|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
1-383 |
0e+00 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 743.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 1 MAASTFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAG 80
Cdd:PRK09860 1 MAASTFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 81 LKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIK 160
Cdd:PRK09860 81 LKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 161 MAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAR 240
Cdd:PRK09860 161 MAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 241 EAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGA 320
Cdd:PRK09860 241 EAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49176377 321 EACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAAM 383
Cdd:PRK09860 321 EACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAAM 383
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
4-380 |
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: 676.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 4 STFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKL 83
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 84 LKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAI 163
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 164 VDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAM 243
Cdd:cd08188 161 VDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKDLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 244 AYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEAC 323
Cdd:cd08188 241 AYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGENTEGLSDEEAAEAA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 49176377 324 INAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYR 380
Cdd:cd08188 321 IEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENALKDACGPTNPRQATKEDVIAIYR 377
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
5-383 |
0e+00 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 528.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 5 TFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLL 84
Cdd:COG1454 4 TFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 85 KENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIV 164
Cdd:COG1454 84 REFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVKKGIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 165 DKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMA 244
Cdd:COG1454 164 DPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLEAREKMA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 245 YAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNvTGKNDAEGAEACI 324
Cdd:COG1454 244 LASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARALGLD-VGLSDEEAAEALI 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 49176377 325 NAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAAM 383
Cdd:COG1454 323 EAIRELLRDLGIPTRLSELGVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
5-380 |
1.43e-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: 1.43e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 5 TFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLL 84
Cdd:cd08176 2 RFVLNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 85 KENNCDSVISLGGGSPHDCAKGIALVAANGG-DIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAI 163
Cdd:cd08176 82 KESGADGIIAVGGGSSIDTAKAIGIIVANPGaDVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKRKFVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 164 VDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAM 243
Cdd:cd08176 162 VDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNVEARENM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 244 AYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEAC 323
Cdd:cd08176 242 ALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDEEAAEAA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 49176377 324 INAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYR 380
Cdd:cd08176 322 VDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDALNDVCTPGNPREATKEDIIALYK 378
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
9-379 |
6.83e-160 |
|
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: 453.44 E-value: 6.83e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 9 PSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENN 88
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 89 CDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHV 168
Cdd:cd08551 81 ADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 169 TPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQF 248
Cdd:cd08551 161 LPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLASL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 249 LAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINAIR 328
Cdd:cd08551 241 LAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVR 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 49176377 329 ELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTN-PIQATHEEIVAIY 379
Cdd:cd08551 321 ELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNnPRPLTEEDIREIY 372
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-379 |
9.16e-154 |
|
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: 438.13 E-value: 9.16e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 6 FFIPSVnVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLK 85
Cdd:cd17814 2 FVAPEF-IFGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 86 ENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVD 165
Cdd:cd17814 81 EEGCDGIVAVGGGSPIDCAKGIGIVVSNGGHILDYEGVDKVRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 166 KHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAY 245
Cdd:cd17814 161 KTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 246 AQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACIN 325
Cdd:cd17814 241 ASLQAGLAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLDVDGLDDEEVAERLIE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 49176377 326 AIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIY 379
Cdd:cd17814 321 AIRDLREDLGIPETLSELGVDEEDIPELAKRAMKDPCLVTNPRRPTREDIEEIY 374
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
6-379 |
6.67e-150 |
|
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: 428.39 E-value: 6.67e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 6 FFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLK 85
Cdd:TIGR02638 4 LILNETSYFGAGAIEDIVDEVKRRGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVAAFK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 86 ENNCDSVISLGGGSPHDCAKGIALVAAN--GGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAI 163
Cdd:TIGR02638 84 ASGADYLIAIGGGSPIDTAKAIGIISNNpeFADVRSLEGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEENKRKFVC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 164 VDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAM 243
Cdd:TIGR02638 164 VDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGGKDLEAREQM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 244 AYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEAC 323
Cdd:TIGR02638 244 ALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAEFTGEKYREIAKAMGVKTEGMSDEEARDAA 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 49176377 324 INAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIY 379
Cdd:TIGR02638 324 VEAVKTLSKRVGIPEGLSELGVKEEDIPALAEAALADVCTGGNPRETTVEEIEELY 379
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
13-361 |
6.27e-149 |
|
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: 426.11 E-value: 6.27e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 13 VIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSV 92
Cdd:cd08189 9 FEGAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 93 ISLGGGSPHDCAKGIALVAANGG-DIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPL 171
Cdd:cd08189 89 IAIGGGSVIDCAKVIAARAANPKkSVRKLKGLLKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPKLIPD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 172 LSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAG 251
Cdd:cd08189 169 AAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEARENMLLASYYAG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 252 MAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELA 331
Cdd:cd08189 249 LAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGDSGESDSEKAEAFIAAIRELN 328
|
330 340 350
....*....|....*....|....*....|
gi 49176377 332 KKVDIPAGLRDLnvKEEDFAVLATNALKDA 361
Cdd:cd08189 329 RRMGIPTTLEEL--KEEDIPEIAKRALKEA 356
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-382 |
5.00e-146 |
|
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: 418.47 E-value: 5.00e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 9 PSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENN 88
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 89 CDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHV 168
Cdd:cd08194 81 CDFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 169 TPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQF 248
Cdd:cd08194 161 LPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 249 LAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINAIR 328
Cdd:cd08194 241 EAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 49176377 329 ELAKKVDIPaGLRDLNVKEEDF-AVL---ATNALKDACGFTNPIQATHEEIVAIYRAA 382
Cdd:cd08194 321 RLCADLEIP-TLREYGIDEEEFeAALdkmAEDALASGSPANNPRVPTKEEIIELYREA 377
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
9-375 |
2.06e-144 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 413.92 E-value: 2.06e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 9 PSVNVIGADSLTDAMNMMADYGFtRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENN 88
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGA-RALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 89 CDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHV 168
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 169 TPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQF 248
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLAST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 249 LAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGvnvtGKNDAEGAEACINAIR 328
Cdd:pfam00465 240 LAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALG----EDSDEEAAEEAIEALR 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 49176377 329 ELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEI 375
Cdd:pfam00465 316 ELLRELGLPTTLSELGVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
30-383 |
1.00e-133 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 387.43 E-value: 1.00e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 30 GFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIAL 109
Cdd:PRK10624 29 GFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYLIAIGGGSPQDTCKAIGI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 110 VAANG--GDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSL 187
Cdd:PRK10624 109 ISNNPefADVRSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFVDADMMDSMPPGL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 188 TAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDgsNAKAREAMAYAQFLAGMAFNNASLGYVHAMAH 267
Cdd:PRK10624 189 KAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAG--DKEAGEGMALGQYIAGMGFSNVGLGLVHGMAH 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 268 QLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKE 347
Cdd:PRK10624 267 PLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKE 346
|
330 340 350
....*....|....*....|....*....|....*.
gi 49176377 348 EDFAVLATNALKDACGFTNPIQATHEEIVAIYRAAM 383
Cdd:PRK10624 347 EDIPALAQAAFDDVCTGGNPREATLEDIVELYKKAW 382
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-383 |
2.08e-131 |
|
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: 381.50 E-value: 2.08e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 7 FIPSVNVI-GADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLK 85
Cdd:cd14865 3 FFNPTKIVsGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 86 ENNCDSVISLGGGSPHDCAKGIALVAANGG-DIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIV 164
Cdd:cd14865 83 EAGADGIIAVGGGSVIDTAKGVNILLSEGGdDLDDYGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 165 DKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMA 244
Cdd:cd14865 163 SPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGKDLEARLALA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 245 YAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAM--GVNVTGKNDAEGAEA 322
Cdd:cd14865 243 IAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALayGVTPAGRRAEEAIEA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49176377 323 CINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAAM 383
Cdd:cd14865 323 AIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELALNDGAILFNPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-382 |
1.56e-129 |
|
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: 376.88 E-value: 1.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 5 TFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLL 84
Cdd:cd14863 1 TYSQLTPVIFGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 85 KENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSA-KPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAI 163
Cdd:cd14863 81 REEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDYALAGPPVpKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 164 VDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAM 243
Cdd:cd14863 161 LGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 244 AYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEAC 323
Cdd:cd14863 241 LLASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 49176377 324 INAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAA 382
Cdd:cd14863 321 ADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVLKDPFAMFNPRPITEEEVAEILEAI 379
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-380 |
9.05e-122 |
|
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: 356.81 E-value: 9.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 6 FFIPsVNVI-GADSLTDAMNMMADYGfTRTLIVTDN-MLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKL 83
Cdd:cd08185 1 YYQP-TRILfGAGKLNELGEEALRPG-KKALIVTGKgSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 84 LKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDY----EGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHI 159
Cdd:cd08185 79 AKEEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYifggTGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 160 KMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKA 239
Cdd:cd08185 159 KKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 240 REAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFY-NLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAmgvNVTGKNDAE 318
Cdd:cd08185 239 REKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVARA---EASGLSDAK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49176377 319 GAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALK--DACGFTNPIQATHEEIVAIYR 380
Cdd:cd08185 316 AAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMEtmGGLFANNPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
15-383 |
1.20e-121 |
|
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: 356.44 E-value: 1.20e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 15 GADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVIS 94
Cdd:cd14861 9 GAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDGIIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 95 LGGGSPHDCAKGIALVAANGGDIRDYE----GVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTP 170
Cdd:cd14861 89 LGGGSAIDAAKAIALMATHPGPLWDYEdgegGPAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSPKLLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 171 LLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLA 250
Cdd:cd14861 169 KVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDLEARGEMMMAALMG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 251 GMAFNNaSLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVnvtgknDAEGAEACINAIREL 330
Cdd:cd14861 249 AVAFQK-GLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALGL------GLGGFDDFIAWVEDL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 49176377 331 AKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAAM 383
Cdd:cd14861 322 NERLGLPATLSELGVTEDDLDELAELALADPCHATNPRPVTAEDYRALLREAL 374
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
6-382 |
1.48e-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: 333.39 E-value: 1.48e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 6 FFIPSVNVIGADSLTdamnMMADYGFTRTLIVTD-NMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLL 84
Cdd:cd08179 2 FFVPRDIYFGEGALE----YLKTLKGKRAFIVTGgGSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 85 KENNCDSVISLGGGSPHDCAKGIALVAANggdiRDYEGVDRSAKPQLP-------MIAINTTAGTASEMTRFCIITDEAR 157
Cdd:cd08179 78 REFEPDWIIAIGGGSVIDAAKAMWVFYEY----PELTFEDALVPFPLPelrkkarFIAIPSTSGTGSEVTRASVITDTEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 158 HIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNA 237
Cdd:cd08179 154 GIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 238 KAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAamgvnVTGKNDA 317
Cdd:cd08179 234 EAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAAL-----LIGLTDE 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 49176377 318 EGAEACINAIRELAKKVDIPAGLRDLNVKEEDFA----VLATNALKDACGFTNPIQATHEEIVAIYRAA 382
Cdd:cd08179 309 ELVEDLIEAIEELNKKLGIPLSFKEAGIDEDEFFakldEMAENAMNDACTGTNPRKPTVEEMKELLKAA 377
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
29-380 |
4.05e-111 |
|
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: 330.69 E-value: 4.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 29 YGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIA 108
Cdd:cd08178 21 PGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFKPDVIIALGGGSAMDAAKIMW 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 109 L-----------VAANGGDIRD--YEGVDRSAKPQLpmIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVN 175
Cdd:cd08178 101 LfyehpetkfedLAQRFMDIRKrvYKFPKLGKKAKL--VAIPTTSGTGSEVTPFAVITDDKTGKKYPLADYALTPDMAIV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 176 DSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAGMAFN 255
Cdd:cd08178 179 DPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGNDIEAREKMHNAATIAGMAFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 256 NASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSK---------------VAAARLRDCAAAMGvnVTGKNDAEGA 320
Cdd:cd08178 259 NAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATdpptkqaafpqykyyVAKERYAEIADLLG--LGGKTPEEKV 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49176377 321 EACINAIRELAKKVDIPAGLRDLNVKEEDF--AV--LATNALKDACGFTNPIQATHEEIVAIYR 380
Cdd:cd08178 337 ESLIKAIEDLKKDLGIPTSIREAGIDEADFlaAVdkLAEDAFDDQCTGANPRYPLISELKEILL 400
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
21-380 |
3.85e-110 |
|
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: 325.60 E-value: 3.85e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 21 DAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSvIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSP 100
Cdd:cd08180 12 DSLERLKELKGKRVFIVTDPFMVKSGMVDKVTDELDKSNEVE-IFSDVVPDPSIEVVAKGLAKILEFKPDTIIALGGGSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 101 HDCAKGIALVAANGGDIRDyegvdrsaKPQLpmIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLM 180
Cdd:cd08180 91 IDAAKAIIYFALKQKGNIK--------KPLF--IAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSMLPDIAILDPELV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 181 IGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAGMAFNNASLG 260
Cdd:cd08180 161 KSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNASCMAGIAFNNAGLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 261 YVHAMAHQLGGFYNLPHGVCNAVLLPHVqvfnskvaaarlrdcaaamgvnvtgkndaegAEACINAIRELAKKVDIPAGL 340
Cdd:cd08180 241 INHSLAHALGGRFHIPHGRANAILLPYV-------------------------------IEFLIAAIRRLNKKLGIPSTL 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 49176377 341 RDLNVKEEDFA----VLATNALKDACGFTNPIQATHEEIVAIYR 380
Cdd:cd08180 290 KELGIDEEEFEkaidEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
13-382 |
9.51e-105 |
|
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: 313.68 E-value: 9.51e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 13 VIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSV 92
Cdd:cd08193 8 ICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAGADGV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 93 ISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEArHIKMAIVDKHVTPLL 172
Cdd:cd08193 88 IGFGGGSSMDVAKLVALLAGSDQPLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIVTTGE-TEKKGVVSPQLLPDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 173 SVNDSSLMIGMPKSLTAATGMDALTHAIEAYVS-IAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAG 251
Cdd:cd08193 167 ALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDALAREALRLLGANLRRAVEDGSDLEAREAMLLGSMLAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 252 MAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELA 331
Cdd:cd08193 247 QAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEELV 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 49176377 332 KKVDIPAGLRDLNVKEEDFAVLATNALKDACGFT-NPIQATHEEIVAIYRAA 382
Cdd:cd08193 327 EASGLPTRLRDVGVTEEDLPMLAEDAMKQTRLLVnNPREVTEEDALAIYQAA 378
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-379 |
8.73e-103 |
|
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: 307.97 E-value: 8.73e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 5 TFFIPsVNVI-GADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFsvIYDGTQPNPTTENVAAGLKL 83
Cdd:cd08196 2 SYYQP-VKIIfGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVA--VFSDVEPNPTVENVDKCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 84 LKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDY-EGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMA 162
Cdd:cd08196 79 ARENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYlEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 163 IVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREA 242
Cdd:cd08196 159 LVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPNDKEAREK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 243 MAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNvtgkndaeGAEA 322
Cdd:cd08196 239 MALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQLGFK--------DAEE 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 49176377 323 CINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIY 379
Cdd:cd08196 311 LADKIEELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
17-382 |
3.51e-102 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 320.98 E-value: 3.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 17 DSLTDAMNMMadYGFTRTLIVTDNMLTKLGMAGDVQKALEER--NIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVIS 94
Cdd:PRK13805 468 GSLPYLLDEL--DGKKRAFIVTDRFMVELGYVDKVTDVLKKRenGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 95 LGGGSPHDCAKGIAL-----------VAANGGDIRDyegvdRSAK-PQLP----MIAINTTAGTASEMTRFCIITDEARH 158
Cdd:PRK13805 546 LGGGSPMDAAKIMWLfyehpetdfedLAQKFMDIRK-----RIYKfPKLGkkakLVAIPTTSGTGSEVTPFAVITDDKTG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 159 IKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGS-NA 237
Cdd:PRK13805 621 VKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGAkDP 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 238 KAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSK--------------VAAARLRDC 303
Cdd:PRK13805 701 EAREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATdppkqaafpqyeypRADERYAEI 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 304 AAAMGvnVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDF--AV--LATNALKDACGFTNPIQATHEEIVAIY 379
Cdd:PRK13805 781 ARHLG--LPGSTTEEKVESLIKAIEELKAELGIPMSIKEAGVDEADFlaKLdeLAELAFDDQCTGANPRYPLISELKEIL 858
|
...
gi 49176377 380 RAA 382
Cdd:PRK13805 859 LDA 861
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
27-378 |
9.64e-102 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 305.97 E-value: 9.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 27 ADYGfTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTqPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKG 106
Cdd:cd08183 19 AELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVS-GEPTVETVDAAVALAREAGCDVVIAIGGGSVIDAAKA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 107 IALVAANGGDIRDYEGVDRSAKPQ----LPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIG 182
Cdd:cd08183 97 IAALLTNEGSVLDYLEVVGKGRPLteppLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLRSPSMLPDVALVDPELTLS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 183 MPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAGMAFNNASLGYV 262
Cdd:cd08183 177 LPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLGGLALANAGLGAV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 263 HAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAA-----AMGVNVTGKNDAeGAEACINAIRELAKKVDIP 337
Cdd:cd08183 257 HGLAGPLGGMFGAPHGAICAALLPPVLEANLRALREREPDSPAlaryrELAGILTGDPDA-AAEDGVEWLEELCEELGIP 335
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 49176377 338 aGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAI 378
Cdd:cd08183 336 -RLSEYGLTEEDFPEIVEKARGSSSMKGNPIELSDEELLEI 375
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
26-383 |
7.99e-101 |
|
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: 304.85 E-value: 7.99e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 26 MADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAK 105
Cdd:cd08190 18 LKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVAVGGGSVIDTAK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 106 GIALVAANGGDIRDY----EGVDRSAKPQL-PMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLM 180
Cdd:cd08190 98 AANLYATHPGDFLDYvnapIGKGKPVPGPLkPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISSRYLRPTLAIVDPLLT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 181 IGMPKSLTAATGMDALTHAIEAYVSIA------------------ATPITDACALKAVTMIAENLPLAVEDGSNAKAREA 242
Cdd:cd08190 178 LTLPPRVTASSGFDVLCHALESYTARPynarprpanpderpayqgSNPISDVWAEKAIELIGKYLRRAVNDGDDLEARSN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 243 MAYAQFLAGMAFNNASLGYVHAMAHQLGG--------FYN-----LPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGV 309
Cdd:cd08190 258 MLLASTLAGIGFGNAGVHLPHAMAYPIAGlvkdyrppGYPvdhphVPHGLSVALTAPAVFRFTAPACPERHLEAAELLGA 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49176377 310 NVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALK----DACgftNPIQATHEEIVAIYRAAM 383
Cdd:cd08190 338 DTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPqqrlLKL---NPRPVTEEDLEEIFEDAL 412
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-375 |
4.18e-96 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 291.44 E-value: 4.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 5 TFFIPSVNVIGADSLtdamNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLL 84
Cdd:cd14862 2 WYFSSPKIVFGEDAL----SHLEQLSGKRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 85 KENNCDSVISLGGGSPHDCAKGIALVAANggDIRDYEGVD------RSAKPQLpmIAINTTAGTASEMTRFCIITDEARH 158
Cdd:cd14862 78 REFEPDLIIALGGGSVMDAAKAAWVLYER--PDLDPEDISpldllgLRKKAKL--IAIPTTSGTGSEATWAIVLTDTEEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 159 IKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAK 238
Cdd:cd14862 154 RKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGDDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 239 AREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAmgvNVTGKNDAE 318
Cdd:cd14862 234 AREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKLL---GIEARDEEE 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49176377 319 GAEACINAIRELAKKVDIPAGLRDLNVKEEDFA----VLATNALKDACGFTNPIQATHEEI 375
Cdd:cd14862 311 ALKKLVEAIRELYKEVGQPLSIKDLGISEEEFEekldELVEYAMEDSCTITSPRPPSEEDL 371
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-383 |
2.49e-94 |
|
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: 287.20 E-value: 2.49e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 6 FFIPSVNVIGADSLTDAMNMMADYGfTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLK 85
Cdd:cd08191 1 LRSPSRLLFGPGARRALGRVAARLG-SRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 86 ENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVD 165
Cdd:cd08191 80 AFDPDVVIGLGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 166 KHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIA---------------ATPITDACALKAVTMIAENLPLA 230
Cdd:cd08191 160 PYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDfppfprldpdpvyvgKNPLTDLLALEAIRLIGRHLPRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 231 VEDGSNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVN 310
Cdd:cd08191 240 VRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVT 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49176377 311 VTGKNDaEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDA-CGFTNPIQATHEEIVAIYRAAM 383
Cdd:cd08191 320 TAGTSE-EAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTrLIANNPRPPTEEDLLRILRAAF 392
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
5-382 |
9.44e-78 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 244.94 E-value: 9.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 5 TFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLL 84
Cdd:PRK15454 23 TFSVPPVTLCGPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 85 KENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIV 164
Cdd:PRK15454 103 RESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 165 DKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMA 244
Cdd:PRK15454 183 HASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESML 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 245 YAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAegaeacI 324
Cdd:PRK15454 263 LASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRALRTKKSDDRDA------I 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 49176377 325 NAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAA 382
Cdd:PRK15454 337 NAVSELIAEVGIGKRLGDVGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLYAAA 394
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
5-380 |
1.75e-75 |
|
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: 238.49 E-value: 1.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 5 TFFIPsVNVI-GADSLTDAMNMMADYGfTRTLIVTD-NMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLK 82
Cdd:cd08187 3 TFYNP-TKIIfGKGAIEELGEEIKKYG-KKVLLVYGgGSIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 83 LLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYegVDRSAKPQ--LPMIAINTTAGTASEMTRFCIITDEARHIK 160
Cdd:cd08187 81 LAREENVDFILAVGGGSVIDAAKAIAAGAKYDGDVWDF--FTGKAPPEkaLPVGTVLTLAATGSEMNGGAVITNEETKEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 161 MAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVS-IAATPITDA---CALKavTMIaENLPLAVEDGSN 236
Cdd:cd08187 159 LGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTgTEDAPLQDRlaeGLLR--TVI-ENGPKALKDPDD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 237 AKAREAMAYAqflAGMAFNN-ASLGY-----VHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLrdcaAAMGVN 310
Cdd:cd08187 236 YEARANLMWA---ATLALNGlLGAGRggdwaTHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERF----AQFARR 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49176377 311 V----TGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYR 380
Cdd:cd08187 309 VfgidPGGDDEETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGFKPLTREDIEEILK 382
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
27-380 |
2.14e-75 |
|
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: 237.89 E-value: 2.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 27 ADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFsVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKG 106
Cdd:cd08182 19 GGLGARRVLLVTGPSAVRESGAADILDALGGRIPV-VVFSDFSPNPDLEDLERGIELFRESGPDVIIAVGGGSVIDTAKA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 107 IALVAANGGDIRDY--EGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMP 184
Cdd:cd08182 98 IAALLGSPGENLLLlrTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPSLYPDAAILDPELTLSLP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 185 KSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAGMAFNNASLGYVHA 264
Cdd:cd08182 178 LYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEASLLAGLAISITKTTAAHA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 265 MAHQLGGFYNLPHGVCNAVLLPHVQVFNSKV-----AAARLRDCAAAMGvnvtGKNDAEGAEacinAIRELAKKVDIPAG 339
Cdd:cd08182 258 ISYPLTSRYGVPHGHACALTLPAVLRYNAGAddecdDDPRGREILLALG----ASDPAEAAE----RLRALLESLGLPTR 329
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 49176377 340 LRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYR 380
Cdd:cd08182 330 LSEYGVTAEDLEALAASVNTPERLKNNPVRLSEEDLLRLLE 370
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
6-380 |
6.12e-71 |
|
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: 226.31 E-value: 6.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 6 FFIPSVNVIGADSLTDAMNMMADYGfTRTLIVT-DNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLL 84
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELAALG-KKALIVTgKHSAKKNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 85 KENNCDSVISLGGGSPHDCAKGIALVAANGGDIRD--YEGVDRSAkpqLPMIAINTTAGTASEMTRFCIITDEARHIKMA 162
Cdd:cd08181 80 RKEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDlfQNGKYNPP---LPIVAIPTTAGTGSEVTPYSILTDHEKGTKKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 163 IVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREA 242
Cdd:cd08181 157 FGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDELDEEDREK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 243 MAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEgaea 322
Cdd:cd08181 237 LMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLGFGSIEEFQKF---- 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 49176377 323 cinaIRELAKKVDIpaglrdlnVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYR 380
Cdd:cd08181 313 ----LNRLLGKKEE--------LSEEELEKYADEAMKAKNKKNTPGNVTKEDILRIYR 358
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-359 |
2.56e-69 |
|
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: 222.56 E-value: 2.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 6 FFIPSVNVIGADSLTDAMNMMADYGfTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLK 85
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVKEYG-SRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 86 ENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEA-RHIKMaIV 164
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRsREVKL-LK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 165 DKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMA 244
Cdd:cd14864 159 AQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEELLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 245 YAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACI 324
Cdd:cd14864 239 QAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAV 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 49176377 325 NAIRELAKKVDIPAGLRDLNV--KEEDFAVLATNALK 359
Cdd:cd14864 319 EGVRRLIAQLNLPTRLKDLDLasSLEQLAAIAEDAPK 355
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
13-382 |
3.03e-68 |
|
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: 219.81 E-value: 3.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 13 VIGADSLTDAMNMMADYGFTRTLIVTDNML-TKLGMAGDVQKALEERnifSV-IYDGTQPNPTTENVAAGLKLLKENNCD 90
Cdd:cd08192 5 SYGPGAVEALLHELATLGASRVFIVTSKSLaTKTDVIKRLEEALGDR---HVgVFSGVRQHTPREDVLEAARAVREAGAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 91 SVISLGGGSPHDCAKGIALVAANG----GDIRDYEGVDRSAK----PQLPMIAINTTAgTASEMTRFCIITDEARHIKMA 162
Cdd:cd08192 82 LLVSLGGGSPIDAAKAVALALAEDvtdvDQLDALEDGKRIDPnvtgPTLPHIAIPTTL-SGAEFTAGAGATDDDTGHKQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 163 IVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREA 242
Cdd:cd08192 161 FAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADPEDLEARLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 243 MAYAQFLAGMAF-NNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVnVTGKNDAEGAE 321
Cdd:cd08192 241 CQLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALGL-VTGGLGREAAD 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49176377 322 ACiNAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATH-EEIVAIYRAA 382
Cdd:cd08192 320 AA-DAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRPITDkDDVLEILESA 380
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
15-383 |
2.66e-67 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 217.52 E-value: 2.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 15 GADSLTDAMNMMADYGFTRTLIVTDNMLTKL-GMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVI 93
Cdd:cd08186 7 GVGAIAKIKDILKDLGIDKVIIVTGRSSYKKsGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 94 SLGGGSPHDCAKGIALVAANGGDIRD--YEGVdRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPL 171
Cdd:cd08186 87 AIGGGSPIDTAKSVAVLLAYGGKTARdlYGFR-FAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 172 LSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAG 251
Cdd:cd08186 166 YAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYASMIAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 252 MAFNNASLGYVHAMAHQLGGFY-NLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKndAEGAEACINAIREL 330
Cdd:cd08186 246 IAIDNGLLHLTHALEHPLSGLKpELPHGLGLALLGPAVVKYIYKAVPETLADILRPIVPGLKGT--PDEAEKAARGVEEF 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 49176377 331 AKKVDIPAGLRDLNVKEEDFAVLATNALK----DACGFTNPIQATHEEIVAIYRAAM 383
Cdd:cd08186 324 LFSVGFTEKLSDYGFTEDDVDRLVELAFTtpslDLLLSLAPVEVTEEVVREIYEESL 380
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
15-382 |
1.32e-60 |
|
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: 200.15 E-value: 1.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 15 GADSLTDAMNMMADYGFTRTLIVTD-NMLTKLGMAGDVQKALEERniFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVI 93
Cdd:cd14866 11 GRGALARLGRELDRLGARRALVVCGsSVGANPDLMDPVRAALGDR--LAGVFDGVRPHSPLETVEAAAEALREADADAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 94 SLGGGSPHDCAKGIALVAANGGDIRDY------EGVDRSAK---PQLPMIAINTTAGTASEMTRFCIITDEARHiKMAIV 164
Cdd:cd14866 89 AVGGGSAIVTARAASILLAEDRDVRELctrraeDGLMVSPRldaPKLPIFVVPTTPTTADVKAGSAVTDPPAGQ-RLALF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 165 DKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPlAVEDGSNAKAREAMA 244
Cdd:cd14866 168 DPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLP-RLADDDDPAARADLV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 245 YAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGknDAEGAEACI 324
Cdd:cd14866 247 LAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGVADAG--DEASAAAVV 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 49176377 325 NAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATH-EEIVAIYRAA 382
Cdd:cd14866 325 DAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNNPRPVPTaEELEALLEAA 383
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
44-383 |
4.87e-58 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 193.36 E-value: 4.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 44 KLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYegV 123
Cdd:COG1979 44 KNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDI--L 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 124 DRSAKPQ--LPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIE 201
Cdd:COG1979 122 TGKAPVEkaLPLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVME 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 202 AYVSIAA-TPITD--ACA-LKavTMIaENLPLAVEDGSNAKAREAMAYAqflAGMAFNN-ASLGY-----VHAMAHQLGG 271
Cdd:COG1979 202 QYFTYPVdAPLQDrfAEGlLR--TLI-EEGPKALKDPEDYDARANLMWA---ATLALNGlIGAGVpqdwaTHMIEHELSA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 272 FYNLPHGVCNAVLLPHVQVFNSKVAAARLrdcaAAMGVNV---TGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEE 348
Cdd:COG1979 276 LYDIDHGAGLAIVLPAWMRYVLEEKPEKF----AQYAERVwgiTEGDDEERALEGIEATEEFFESLGLPTRLSEYGIDEE 351
|
330 340 350
....*....|....*....|....*....|....*...
gi 49176377 349 DFAVLATNALK---DACGFTNPIqaTHEEIVAIYRAAM 383
Cdd:COG1979 352 DIEEMAEKATAhgmTALGEFKDL--TPEDVREILELAL 387
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
13-383 |
4.30e-55 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341456 [Multi-domain] Cd Length: 337 Bit Score: 184.24 E-value: 4.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 13 VIGADSLTDAMNMMADYGFTRTLIVTDNmlTKLGMAGDVQKALEERNIfsVIYDGTQPNPTTENVAAGLKLLKENNCDSV 92
Cdd:cd08177 5 VFGAGTLAELAEELERLGARRALVLSTP--RQRALAERVAALLGDRVA--GVFDGAVMHVPVEVAERALAAAREAGADGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 93 ISLGGGSPHDCAKGIALvaanggdirdyegvdRSAkpqLPMIAINTT-AGtaSEMTRFCIITDEARhiKMAIVDKHVTPL 171
Cdd:cd08177 81 VAIGGGSAIGLAKAIAL---------------RTG---LPIVAVPTTyAG--SEMTPIWGETEDGV--KTTGRDPRVLPR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 172 LSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAG 251
Cdd:cd08177 139 TVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 252 MAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVnvtgkNDAEGaeacinAIRELA 331
Cdd:cd08177 219 VVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGG-----GDAAG------GLYDLA 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 49176377 332 KKVDIPAGLRDLNVKEEDFAVLATNALKDAcgFTNPIQATHEEIVAIYRAAM 383
Cdd:cd08177 288 RRLGAPTSLRDLGMPEDDIDRAADLALANP--YPNPRPVERDALRALLERAW 337
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
72-381 |
6.62e-38 |
|
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: 140.04 E-value: 6.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 72 PTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKgiALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCI 151
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAK--LLALKGISPVLDLFDGKIPLIKEKELIIVPTTCGTGSEVTNISI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 152 ITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAV 231
Cdd:cd14860 140 VELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEGYQEIA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 232 EDGSNAKAR--EAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHV----QVFNSKVAAARLRD-CA 304
Cdd:cd14860 220 EKGEEARFPllGDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVlknyQEKNPDGEIKKLNEfLA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 305 AAMGvnvTGKNDA-EGAEACINAIreLAKKvdipaGLRDLNVKEED---FAV--------LATNalkdacgftNPIQATH 372
Cdd:cd14860 300 KILG---CDEEDVyDELEELLNKI--LPKK-----PLHEYGMKEEEideFADsvmenqqrLLAN---------NYVPLDR 360
|
....*....
gi 49176377 373 EEIVAIYRA 381
Cdd:cd14860 361 EDVAEIYKE 369
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
30-358 |
1.16e-29 |
|
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: 115.15 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 30 GFTRTLIVTDNMLTKlGMAGDVQKALEERNIFSvIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIAL 109
Cdd:cd07766 21 GFDRALVVSDEGVVK-GVGEKVADSLKKGLAVA-IFDFVGENPTFEEVKNAVERARAAEADAVIAVGGGSTLDTAKAVAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 110 VaanggdirdyegvdrsAKPQLPMIAINTTAGTASEMTRFCIITDEARhiKMAIVDKHVTPLLSVNDSSLMIGMPKSLTA 189
Cdd:cd07766 99 L----------------LNRGIPFIIVPTTASTDSEVSPKSVITDKGG--KNKQVGPHYNPDVVFVDTDITKGLPPRQVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 190 ATGMDALTHAIEayvsiaatpitdacalkavtmiaenlplavedgsnakaREAMAYAQFLAGMA-FNNASLGYVHAMAHQ 268
Cdd:cd07766 161 SGGVDALAHAVE--------------------------------------LEKVVEAATLAGMGlFESPGLGLAHAIGHA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 269 LGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDcaaamgvnvtgkndaegaeacINAIRELAKKVDIPAGLRDLNVKEE 348
Cdd:cd07766 203 LTAFEGIPHGEAVAVGLPYVLKVANDMNPEPEAA---------------------IEAVFKFLEDLGLPTHLADLGVSKE 261
|
330
....*....|
gi 49176377 349 DFAVLATNAL 358
Cdd:cd07766 262 DIPKLAEKAL 271
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
58-281 |
1.70e-24 |
|
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: 102.73 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 58 RNIFSVIYDGTQPNPTTENV-AAGLKLLKEN--NCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMI 134
Cdd:cd08184 49 QNGDLLIFVDTTDEPKTDQIdALRAQIRAENdkLPAAVVGIGGGSTMDIAKAVSNMLTNPGSAADYQGWDLVKNPGIYKI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 135 AINTTAGTASEMTRFCIITDEARhiKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDA 214
Cdd:cd08184 129 GVPTLSGTGAEASRTAVLTGPEK--KLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDA 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 49176377 215 CALKAVTMIAEnlPLAVEDGSNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCN 281
Cdd:cd08184 207 YAEKALELCRD--VFLSDDMMSPENREKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVAN 271
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
44-342 |
4.10e-21 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 93.71 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 44 KLGMAGDVQKALEERNIFSviYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIAlVAANGGDIRD---- 119
Cdd:PRK15138 43 KTGVLDQVLDALKGMDVLE--FGGIEPNPTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKFIA-AAANYPENIDpwhi 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 120 YEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHA 199
Cdd:PRK15138 120 LETGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHT 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 200 IEAYVSIAA-TPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAqflAGMAFNNASLGYV------HAMAHQLGGF 272
Cdd:PRK15138 200 VEQYVTYPVdAKIQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWA---ATQALNGLIGAGVpqdwatHMLGHELTAM 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 49176377 273 YNLPHGVCNAVLLPhvQVFNSKVAAARLRDCAAAMGV-NVTGKNDAEGAEACINAIRELAKKVDIPAGLRD 342
Cdd:PRK15138 277 HGLDHAQTLAIVLP--ALWNEKRDTKRAKLLQYAERVwNITEGSDDERIDAAIAATRNFFEQMGVPTRLSD 345
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
5-382 |
4.16e-17 |
|
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: 81.75 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 5 TFFIPSVNVIGADSLTDAMNMMADYGfTRTLIVTDNmlTKLGMAGD-VQKALEERNI--FSVIYDGtqpNPTTENVAAGL 81
Cdd:COG0371 2 VIILPRRYVQGEGALDELGEYLADLG-KRALIITGP--TALKAAGDrLEESLEDAGIevEVEVFGG---ECSEEEIERLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 82 KLLKENNCDSVISLGGGSPHDCAKGIAlvaanggdirDYEGvdrsakpqLPMIAINTTAGTASEMTRFCII-TDEARHIK 160
Cdd:COG0371 76 EEAKEQGADVIIGVGGGKALDTAKAVA----------YRLG--------LPVVSVPTIASTDAPASPLSVIyTEDGAFDG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 161 MAIVDKhvTPLLSVNDSSLMIGMPKSLTAAtGM-DALTHAIEAYVSIAA------TPITDAC---ALKAVTMIAENLPLA 230
Cdd:COG0371 138 YSFLAK--NPDLVLVDTDIIAKAPVRLLAA-GIgDALAKWYEARDWSLAhrdlagEYYTEAAvalARLCAETLLEYGEAA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 231 VEDGSNAKAREA----MAYAQFLAGMAFN----NASLGYVHAMAH---QLGGFYNLPHGvcnavllphvqvfnSKVAAAR 299
Cdd:COG0371 215 IKAVEAGVVTPAlervVEANLLLSGLAMGigssRPGSGAAHAIHNgltALPETHHALHG--------------EKVAFGT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 300 LrdCAAAMgvnvtgkndaEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNAlKDAC--GFT---NPIQATHEE 374
Cdd:COG0371 281 L--VQLVL----------EGRPEEIEELLDFLRSVGLPTTLADLGLDDETEEELLTVA-EAARpeRYTilnLPFEVTPEA 347
|
....*...
gi 49176377 375 IVAIYRAA 382
Cdd:COG0371 348 VEAAILAT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
15-381 |
6.46e-10 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 59.86 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 15 GADSLTDAMNMMADYGfTRTLIVTDNmlTKLGMAGD-VQKALEERNIF--SVIYDGtqpNPTTENVAAGLKLLKENNCDS 91
Cdd:cd08550 7 EPGILAKAGEYIAPLG-KKALIIGGK--TALEAVGEkLEKSLEEAGIDyeVEVFGG---ECTEENIERLAEKAKEEGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 92 VISLGGGSPHDCAKGIALVAanggdirdyegvdrsakpQLPMIAINTTAGTASEMTRFCII-TDEARHIKMAIVDKhvTP 170
Cdd:cd08550 81 IIGIGGGKVLDTAKAVADRL------------------GLPVVTVPTIAATCAAWSALSVLyDEEGEFLGYSLLKR--SP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 171 LLSVNDSSLMIGMPKSLTAAtGM-DALTHAIEAYVSIAATPitDACALKAVTMIAENL--------PLAVED---GSNAK 238
Cdd:cd08550 141 DLVLVDTDIIAAAPVRYLAA-GIgDTLAKWYEARPSSRGGP--DDLALQAAVQLAKLAydllleygVQAVEDvrqGKVTP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 239 AREAMAYAQF-LAGMAFNNASLGYVHAMAHqlgGFYN----LP------HG----VCNAVLLphvqVFNskvaaarlrdc 303
Cdd:cd08550 218 ALEDVVDAIIlLAGLVGSLGGGGCRTAAAH---AIHNgltkLPethgtlHGekvaFGLLVQL----ALE----------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 304 aaamgvnvtGKNDAEgaeacINAIRELAKKVDIPAGLRDLNVK--EEDFAVLATNALKDA-CGFTNPIQATHEEIV-AIY 379
Cdd:cd08550 280 ---------GRSEEE-----IEELIEFLRRLGLPVTLEDLGLEltEEELRKIAEYACDPPdMAHMLPFPVTPEMLAeAIL 345
|
..
gi 49176377 380 RA 381
Cdd:cd08550 346 AA 347
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
13-382 |
9.73e-07 |
|
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: 50.10 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 13 VIGADSLTDAMNMMADYGfTRTLIVTDNmlTKLGMAGD-VQKALEERNIfSVIYDGTQPNPTTENVAAGLKLLKENNCDS 91
Cdd:cd08170 5 VQGPGALDRLGEYLAPLG-KKALVIADP--FVLDLVGErLEESLEKAGL-EVVFEVFGGECSREEIERLAAIARANGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 92 VISLGGGSPHDCAKGIAlvaanggdirDYEGvdrsakpqLPMIAINTTAGTASEMTRFCII-TDEARHIKMAIVDKHvtP 170
Cdd:cd08170 81 VIGIGGGKTIDTAKAVA----------DYLG--------LPVVIVPTIASTDAPCSALSVIyTEDGEFDEYLFLPRN--P 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 171 LLSVNDSSLMIGMPKSLTAAtGM-DALTHAIEA--------------YVSIAATPITDAC-------ALKAVtmiaenlp 228
Cdd:cd08170 141 DLVLVDTEIIAKAPVRFLVA-GMgDALATYFEAracarsgapnmaggRPTLAALALAELCydtlleyGVAAK-------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 229 LAVEDGSNAKAREAMAYAQ-FLAGMAFNNASLGYVHAMAH---QLGGFYNLPHGvcnavllphvqvfnSKVaaarlrdca 304
Cdd:cd08170 212 AAVEAGVVTPALEAVIEANtLLSGLGFESGGLAAAHAIHNgltALPETHHLLHG--------------EKV--------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 305 aAMGVNV----TGKNDAEgaeacINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKdAC--GFT---NPIQATHEEI 375
Cdd:cd08170 269 -AFGTLVqlvlEGRPDEE-----IEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVAEA-ACapGETihnMPFPVTPEDV 341
|
....*..
gi 49176377 376 VAIYRAA 382
Cdd:cd08170 342 VDAILAA 348
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
5-264 |
1.69e-06 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 49.43 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 5 TFFIPSVNVIGADSLTDAMNMMADYGfTRTLIVTDNMLtkLGMAGD-VQKALEERNIfSVIYDGTQPNPTTENVAAGLKL 83
Cdd:PRK09423 4 IFISPSKYVQGKGALARLGEYLKPLG-KRALVIADEFV--LGIVGDrVEASLKEAGL-TVVFEVFNGECSDNEIDRLVAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 84 LKENNCDSVISLGGGSPHDCAKGIAlvaanggdirDYEGVdrsakpqlPMIAINTTAGTASEMTRFCII-TDEARHIKMA 162
Cdd:PRK09423 80 AEENGCDVVIGIGGGKTLDTAKAVA----------DYLGV--------PVVIVPTIASTDAPTSALSVIyTEEGEFERYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 163 IVDKHvtPLLSVNDSSLMIGMPKSLTAAtGM-DALTHAIEAYV--------------SIAATPITDAC-------ALKAV 220
Cdd:PRK09423 142 FLPKN--PDLVLVDTAIIAKAPARFLAA-GIgDALATWFEARAcsrsggttmaggkpTLAALALAELCyetlledGLKAK 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 49176377 221 tmiaenlpLAVEDGSNAKAREAMAYAQ-FLAGMAFNNASLGYVHA 264
Cdd:PRK09423 219 --------LAVEAKVVTPALENVIEANtLLSGLGFESGGLAAAHA 255
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
8-190 |
4.84e-05 |
|
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: 44.85 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 8 IPSVNVIGADSLTDAMNMMADYGFTRT-LIVTDNMLTKLgmAGD-VQKALEERNIFSVIYDgtqpNPTTENVAAG---LK 82
Cdd:cd08173 1 LPRNVVVGHGAINKIGEVLKKLLLGKRaLIITGPNTYKI--AGKrVEDLLESSGVEVVIVD----IATIEEAAEVekvKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 83 LLKENNCDSVISLGGGSPHDCAKGIAlvaanggdirdyegvdrsAKPQLPMIAINTTA---GTASEMTrfCIITDEARHI 159
Cdd:cd08173 75 LIKESKADFIIGVGGGKVIDVAKYAA------------------YKLNLPFISIPTSAshdGIASPFA--SIKGGDKPYS 134
|
170 180 190
....*....|....*....|....*....|.
gi 49176377 160 KMAivdkhVTPLLSVNDSSLMIGMPKSLTAA 190
Cdd:cd08173 135 IKA-----KAPIAIIADTEIISKAPKRLLAA 160
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
13-190 |
8.50e-05 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 44.11 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 13 VIGADSLTDAMNMMADYGFT-RTLIVTDNmlTKLGMAGD-VQKALEERNIFSVIydgTQPNPTTENVAAGLKLLKENNCD 90
Cdd:PRK00843 15 VVGHGVLDDIGDVCSDLKLTgRALIVTGP--TTKKIAGDrVEENLEDAGDVEVV---IVDEATMEEVEKVEEKAKDVNAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 91 SVISLGGGSPHDCAKgiaLVAANGGdirdyegvdrsakpqLPMIAINTTA---GTASemTRFCIITDEARHIKMAivdkh 167
Cdd:PRK00843 90 FLIGVGGGKVIDVAK---LAAYRLG---------------IPFISVPTAAshdGIAS--PRASIKGGGKPVSVKA----- 144
|
170 180
....*....|....*....|...
gi 49176377 168 VTPLLSVNDSSLMIGMPKSLTAA 190
Cdd:PRK00843 145 KPPLAVIADTEIIAKAPYRLLAA 167
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
9-140 |
3.37e-04 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 42.12 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176377 9 PSVNVIGADSLTDAMNMMADY--GFTRTLIVTDNMLTKLgMAGDVQKALEERNIFSVIYDGTqpNPTTENVAagLKLLKE 86
Cdd:cd08174 1 PLILKIEEGALEHLGKYLADRnqGFGKVAIVTGEGIDEL-LGEDILESLEEAGEIVTVEENT--DNSAEELA--EKAFSL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 49176377 87 NNCDSVISLGGGSPHDCAKGIALVAanggdirdyegvdrsakpQLPMIAINTTA 140
Cdd:cd08174 76 PKVDAIVGIGGGKVLDVAKYAAFLS------------------KLPFISVPTSL 111
|
|
| |
