRGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVAAFKAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 85 NCDFIVSIGGGSPQDCGKAISVLATN--GGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVD 162
Cdd:TIGR02638 86 GADYLIAIGGGSPIDTAKAIGIISNNpeFADVRSLEGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEENKRKFVCVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 163 RNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCY 242
Cdd:TIGR02638 166 PHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGGKDLEAREQMAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 243 ACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEECMDFVIG 322
Cdd:TIGR02638 246 GQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAEFTGEKYREIAKAMGVKTEGMSDEEARDAAVE 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 496558464 323 KIKELSERVGIPKTLSELGVENPDFETLAENSMKDACAGANP 364
Cdd:TIGR02638 326 AVKTLSKRVGIPEGLSELGVKEEDIPALAEAALADVCTGGNP 367
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
6-370 |
3.25e-147 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 420.86 E-value: 3.25e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 6 PAVNLVGRGCLAQLKDEIGTLGcKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKEN 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLG-ARALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 86 CDFIVSIGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNT 165
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 166 LASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACF 245
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLAST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 246 LNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGmdveGKTDEECMDFVIGKIK 325
Cdd:pfam00465 240 LAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALG----EDSDEEAAEEAIEALR 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 496558464 326 ELSERVGIPKTLSELGVENPDFETLAENSMKDACAGANPVFFDKE 370
Cdd:pfam00465 316 ELLRELGLPTTLSELGVTEEDLDALAEAALRDRSLANNPRPLTAE 360
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-365 |
1.69e-140 |
|
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: 404.23 E-value: 1.69e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFIVS 91
Cdd:cd17814 10 GVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 92 IGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLASITV 171
Cdd:cd17814 90 VGGGSPIDCAKGIGIVVSNGGHILDYEGVDKVRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVSL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 172 NDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLNGIAF 251
Cdd:cd17814 170 IDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMMLASLQAGLAF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 252 SNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEECMDFVIGKIKELSERV 331
Cdd:cd17814 250 SNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLREDL 329
|
330 340 350
....*....|....*....|....*....|....
gi 496558464 332 GIPKTLSELGVENPDFETLAENSMKDACAGANPV 365
Cdd:cd17814 330 GIPETLSELGVDEEDIPELAKRAMKDPCLVTNPR 363
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
3-379 |
1.13e-139 |
|
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: 402.23 E-value: 1.13e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 3 YRIPAVnLVGRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLK 82
Cdd:cd08189 3 WPEPEL-FEGAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 83 KENCDFIVSIGGGSPQDCGKAISVLATNGGK-ITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMV 161
Cdd:cd08189 82 ENGCDAIIAIGGGSVIDCAKVIAARAANPKKsVRKLKGLLKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 162 DRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMC 241
Cdd:cd08189 162 DPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEARENML 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 242 YACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEECMDFVI 321
Cdd:cd08189 242 LASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGDSGESDSEKAEAFI 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496558464 322 GKIKELSERVGIPKTLSELGVEnpDFETLAENSMKDacagAN-----PVFFDKELLIKLFKKI 379
Cdd:cd08189 322 AAIRELNRRMGIPTTLEELKEE--DIPEIAKRALKE----ANplypvPRIMDRKDCEELLRKV 378
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
1-379 |
2.33e-137 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 396.67 E-value: 2.33e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 1 MVYRI--PAVNLVGRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGL 78
Cdd:PRK10624 1 MANRMilNETAYFGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 79 EVLKKENCDFIVSIGGGSPQDCGKAISVLATNG--GKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHI 156
Cdd:PRK10624 81 EVFKASGADYLIAIGGGSPQDTCKAIGIISNNPefADVRSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 157 KMIMVDRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENgqDIEA 236
Cdd:PRK10624 161 KFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAG--DKEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 237 REQMCYACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEEC 316
Cdd:PRK10624 239 GEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVKVEGMSLEEA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496558464 317 MDFVIGKIKELSERVGIPKTLSELGVENPDFETLAENSMKDACAGANPVFFDKELLIKLFKKI 379
Cdd:PRK10624 319 RNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAFDDVCTGGNPREATLEDIVELYKKA 381
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-379 |
9.57e-136 |
|
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: 392.28 E-value: 9.57e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 6 PAVNLVGRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKEN 85
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 86 CDFIVSIGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNT 165
Cdd:cd08194 81 CDFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 166 LASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACF 245
Cdd:cd08194 161 LPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 246 LNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEECMDFVIGKIK 325
Cdd:cd08194 241 EAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 496558464 326 ELSERVGIPkTLSELGVENPDFETLAENSMKDACA----GANPVFFDKELLIKLFKKI 379
Cdd:cd08194 321 RLCADLEIP-TLREYGIDEEEFEAALDKMAEDALAsgspANNPRVPTKEEIIELYREA 377
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
10-379 |
2.29e-134 |
|
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: 388.82 E-value: 2.29e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 10 LVGRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFI 89
Cdd:cd14863 9 IFGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 90 VSIGGGSPQDCGKAISVLATNGGKITDYEG-VNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLAS 168
Cdd:cd14863 89 IGIGGGSVLDTAKAIAVLLTNPGPIIDYALaGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVPD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 169 ITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLNG 248
Cdd:cd14863 169 LAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENMLLASNLAG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 249 IAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEECMDFVIGKIKELS 328
Cdd:cd14863 249 IAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREFM 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 496558464 329 ERVGIPKTLSELGVENPDFETLAENSMKDACAGANPVFFDKELLIKLFKKI 379
Cdd:cd14863 329 KELGIPSLFEDYGIDKEDLDKIAEAVLKDPFAMFNPRPITEEEVAEILEAI 379
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
2-365 |
4.06e-134 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 388.54 E-value: 4.06e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 2 VYRIPAVNLVGRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVL 81
Cdd:PRK09860 5 TFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 82 KKENCDFIVSIGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMV 161
Cdd:PRK09860 85 KENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 162 DRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMC 241
Cdd:PRK09860 165 DKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 242 YACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEECMDFVI 321
Cdd:PRK09860 245 YAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACI 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 496558464 322 GKIKELSERVGIPKTLSELGVENPDFETLAENSMKDACAGANPV 365
Cdd:PRK09860 325 NAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPI 368
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
12-378 |
4.53e-123 |
|
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: 359.90 E-value: 4.53e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFIVS 91
Cdd:cd14861 9 GAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDGIIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 92 IGGGSPQDCGKAISVLATNGGKITDYE----GVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLA 167
Cdd:cd14861 89 LGGGSAIDAAKAIALMATHPGPLWDYEdgegGPAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSPKLLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 168 SITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLN 247
Cdd:cd14861 169 KVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDLEARGEMMMAALMG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 248 GIAFSNaGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDeecmdfVIGKIKEL 327
Cdd:cd14861 249 AVAFQK-GLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALGLGLGGFDD------FIAWVEDL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 496558464 328 SERVGIPKTLSELGVENPDFETLAENSMKDACAGANPVFFDKELLIKLFKK 378
Cdd:cd14861 322 NERLGLPATLSELGVTEDDLDELAELALADPCHATNPRPVTAEDYRALLRE 372
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
3-377 |
6.50e-123 |
|
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: 359.89 E-value: 6.50e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 3 YRIPaVNLV-GRGCLAQLKDEIGTLGcKKALVVSDK-FLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEV 80
Cdd:cd08185 1 YYQP-TRILfGAGKLNELGEEALRPG-KKALIVTGKgSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 81 LKKENCDFIVSIGGGSPQDCGKAISVLATNGGKITDY----EGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHI 156
Cdd:cd08185 79 AKEEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYifggTGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 157 KMIMVDRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEA 236
Cdd:cd08185 159 KKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 237 REQMCYACFLNGIAFSNAGLGNVHAMAHQLGGLY-DLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEe 315
Cdd:cd08185 239 REKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVARAEASGLSDAKAA- 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496558464 316 cMDFvIGKIKELSERVGIPKTLSELGVENPDFETLAENSMK--DACAGANPVFFDKELLIKLFK 377
Cdd:cd08185 318 -EDF-IEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMEtmGGLFANNPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-378 |
5.96e-117 |
|
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: 344.52 E-value: 5.96e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFIVS 91
Cdd:cd14865 12 GAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAGADGIIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 92 IGGGSPQDCGKAISVLATNGGKITDYE-GVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLASIT 170
Cdd:cd14865 92 VGGGSVIDTAKGVNILLSEGGDDLDDYgGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVSPFLLPDVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 171 VNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLNGIA 250
Cdd:cd14865 172 ILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGKDLEARLALAIAATMAGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 251 FSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAE--TIGMDVEGKTDEECMDFVIGKIKELS 328
Cdd:cd14865 252 FSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALalAYGVTPAGRRAEEAIEAAIDLVRRLH 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 496558464 329 ERVGIPKTLSELGVENPDFETLAENSMKDACAGANPVFFDKELLIKLFKK 378
Cdd:cd14865 332 ELCGLPTRLRDVGVPEEQLEAIAELALNDGAILFNPREVDPEDILAILEA 381
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
12-379 |
2.98e-112 |
|
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: 332.62 E-value: 2.98e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKdeigTLGCKKALVVSDK-FLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFIV 90
Cdd:cd08179 11 GEGALEYLK----TLKGKRAFIVTGGgSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDWII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 91 SIGGGSPQDCGKAISVLATNggkiTDYEGVNKSQKKCLP-------IVAIATTAGTSAEVTINYVITDEETHIKMIMVDR 163
Cdd:cd08179 87 AIGGGSVIDAAKAMWVFYEY----PELTFEDALVPFPLPelrkkarFIAIPSTSGTGSEVTRASVITDTEKGIKYPLASF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 164 NTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYA 243
Cdd:cd08179 163 EITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKDLEAREKMHNA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 244 CFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIgmdveGKTDEECMDFVIGK 323
Cdd:cd08179 243 SCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAALLI-----GLTDEELVEDLIEA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 324 IKELSERVGIPKTLSELGVENPDF----ETLAENSMKDACAGANPVFFDKELLIKLFKKI 379
Cdd:cd08179 318 IEELNKKLGIPLSFKEAGIDEDEFfaklDEMAENAMNDACTGTNPRKPTVEEMKELLKAA 377
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
12-377 |
1.16e-107 |
|
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: 320.60 E-value: 1.16e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGcKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYnDVKQNPSVANVEGGLEVLKKENCDFIVS 91
Cdd:cd08183 7 GRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALF-SVSGEPTVETVDAAVALAREAGCDVVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 92 IGGGSPQDCGKAISVLATNGGKITDY-EGVNKSQK---KCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLA 167
Cdd:cd08183 85 IGGGSVIDAAKAIAALLTNEGSVLDYlEVVGKGRPltePPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLRSPSMLP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 168 SITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLN 247
Cdd:cd08183 165 DVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 248 GIAFSNAGLGNVHAMAHQLGGLYDLPHG-VCnAMLLPIVEEENAK---------QAPAKFRVMAETIGMDVEGKTDEecm 317
Cdd:cd08183 245 GLALANAGLGAVHGLAGPLGGMFGAPHGaIC-AALLPPVLEANLRalrerepdsPALARYRELAGILTGDPDAAAED--- 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 318 dfVIGKIKELSERVGIPKtLSELGVENPDFETLAENSMKDACAGANPVFFDKELLIKLFK 377
Cdd:cd08183 321 --GVEWLEELCEELGIPR-LSEYGLTEEDFPEIVEKARGSSSMKGNPIELSDEELLEILE 377
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
10-377 |
6.75e-106 |
|
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: 314.82 E-value: 6.75e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 10 LVGRGCLAQLKDeigtLGCKKALVVSDKFLTENGVVEKVTKVLDQvGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFI 89
Cdd:cd08180 8 YSGEDSLERLKE----LKGKRVFIVTDPFMVKSGMVDKVTDELDK-SNEVEIFSDVVPDPSIEVVAKGLAKILEFKPDTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 90 VSIGGGSPQDCGKAISVLATNggkitdyegVNKSQKKCLPIvAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLASI 169
Cdd:cd08180 83 IALGGGSAIDAAKAIIYFALK---------QKGNIKKPLFI-AIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSMLPDI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 170 TVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLNGI 249
Cdd:cd08180 153 AILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNASCMAGI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 250 AFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVeeenakqapakfrvmaetigmdvegktdeecMDFVIGKIKELSE 329
Cdd:cd08180 233 AFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYV-------------------------------IEFLIAAIRRLNK 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 496558464 330 RVGIPKTLSELGVENPDFE----TLAENSMKDACAGANPVFFDKELLIKLFK 377
Cdd:cd08180 282 KLGIPSTLKELGIDEEEFEkaidEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
4-366 |
6.29e-105 |
|
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: 314.51 E-value: 6.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 4 RIPAVNLVGRGCLAQLKDEigTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKK 83
Cdd:cd08178 1 KVPPKIYFEPGCLPYLLLE--LPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 84 ENCDFIVSIGGGSPQDCGKAISVLATNGGkiTDYEGVN--------------KSQKKCLpIVAIATTAGTSAEVTINYVI 149
Cdd:cd08178 79 FKPDVIIALGGGSAMDAAKIMWLFYEHPE--TKFEDLAqrfmdirkrvykfpKLGKKAK-LVAIPTTSGTGSEVTPFAVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 150 TDEETHIKMIMVDRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVE 229
Cdd:cd08178 156 TDDKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 230 NGQDIEAREQMCYACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKF------------ 297
Cdd:cd08178 236 NGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDPPTKQaafpqykyyvak 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496558464 298 -RVMAETIGMDVEGKTDEECMDFVIGKIKELSERVGIPKTLSELGVENPDF----ETLAENSMKDACAGANPVF 366
Cdd:cd08178 316 eRYAEIADLLGLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADFlaavDKLAEDAFDDQCTGANPRY 389
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
13-364 |
6.87e-100 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 314.82 E-value: 6.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 13 RGCLAQLKDEIgtLGCKKALVVSDKFLTENGVVEKVTKVLDQV--GIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFIV 90
Cdd:PRK13805 467 RGSLPYLLDEL--DGKKRAFIVTDRFMVELGYVDKVTDVLKKRenGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTII 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 91 SIGGGSPQDCGKAISVLATNGGkiTDYEGV------------------NKSQkkclpIVAIATTAGTSAEVTINYVITDE 152
Cdd:PRK13805 545 ALGGGSPMDAAKIMWLFYEHPE--TDFEDLaqkfmdirkriykfpklgKKAK-----LVAIPTTSGTGSEVTPFAVITDD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 153 ETHIKMIMVDRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENG- 231
Cdd:PRK13805 618 KTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGa 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 232 QDIEAREQMCYACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAK--------------QAPAKF 297
Cdd:PRK13805 698 KDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATdppkqaafpqyeypRADERY 777
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496558464 298 RVMAETIGmdVEGKTDEECMDFVIGKIKELSERVGIPKTLSELGVENPDFE----TLAENSMKDACAGANP 364
Cdd:PRK13805 778 AEIARHLG--LPGSTTEEKVESLIKAIEELKAELGIPMSIKEAGVDEADFLakldELAELAFDDQCTGANP 846
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
21-376 |
2.80e-99 |
|
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: 299.53 E-value: 2.80e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 21 DEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFIVSIGGGSPQDC 100
Cdd:cd14862 17 SHLEQLSGKRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 101 GKAISVLATNggKITDYEGVNKSQ-----KKCLpIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLASITVNDPE 175
Cdd:cd14862 97 AKAAWVLYER--PDLDPEDISPLDllglrKKAK-LIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 176 LMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLNGIAFSNAG 255
Cdd:cd14862 174 FVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGDDLEAREKMHNAATIAGLAFGNSQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 256 LGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAEtigMDVEGKTDEECMDFVIGKIKELSERVGIPK 335
Cdd:cd14862 254 AGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKL---LGIEARDEEEALKKLVEAIRELYKEVGQPL 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 496558464 336 TLSELGVENPDFE----TLAENSMKDACAGANPVFFDKELLIKLF 376
Cdd:cd14862 331 SIKDLGISEEEFEekldELVEYAMEDSCTITSPRPPSEEDLKKLF 375
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
12-378 |
1.89e-97 |
|
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: 295.99 E-value: 1.89e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFIVS 91
Cdd:cd08190 7 GPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 92 IGGGSPQDCGKAISVLATNGGKITDYegVNKSQKKCLPI-------VAIATTAGTSAEVTINYVITDEETHIKMIMVDRN 164
Cdd:cd08190 87 VGGGSVIDTAKAANLYATHPGDFLDY--VNAPIGKGKPVpgplkplIAIPTTAGTGSETTGVAIFDLEELKVKTGISSRY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 165 TLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVA------------------NGAIDVTDATALYAIKQIFEYLPR 226
Cdd:cd08190 165 LRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTArpynarprpanpderpayQGSNPISDVWAEKAIELIGKYLRR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 227 AVENGQDIEAREQMCYACFLNGIAFSNAGLGNVHAMAHQLGGL-------------YDLPHGVCNAMLLPIVEEENAKQA 293
Cdd:cd08190 245 AVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLvkdyrppgypvdhPHVPHGLSVALTAPAVFRFTAPAC 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 294 PAKFRVMAETIGMDVEGKTDEECMDFVIGKIKELSERVGIPKTLSELGVENPDFETLAENSMK----DACagaNPVFFDK 369
Cdd:cd08190 325 PERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPqqrlLKL---NPRPVTE 401
|
....*....
gi 496558464 370 ELLIKLFKK 378
Cdd:cd08190 402 EDLEEIFED 410
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-376 |
2.39e-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: 341475 [Multi-domain] Cd Length: 367 Bit Score: 291.41 E-value: 2.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIehTLYNDVKQNPSVANVEGGLEVLKKENCDFIVS 91
Cdd:cd08196 12 GEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIV--AVFSDVEPNPTVENVDKCARLARENGADFVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 92 IGGGSPQDCGKAISVLATNGGKITDY-EGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLASIT 170
Cdd:cd08196 90 IGGGSVLDTAKAAACLAKTDGSIEDYlEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLVSPGFYPDIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 171 VNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLNGIA 250
Cdd:cd08196 170 IVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPNDKEAREKMALASLLAGLA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 251 FSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGM-DVEGKTDeecmdfvigKIKELSE 329
Cdd:cd08196 250 FSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQLGFkDAEELAD---------KIEELKK 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 496558464 330 RVGIPKTLSELGVENPDFETLAENSMKDACAGANPVFFDKELLIKLF 376
Cdd:cd08196 321 RIGLRTRLSELGITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
3-356 |
5.92e-89 |
|
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: 273.34 E-value: 5.92e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 3 YRIPAVNLVGRGCLAQLKDEIGTLGcKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLK 82
Cdd:cd08191 1 LRSPSRLLFGPGARRALGRVAARLG-SRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 83 KENCDFIVSIGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVD 162
Cdd:cd08191 80 AFDPDVVIGLGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 163 RNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVAN---------------GAIDVTDATALYAIKQIFEYLPRA 227
Cdd:cd08191 160 PYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARdfppfprldpdpvyvGKNPLTDLLALEAIRLIGRHLPRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 228 VENGQDIEAREQMCYACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMD 307
Cdd:cd08191 240 VRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVT 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 496558464 308 VEGkTDEECMDFVIGKIKELSERVGIPKTLSELGVENPDFETLAENSMK 356
Cdd:cd08191 320 TAG-TSEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALS 367
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
10-356 |
3.88e-86 |
|
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: 265.92 E-value: 3.88e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 10 LVGRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFI 89
Cdd:cd08193 8 ICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAGADGV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 90 VSIGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHiKMIMVDRNTLASI 169
Cdd:cd08193 88 IGFGGGSSMDVAKLVALLAGSDQPLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIVTTGETE-KKGVVSPQLLPDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 170 TVNDPELMLSKPAGLTAATGMDALTHAMEAV---VANGAIdvTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFL 246
Cdd:cd08193 167 ALLDAELTLGLPPHVTAATGIDAMVHAIEAYtsrHKKNPI--SDALAREALRLLGANLRRAVEDGSDLEAREAMLLGSML 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 247 NGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEECMDFVIGKIKE 326
Cdd:cd08193 245 AGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEE 324
|
330 340 350
....*....|....*....|....*....|
gi 496558464 327 LSERVGIPKTLSELGVENPDFETLAENSMK 356
Cdd:cd08193 325 LVEASGLPTRLRDVGVTEEDLPMLAEDAMK 354
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
12-377 |
4.82e-82 |
|
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: 255.44 E-value: 4.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGcKKALVVSDK-FLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFIV 90
Cdd:cd08187 13 GKGAIEELGEEIKKYG-KKVLLVYGGgSIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVDFIL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 91 SIGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLASIT 170
Cdd:cd08187 92 AVGGGSVIDAAKAIAAGAKYDGDVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLRPKFS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 171 VNDPELMLSKPAGLTAATGMDALTHAMEAVVANGA-IDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACF--LN 247
Cdd:cd08187 172 ILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEdAPLQDRLAEGLLRTVIENGPKALKDPDDYEARANLMWAATlaLN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 248 GIAfsNAGLGN---VHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIgMDVE-GKTDEECMDFVIGK 323
Cdd:cd08187 252 GLL--GAGRGGdwaTHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRV-FGIDpGGDDEETALEGIEA 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 496558464 324 IKELSERVGIPKTLSELGVENPDFETLAENSMKDACAGANPVFFDKELLIKLFK 377
Cdd:cd08187 329 LEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGFKPLTREDIEEILK 382
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
10-376 |
1.24e-81 |
|
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: 254.07 E-value: 1.24e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 10 LVGRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQvGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFI 89
Cdd:cd08182 5 IFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDALGG-RIPVVVFSDFSPNPDLEDLERGIELFRESGPDVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 90 VSIGGGSPQDCGKAISVLATNGGKITDY--EGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLA 167
Cdd:cd08182 84 IAVGGGSVIDTAKAIAALLGSPGENLLLlrTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPSLYP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 168 SITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLN 247
Cdd:cd08182 164 DAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEASLLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 248 GIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMA-ETIGMDVEGKTDEECMDfvigKIKE 326
Cdd:cd08182 244 GLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDECDDDPRgREILLALGASDPAEAAE----RLRA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 496558464 327 LSERVGIPKTLSELGVENPDFETLAENSMKDACAGANPVFFDKELLIKLF 376
Cdd:cd08182 320 LLESLGLPTRLSEYGVTAEDLEALAASVNTPERLKNNPVRLSEEDLLRLL 369
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
3-377 |
2.48e-78 |
|
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: 245.19 E-value: 2.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 3 YRIPAVNLVGRGCLAQLKDEIGTLGcKKALVVSDKF-LTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVL 81
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELAALG-KKALIVTGKHsAKKNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 82 KKENCDFIVSIGGGSPQDCGKAISVLATNGGKITDYEGVNKSqKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMV 161
Cdd:cd08181 80 RKEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDLFQNGKY-NPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 162 DRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMC 241
Cdd:cd08181 159 NPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDELDEEDREKLM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 242 YACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMdvegKTDEECMDFvi 321
Cdd:cd08181 239 YASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLGF----GSIEEFQKF-- 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 496558464 322 gkikeLSERVGIPKTLSELGVENPDFETLAENSMKdacagANPVFFDKELLIKLFK 377
Cdd:cd08181 313 -----LNRLLGKKEELSEEELEKYADEAMKAKNKK-----NTPGNVTKEDILRIYR 358
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
3-376 |
3.07e-70 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 225.68 E-value: 3.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 3 YRIPAVNLVGRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLK 82
Cdd:PRK15454 24 FSVPPVTLCGPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 83 KENCDFIVSIGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVD 162
Cdd:PRK15454 104 ESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 163 RNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCY 242
Cdd:PRK15454 184 ASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESMLL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 243 ACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFrvmaETIGMDVEGKTDEEcMDfVIG 322
Cdd:PRK15454 264 ASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERF----SQIGRALRTKKSDD-RD-AIN 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 496558464 323 KIKELSERVGIPKTLSELGVENPDFETLAENSMKDACAGANPVFFDKELLIKLF 376
Cdd:PRK15454 338 AVSELIAEVGIGKRLGDVGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLY 391
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
12-356 |
5.23e-65 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 211.47 E-value: 5.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGcKKALVV----SDKfltENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCD 87
Cdd:COG1979 15 GKGQIAKLGEEIPKYG-KKVLLVygggSIK---KNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGID 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 88 FIVSIGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLA 167
Cdd:COG1979 91 FILAVGGGSVIDGAKAIAAGAKYDGDPWDILTGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 168 SITVNDPELMLSKPAGLTAATGMDALTHAMEA---VVANGaiDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYAC 244
Cdd:COG1979 171 KFSILDPELTYTLPKRQTANGIVDIFSHVMEQyftYPVDA--PLQDRFAEGLLRTLIEEGPKALKDPEDYDARANLMWAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 245 F--LNGIafsnAGLGN-----VHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIgMDVEGKTDEECM 317
Cdd:COG1979 249 TlaLNGL----IGAGVpqdwaTHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAERV-WGITEGDDEERA 323
|
330 340 350
....*....|....*....|....*....|....*....
gi 496558464 318 DFVIGKIKELSERVGIPKTLSELGVENPDFETLAENSMK 356
Cdd:COG1979 324 LEGIEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATA 362
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
12-377 |
2.12e-64 |
|
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: 209.81 E-value: 2.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGCKKALVVSDKF-LTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENCDFIV 90
Cdd:cd08186 7 GVGAIAKIKDILKDLGIDKVIIVTGRSsYKKSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 91 SIGGGSPQDCGKAISVLATNGGKITD--YEGVnKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNTLAS 168
Cdd:cd08186 87 AIGGGSPIDTAKSVAVLLAYGGKTARdlYGFR-FAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 169 ITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLNG 248
Cdd:cd08186 166 YAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYASMIAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 249 IAFSNAGLGNVHAMAHQLGGLY-DLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEEcmDFVIGKIKEL 327
Cdd:cd08186 246 IAIDNGLLHLTHALEHPLSGLKpELPHGLGLALLGPAVVKYIYKAVPETLADILRPIVPGLKGTPDEA--EKAARGVEEF 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 496558464 328 SERVGIPKTLSELGVENPDFETLAENSMK----DACAGANPVFFDKELLIKLFK 377
Cdd:cd08186 324 LFSVGFTEKLSDYGFTEDDVDRLVELAFTtpslDLLLSLAPVEVTEEVVREIYE 377
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-364 |
2.39e-64 |
|
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: 209.78 E-value: 2.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGCKKALVVSDKFLTENGVVekVTKVLDQVGIEHT-LYNDVKQNPSVANVEGGLEVLKKENCDFIV 90
Cdd:cd14866 11 GRGALARLGRELDRLGARRALVVCGSSVGANPDL--MDPVRAALGDRLAgVFDGVRPHSPLETVEAAAEALREADADAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 91 SIGGGSPQDCGKAISVLATNGGKITDY------EGVNKSQK----KcLPIVAIATTAgTSAEVTINYVITDEETHIKMIM 160
Cdd:cd14866 89 AVGGGSAIVTARAASILLAEDRDVRELctrraeDGLMVSPRldapK-LPIFVVPTTP-TTADVKAGSAVTDPPAGQRLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 161 VDRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGqDIEAREQM 240
Cdd:cd14866 167 FDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLADDD-DPAARADL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 241 CYACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAEtiGMDVEGKTDEECMDFV 320
Cdd:cd14866 246 VLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAE--ALGVADAGDEASAAAV 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 496558464 321 IGKIKELSERVGIPKTLSELGVENPDFETLAENSMKDACAGANP 364
Cdd:cd14866 324 VDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNNP 367
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
12-375 |
4.58e-64 |
|
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: 207.74 E-value: 4.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGCKKALVVSDKflTENGVVEKVTKVLDQVGIEHtlYNDVKQNPSVANVEGGLEVLKKENCDFIVS 91
Cdd:cd08177 7 GAGTLAELAEELERLGARRALVLSTP--RQRALAERVAALLGDRVAGV--FDGAVMHVPVEVAERALAAAREAGADGLVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 92 IGGGSPQDCGKAISVlaTNGgkitdyegvnksqkkcLPIVAIATT-AGtsAEVTINYVITDEEThiKMIMVDRNTLASIT 170
Cdd:cd08177 83 IGGGSAIGLAKAIAL--RTG----------------LPIVAVPTTyAG--SEMTPIWGETEDGV--KTTGRDPRVLPRTV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 171 VNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMCYACFLNGIA 250
Cdd:cd08177 141 IYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 251 FSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGmdvegkTDEecmdfVIGKIKELSER 330
Cdd:cd08177 221 LGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALG------GGD-----AAGGLYDLARR 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 496558464 331 VGIPKTLSELGVENPDFETLAENSMKDacAGANPVFFDKELLIKL 375
Cdd:cd08177 290 LGAPTSLRDLGMPEDDIDRAADLALAN--PYPNPRPVERDALRAL 332
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
12-365 |
4.50e-63 |
|
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: 206.33 E-value: 4.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGCKKALVVSDKFLTEN-GVVEKVTKVLDQ--VGIehtlYNDVKQNPSVANVEGGLEVLKKENCDF 88
Cdd:cd08192 7 GPGAVEALLHELATLGASRVFIVTSKSLATKtDVIKRLEEALGDrhVGV----FSGVRQHTPREDVLEAARAVREAGADL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 89 IVSIGGGSPQDCGKAISVL----ATNGGKITDYEGVNKSQKKC----LPIVAIATT-AGtsAEVTINYVITDEETHIKMI 159
Cdd:cd08192 83 LVSLGGGSPIDAAKAVALAlaedVTDVDQLDALEDGKRIDPNVtgptLPHIAIPTTlSG--AEFTAGAGATDDDTGHKQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 160 MVDRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQ 239
Cdd:cd08192 161 FAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADPEDLEARLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 240 MCYACFLNGIAF-SNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAK---FRVMAETIGMDVEGKTDEE 315
Cdd:cd08192 241 CQLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERqrlIARALGLVTGGLGREAADA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 496558464 316 CmDFVIGKIKELservGIPKTLSELGVENPDFETLAENSMKDACAGANPV 365
Cdd:cd08192 321 A-DAIDALIREL----GLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPR 365
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-375 |
3.19e-59 |
|
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: 196.37 E-value: 3.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 3 YRIPAVNLVGRGCLAQLKDEIGTLGcKKALVVSDKFLTENGVVEKVTKVLDQVGIEHTLYNDVKQNPSVANVEGGLEVLK 82
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVKEYG-SRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 83 KENCDFIVSIGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETH-IKMIMV 161
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSReVKLLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 162 dRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRAVENGQDIEAREQMC 241
Cdd:cd14864 160 -QPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEELLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 242 YACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIGMDVEGKTDEECMDFVI 321
Cdd:cd14864 239 QAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAV 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 496558464 322 GKIKELSERVGIPKTLSELGVEN--PDFETLAENSMKDACAGANPVFFDKELLIKL 375
Cdd:cd14864 319 EGVRRLIAQLNLPTRLKDLDLASslEQLAAIAEDAPKLNGLPRSMSSDDIFDILKA 374
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
6-352 |
2.84e-36 |
|
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: 132.87 E-value: 2.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 6 PAVNLVGRGCLAQLKdEIGTLGCKKALVVSDKFLTEnGVVEKVTKVLDQVGIEHtLYNDVKQNPSVANVEGGLEVLKKEN 85
Cdd:cd07766 1 PTRIVFGEGAIAKLG-EIKRRGFDRALVVSDEGVVK-GVGEKVADSLKKGLAVA-IFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 86 CDFIVSIGGGSPQDCGKAISVLATNGgkitdyegvnksqkkcLPIVAIATTAGTSAEVTINYVITDEETHIKMIMVDRNT 165
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAALLNRG----------------IPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGPHYNP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 166 LASITvnDPELMLSKPAGLTAATGMDALTHAMEavvangaidvtdatalyaikqifeylpravengqdieaREQMCYACF 245
Cdd:cd07766 142 DVVFV--DTDITKGLPPRQVASGGVDALAHAVE--------------------------------------LEKVVEAAT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 246 LNGIAFSNA-GLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAkfrvmaetIGMDVEGktdeecmdfvigkI 324
Cdd:cd07766 182 LAGMGLFESpGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPE--------PEAAIEA-------------V 240
|
330 340
....*....|....*....|....*...
gi 496558464 325 KELSERVGIPKTLSELGVENPDFETLAE 352
Cdd:cd07766 241 FKFLEDLGLPTHLADLGVSKEDIPKLAE 268
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
69-378 |
2.36e-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: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 69 PSVANVEGGLEVLKKENCDFIVSIGGGSPQDCGKaISVLATNGGKITDYEGVNKSQKKClPIVAIATTAGTSAEVTiNYV 148
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAK-LLALKGISPVLDLFDGKIPLIKEK-ELIIVPTTCGTGSEVT-NIS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 149 ITD-EETHIKMIMVDRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKQIFEYLPRA 227
Cdd:cd14860 139 IVElTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEGYQEI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 228 VENGQD--IEAREQMCYACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCN-AMLLPIVEEENAKQAPAKFRVMAETI 304
Cdd:cd14860 219 AEKGEEarFPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANyAVFTGVLKNYQEKNPDGEIKKLNEFL 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496558464 305 GmDVEGKTDEECMDfvigKIKELSERVGIPKTLSELGVENPDFETLAENSMKDA--CAGANPVFFDKELLIKLFKK 378
Cdd:cd14860 299 A-KILGCDEEDVYD----ELEELLNKILPKKPLHEYGMKEEEIDEFADSVMENQqrLLANNYVPLDREDVAEIYKE 369
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
2-358 |
4.78e-23 |
|
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: 98.70 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 2 VYRIPAVNLVGRGCLAQLKDEIGTLGcKKALVVSDKFLTENgVVEKVTKVLDQVGIEHTLYNdVKQNPSVANVEGGLEVL 81
Cdd:COG0371 2 VIILPRRYVQGEGALDELGEYLADLG-KRALIITGPTALKA-AGDRLEESLEDAGIEVEVEV-FGGECSEEEIERLAEEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 82 KKENCDFIVSIGGGSPQDCGKAISvlatnggkitDYEGvnksqkkcLPIVAIATTAGTSAEVTINYVI-TDEETHIKMIM 160
Cdd:COG0371 79 KEQGADVIIGVGGGKALDTAKAVA----------YRLG--------LPVVSVPTIASTDAPASPLSVIyTEDGAFDGYSF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 161 VDRNTLASITvnDPELMLSKPAGLTAAtGM-DAL-TH-AMEAVVANGAIDVTDATALYAI-------KQIFEYLP---RA 227
Cdd:COG0371 141 LAKNPDLVLV--DTDIIAKAPVRLLAA-GIgDALaKWyEARDWSLAHRDLAGEYYTEAAValarlcaETLLEYGEaaiKA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 228 VENGQDIEAREQMCYACF-LNGIAF----SNAGLGNVHAMAH---QLGGLYDLPHGVCNAM-LLpiveeenakqapakfr 298
Cdd:COG0371 218 VEAGVVTPALERVVEANLlLSGLAMgigsSRPGSGAAHAIHNgltALPETHHALHGEKVAFgTL---------------- 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496558464 299 VMaetigMDVEGKTDEecmdfvIGKIKELSERVGIPKTLSELGVENPDFE---TLAENSMKDA 358
Cdd:COG0371 282 VQ-----LVLEGRPEE------IEELLDFLRSVGLPTTLADLGLDDETEEellTVAEAARPER 333
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
10-302 |
7.66e-23 |
|
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: 98.11 E-value: 7.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 10 LVGRGCLAQLKDEIGTLGC---KKALVVSDKFLTENGVVEKvtkvLDQVGIEHTLYNDVKQNPSVANVEGGLEVLKKENC 86
Cdd:cd08184 5 LFGRGSFDQLGELLAERRKsnnDYVVFFIDDVFKGKPLLDR----LPLQNGDLLIFVDTTDEPKTDQIDALRAQIRAEND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 87 ---DFIVSIGGGSPQDCGKAISVLATNGGKITDYEGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEEthIKMIMVDR 163
Cdd:cd08184 81 klpAAVVGIGGGSTMDIAKAVSNMLTNPGSAADYQGWDLVKNPGIYKIGVPTLSGTGAEASRTAVLTGPE--KKLGINSD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 164 NTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVANGAIDVTDATALYAIKqifeyLPRAV---ENGQDIEAREQM 240
Cdd:cd08184 159 YTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALE-----LCRDVflsDDMMSPENREKL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496558464 241 CYACFLNGIAFSNAGLGNVHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQApAKFRVMAE 302
Cdd:cd08184 234 MVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCIVFNVLEEFYPEGV-KEFREMLE 294
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
12-355 |
3.47e-19 |
|
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: 87.47 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGcKKALVVSDKFLtENGVVEKVTKVLDQVGIEHTLYNDVKQNpSVANVEGGLEVLKKENCDFIVS 91
Cdd:cd08170 7 GPGALDRLGEYLAPLG-KKALVIADPFV-LDLVGERLEESLEKAGLEVVFEVFGGEC-SREEIERLAAIARANGADVVIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 92 IGGGSPQDCGKAISvlatnggkitDYEGvnksqkkcLPIVAIATTAGTSAEVTINYVI-TDEETHIKMIMVDRNtlASIT 170
Cdd:cd08170 84 IGGGKTIDTAKAVA----------DYLG--------LPVVIVPTIASTDAPCSALSVIyTEDGEFDEYLFLPRN--PDLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 171 VNDPELMLSKPAGLTAAtGM-DALTHAMEA--VVANGAIDVTDATAL---YAI-----KQIFEYLP---RAVENGQDIEA 236
Cdd:cd08170 144 LVDTEIIAKAPVRFLVA-GMgDALATYFEAraCARSGAPNMAGGRPTlaaLALaelcyDTLLEYGVaakAAVEAGVVTPA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 237 REQMCYAC-FLNGIAFSNAGLGNVHAMAH---QLGGLYDLPHGvcnamllpiveEENAkqapakFRVMAEtigMDVEGKT 312
Cdd:cd08170 223 LEAVIEANtLLSGLGFESGGLAAAHAIHNgltALPETHHLLHG-----------EKVA------FGTLVQ---LVLEGRP 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 496558464 313 DEEcmdfvIGKIKELSERVGIPKTLSELGVENPDFETL---AENSM 355
Cdd:cd08170 283 DEE-----IEEVIRFCRSVGLPVTLADLGLEDVTDEELrkvAEAAC 323
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
6-350 |
1.64e-18 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 86.00 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 6 PAVNLVGRGCLAQLKDEIGtlgcKKALVVsdkfLTENGVVEKVTKVLDQV-----GIEHTLYNDVKQNPSVANVEGGLEV 80
Cdd:PRK15138 9 PTRILFGKGAIAGLREQIP----ADARVL----ITYGGGSVKKTGVLDQVldalkGMDVLEFGGIEPNPTYETLMKAVKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 81 LKKENCDFIVSIGGGSPQDCGKAISVLATNGGKITDY---EGVNKSQKKCLPIVAIATTAGTSAEVTINYVITDEETHIK 157
Cdd:PRK15138 81 VREEKITFLLAVGGGSVLDGTKFIAAAANYPENIDPWhilETGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 158 MIMVDRNTLASITVNDPELMLSKPAGLTAATGMDALTHAMEAVVA---NGAIDvtDATALYAIKQIFEYLPRAVENGQDI 234
Cdd:PRK15138 161 QAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTypvDAKIQ--DRFAEGILLTLIEEGPKALKEPENY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 235 EAREQMCYACF--LNGIAfsNAGLGN---VHAMAHQLGGLYDLPHGVCNAMLLPIVEEENAKQAPAKFRVMAETIgMDVE 309
Cdd:PRK15138 239 DVRANVMWAATqaLNGLI--GAGVPQdwaTHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERV-WNIT 315
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 496558464 310 GKTDEECMDFVIGKIKELSERVGIPKTLSELGVENPDFETL 350
Cdd:PRK15138 316 EGSDDERIDAAIAATRNFFEQMGVPTRLSDYGLDGSSIPAL 356
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
12-362 |
1.58e-14 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 74.08 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 12 GRGCLAQLKDEIGTLGcKKALVVSDKFLTENgVVEKVTKVLDQVGIEHTlYNDVKQNPSVANVEGGLEVLKKENCDFIVS 91
Cdd:PRK09423 14 GKGALARLGEYLKPLG-KRALVIADEFVLGI-VGDRVEASLKEAGLTVV-FEVFNGECSDNEIDRLVAIAEENGCDVVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 92 IGGGSPQDCGKAISvlatnggkitDYEGVnksqkkclPIVAIATTAGTSAEVTINYVI-TDEETHIKMIMVDRNtlASIT 170
Cdd:PRK09423 91 IGGGKTLDTAKAVA----------DYLGV--------PVVIVPTIASTDAPTSALSVIyTEEGEFERYLFLPKN--PDLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 171 VNDPELMLSKPAGLTAAtGM-DALTHAMEA--VVANGAIDVTDAT---ALYAIKQ-----IFEYLPRA---VENGQDIEA 236
Cdd:PRK09423 151 LVDTAIIAKAPARFLAA-GIgDALATWFEAraCSRSGGTTMAGGKptlAALALAElcyetLLEDGLKAklaVEAKVVTPA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 237 REQMCYA-CFLNGIAFSNAGLGNVHAMaH----QLGGLYDLPHGvcnamllpiveEENAkqapakFRVMAEtigMDVEGK 311
Cdd:PRK09423 230 LENVIEAnTLLSGLGFESGGLAAAHAI-HngltALEDTHHLTHG-----------EKVA------FGTLTQ---LVLENR 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 496558464 312 TDEEcmdfvIGKIKELSERVGIPKTLSELGVENPDFETLAENSmKDACAGA 362
Cdd:PRK09423 289 PKEE-----IEEVIDFCHAVGLPTTLADLGLKEDSDEELRKVA-EAACAEG 333
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
6-379 |
3.61e-14 |
|
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: 72.95 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 6 PAVNLVGRGCLAQLKDEIGTLGcKKALVVSDKFLTENgVVEKVTKVLDQVGI--EHTLYNDVkqnPSVANVEGGLEVLKK 83
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLG-KKALIIGGKTALEA-VGEKLEKSLEEAGIdyEVEVFGGE---CTEENIERLAEKAKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 84 ENCDFIVSIGGGSPQDCGKAISVLATnggkitdyegvnksqkkcLPIVAIATTAGTSAEVTINYVITDEETHIK-MIMVD 162
Cdd:cd08550 76 EGADVIIGIGGGKVLDTAKAVADRLG------------------LPVVTVPTIAATCAAWSALSVLYDEEGEFLgYSLLK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 163 RNTLASITvnDPELMLSKPAGLTAAtGM-DALT--HAMEAVVANGAIDVTD----ATALYAIKQIFEYLPRAVE---NGQ 232
Cdd:cd08550 138 RSPDLVLV--DTDIIAAAPVRYLAA-GIgDTLAkwYEARPSSRGGPDDLALqaavQLAKLAYDLLLEYGVQAVEdvrQGK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 233 DIEAREQMCYACFLN-GIAFSNAGLGNVHAMAHqlgGLYD----LP------HG-------VCNAMLlpiveeenakqap 294
Cdd:cd08550 215 VTPALEDVVDAIILLaGLVGSLGGGGCRTAAAH---AIHNgltkLPethgtlHGekvafglLVQLAL------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 295 akfrvmaetigmdvEGKTDEEcmdfvIGKIKELSERVGIPKTLSELGVEN--PDFETLAENSMKDACAGANPVF-FDKEL 371
Cdd:cd08550 279 --------------EGRSEEE-----IEELIEFLRRLGLPVTLEDLGLELteEELRKIAEYACDPPDMAHMLPFpVTPEM 339
|
....*...
gi 496558464 372 LIKLFKKI 379
Cdd:cd08550 340 LAEAILAA 347
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
14-350 |
1.74e-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: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 14 GCLAQLKDEIGTLGCKKALVVSDKfltenGVVEKVTKVLDQ---VGIEHTLYNdvkQNPSVANVEGGLEVLKKENCDFIV 90
Cdd:cd08172 9 GALKELPELLSEFGIKRPLIIHGE-----KSWQAAKPYLPKlfeIEYPVLRYD---GECSYEEIDRLAEEAKEHQADVII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 91 SIGGGSPQDCGKAISVLAtnggkitdyegvnksqkkCLPIVAIATTAGTSAEVT---INYviTDEETHIKMIMVDRNtlA 167
Cdd:cd08172 81 GIGGGKVLDTAKAVADKL------------------NIPLILIPTLASNCAAWTplsVIY--DEDGEFIGYDYFPRS--A 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 168 SITVNDPELMLSKPAG-LTAATG--------MDALTHAMEavvangAIDVTDATALYAIKQIFEYLpraVENGQD-IEAR 237
Cdd:cd08172 139 YLVLVDPRLLLDSPKDyFVAGIGdtlakwyeADAILRQLE------ELPAFLQLARQAAKLCRDIL---LKDSEQaLADL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 238 EQMCY-ACFLNGI--AFSNAGLgnvhamahqLGGLYDL------PHGVCNAM-LLPiveeenakqapakfrvmaETI--- 304
Cdd:cd08172 210 EAGKLtPAFIKVVetIIALAGM---------VGGFGDEygrsagAHAIHNGLtKLP------------------ETHhfl 262
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 496558464 305 -GMDV----------EGKTDEecmdfvIGKIKELSERVGIPKTLSELGVENPDFETL 350
Cdd:cd08172 263 hGEKVaygilvqlalEGKWDE------IKKLLPFYRRLGLPTSLADLGLTDDTEEAL 313
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
10-105 |
3.99e-04 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 42.15 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558464 10 LVGRGCLAQLKDEIGTLG-CKKALVVSDKFlTENGVVEKVTKVLDQVGIEHTLYNDVKQNpSVANVEGGLEVLKKENCDF 88
Cdd:cd08173 6 VVGHGAINKIGEVLKKLLlGKRALIITGPN-TYKIAGKRVEDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKESKADF 83
|
90
....*....|....*..
gi 496558464 89 IVSIGGGSPQDCGKAIS 105
Cdd:cd08173 84 IIGVGGGKVIDVAKYAA 100
|
|
| |
