|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
1-382 |
0e+00 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 787.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 1 MANRMILNETAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGL 80
Cdd:PRK10624 1 MANRMILNETAYFGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 81 GVFQNSGADYLIAIGGGSPQDTCKAIGIISNNPEFADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRR 160
Cdd:PRK10624 81 EVFKASGADYLIAIGGGSPQDTCKAIGIISNNPEFADVRSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 161 KFVCVDPHDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKDAGE 240
Cdd:PRK10624 161 KFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAGDKEAGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 241 EMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARN 320
Cdd:PRK10624 241 GMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVKVEGMSLEEARN 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749579 321 AAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELYHTAW 382
Cdd:PRK10624 321 AAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAFDDVCTGGNPREATLEDIVELYKKAW 382
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
2-378 |
0e+00 |
|
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase (pfam00465) proteins is generally found in apparent operons for the catabolism of rhamnose or fucose. Catabolism of both of these monosaccharides results in lactaldehyde which is reduced by this enzyme to 1,2 propanediol. This protein is alternatively known by the name 1,2 propanediol oxidoreductase. This enzyme is active under anaerobic conditions in E. coli while being inactivated by reactive oxygen species under aerobic conditions. Under aerobic conditions the lactaldehyde product of rhamnose and fucose catabolism is believed to be oxidized to lactate by a separate enzyme, lactaldehyde dehydrogenase. [Energy metabolism, Sugars]
Pssm-ID: 131686 [Multi-domain] Cd Length: 379 Bit Score: 694.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 2 ANRMILNETAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLG 81
Cdd:TIGR02638 1 SNRLILNETSYFGAGAIEDIVDEVKRRGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 82 VFQNSGADYLIAIGGGSPQDTCKAIGIISNNPEFADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRK 161
Cdd:TIGR02638 81 AFKASGADYLIAIGGGSPIDTAKAIGIISNNPEFADVRSLEGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEENKRK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 162 FVCVDPHDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAG--DKDAG 239
Cdd:TIGR02638 161 FVCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGgkDLEAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 240 EEMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEAR 319
Cdd:TIGR02638 241 EQMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAEFTGEKYREIAKAMGVKTEGMSDEEAR 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749579 320 NAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELY 378
Cdd:TIGR02638 321 DAAVEAVKTLSKRVGIPEGLSELGVKEEDIPALAEAALADVCTGGNPRETTVEEIEELY 379
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
3-379 |
0e+00 |
|
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: 648.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 3 NRMILNETAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGV 82
Cdd:cd08176 1 NRFVLNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 83 FQNSGADYLIAIGGGSPQDTCKAIGIISNNPeFADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKF 162
Cdd:cd08176 81 YKESGADGIIAVGGGSSIDTAKAIGIIVANP-GADVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKRKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 163 VCVDPHDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGD--KDAGE 240
Cdd:cd08176 160 VCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPnnVEARE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 241 EMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARN 320
Cdd:cd08176 240 NMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDEEAAE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749579 321 AAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELYH 379
Cdd:cd08176 320 AAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDALNDVCTPGNPREATKEDIIALYK 378
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
13-378 |
0e+00 |
|
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.
Pssm-ID: 341467 [Multi-domain] Cd Length: 377 Bit Score: 514.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd08188 11 FGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKENGCDFII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPefADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQ 172
Cdd:cd08188 91 SVGGGSAHDCAKAIGILATNG--GEIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVDWNVTPT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 173 VAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQYVAG 250
Cdd:cd08188 169 IAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVAngKDLEARENMAYAQFLAG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 251 MGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARNAAVEAVFALN 330
Cdd:cd08188 249 MAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGENTEGLSDEEAAEAAIEAIRKLS 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1134749579 331 RDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELY 378
Cdd:cd08188 329 RRVGIPSGLKELGVKEEDFPLLAENALKDACGPTNPRQATKEDVIAIY 376
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-382 |
7.19e-174 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 489.25 E-value: 7.19e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 1 MANRMILNETAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGL 80
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 81 GVFQNSGADYLIAIGGGSPQDTCKAIGIISNNPEfaDVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRR 160
Cdd:COG1454 81 AAAREFGADVVIALGGGSAIDAAKAIALLATNPG--DLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 161 KFVCVDPHDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDA 238
Cdd:COG1454 159 KKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVAdgDDLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 239 GEEMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVeGMSLEEA 318
Cdd:COG1454 239 REKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARALGLDV-GLSDEEA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134749579 319 RNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELYHTAW 382
Cdd:COG1454 318 AEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
13-378 |
1.40e-162 |
|
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: 460.38 E-value: 1.40e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd08551 6 FGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGADLVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPEfaDVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQ 172
Cdd:cd08551 86 AVGGGSVLDTAKAIAVLATNGG--SIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLLPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 173 VAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQYVAG 250
Cdd:cd08551 164 VAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVAdgSDLEAREAMLLASLLAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 251 MGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARNAAVEAVFALN 330
Cdd:cd08551 244 IAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELL 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1134749579 331 RDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGN-PREATLEDIVELY 378
Cdd:cd08551 324 RDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNnPRPLTEEDIREIY 372
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
13-382 |
4.76e-139 |
|
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: 400.75 E-value: 4.76e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd08194 6 IGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGCDFIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPEfaDVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQ 172
Cdd:cd08194 86 ALGGGSPIDTAKAIAVLATNGG--PIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPALLPA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 173 VAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQYVAG 250
Cdd:cd08194 164 VAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYAdgDDLEAREAMMLAALEAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 251 MGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARNAAVEAVFALN 330
Cdd:cd08194 244 IAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALERLC 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749579 331 RDVGIpPHLRDVGVRKED----IPALAQAALDDVCTGGNPREATLEDIVELYHTAW 382
Cdd:cd08194 324 ADLEI-PTLREYGIDEEEfeaaLDKMAEDALASGSPANNPRVPTKEEIIELYREAW 378
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
13-374 |
8.42e-138 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 396.97 E-value: 8.42e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYqKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:pfam00465 6 FGAGALAELGEELKRLGA-RALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGADVII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPEfaDVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQ 172
Cdd:pfam00465 85 AVGGGSVIDTAKAIALLLTNPG--DVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKLLPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 173 VAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQYVAG 250
Cdd:pfam00465 163 LAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVAdgEDLEARENMLLASTLAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 251 MGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKvegmSLEEARNAAVEAVFALN 330
Cdd:pfam00465 243 LAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGED----SDEEAAEEAIEALRELL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1134749579 331 RDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDI 374
Cdd:pfam00465 319 RELGLPTTLSELGVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-378 |
1.07e-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: 341489 [Multi-domain] Cd Length: 374 Bit Score: 376.88 E-value: 1.07e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd17814 9 FGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPefADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQ 172
Cdd:cd17814 89 AVGGGSPIDCAKGIGIVVSNG--GHILDYEGVDKVRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 173 VAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQYVAG 250
Cdd:cd17814 167 VSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVAdpDDLEAREKMMLASLQAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 251 MGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARNAAVEAVFALN 330
Cdd:cd17814 247 LAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLR 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1134749579 331 RDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELY 378
Cdd:cd17814 327 EDLGIPETLSELGVDEEDIPELAKRAMKDPCLVTNPRRPTREDIEEIY 374
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-382 |
1.77e-124 |
|
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: 363.78 E-value: 1.77e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd14865 11 SGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAGADGII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGI-ISNNPEfaDVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIP 171
Cdd:cd14865 91 AVGGGSVIDTAKGVNIlLSEGGD--DLDDYGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVSPFLLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 172 QVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQYVA 249
Cdd:cd14865 169 DVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKngKDLEARLALAIAATMA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 250 GMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVM--GVKVEGMSLEEARNAAVEAVF 327
Cdd:cd14865 249 GIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALayGVTPAGRRAEEAIEAAIDLVR 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1134749579 328 ALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELYHTAW 382
Cdd:cd14865 329 RLHELCGLPTRLRDVGVPEEQLEAIAELALNDGAILFNPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-357 |
4.43e-120 |
|
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: 352.54 E-value: 4.43e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 14 GRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLIA 93
Cdd:cd08189 11 GAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 94 IGGGSPQDTCKAIGIISNNPEfADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQV 173
Cdd:cd08189 91 IGGGSVIDCAKVIAARAANPK-KSVRKLKGLLKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPKLIPDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 174 AFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQYVAGM 251
Cdd:cd08189 170 AVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEdgSDLEARENMLLASYYAGL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 252 GFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARNAAVEAVFALNR 331
Cdd:cd08189 250 AFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGDSGESDSEKAEAFIAAIRELNR 329
|
330 340
....*....|....*....|....*.
gi 1134749579 332 DVGIPPHLrdVGVRKEDIPALAQAAL 357
Cdd:cd08189 330 RMGIPTTL--EELKEEDIPEIAKRAL 353
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
12-382 |
1.55e-117 |
|
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: 346.04 E-value: 1.55e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 12 WFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYL 91
Cdd:cd14861 7 RFGAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 92 IAIGGGSPQDTCKAIGIISNNP----EFADVRslEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDP 167
Cdd:cd14861 87 IALGGGSAIDAAKAIALMATHPgplwDYEDGE--GGPAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 168 HDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALG 245
Cdd:cd14861 165 KLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVAdgSDLEARGEMMMA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 246 QYVAGMGFSNvGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGmsleeaRNAAVEA 325
Cdd:cd14861 245 ALMGAVAFQK-GLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALGLGLGG------FDDFIAW 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749579 326 VFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELYHTAW 382
Cdd:cd14861 318 VEDLNERLGLPATLSELGVTEDDLDELAELALADPCHATNPRPVTAEDYRALLREAL 374
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-377 |
1.78e-113 |
|
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: 335.66 E-value: 1.78e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd14863 10 FGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPEfADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQ 172
Cdd:cd14863 90 GIGGGSVLDTAKAIAVLLTNPG-PIIDYALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVPD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 173 VAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQYVAG 250
Cdd:cd14863 169 LAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKdgDNLEARENMLLASNLAG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 251 MGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARNAAVEAVFALN 330
Cdd:cd14863 249 IAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREFM 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1134749579 331 RDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVEL 377
Cdd:cd14863 329 KELGIPSLFEDYGIDKEDLDKIAEAVLKDPFAMFNPRPITEEEVAEI 375
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
13-382 |
4.03e-109 |
|
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: 324.53 E-value: 4.03e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALtdevKRRGYQKALIVTDK-TLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYL 91
Cdd:cd08179 10 FGEGALEYL----KTLKGKRAFIVTGGgSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDWI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 92 IAIGGGSPQDTCKAIGIISNNPEFAdvrSLEGLSPTNKPSVP----ILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDP 167
Cdd:cd08179 86 IAIGGGSVIDAAKAMWVFYEYPELT---FEDALVPFPLPELRkkarFIAIPSTSGTGSEVTRASVITDTEKGIKYPLASF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 168 HDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKD--AGEEMALG 245
Cdd:cd08179 163 EITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKDleAREKMHNA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 246 QYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARvmgvkVEGMSLEEARNAAVEA 325
Cdd:cd08179 243 SCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAAL-----LIGLTDEELVEDLIEA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749579 326 VFALNRDVGIPPHLRDVGVRKED----IPALAQAALDDVCTGGNPREATLEDIVELYHTAW 382
Cdd:cd08179 318 IEELNKKLGIPLSFKEAGIDEDEffakLDEMAENAMNDACTGTNPRKPTVEEMKELLKAAY 378
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
14-381 |
5.21e-109 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 324.60 E-value: 5.21e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 14 GRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLIA 93
Cdd:PRK09860 15 GADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVIS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 94 IGGGSPQDTCKAIGIISNNPefADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQV 173
Cdd:PRK09860 95 LGGGSPHDCAKGIALVAANG--GDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 174 AFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSV--AGDKDAGEEMALGQYVAGM 251
Cdd:PRK09860 173 SVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVedGSNAKAREAMAYAQFLAGM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 252 GFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARNAAVEAVFALNR 331
Cdd:PRK09860 253 AFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAK 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1134749579 332 DVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELYHTA 381
Cdd:PRK09860 333 KVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAA 382
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
13-382 |
3.52e-102 |
|
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: 307.93 E-value: 3.52e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd08190 6 FGPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPefADVRSL------EGLSPTNkPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVD 166
Cdd:cd08190 86 AVGGGSVIDTAKAANLYATHP--GDFLDYvnapigKGKPVPG-PLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 167 PHDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITR------------------GAWALTDALHIKAIEIIAGAL 228
Cdd:cd08190 163 RYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARpynarprpanpderpayqGSNPISDVWAEKAIELIGKYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 229 RGSVA--GDKDAGEEMALGQYVAGMGFSNVGLGLVHGMAHPLG--------AFYN-----TPHGVANAILLPHVMRYNAD 293
Cdd:cd08190 243 RRAVNdgDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAglvkdyrpPGYPvdhphVPHGLSVALTAPAVFRFTAP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 294 FTGEKYRDIARVMGVKVEGMSLEEARNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDV-CTGGNPREATLE 372
Cdd:cd08190 323 ACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQrLLKLNPRPVTEE 402
|
410
....*....|
gi 1134749579 373 DIVELYHTAW 382
Cdd:cd08190 403 DLEEIFEDAL 412
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
13-377 |
6.80e-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: 6.80e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGyQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDgVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd08183 6 FGRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALFS-VSGEPTVETVDAAVALAREAGCDVVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPEfaDV-RSLEGLS---PTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPH 168
Cdd:cd08183 84 AIGGGSVIDAAKAIAALLTNEG--SVlDYLEVVGkgrPLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLRSPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 169 DIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQ 246
Cdd:cd08183 162 MLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEdgEDLEAREDMALAS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 247 YVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIA-----RVMGVKVEGmSLEEARNA 321
Cdd:cd08183 242 LLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRALREREPDSPalaryRELAGILTG-DPDAAAED 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1134749579 322 AVEAVFALNRDVGIPPhLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVEL 377
Cdd:cd08183 321 GVEWLEELCEELGIPR-LSEYGLTEEDFPEIVEKARGSSSMKGNPIELSDEELLEI 375
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
13-379 |
4.38e-100 |
|
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: 301.72 E-value: 4.38e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGyQKALIVTDK-TLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYL 91
Cdd:cd08185 9 FGAGKLNELGEEALRPG-KKALIVTGKgSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGCDFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 92 IAIGGGSPQDTCKAIGIISNNPEFAD--VRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHD 169
Cdd:cd08185 88 IGLGGGSSMDAAKAIAFMATNPGDIWdyIFGGTGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKKGIGHPAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 170 IPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQY 247
Cdd:cd08185 168 FPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKdgSDLEAREKMAWAST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 248 VAGMGFSNVGLGLVHGMAHPLGAFY-NTPHGVANAILLPHVMRYNADFTGEKYRDIARvmgVKVEGMSLEEARNAAVEAV 326
Cdd:cd08185 248 LAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVAR---AEASGLSDAKAAEDFIEAL 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749579 327 FALNRDVGIPPHLRDVGVRKEDIPALAQAALDDvcTGG----NPREATLEDIVELYH 379
Cdd:cd08185 325 RKLLKDIGLDDLLSDLGVTEEDIPWLAENAMET--MGGlfanNPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-378 |
2.83e-98 |
|
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: 296.83 E-value: 2.83e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRgyqkALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd14862 11 FGEDALSHLEQLSGKR----ALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPEfADVRSLEGLSPTNKPSVPIL-AIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIP 171
Cdd:cd14862 87 ALGGGSVMDAAKAAWVLYERPD-LDPEDISPLDLLGLRKKAKLiAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 172 QVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAG--DKDAGEEMALGQYVA 249
Cdd:cd14862 166 DVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDgdDLEAREKMHNAATIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 250 GMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARvmgVKVEGMSLEEARNAAVEAVFAL 329
Cdd:cd14862 246 GLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKL---LGIEARDEEEALKKLVEAIREL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1134749579 330 NRDVGIPPHLRDVGVRKED----IPALAQAALDDVCTGGNPREATLEDIVELY 378
Cdd:cd14862 323 YKEVGQPLSIKDLGISEEEfeekLDELVEYAMEDSCTITSPRPPSEEDLKKLF 375
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
13-382 |
1.27e-95 |
|
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: 290.18 E-value: 1.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd08193 9 CGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAGADGVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPEfaDVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVcVDPHDIPQ 172
Cdd:cd08193 89 GFGGGSSMDVAKLVALLAGSDQ--PLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIVTTGETEKKGV-VSPQLLPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 173 VAFIDADMMDGMPPALKAATGVDALTHAIEGYITR-GAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQYVA 249
Cdd:cd08193 166 VALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRhKKNPISDALAREALRLLGANLRRAVEdgSDLEAREAMLLGSMLA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 250 GMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARNAAVEAVFAL 329
Cdd:cd08193 246 GQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEEL 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1134749579 330 NRDVGIPPHLRDVGVRKEDIPALAQAA-LDDVCTGGNPREATLEDIVELYHTAW 382
Cdd:cd08193 326 VEASGLPTRLRDVGVTEEDLPMLAEDAmKQTRLLVNNPREVTEEDALAIYQAAL 379
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
13-378 |
4.05e-95 |
|
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: 289.47 E-value: 4.05e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRgyQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd08178 8 FEPGCLPYLLLELPGV--KRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFKPDVII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPEfadvRSLEGLSPT---NKPSV---PIL-------AIPTTAGTAAEVTINYVITDEEKR 159
Cdd:cd08178 86 ALGGGSAMDAAKIMWLFYEHPE----TKFEDLAQRfmdIRKRVykfPKLgkkaklvAIPTTSGTGSEVTPFAVITDDKTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 160 RKFVCVDPHDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKD-- 237
Cdd:cd08178 162 KKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGNDie 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 238 AGEEMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNAD---------------FTGEKYRDI 302
Cdd:cd08178 242 AREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATdpptkqaafpqykyyVAKERYAEI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 303 ARVMGVKveGMSLEEARNAAVEAVFALNRDVGIPPHLRDVGVRKED----IPALAQAALDDVCTGGNPREATLEDIVELY 378
Cdd:cd08178 322 ADLLGLG--GKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADflaaVDKLAEDAFDDQCTGANPRYPLISELKEIL 399
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
12-379 |
8.64e-93 |
|
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: 281.30 E-value: 8.64e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 12 WFGRGAVGALtdevKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAgLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYL 91
Cdd:cd08180 8 YSGEDSLERL----KELKGKRVFIVTDPFMVKSGMVDKVTDELDKS-NEVEIFSDVVPDPSIEVVAKGLAKILEFKPDTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 92 IAIGGGSPQDTCKAIGIISnnpefadvrsLEGLSPTNKPsvPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIP 171
Cdd:cd08180 83 IALGGGSAIDAAKAIIYFA----------LKQKGNIKKP--LFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSMLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 172 QVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQYVA 249
Cdd:cd08180 151 DIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRdgDDLEAREKMHNASCMA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 250 GMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYnadftgekyrdiarvmgvkvegmsleearnaAVEAVFAL 329
Cdd:cd08180 231 GIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF-------------------------------LIAAIRRL 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1134749579 330 NRDVGIPPHLRDVGVRKED----IPALAQAALDDVCTGGNPREATLEDIVELYH 379
Cdd:cd08180 280 NKKLGIPSTLKELGIDEEEfekaIDEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
13-382 |
1.12e-91 |
|
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: 280.65 E-value: 1.12e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGyQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd08191 9 FGPGARRALGRVAARLG-SRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDPDVVI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPefADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQ 172
Cdd:cd08191 88 GLGGGSNMDLAKVVALLLAHG--GDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 173 VAFIDADMMDGMPPALKAATGVDALTHAIEGYITR---------------GAWALTDALHIKAIEIIAGALRGSVA--GD 235
Cdd:cd08191 166 VAIVDPELTLTCPPGVTADSGIDALTHAIESYTARdfppfprldpdpvyvGKNPLTDLLALEAIRLIGRHLPRAVRdgDD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 236 KDAGEEMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSL 315
Cdd:cd08191 246 LEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVTTAGTSE 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749579 316 EEARnAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDV-CTGGNPREATLEDIVELYHTAW 382
Cdd:cd08191 326 EAAD-RAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTrLIANNPRPPTEEDLLRILRAAF 392
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
13-382 |
3.64e-91 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 292.09 E-value: 3.64e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVkrRGYQKALIVTDKTLVQCGVVAKVTDKMDA--AGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADY 90
Cdd:PRK13805 465 FERGSLPYLLDEL--DGKKRAFIVTDRFMVELGYVDKVTDVLKKreNGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDT 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 91 LIAIGGGSPQDTCKAIGIISNNPE---------FADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRK 161
Cdd:PRK13805 543 IIALGGGSPMDAAKIMWLFYEHPEtdfedlaqkFMDIRKRIYKFPKLGKKAKLVAIPTTSGTGSEVTPFAVITDDKTGVK 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 162 FVCVDPHDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSV---AGDKDA 238
Cdd:PRK13805 623 YPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYkngAKDPEA 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 239 GEEMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNAD--------------FTGEKYRDIAR 304
Cdd:PRK13805 703 REKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATdppkqaafpqyeypRADERYAEIAR 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 305 VMGVKveGMSLEEARNAAVEAVFALNRDVGIPPHLRDVGVRKED----IPALAQAALDDVCTGGNPREATLEDIVELYHT 380
Cdd:PRK13805 783 HLGLP--GSTTEEKVESLIKAIEELKAELGIPMSIKEAGVDEADflakLDELAELAFDDQCTGANPRYPLISELKEILLD 860
|
..
gi 1134749579 381 AW 382
Cdd:PRK13805 861 AY 862
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-378 |
2.01e-88 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 271.37 E-value: 2.01e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAwaIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd08196 11 FGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVA--VFSDVEPNPTVENVDKCARLARENGADFVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPEfaDVRS-LEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIP 171
Cdd:cd08196 89 AIGGGSVLDTAKAAACLAKTDG--SIEDyLEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLVSPGFYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 172 QVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAG--DKDAGEEMALGQYVA 249
Cdd:cd08196 167 DIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNpnDKEAREKMALASLLA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 250 GMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKvegmsleeARNAAVEAVFAL 329
Cdd:cd08196 247 GLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQLGFK--------DAEELADKIEEL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1134749579 330 NRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELY 378
Cdd:cd08196 319 KKRIGLRTRLSELGITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-357 |
1.30e-81 |
|
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: 250.74 E-value: 1.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 8 NETAWFGRGAVGALTdEVKRRGYQKALIVTDKTLVQcGVVAKVTDKMDAaGLAWAIYDGVVPNPTITVVKEGLGVFQNSG 87
Cdd:cd07766 1 PTRIVFGEGAIAKLG-EIKRRGFDRALVVSDEGVVK-GVGEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 88 ADYLIAIGGGSPQDTCKAIGIISNnpefadvrsleglsptnkPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCvdP 167
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAALLN------------------RGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVG--P 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 168 HDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEgyitrgawaltdalhikaieiiagalrgsvagdkdaGEEMALGQY 247
Cdd:cd07766 138 HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE------------------------------------LEKVVEAAT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 248 VAGMGFSN-VGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEkyrdiarvmgvkvegmsleeaRNAAVEAV 326
Cdd:cd07766 182 LAGMGLFEsPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPE---------------------PEAAIEAV 240
|
330 340 350
....*....|....*....|....*....|.
gi 1134749579 327 FALNRDVGIPPHLRDVGVRKEDIPALAQAAL 357
Cdd:cd07766 241 FKFLEDLGLPTHLADLGVSKEDIPKLAEKAL 271
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
14-381 |
5.58e-78 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 245.71 E-value: 5.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 14 GRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLIA 93
Cdd:PRK15454 33 GPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 94 IGGGSPQDTCKAIGIISNNPEfadvRSLEGLSPTN--KPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIP 171
Cdd:PRK15454 113 FGGGSVLDAAKAVALLVTNPD----STLAEMSETSvlQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASLMP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 172 QVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKD--AGEEMALGQYVA 249
Cdd:PRK15454 189 DVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDlaARESMLLASCMA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 250 GMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKvegmslEEARNAAVEAVFAL 329
Cdd:PRK15454 269 GMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRALRTK------KSDDRDAINAVSEL 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1134749579 330 NRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELYHTA 381
Cdd:PRK15454 343 IAEVGIGKRLGDVGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLYAAA 394
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
12-378 |
6.91e-77 |
|
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: 241.75 E-value: 6.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 12 WFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMdAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYL 91
Cdd:cd08182 5 IFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDAL-GGRIPVVVFSDFSPNPDLEDLERGIELFRESGPDVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 92 IAIGGGSPQDTCKAIGIISNNPEFADVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIP 171
Cdd:cd08182 84 IAVGGGSVIDTAKAIAALLGSPGENLLLLRTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPSLYP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 172 QVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVA--GDKDAGEEMALGQYVA 249
Cdd:cd08182 164 DAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLEnlPNLEAREAMAEASLLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 250 GMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNA-----DFTGEKYRDIARVMGvkveGMSLEEARnaavE 324
Cdd:cd08182 244 GLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAgaddeCDDDPRGREILLALG----ASDPAEAA----E 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1134749579 325 AVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELY 378
Cdd:cd08182 316 RLRALLESLGLPTRLSEYGVTAEDLEALAASVNTPERLKNNPVRLSEEDLLRLL 369
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
13-378 |
4.37e-74 |
|
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: 234.40 E-value: 4.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGyQKALIVTDKTLVQ-CGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYL 91
Cdd:cd08181 9 FGKNCVEKHADELAALG-KKALIVTGKHSAKkNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELARKEGADFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 92 IAIGGGSPQDTCKAIGIISNNPEFADVRSLEGLsptNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIP 171
Cdd:cd08181 88 IGIGGGSPLDAAKAIALLAANKDGDEDLFQNGK---YNPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFGNPLIFP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 172 QVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAG---ALRGSVAGDKDAgEEMALGQYV 248
Cdd:cd08181 165 KLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGEclpNLLGDELDEEDR-EKLMYASTL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 249 AGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKvegmSLEEarnaaveavFA 328
Cdd:cd08181 244 AGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLGFG----SIEE---------FQ 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1134749579 329 --LNRDVGIPPHlrdvgVRKEDIPALAQAALDDVCTGGNPREATLEDIVELY 378
Cdd:cd08181 311 kfLNRLLGKKEE-----LSEEELEKYADEAMKAKNKKNTPGNVTKEDILRIY 357
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
13-378 |
8.54e-71 |
|
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: 226.55 E-value: 8.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGyQKALIVTDKT-LVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYL 91
Cdd:cd08187 12 FGKGAIEELGEEIKKYG-KKVLLVYGGGsIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVDFI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 92 IAIGGGSPQDTCKAIGIISNNPEfaDVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIP 171
Cdd:cd08187 91 LAVGGGSVIDAAKAIAAGAKYDG--DVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLRP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 172 QVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWA-LTDalhikaiEIIAGALRgSV--AGDK--------DAGE 240
Cdd:cd08187 169 KFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDApLQD-------RLAEGLLR-TVieNGPKalkdpddyEARA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 241 EMALGQYVAGMGFSNVGLGL---VHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIA-RVMGVKVEGmSLE 316
Cdd:cd08187 241 NLMWAATLALNGLLGAGRGGdwaTHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFArRVFGIDPGG-DDE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134749579 317 EARNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVELY 378
Cdd:cd08187 320 ETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGFKPLTREDIEEIL 381
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-382 |
1.50e-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: 222.95 E-value: 1.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGyQKALIVTDKTLVQCGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd14864 9 FGADSLERIGEEVKEYG-SRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAGADGII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIGIISNNPEFADvRSLEGLSPTNKPsVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQ 172
Cdd:cd14864 88 AVGGGKVLDTAKAVAILANNDGGAY-DFLEGAKPKKKP-LPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKAQPGLPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 173 VAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKDAGEE--MALGQYVAG 250
Cdd:cd14864 166 AVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEelLAQAGCLAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 251 MGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEARNAAVEAVFALN 330
Cdd:cd14864 246 LAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLI 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1134749579 331 RDVGIPPHLRDVGVrKEDIPALAQAALDDVCTGGNPREATLEDIVELYHTAW 382
Cdd:cd14864 326 AQLNLPTRLKDLDL-ASSLEQLAAIAEDAPKLNGLPRSMSSDDIFDILKAAF 376
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-382 |
4.11e-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: 341488 [Multi-domain] Cd Length: 384 Bit Score: 222.11 E-value: 4.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQKALIVTDKTlvqcgvVAKVTDKMD----AAG--LAwAIYDGVVPNPTITVVKEGLGVFQNS 86
Cdd:cd14866 10 SGRGALARLGRELDRLGARRALVVCGSS------VGANPDLMDpvraALGdrLA-GVFDGVRPHSPLETVEAAAEALREA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 87 GADYLIAIGGGSPQDTCKAIGIIsnnpeFADVRSLEGL-----------SPT-NKPSVPILAIPTTAGTAaEVTINYVIT 154
Cdd:cd14866 83 DADAVVAVGGGSAIVTARAASIL-----LAEDRDVRELctrraedglmvSPRlDAPKLPIFVVPTTPTTA-DVKAGSAVT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 155 DEEKRRKFVCVDPHDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAG 234
Cdd:cd14866 157 DPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLADD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 235 -DKDAGEEMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGM 313
Cdd:cd14866 237 dDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGVADAGD 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 314 slEEARNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPR-EATLEDIVELYHTAW 382
Cdd:cd14866 317 --EASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNNPRpVPTAEELEALLEAAW 384
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
13-382 |
1.47e-61 |
|
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: 201.19 E-value: 1.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQKALIVTdkTLVQCGVVAKVTDkmDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYLI 92
Cdd:cd08177 6 FGAGTLAELAEELERLGARRALVLS--TPRQRALAERVAA--LLGDRVAGVFDGAVMHVPVEVAERALAAAREAGADGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 93 AIGGGSPQDTCKAIgiisnnpefadvrSLE-GLsptnkpsvPILAIPTT-AGtaAEVTINYVITDEEkrRKFVCVDPHDI 170
Cdd:cd08177 82 AIGGGSAIGLAKAI-------------ALRtGL--------PIVAVPTTyAG--SEMTPIWGETEDG--VKTTGRDPRVL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 171 PQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAG--DKDAGEEMALGQYV 248
Cdd:cd08177 137 PRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADpsDLEARSDALYGAWL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 249 AGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVkvegmsleearNAAVEAVFA 328
Cdd:cd08177 217 AGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGG-----------GDAAGGLYD 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1134749579 329 LNRDVGIPPHLRDVGVRKEDIPALAQAALDDVctGGNPREATLEDIVELYHTAW 382
Cdd:cd08177 286 LARRLGAPTSLRDLGMPEDDIDRAADLALANP--YPNPRPVERDALRALLERAW 337
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
13-381 |
1.79e-60 |
|
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: 199.78 E-value: 1.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQKALIVTDKTL-VQCGVVAKVTDkmdAAGLAWA-IYDGVVPNPTITVVKEGLGVFQNSGADY 90
Cdd:cd08192 6 YGPGAVEALLHELATLGASRVFIVTSKSLaTKTDVIKRLEE---ALGDRHVgVFSGVRQHTPREDVLEAARAVREAGADL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 91 LIAIGGGSPQDTCKAIGI-ISNN-PEFADVRSLEGLSPTNK----PSVPILAIPTTAgTAAEVTINYVITDEEKRRKFVC 164
Cdd:cd08192 83 LVSLGGGSPIDAAKAVALaLAEDvTDVDQLDALEDGKRIDPnvtgPTLPHIAIPTTL-SGAEFTAGAGATDDDTGHKQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 165 VDPHDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAG--DKDAGEEM 242
Cdd:cd08192 162 AHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADpeDLEARLKC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 243 ALGQYVAGMGF-SNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSLEEArnA 321
Cdd:cd08192 242 QLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALGLVTGGLGREAA--D 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134749579 322 AVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPR-EATLEDIVELYHTA 381
Cdd:cd08192 320 AADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRpITDKDDVLEILESA 380
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
13-381 |
3.87e-51 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 175.26 E-value: 3.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGyQKALIVTDKTLVQC-GVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADYL 91
Cdd:COG1979 14 FGKGQIAKLGEEIPKYG-KKVLLVYGGGSIKKnGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 92 IAIGGGSPQDTCKAIGI-ISNNPEFADVrsLEGLSPTNKPsVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDI 170
Cdd:COG1979 93 LAVGGGSVIDGAKAIAAgAKYDGDPWDI--LTGKAPVEKA-LPLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 171 PQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWA-LTDalhikaiEIIAGALR-----GSVA----GDKDAGE 240
Cdd:COG1979 170 PKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDApLQD-------RFAEGLLRtlieeGPKAlkdpEDYDARA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 241 EMalgQYVAGMGFSN-VGLGL-----VHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIA-RVMGvkVEGM 313
Cdd:COG1979 243 NL---MWAATLALNGlIGAGVpqdwaTHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAeRVWG--ITEG 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134749579 314 SLEEARNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTG-GNPREATLEDIVELYHTA 381
Cdd:COG1979 318 DDEERALEGIEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMTAlGEFKDLTPEDVREILELA 386
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-378 |
1.92e-48 |
|
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: 168.21 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 10 TAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQ-CGVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGA 88
Cdd:cd08186 3 TLYFGVGAIAKIKDILKDLGIDKVIIVTGRSSYKkSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 89 DYLIAIGGGSPQDTCKAIGIISNNPEFAdVRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPH 168
Cdd:cd08186 83 DAVIAIGGGSPIDTAKSVAVLLAYGGKT-ARDLYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 169 DIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKDAGEE--MALGQ 246
Cdd:cd08186 162 IYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARywLLYAS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 247 YVAGMGFSNVGLGLVHGMAHPLGAFY-NTPHGVANAILLPHVMRYNADFTGEKYRDIARVMGVKVEGMSlEEARNAAvEA 325
Cdd:cd08186 242 MIAGIAIDNGLLHLTHALEHPLSGLKpELPHGLGLALLGPAVVKYIYKAVPETLADILRPIVPGLKGTP-DEAEKAA-RG 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1134749579 326 VFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGG----NPREATLEDIVELY 378
Cdd:cd08186 320 VEEFLFSVGFTEKLSDYGFTEDDVDRLVELAFTTPSLDLllslAPVEVTEEVVREIY 376
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
71-378 |
3.50e-28 |
|
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: 113.46 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 71 PTITVVKEGLGVFQNSGADYLIAIGGGSPQDTCKAIGIISNNPefadVRSL-EGLSPTNKpSVPILAIPTTAGTAAEVTi 149
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLALKGISP----VLDLfDGKIPLIK-EKELIIVPTTCGTGSEVT- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 150 NYVITdEEKRR--KFVCVDPHDIPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGA 227
Cdd:cd14860 136 NISIV-ELTSLgtKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 228 LRGSVAGDKDAGEEMaLGQYV-----AGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRY----NAD-FTGE 297
Cdd:cd14860 215 YQEIAEKGEEARFPL-LGDFLiasnyAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNyqekNPDgEIKK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 298 KYRDIARVMGVKVEG--MSLEEarnaaveavfALNRDVGIPPhLRDVGVRKEDIPALAqaalDDVCTG------GNPREA 369
Cdd:cd14860 294 LNEFLAKILGCDEEDvyDELEE----------LLNKILPKKP-LHEYGMKEEEIDEFA----DSVMENqqrllaNNYVPL 358
|
....*....
gi 1134749579 370 TLEDIVELY 378
Cdd:cd14860 359 DREDVAEIY 367
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
13-382 |
4.67e-20 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 90.62 E-value: 4.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRrgyQKALIVT--DKTLVQCGVVAKVTDKMdaAGLAWAIYDGVVPNPTITVVKEGLGVFQNSGADY 90
Cdd:PRK15138 14 FGKGAIAGLREQIPA---DARVLITygGGSVKKTGVLDQVLDAL--KGMDVLEFGGIEPNPTYETLMKAVKLVREEKITF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 91 LIAIGGGSPQDTCKAIGIISNNPEFADV-RSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHD 169
Cdd:PRK15138 89 LLAVGGGSVLDGTKFIAAAANYPENIDPwHILETGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGDKQAFHSPHV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 170 IPQVAFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWA-----LTDALHIKAIEIIAGALRGSVAGDKDAGEEMAL 244
Cdd:PRK15138 169 QPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAkiqdrFAEGILLTLIEEGPKALKEPENYDVRANVMWAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 245 GQYVAGMgfsnVGLGL-----VHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYRDIA-RVMGVKvEGmSLEEA 318
Cdd:PRK15138 249 TQALNGL----IGAGVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAeRVWNIT-EG-SDDER 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749579 319 RNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTG-GNPREATLEDIVELYHTAW 382
Cdd:PRK15138 323 IDAAIAATRNFFEQMGVPTRLSDYGLDGSSIPALLKKLEEHGMTQlGEHHDITLDVSRRIYEAAR 387
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
91-306 |
9.84e-20 |
|
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: 89.25 E-value: 9.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 91 LIAIGGGSPQDTCKAIGIISNNPEFAdvRSLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKrrKFVCVDPHDI 170
Cdd:cd08184 86 VVGIGGGSTMDIAKAVSNMLTNPGSA--ADYQGWDLVKNPGIYKIGVPTLSGTGAEASRTAVLTGPEK--KLGINSDYTV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 171 PQVAFIDADMMDGMPPALKAATGVDALTHAIEgyITRGAW--ALTDALHIKAIEIIAGALRGSVAGDKDAGEEMALGQYV 248
Cdd:cd08184 162 FDQVILDPELIATVPRDQYFYTGMDCYIHCVE--SLNGTYrnAFGDAYAEKALELCRDVFLSDDMMSPENREKLMVASYL 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749579 249 AGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAIllphVMRYNADFTGEKYRDIARVM 306
Cdd:cd08184 240 GGSSIANSQVGVCHALSYGLSVVLGTHHGVANCI----VFNVLEEFYPEGVKEFREML 293
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
14-381 |
2.16e-12 |
|
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: 67.50 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 14 GRGAVGALTDEVKRRGyQKALIVTDKTLVQcGVVAKVTDKMDAAGLA--WAIYDGvvpNPTITVVKEGLGVFQNSGADYL 91
Cdd:COG0371 12 GEGALDELGEYLADLG-KRALIITGPTALK-AAGDRLEESLEDAGIEveVEVFGG---ECSEEEIERLAEEAKEQGADVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 92 IAIGGGSPQDTCKAIGIISNnpefadvrsleglsptnkpsVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHdIP 171
Cdd:COG0371 87 IGVGGGKALDTAKAVAYRLG--------------------LPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAK-NP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 172 QVAFIDADMMDGMPPALKAAtGV-DAL-------------THAIEGYITRGAWAL----TDALHIKAIEIIAGALRGSVA 233
Cdd:COG0371 146 DLVLVDTDIIAKAPVRLLAA-GIgDALakwyeardwslahRDLAGEYYTEAAVALarlcAETLLEYGEAAIKAVEAGVVT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 234 gdkDAGEEM-----ALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTP---HG--VANAILlphVMrynadftgekyrdia 303
Cdd:COG0371 225 ---PALERVveanlLLSGLAMGIGSSRPGSGAAHAIHNGLTALPETHhalHGekVAFGTL---VQ--------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 304 rvmgvkvegMSLEEaRNAAVEAVFALNRDVGIPPHLRDVGVRK---EDIPALAQAALDDVCT-GGNPREATLEDIVELYH 379
Cdd:COG0371 284 ---------LVLEG-RPEEIEELLDFLRSVGLPTTLADLGLDDeteEELLTVAEAARPERYTiLNLPFEVTPEAVEAAIL 353
|
..
gi 1134749579 380 TA 381
Cdd:COG0371 354 AT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
14-376 |
3.49e-12 |
|
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: 66.79 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 14 GRGAVGALTDEVKRRGyQKALIVTDKTLVQCgVVAKVTDKMDAAGLAW--AIYDGVvpnPTITVVKEGLGVFQNSGADYL 91
Cdd:cd08550 7 EPGILAKAGEYIAPLG-KKALIIGGKTALEA-VGEKLEKSLEEAGIDYevEVFGGE---CTEENIERLAEKAKEEGADVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 92 IAIGGGSPQDTCKAIGiisnnpefadvrsleglsptNKPSVPILAIPTTAGTAAEVTINYVITDEEKRrkFVCVDPHD-I 170
Cdd:cd08550 82 IGIGGGKVLDTAKAVA--------------------DRLGLPVVTVPTIAATCAAWSALSVLYDEEGE--FLGYSLLKrS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 171 PQVAFIDADMMDGMPPALKAATGVDAL----------THAIEGYITRGAWAL----TDALHIKAIEIIAGALRGSVAgdk 236
Cdd:cd08550 140 PDLVLVDTDIIAAAPVRYLAAGIGDTLakwyearpssRGGPDDLALQAAVQLaklaYDLLLEYGVQAVEDVRQGKVT--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 237 DAGEEMAlgqyvagmgFSNVGL-GLVHGMAhplGAFYNTphGVANAIllphvmrYNAdFT----------GEKyrdiarV 305
Cdd:cd08550 217 PALEDVV---------DAIILLaGLVGSLG---GGGCRT--AAAHAI-------HNG-LTklpethgtlhGEK------V 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749579 306 -MGVKVEgMSLEEARNAAVEAVFALNRDVGIPPHLRDVGV--RKEDIPALAQAALDDV-CTGGNPREATLEDIVE 376
Cdd:cd08550 269 aFGLLVQ-LALEGRSEEEIEELIEFLRRLGLPVTLEDLGLelTEEELRKIAEYACDPPdMAHMLPFPVTPEMLAE 342
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
14-376 |
4.79e-10 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 60.50 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 14 GRGAVGALTDEVKRRGyQKALIVTDKTlVQCGVVAKVTDKMDAAGLAW--AIYDGVVpnpTITVVKEGLGVFQNSGADYL 91
Cdd:cd08170 7 GPGALDRLGEYLAPLG-KKALVIADPF-VLDLVGERLEESLEKAGLEVvfEVFGGEC---SREEIERLAAIARANGADVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 92 IAIGGGSPQDTCKAIGIISNnpefadvrsleglsptnkpsVPILAIPTTAGTAAEVTINYVITDEEKRrkFVCVDPHDI- 170
Cdd:cd08170 82 IGIGGGKTIDTAKAVADYLG--------------------LPVVIVPTIASTDAPCSALSVIYTEDGE--FDEYLFLPRn 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 171 PQVAFIDADMMDGMPPALKAAtGV-DALTHAIE--------------GYITRGAWALTDALHikaiEIIagaLRGSVAGd 235
Cdd:cd08170 140 PDLVLVDTEIIAKAPVRFLVA-GMgDALATYFEaracarsgapnmagGRPTLAALALAELCY----DTL---LEYGVAA- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 236 KDAGEEMALGQ----------YVAGMGFSNVGLGLVHGMAHPLGAFYNTPHgvanailLPHvmrynadftGEKyrdIArv 305
Cdd:cd08170 211 KAAVEAGVVTPaleavieantLLSGLGFESGGLAAAHAIHNGLTALPETHH-------LLH---------GEK---VA-- 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134749579 306 MGVKVEgMSLEEARNAAVEAVFALNRDVGIPPHLRDVG---VRKEDIPALAQAALDDVCTGGN-PREATLEDIVE 376
Cdd:cd08170 270 FGTLVQ-LVLEGRPDEEIEEVIRFCRSVGLPVTLADLGledVTDEELRKVAEAACAPGETIHNmPFPVTPEDVVD 343
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
16-176 |
8.86e-06 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 47.13 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 16 GAVGALTDEVKRRGYQKALIVTDKTLVQcgVVAKVTDKMDAAGLAWAIYDGVVPNPTITVVKEglgVFQNSGADYLIAIG 95
Cdd:cd08172 9 GALKELPELLSEFGIKRPLIIHGEKSWQ--AAKPYLPKLFEIEYPVLRYDGECSYEEIDRLAE---EAKEHQADVIIGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 96 GGSPQDTCKAIGiisnnpefadvrsleglsptNKPSVPILAIPTTAGTAAEVTINYVITDEEKRrkFVCVDPHdiPQVAF 175
Cdd:cd08172 84 GGKVLDTAKAVA--------------------DKLNIPLILIPTLASNCAAWTPLSVIYDEDGE--FIGYDYF--PRSAY 139
|
.
gi 1134749579 176 I 176
Cdd:cd08172 140 L 140
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
13-141 |
1.25e-04 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 43.70 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 13 FGRGAVGALTDEVKRRGYQK-ALIVTDKTLvqCGVVAK-VTDKMDAAGLAWAIYDGVVPNPTITVVKEGlGVFQNSGADY 90
Cdd:cd08173 7 VGHGAINKIGEVLKKLLLGKrALIITGPNT--YKIAGKrVEDLLESSGVEVVIVDIATIEEAAEVEKVK-KLIKESKADF 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1134749579 91 LIAIGGGSPQDTCKAIgiisnnpefadvrsleglspTNKPSVPILAIPTTA 141
Cdd:cd08173 84 IIGVGGGKVIDVAKYA--------------------AYKLNLPFISIPTSA 114
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
14-193 |
9.57e-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: 40.97 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 14 GRGAVGALTDEVKRR--GYQKALIVTDKTLVQcGVVAKVTDKMDAAGLAWAIYDGVVpnptITVVKEGLGVFQNSGADYL 91
Cdd:cd08174 7 EEGALEHLGKYLADRnqGFGKVAIVTGEGIDE-LLGEDILESLEEAGEIVTVEENTD----NSAEELAEKAFSLPKVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 92 IAIGGGSPQDTCKAIGIISNnpefadvrsleglsptnkpsVPILAIPTTA---GTAAEVTinyVITDEEKRRKFVCVdph 168
Cdd:cd08174 82 VGIGGGKVLDVAKYAAFLSK--------------------LPFISVPTSLsndGIASPVA---VLKVDGKRKSLGAK--- 135
|
170 180
....*....|....*....|....*.
gi 1134749579 169 dIPQVAFIDADMMDGMPPAL-KAATG 193
Cdd:cd08174 136 -MPYGVIVDLDVIKSAPRRLiLAGIG 160
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
88-376 |
2.05e-03 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341450 Cd Length: 345 Bit Score: 39.81 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 88 ADYLIAIGGGSPQDTCKAIGIISNNPEFadvrsleglsptnkpsvpilAIPTTAGTAAEVT-INYVITDEEKRRKFvcVD 166
Cdd:cd08171 79 ADMIFAVGGGKAIDTVKVLADRLNKPVF--------------------TFPTIASNCAAVTaVSVMYNPDGSFKEY--YF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 167 PHDIPQVAFIDADMMDGMP-PALKAATGvDALTHAIEGYI-TRGA-WALTDALHIKA--------IEIIAGALRGSVAGD 235
Cdd:cd08171 137 LKRPPVHTFIDTEIIAEAPeKYLWAGIG-DTLAKYYEVEFsARGDeLDHTNALGVAIskmcseplLKYGVQALEDCRANK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 236 -KDAGEEMALGQYVAgmgfsnvgLGLVHGMAHPlgaFYNTphGVANAI-----LLPHVmrynadftGEKYRDIARVM-GV 308
Cdd:cd08171 216 vSDALEQVVLDIIVT--------TGLVSNLVEP---DYNS--SLAHALyygltTLPQI--------EEEHLHGEVVSyGV 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134749579 309 KVegMSLEEARNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDVCTGGNPREATLEDIVE 376
Cdd:cd08171 275 LV--LLTVDGQFEELEKVYAFNKSIGLPTCLADLGLTVEDLEKVLDKALKTKDLRHSPYPITKEMFEE 340
|
|
| PncC_domain |
TIGR00199 |
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is ... |
10-123 |
2.14e-03 |
|
amidohydrolase, PncC family; CinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species. Several bacterial species have a protein consisting largely of the C-terminal domain of CinA but lacking the N-terminal domain, including nicotinamide mononucleotide (NMN) deamidase (3.5.1.42) proteins PncC in Shewanella oneidensis and ygaD in E. coli. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129303 [Multi-domain] Cd Length: 146 Bit Score: 38.15 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 10 TAWFGRGAVgALTDEVKrrgyQKALIVTDKTLVQCGVVAKVTdkmdAAGLAwaiydgvvpnptitvvkegLGVFQNSGAD 89
Cdd:TIGR00199 34 SKYFGGGVV-CYTNQVK----INLLGVSQETLARFGAVSEEC----AAEMA-------------------LGVKERFGAD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1134749579 90 YLIAIGG---------GSPQDTCKAIGIISNNPEFADVRSLEG 123
Cdd:TIGR00199 86 VGIAISGiagpdggeeEKPGGTVWFIWIIAKGQAYTAEMHFAG 128
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
14-375 |
2.59e-03 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 39.41 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 14 GRGAVGALTDEVKRRGyQKALIVTDKTLVQCgVVAKVTDKMDAAGLAwAIYDGVVPNPTITVVKEGLGVFQNSGADYLIA 93
Cdd:PRK09423 14 GKGALARLGEYLKPLG-KRALVIADEFVLGI-VGDRVEASLKEAGLT-VVFEVFNGECSDNEIDRLVAIAEENGCDVVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 94 IGGGSPQDTCKAIGIISNnpefadvrsleglsptnkpsVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDiPQV 173
Cdd:PRK09423 91 IGGGKTLDTAKAVADYLG--------------------VPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKN-PDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 174 AFIDADMMDGMPPALKAATGVDALTHAIEGYITRGAWALTdalhikaieiIAGAlRGSVAGdkdageeMALGQ------- 246
Cdd:PRK09423 150 VLVDTAIIAKAPARFLAAGIGDALATWFEARACSRSGGTT----------MAGG-KPTLAA-------LALAElcyetll 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 247 ---------------------------YVAGMGFSNVGLGLVHGMAHPLGAFYNTPHgvanailLPHvmrynadftGEKY 299
Cdd:PRK09423 212 edglkaklaveakvvtpalenvieantLLSGLGFESGGLAAAHAIHNGLTALEDTHH-------LTH---------GEKV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134749579 300 rdiarVMGVKVEgMSLEEARNAAVEAVFALNRDVGIPPHLRDVGVR---KEDIPALAQAALDDVCTGGN-PREATLEDIV 375
Cdd:PRK09423 276 -----AFGTLTQ-LVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKedsDEELRKVAEAACAEGETIHNmPFKVTPEDVA 349
|
|
| |
