|
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: 753.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 1 MVNRIVLNETSYHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGV 80
Cdd:PRK10624 1 MANRMILNETAYFGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 81 EAYKKSGADYIIAVGGGSSMDTAKAIGIIINNKEFEDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNR 160
Cdd:PRK10624 81 EVFKASGADYLIAIGGGSPQDTCKAIGIISNNPEFADVRSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 161 KFVCVDTHDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENTPEGRE 240
Cdd:PRK10624 161 KFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAGDKEAGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 241 GMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVEnTENMTVEEYR 320
Cdd:PRK10624 241 GMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVK-VEGMSLEEAR 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 373228229 321 KAAVDAVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITLYESLM 382
Cdd:PRK10624 320 NAAVEAVKALNRDVGIPPHLRDVgVKEEDIPALAQAAFDDVCTGGNPREATLEDIVELYKKAW 382
|
|
| 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: 659.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 3 NRIVLNETSYHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEA 82
Cdd:cd08176 1 NRFVLNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 83 YKKSGADYIIAVGGGSSMDTAKAIGIIINNkEFEDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKF 162
Cdd:cd08176 81 YKESGADGIIAVGGGSSIDTAKAIGIIVAN-PGADVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKRKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 163 VCVDTHDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENT--PEGRE 240
Cdd:cd08176 160 VCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPnnVEARE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 241 GMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVENTeNMTVEEYR 320
Cdd:cd08176 240 NMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTT-GMSDEEAA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 321 KAAVDAVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITLYE 379
Cdd:cd08176 319 EAAVDAVKKLSKDVGIPQKLSELgVKEEDIEALAEDALNDVCTPGNPREATKEDIIALYK 378
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
3-378 |
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: 609.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 3 NRIVLNETSYHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEA 82
Cdd:TIGR02638 2 NRLILNETSYFGAGAIEDIVDEVKRRGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 83 YKKSGADYIIAVGGGSSMDTAKAIGIIINNKEFEDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKF 162
Cdd:TIGR02638 82 FKASGADYLIAIGGGSPIDTAKAIGIISNNPEFADVRSLEGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEENKRKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 163 VCVDTHDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENT--PEGRE 240
Cdd:TIGR02638 162 VCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGGkdLEARE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 241 GMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVEnTENMTVEEYR 320
Cdd:TIGR02638 242 QMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAEFTGEKYREIAKAMGVK-TEGMSDEEAR 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 373228229 321 KAAVDAVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITLY 378
Cdd:TIGR02638 321 DAAVEAVKTLSKRVGIPEGLSELgVKEEDIPALAEAALADVCTGGNPRETTVEEIEELY 379
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
10-379 |
7.84e-175 |
|
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: 491.64 E-value: 7.84e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 10 TSYHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGAD 89
Cdd:cd08188 8 VNLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKENGCD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 90 YIIAVGGGSSMDTAKAIGIIINNKEfeDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHD 169
Cdd:cd08188 88 FIISVGGGSAHDCAKAIGILATNGG--EIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVDWNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 170 IPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENTP--EGREGMALGQY 247
Cdd:cd08188 166 TPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKdlEARENMAYAQF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 248 IAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGvENTENMTVEEYRKAAVDAV 327
Cdd:cd08188 246 LAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALG-ENTEGLSDEEAAEAAIEAI 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 373228229 328 KKLSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITLYE 379
Cdd:cd08188 325 RKLSRRVGIPSGLKELgVKEEDFPLLAENALKDACGPTNPRQATKEDVIAIYR 377
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-382 |
5.03e-173 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 486.93 E-value: 5.03e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 1 MVNRIVLNETSYHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGV 80
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 81 EAYKKSGADYIIAVGGGSSMDTAKAIGIIINNKEfeDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNR 160
Cdd:COG1454 81 AAAREFGADVVIALGGGSAIDAAKAIALLATNPG--DLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 161 KFVCVDTHDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVEN--TPEG 238
Cdd:COG1454 159 KKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADgdDLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 239 REGMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVEntENMTVEE 318
Cdd:COG1454 239 REKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARALGLD--VGLSDEE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 373228229 319 YRKAAVDAVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITLYESLM 382
Cdd:COG1454 317 AAEALIEAIRELLRDLGIPTRLSELgVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
12-378 |
2.37e-158 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 449.59 E-value: 2.37e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYI 91
Cdd:cd08551 5 VFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGADLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 92 IAVGGGSSMDTAKAIGIIINNKEfeDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIP 171
Cdd:cd08551 85 IAVGGGSVLDTAKAIAVLATNGG--SIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 172 VVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENT--PEGREGMALGQYIA 249
Cdd:cd08551 163 DVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGsdLEAREAMLLASLLA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 250 GMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGvENTENMTVEEYRKAAVDAVKK 329
Cdd:cd08551 243 GIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALG-EDVEGLSDEEAAEAAVEAVRE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 373228229 330 LSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGN-PMETSVEDIITLY 378
Cdd:cd08551 322 LLRDLGIPTSLSELgVTEEDIPELAEDAMKSGRLLSNnPRPLTEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
12-374 |
6.20e-141 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 405.06 E-value: 6.20e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIVTEVKGRGfKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYI 91
Cdd:pfam00465 5 VFGAGALAELGEELKRLG-ARALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGADVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 92 IAVGGGSSMDTAKAIGIIINNKEfeDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIP 171
Cdd:pfam00465 84 IAVGGGSVIDTAKAIALLLTNPG--DVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKLLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 172 VVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVEN--TPEGREGMALGQYIA 249
Cdd:pfam00465 162 DLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADgeDLEARENMLLASTLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 250 GMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVEntenmTVEEYRKAAVDAVKK 329
Cdd:pfam00465 242 GLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGED-----SDEEAAEEAIEALRE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 373228229 330 LSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDI 374
Cdd:pfam00465 317 LLRELGLPTTLSELgVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-378 |
2.60e-127 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 370.72 E-value: 2.60e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYIIA 93
Cdd:cd17814 10 GVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 94 VGGGSSMDTAKAIGIIINNKEfeDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIPVV 173
Cdd:cd17814 90 VGGGSPIDCAKGIGIVVSNGG--HILDYEGVDKVRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 174 AIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVEN--TPEGREGMALGQYIAGM 251
Cdd:cd17814 168 SLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADpdDLEAREKMMLASLQAGL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 252 GFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVEnTENMTVEEYRKAAVDAVKKLS 331
Cdd:cd17814 248 AFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLD-VDGLDDEEVAERLIEAIRDLR 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 373228229 332 EDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITLY 378
Cdd:cd17814 327 EDLGIPETLSELgVDEEDIPELAKRAMKDPCLVTNPRRPTREDIEEIY 374
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-381 |
5.93e-126 |
|
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: 367.63 E-value: 5.93e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYIIA 93
Cdd:cd08194 7 GGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGCDFIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 94 VGGGSSMDTAKAIGIIINNKEfeDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIPVV 173
Cdd:cd08194 87 LGGGSPIDTAKAIAVLATNGG--PIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPALLPAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 174 AIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENtP---EGREGMALGQYIAG 250
Cdd:cd08194 165 AIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYAD-GddlEAREAMMLAALEAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 251 MGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVEnTENMTVEEYRKAAVDAVKKL 330
Cdd:cd08194 244 IAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIA-TEGDSDEEAAEKLVEALERL 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 373228229 331 SEDVGIPANLKDIVKKEDIRFLAESAYNDACRPG----NPMETSVEDIITLYESL 381
Cdd:cd08194 323 CADLEIPTLREYGIDEEEFEAALDKMAEDALASGspanNPRVPTKEEIIELYREA 377
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-379 |
5.34e-121 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 354.93 E-value: 5.34e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 13 HGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYII 92
Cdd:cd14865 11 SGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAGADGII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 93 AVGGGSSMDTAKAIGIIINNkEFEDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIPV 172
Cdd:cd14865 91 AVGGGSVIDTAKGVNILLSE-GGDDLDDYGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVSPFLLPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 173 VAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENT--PEGREGMALGQYIAG 250
Cdd:cd14865 170 VAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGkdLEARLALAIAATMAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 251 MGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGV-ENTENMTVEEYRKAAVDAVKK 329
Cdd:cd14865 250 IAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALAYgVTPAGRRAEEAIEAAIDLVRR 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 373228229 330 LSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITLYE 379
Cdd:cd14865 330 LHELCGLPTRLRDVgVPEEQLEAIAELALNDGAILFNPREVDPEDILAILE 380
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-377 |
4.28e-120 |
|
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: 352.61 E-value: 4.28e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYIIA 93
Cdd:cd14863 11 GAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 94 VGGGSSMDTAKAIGIIINNKEfEDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIPVV 173
Cdd:cd14863 91 IGGGSVLDTAKAIAVLLTNPG-PIIDYALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVPDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 174 AIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENtP---EGREGMALGQYIAG 250
Cdd:cd14863 170 AILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKD-GdnlEARENMLLASNLAG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 251 MGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVENTEnMTVEEYRKAAVDAVKKL 330
Cdd:cd14863 249 IAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVSFPG-ESDEELGEAVADAIREF 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 373228229 331 SEDVGIPANLKD-IVKKEDIRFLAESAYNDACRPGNPMETSVEDIITL 377
Cdd:cd14863 328 MKELGIPSLFEDyGIDKEDLDKIAEAVLKDPFAMFNPRPITEEEVAEI 375
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
10-381 |
1.26e-116 |
|
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: 343.68 E-value: 1.26e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 10 TSYHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGAD 89
Cdd:cd08189 7 ELFEGAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 90 YIIAVGGGSSMDTAKAIGIIINNKEfEDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHD 169
Cdd:cd08189 87 AIIAIGGGSVIDCAKVIAARAANPK-KSVRKLKGLLKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 170 IPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVEN--TPEGREGMALGQY 247
Cdd:cd08189 166 IPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDgsDLEARENMLLASY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 248 IAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVEnTENMTVEEYRKAAVDAV 327
Cdd:cd08189 246 YAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLG-DSGESDSEKAEAFIAAI 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 373228229 328 KKLSEDVGIPANLKDIvKKEDIRFLAESAYNDAcRPGNP----MetSVEDIITLYESL 381
Cdd:cd08189 325 RELNRRMGIPTTLEEL-KEEDIPEIAKRALKEA-NPLYPvpriM--DRKDCEELLRKV 378
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
14-382 |
5.56e-116 |
|
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: 341.80 E-value: 5.56e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYIIA 93
Cdd:cd14861 9 GAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDGIIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 94 VGGGSSMDTAKAIGIIINN----KEFEDVvsLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHD 169
Cdd:cd14861 89 LGGGSAIDAAKAIALMATHpgplWDYEDG--EGGPAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSPKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 170 IPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYitgaaweMTDMFH-------LKAIELISKHLRGAVEN--TPEGRE 240
Cdd:cd14861 167 LPKVAICDPELTLGLPPRLTAATGMDALTHCIEAY-------LSPGFHpmadgiaLEGLRLISEWLPRAVADgsDLEARG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 241 GMALGQYIAGMGFSNvGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVENTEnmtveeyR 320
Cdd:cd14861 240 EMMMAALMGAVAFQK-GLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALGLGLGG-------F 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 373228229 321 KAAVDAVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITLYESLM 382
Cdd:cd14861 312 DDFIAWVEDLNERLGLPATLSELgVTEDDLDELAELALADPCHATNPRPVTAEDYRALLREAL 374
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
12-380 |
3.93e-111 |
|
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: 329.92 E-value: 3.93e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIvTEVKGrgfKKAFLCSDPD-LVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADY 90
Cdd:cd08179 9 YFGEGALEYL-KTLKG---KRAFIVTGGGsMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 91 IIAVGGGSSMDTAKAIGIIINNKE--FEDVVSLEGVAPTKNKSVpIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTH 168
Cdd:cd08179 85 IIAIGGGSVIDAAKAMWVFYEYPEltFEDALVPFPLPELRKKAR-FIAIPSTSGTGSEVTRASVITDTEKGIKYPLASFE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 169 DIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVEN--TPEGREGMALGQ 246
Cdd:cd08179 164 ITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGgkDLEAREKMHNAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 247 YIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETgdKYKYIAAAMGVENTENMTVEEYrkaaVDA 326
Cdd:cd08179 244 CLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDP--EARARYAALLIGLTDEELVEDL----IEA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 373228229 327 VKKLSEDVGIPANLKDIVKKED-----IRFLAESAYNDACRPGNPMETSVEDIITLYES 380
Cdd:cd08179 318 IEELNKKLGIPLSFKEAGIDEDeffakLDEMAENAMNDACTGTNPRKPTVEEMKELLKA 376
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-379 |
3.34e-104 |
|
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: 312.12 E-value: 3.34e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGfKKAFLCSDPD-LVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYII 92
Cdd:cd08185 10 GAGKLNELGEEALRPG-KKALIVTGKGsSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGCDFVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 93 AVGGGSSMDTAKAIGIIINNKE-FED-VVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRK--FVCVDTh 168
Cdd:cd08185 89 GLGGGSSMDAAKAIAFMATNPGdIWDyIFGGTGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKkgIGHPAL- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 169 dIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENTP--EGREGMALGQ 246
Cdd:cd08185 168 -FPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSdlEAREKMAWAS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 247 YIAGMGFSNVGLGIVHSMAHSLGAVY-DTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVENTEnmtvEEYRKAAVD 325
Cdd:cd08185 247 TLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVARAEASGLSD----AKAAEDFIE 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 373228229 326 AVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYN--DACRPGNPMETSVEDIITLYE 379
Cdd:cd08185 323 ALRKLLKDIGLDDLLSDLgVTEEDIPWLAENAMEtmGGLFANNPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-377 |
4.67e-100 |
|
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: 301.34 E-value: 4.67e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGfKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTnIKANPTIENVKSGVEAYKKSGADYIIA 93
Cdd:cd08183 7 GRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALFS-VSGEPTVETVDAAVALAREAGCDVVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 94 VGGGSSMDTAKAIGIIINNKEfeDVVS-LEGV---APTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKfvcV---D 166
Cdd:cd08183 85 IGGGSVIDAAKAIAALLTNEG--SVLDyLEVVgkgRPLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVK---VslrS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 167 THDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVEN--TPEGREGMAL 244
Cdd:cd08183 160 PSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDgeDLEAREDMAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 245 GQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVENTENM---TVEEYRK 321
Cdd:cd08183 240 ASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRALREREPDSPALARYRELAGIltgDPDAAAE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 373228229 322 AAVDAVKKLSEDVGIPaNLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITL 377
Cdd:cd08183 320 DGVEWLEELCEELGIP-RLSEYgLTEEDFPEIVEKARGSSSMKGNPIELSDEELLEI 375
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
14-382 |
5.97e-100 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 301.49 E-value: 5.97e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYIIA 93
Cdd:PRK09860 15 GADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVIS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 94 VGGGSSMDTAKAIGIIINNKEfeDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIPVV 173
Cdd:PRK09860 95 LGGGSPHDCAKGIALVAANGG--DIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 174 AIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVE--NTPEGREGMALGQYIAGM 251
Cdd:PRK09860 173 SVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEdgSNAKAREAMAYAQFLAGM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 252 GFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVeNTENMTVEEYRKAAVDAVKKLS 331
Cdd:PRK09860 253 AFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGV-NVTGKNDAEGAEACINAIRELA 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 373228229 332 EDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITLYESLM 382
Cdd:PRK09860 332 KKVDIPAGLRDLnVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAAM 383
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
31-378 |
7.05e-99 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 298.37 E-value: 7.05e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 31 KKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYIIAVGGGSSMDTAKAIGIII 110
Cdd:cd14862 25 KRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAKAAWVLY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 111 NNkefeDVVSLEGVAPT----KNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIPVVAIIDPEMMQSMPK 186
Cdd:cd14862 105 ER----PDLDPEDISPLdllgLRKKAKLIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDPEFVLGMPP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 187 GLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENT--PEGREGMALGQYIAGMGFSNVGLGIVHSM 264
Cdd:cd14862 181 KLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGddLEAREKMHNAATIAGLAFGNSQAGLAHAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 265 AHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVENTEnmtvEEYRKAAVDAVKKLSEDVGIPANLKDI- 343
Cdd:cd14862 261 GHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKLLGIEARDE----EEALKKLVEAIRELYKEVGQPLSIKDLg 336
|
330 340 350
....*....|....*....|....*....|....*....
gi 373228229 344 VKKEDIR----FLAESAYNDACRPGNPMETSVEDIITLY 378
Cdd:cd14862 337 ISEEEFEekldELVEYAMEDSCTITSPRPPSEEDLKKLF 375
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
14-382 |
6.24e-97 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 294.84 E-value: 6.24e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYIIA 93
Cdd:cd08190 7 GPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 94 VGGGSSMDTAKAIGIIINNK-EFEDVVSLE-GVA-PTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDI 170
Cdd:cd08190 87 VGGGSVIDTAKAANLYATHPgDFLDYVNAPiGKGkPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISSRYLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 171 PVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYIT------------------GAAWEMTDMFHLKAIELISKHLRGAV 232
Cdd:cd08190 167 PTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTArpynarprpanpderpayQGSNPISDVWAEKAIELIGKYLRRAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 233 ENTP--EGREGMALGQYIAGMGFSNVGLGIVHSMAHSLGAV-------------YDTPHGVANAIILPTVMEYNAEETGD 297
Cdd:cd08190 247 NDGDdlEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLvkdyrppgypvdhPHVPHGLSVALTAPAVFRFTAPACPE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 298 KYKYIAAAMGVeNTENMTVEEYRKAAVDAVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYndacrP------GNPMETS 370
Cdd:cd08190 327 RHLEAAELLGA-DTSGASDRDAGEVLADALIKLMRDIGIPNGLSALgYSEDDIPALVEGTL-----PqqrllkLNPRPVT 400
|
410
....*....|..
gi 373228229 371 VEDIITLYESLM 382
Cdd:cd08190 401 EEDLEEIFEDAL 412
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
12-379 |
3.70e-96 |
|
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: 292.17 E-value: 3.70e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIVTEVKGrgFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYI 91
Cdd:cd08178 7 YFEPGCLPYLLLELPG--VKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFKPDVI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 92 IAVGGGSSMDTAKAIGIIINNKEfedvVSLEGVA-------------PTKNKSVPIIAVPTTAGTAAEVTINYVITDVEK 158
Cdd:cd08178 85 IALGGGSAMDAAKIMWLFYEHPE----TKFEDLAqrfmdirkrvykfPKLGKKAKLVAIPTTSGTGSEVTPFAVITDDKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 159 NRKFVCVDTHDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVEN--TP 236
Cdd:cd08178 161 GKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNgnDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 237 EGREGMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDK------YKY--------- 301
Cdd:cd08178 241 EAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDPPTKqaafpqYKYyvakeryae 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 302 IAAAMGVENTenmTVEEYRKAAVDAVKKLSEDVGIPANLKDI-VKKED----IRFLAESAYNDACRPGNPMETSVEDIIT 376
Cdd:cd08178 321 IADLLGLGGK---TPEEKVESLIKAIEDLKKDLGIPTSIREAgIDEADflaaVDKLAEDAFDDQCTGANPRYPLISELKE 397
|
...
gi 373228229 377 LYE 379
Cdd:cd08178 398 ILL 400
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
12-379 |
7.18e-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: 281.69 E-value: 7.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIvtevKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANlSYELYTNIKANPTIENVKSGVEAYKKSGADYI 91
Cdd:cd08180 8 YSGEDSLERL----KELKGKRVFIVTDPFMVKSGMVDKVTDELDKSN-EVEIFSDVVPDPSIEVVAKGLAKILEFKPDTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 92 IAVGGGSSMDTAKAIGIIINNKEfedvvslegvapTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIP 171
Cdd:cd08180 83 IALGGGSAIDAAKAIIYFALKQK------------GNIKKPLFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSMLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 172 VVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVEN--TPEGREGMALGQYIA 249
Cdd:cd08180 151 DIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDgdDLEAREKMHNASCMA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 250 GMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYnaeetgdkykyiaaamgventenmtveeyrkaAVDAVKK 329
Cdd:cd08180 231 GIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF--------------------------------LIAAIRR 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 373228229 330 LSEDVGIPANLKDI-VKKED----IRFLAESAYNDACRPGNPMETSVEDIITLYE 379
Cdd:cd08180 279 LNKKLGIPSTLKELgIDEEEfekaIDEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-378 |
7.20e-93 |
|
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: 282.55 E-value: 7.20e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYelYTNIKANPTIENVKSGVEAYKKSGADYI 91
Cdd:cd08196 10 IFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVAV--FSDVEPNPTVENVDKCARLARENGADFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 92 IAVGGGSSMDTAKAIGIIINNKE-FEDVvsLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDI 170
Cdd:cd08196 88 IAIGGGSVLDTAKAAACLAKTDGsIEDY--LEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLVSPGFY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 171 PVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENtP---EGREGMALGQY 247
Cdd:cd08196 166 PDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNN-PndkEAREKMALASL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 248 IAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVENTEnmtveeyrkAAVDAV 327
Cdd:cd08196 245 LAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQLGFKDAE---------ELADKI 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 373228229 328 KKLSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITLY 378
Cdd:cd08196 316 EELKKRIGLRTRLSELgITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-375 |
2.52e-92 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 282.19 E-value: 2.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGFKkAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYIIA 93
Cdd:cd08191 10 GPGARRALGRVAARLGSR-VLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDPDVVIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 94 VGGGSSMDTAKAIGIII-NNKEFEDVVSlEGVAPtkNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIPV 172
Cdd:cd08191 89 LGGGSNMDLAKVVALLLaHGGDPRDYYG-EDRVP--GPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 173 VAIIDPEMMQSMPKGLTAATGMDALTHAIEGY-----------ITGAAWE----MTDMFHLKAIELISKHLRGAVEN--T 235
Cdd:cd08191 166 VAIVDPELTLTCPPGVTADSGIDALTHAIESYtardfppfprlDPDPVYVgknpLTDLLALEAIRLIGRHLPRAVRDgdD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 236 PEGREGMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVENTEnmT 315
Cdd:cd08191 246 LEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVTTAG--T 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 373228229 316 VEEYRKAAVDAVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYNdACR-----PGNPMETSVEDII 375
Cdd:cd08191 324 SEEAADRAIERVEELLARIGIPTTLADLgVTEADLPGLAEKALS-VTRliannPRPPTEEDLLRIL 388
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
12-379 |
4.48e-92 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 294.40 E-value: 4.48e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIVTEVKGRgfKKAFLCSDPDLVKFGVTGKVTSILD--EANLSYELYTNIKANPTIENVKSGVEAYKKSGAD 89
Cdd:PRK13805 464 YFERGSLPYLLDELDGK--KRAFIVTDRFMVELGYVDKVTDVLKkrENGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 90 YIIAVGGGSSMDTAKAIGIIINNKEfedvVSLEGVA-------------PTKNKSVPIIAVPTTAGTAAEVTINYVITDV 156
Cdd:PRK13805 542 TIIALGGGSPMDAAKIMWLFYEHPE----TDFEDLAqkfmdirkriykfPKLGKKAKLVAIPTTSGTGSEVTPFAVITDD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 157 EKNRKFVCVDTHDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVEN-- 234
Cdd:PRK13805 618 KTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNga 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 235 -TPEGREGMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEE-----TGDKYKY------- 301
Cdd:PRK13805 698 kDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDppkqaAFPQYEYpradery 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 302 --IAAAMGVENTenmTVEEYRKAAVDAVKKLSEDVGIPANLKDI-VKKED----IRFLAESAYNDACRPGNPMETSVEDI 374
Cdd:PRK13805 778 aeIARHLGLPGS---TTEEKVESLIKAIEELKAELGIPMSIKEAgVDEADflakLDELAELAFDDQCTGANPRYPLISEL 854
|
....*
gi 373228229 375 ITLYE 379
Cdd:PRK13805 855 KEILL 859
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
14-380 |
3.08e-84 |
|
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: 260.91 E-value: 3.08e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYIIA 93
Cdd:cd08193 10 GAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAGADGVIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 94 VGGGSSMDTAKAIGIIINNKefEDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDvEKNRKFVCVDTHDIPVV 173
Cdd:cd08193 90 FGGGSSMDVAKLVALLAGSD--QPLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIVTT-GETEKKGVVSPQLLPDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 174 AIIDPEMMQSMPKGLTAATGMDALTHAIEGYiTGAAW--EMTDMFHLKAIELISKHLRGAVENT--PEGREGMALGQYIA 249
Cdd:cd08193 167 ALLDAELTLGLPPHVTAATGIDAMVHAIEAY-TSRHKknPISDALAREALRLLGANLRRAVEDGsdLEAREAMLLGSMLA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 250 GMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVENTEnMTVEEYRKAAVDAVKK 329
Cdd:cd08193 246 GQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLPGLAF-GSDAAAAEAFIDALEE 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 373228229 330 LSEDVGIPANLKDI-VKKEDIRFLAESA-YNDACRPGNPMETSVEDIITLYES 380
Cdd:cd08193 325 LVEASGLPTRLRDVgVTEEDLPMLAEDAmKQTRLLVNNPREVTEEDALAIYQA 377
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
14-379 |
6.88e-83 |
|
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: 257.15 E-value: 6.88e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEaNLSYELYTNIKANPTIENVKSGVEAYKKSGADYIIA 93
Cdd:cd08182 7 GPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDALGG-RIPVVVFSDFSPNPDLEDLERGIELFRESGPDVIIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 94 VGGGSSMDTAKAIGIIINNKEFEDVVSLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFvCVDTHDI-PV 172
Cdd:cd08182 86 VGGGSVIDTAKAIAALLGSPGENLLLLRTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKY-SLAHPSLyPD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 173 VAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVEN--TPEGREGMALGQYIAG 250
Cdd:cd08182 165 AAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENlpNLEAREAMAEASLLAG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 251 MGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDK-----YKYIAAAMGVENTENmtveeyrkaAVD 325
Cdd:cd08182 245 LAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDECdddprGREILLALGASDPAE---------AAE 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 373228229 326 AVKKLSEDVGIPANLKD-IVKKEDIRFLAESAYNDAcRPGN-PMETSVEDIITLYE 379
Cdd:cd08182 316 RLRALLESLGLPTRLSEyGVTAEDLEALAASVNTPE-RLKNnPVRLSEEDLLRLLE 370
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
12-379 |
1.97e-73 |
|
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.
Pssm-ID: 341460 [Multi-domain] Cd Length: 358 Bit Score: 232.48 E-value: 1.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIVTEVKGRGfKKAFLcsdpdlvkfgVTGK-----------VTSILDEANLSYELYTNIKANPTIENVKSGV 80
Cdd:cd08181 8 YFGKNCVEKHADELAALG-KKALI----------VTGKhsakkngslddVTEALEENGIEYFIFDEVEENPSIETVEKGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 81 EAYKKSGADYIIAVGGGSSMDTAKAIGIIINNKEfEDVVSLEGVAPtkNKSVPIIAVPTTAGTAAEVTINYVITDVEKNR 160
Cdd:cd08181 77 ELARKEGADFVIGIGGGSPLDAAKAIALLAANKD-GDEDLFQNGKY--NPPLPIVAIPTTAGTGSEVTPYSILTDHEKGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 161 KfVCVDTHDI-PVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKH---LRGAvENTP 236
Cdd:cd08181 154 K-KSFGNPLIfPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGEClpnLLGD-ELDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 237 EGREGMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVEntenmTV 316
Cdd:cd08181 232 EDREKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLGFG-----SI 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 373228229 317 EEYRKAavdavkkLSEDVGIpanlKDIVKKEDIRFLAESAYNDACRPGNPMETSVEDIITLYE 379
Cdd:cd08181 307 EEFQKF-------LNRLLGK----KEELSEEELEKYADEAMKAKNKKNTPGNVTKEDILRIYR 358
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-377 |
2.54e-73 |
|
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: 232.96 E-value: 2.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGfKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYIIA 93
Cdd:cd14864 10 GADSLERIGEEVKEYG-SRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAGADGIIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 94 VGGGSSMDTAKAIGIIINNKEF-EDVVSLegvAPTKNKSVPIIAVPTTAGTAAEVTINYVITDvEKNRK-FVCVDTHDIP 171
Cdd:cd14864 89 VGGGKVLDTAKAVAILANNDGGaYDFLEG---AKPKKKPLPLIAVPTTPRSGFEFSDRFPVVD-SRSREvKLLKAQPGLP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 172 VVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVE---NTPEgREGMALGQYI 248
Cdd:cd14864 165 KAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALAdpkNTPA-EELLAQAGCL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 249 AGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGvENTENMTVEEYRKAAVDAVK 328
Cdd:cd14864 244 AGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALG-EDVEGASPEEAAIAAVEGVR 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 373228229 329 KLSEDVGIPANLKDI---VKKEDIRFLAESAYNdacRPGNPMETSVEDIITL 377
Cdd:cd14864 323 RLIAQLNLPTRLKDLdlaSSLEQLAAIAEDAPK---LNGLPRSMSSDDIFDI 371
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
12-379 |
1.04e-70 |
|
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: 226.16 E-value: 1.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIVTEVKGRGfKKAFLCSDPD-LVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADY 90
Cdd:cd08187 11 IFGKGAIEELGEEIKKYG-KKVLLVYGGGsIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 91 IIAVGGGSSMDTAKAIGIIINNKE-FEDVVSLEGVAptkNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHD 169
Cdd:cd08187 90 ILAVGGGSVIDAAKAIAAGAKYDGdVWDFFTGKAPP---EKALPVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 170 IPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAW-EMTDMFhlkaIELIskhLRGAVENTP---------EGR 239
Cdd:cd08187 167 RPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDaPLQDRL----AEGL---LRTVIENGPkalkdpddyEAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 240 EGMALGQYIAGMGFSNVGLG---IVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKY-KYIAAAMGVENTENmt 315
Cdd:cd08187 240 ANLMWAATLALNGLLGAGRGgdwATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFaQFARRVFGIDPGGD-- 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 373228229 316 VEEYRKAAVDAVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITLYE 379
Cdd:cd08187 318 DEETALEGIEALEEFFKSIGLPTTLSELgIDEEDIEEMAEKAVRGGGLGGGFKPLTREDIEEILK 382
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
13-378 |
2.92e-68 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 220.28 E-value: 2.92e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 13 HGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYII 92
Cdd:PRK15454 32 CGPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 93 AVGGGSSMDTAKAIGIIINNKE--FEDVVSLEGVAPtknkSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDI 170
Cdd:PRK15454 112 AFGGGSVLDAAKAVALLVTNPDstLAEMSETSVLQP----RLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASLM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 171 PVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENTPE--GREGMALGQYI 248
Cdd:PRK15454 188 PDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDlaARESMLLASCM 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 249 AGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVENTENmtveeyrKAAVDAVK 328
Cdd:PRK15454 268 AGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRALRTKKSDD-------RDAINAVS 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 373228229 329 KLSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPMETSVEDIITLY 378
Cdd:PRK15454 341 ELIAEVGIGKRLGDVgATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLY 391
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-380 |
1.25e-56 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 189.75 E-value: 1.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIVTEVKGRGFKKAFLCSDP---------DLVKFGVTGKVTSILDEAnlsyelytniKANPTIENVKSGVEA 82
Cdd:cd14866 9 FSGRGALARLGRELDRLGARRALVVCGSsvganpdlmDPVRAALGDRLAGVFDGV----------RPHSPLETVEAAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 83 YKKSGADYIIAVGGGSSMDTAKAIGIII-NNKEFEDV----------VSLEGVAPTknksVPIIAVPTTAGTAaEVTINY 151
Cdd:cd14866 79 LREADADAVVAVGGGSAIVTARAASILLaEDRDVRELctrraedglmVSPRLDAPK----LPIFVVPTTPTTA-DVKAGS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 152 VITDVEKNRKFVCVDTHDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHL-RG 230
Cdd:cd14866 154 AVTDPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLpRL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 231 AVENTPEGREGMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVEN 310
Cdd:cd14866 234 ADDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGVAD 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 373228229 311 TenmTVEEYRKAAVDAVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRPGNPM-ETSVEDIITLYES 380
Cdd:cd14866 314 A---GDEASAAAVVDAVEALLDALGVPTRLRDLgVSREDLPAIAEAAMDDWFMDNNPRpVPTAEELEALLEA 382
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-356 |
7.72e-53 |
|
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: 176.40 E-value: 7.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 8 NETSYHGAGAIkEIVTEVKGRGFKKAFLCSDPDLVKfGVTGKVTSILDEaNLSYELYTNIKANPTIENVKSGVEAYKKSG 87
Cdd:cd07766 1 PTRIVFGEGAI-AKLGEIKRRGFDRALVVSDEGVVK-GVGEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 88 ADYIIAVGGGSSMDTAKAIGIIINNKefedvvslegvaptknksVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCvdT 167
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAALLNRG------------------IPFIIVPTTASTDSEVSPKSVITDKGGKNKQVG--P 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 168 HDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEgyitgaawemtdmfhlkaieliskhlrgaventpegREGMALGQY 247
Cdd:cd07766 138 HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE------------------------------------LEKVVEAAT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 248 IAGMGFSN-VGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDkykyiaaamgventenmtveeyRKAAVDA 326
Cdd:cd07766 182 LAGMGLFEsPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPE----------------------PEAAIEA 239
|
330 340 350
....*....|....*....|....*....|.
gi 373228229 327 VKKLSEDVGIPANLKDI-VKKEDIRFLAESA 356
Cdd:cd07766 240 VFKFLEDLGLPTHLADLgVSKEDIPKLAEKA 270
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
14-379 |
1.32e-50 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 174.10 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGfKKAFLC----SdpdLVKFGVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGAD 89
Cdd:COG1979 15 GKGQIAKLGEEIPKYG-KKVLLVygggS---IKKNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGID 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 90 YIIAVGGGSSMDTAKAIGI-IINNKEFEDVVslEGVAPTKnKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTH 168
Cdd:COG1979 91 FILAVGGGSVIDGAKAIAAgAKYDGDPWDIL--TGKAPVE-KALPLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 169 DIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAW-EMTDMFhlkaIELIskhLRGAVENTP---------EG 238
Cdd:COG1979 168 VFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDaPLQDRF----AEGL---LRTLIEEGPkalkdpedyDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 239 REG------MALGQYIaGMG----FSnvglgiVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEEtgDKYKYIAAAMGV 308
Cdd:COG1979 241 RANlmwaatLALNGLI-GAGvpqdWA------THMIEHELSALYDIDHGAGLAIVLPAWMRYVLEE--KPEKFAQYAERV 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 373228229 309 ENTENMTVEEYRKAAVDAVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYNDACRP-GNPMETSVEDIITLYE 379
Cdd:COG1979 312 WGITEGDDEERALEGIEATEEFFESLGLPTRLSEYgIDEEDIEEMAEKATAHGMTAlGEFKDLTPEDVREILE 384
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-382 |
1.84e-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: 1.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 10 TSYHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKfgVTG---KVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKS 86
Cdd:cd08186 3 TLYFGVGAIAKIKDILKDLGIDKVIIVTGRSSYK--KSGawdDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 87 GADYIIAVGGGSSMDTAKAIGIIINN--KEFEDvvsLEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVC 164
Cdd:cd08186 81 GADAVIAIGGGSPIDTAKSVAVLLAYggKTARD---LYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 165 VDTHDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENtP---EGREG 241
Cdd:cd08186 158 AYDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALAN-PkdlEARYW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 242 MALGQYIAGMGFSNVGLGIVHSMAHSLGAVY-DTPHGVANAIILPTVMEY----NAEETGDKYKYIaaamgveNTENMTV 316
Cdd:cd08186 237 LLYASMIAGIAIDNGLLHLTHALEHPLSGLKpELPHGLGLALLGPAVVKYiykaVPETLADILRPI-------VPGLKGT 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 373228229 317 EEYRKAAVDAVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYNdacRPG-------NPMETSVEDIITLYESLM 382
Cdd:cd08186 310 PDEAEKAARGVEEFLFSVGFTEKLSDYgFTEDDVDRLVELAFT---TPSldlllslAPVEVTEEVVREIYEESL 380
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
12-381 |
6.94e-48 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 166.65 E-value: 6.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIVTEVKGRGFKKAFLcsdpdlvkfgVTGKV----TSILDE-----ANLSYELYTNIKANPTIENVKSGVEA 82
Cdd:cd08192 5 SYGPGAVEALLHELATLGASRVFI----------VTSKSlatkTDVIKRleealGDRHVGVFSGVRQHTPREDVLEAARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 83 YKKSGADYIIAVGGGSSMDTAKAIGIIINNK--EFEDVVSLEGVAPT----KNKSVPIIAVPTTAgTAAEVTINYVITDV 156
Cdd:cd08192 75 VREAGADLLVSLGGGSPIDAAKAVALALAEDvtDVDQLDALEDGKRIdpnvTGPTLPHIAIPTTL-SGAEFTAGAGATDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 157 EKNRKFVCVDTHDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVEN-- 234
Cdd:cd08192 154 DTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADpe 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 235 TPEGREGMALGQYIAGMGF-SNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVENTEN 313
Cdd:cd08192 234 DLEARLKCQLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALGLVTGGL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 314 MTVEEyrkAAVDAVKKLSEDVGIPANLKDI-VKKEDIRFLAESAYND-ACRPGNPMETSVEDIITLYESL 381
Cdd:cd08192 314 GREAA---DAADAIDALIRELGLPRTLRDVgVGRDQLEKIAENALTDvWCRTNPRPITDKDDVLEILESA 380
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
14-356 |
1.04e-44 |
|
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: 157.28 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGFKKAFLCSDPdlvkfGVTGKVTSILDE-ANLSYELYTNIKANPTIENVKSGVEAYKKSGADYII 92
Cdd:cd08177 7 GAGTLAELAEELERLGARRALVLSTP-----RQRALAERVAALlGDRVAGVFDGAVMHVPVEVAERALAAAREAGADGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 93 AVGGGSSMDTAKAIgiiinnkefedvvSLEGvaptknkSVPIIAVPTT-AGtaAEVTINYVITdvEKNRKFVCVDTHDIP 171
Cdd:cd08177 82 AIGGGSAIGLAKAI-------------ALRT-------GLPIVAVPTTyAG--SEMTPIWGET--EDGVKTTGRDPRVLP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 172 VVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVEN--TPEGREGMALGQYIA 249
Cdd:cd08177 138 RTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADpsDLEARSDALYGAWLA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 250 GMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYIAAAMGVENtenmtveeyrkaAVDAVKK 329
Cdd:cd08177 218 GVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGGGD------------AAGGLYD 285
|
330 340
....*....|....*....|....*...
gi 373228229 330 LSEDVGIPANLKDI-VKKEDIRFLAESA 356
Cdd:cd08177 286 LARRLGAPTSLRDLgMPEDDIDRAADLA 313
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
54-381 |
1.34e-39 |
|
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: 144.28 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 54 LDEANLSYELYtnIKANPTIENVKSGVEAYKKSGADYIIAVGGGSSMDTAKaigiiinnkefedVVSLEGVAPTKN---- 129
Cdd:cd14860 47 LDCAVIFQEKY--GTGEPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAK-------------LLALKGISPVLDlfdg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 130 -----KSVPIIAVPTTAGTAAEVTiNYVITDV-EKNRKFVCVDTHDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEG 203
Cdd:cd14860 112 kipliKEKELIIVPTTCGTGSEVT-NISIVELtSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIES 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 204 YITGAAWEMTDMFHLKAIELISKHLRGAVENTPEGREGMaLGQYI-----AGMGFSNVGLGIVHSMAHSLGAVYDTPHGV 278
Cdd:cd14860 191 YLSPKATPYTEMFSYKAIEMILEGYQEIAEKGEEARFPL-LGDFLiasnyAGIAFGNAGCAAVHALSYPLGGKYHVPHGE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 279 ANAIILPTVMEYNAEETGDKY-----KYIAAAMGVENTEnmtveeyrkaAVDAVKKLSEDVGIPANLKDI-VKKEDIRFL 352
Cdd:cd14860 270 ANYAVFTGVLKNYQEKNPDGEikklnEFLAKILGCDEED----------VYDELEELLNKILPKKPLHEYgMKEEEIDEF 339
|
330 340 350
....*....|....*....|....*....|.
gi 373228229 353 AESAYNDACR--PGNPMETSVEDIITLYESL 381
Cdd:cd14860 340 ADSVMENQQRllANNYVPLDREDVAEIYKEL 370
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
91-352 |
3.36e-29 |
|
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: 115.83 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 91 IIAVGGGSSMDTAKAIGIIINN----KEFE--DVVslegvaptKNKSVPIIAVPTTAGTAAEVTINYVITDveKNRKFVC 164
Cdd:cd08184 86 VVGIGGGSTMDIAKAVSNMLTNpgsaADYQgwDLV--------KNPGIYKIGVPTLSGTGAEASRTAVLTG--PEKKLGI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 165 VDTHDIPVVAIIDPEMMQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENTPEGREGMAL 244
Cdd:cd08184 156 NSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELCRDVFLSDDMMSPENREKLMV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 245 GQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYKYiAAAMGVE----NTENMTVEEYR 320
Cdd:cd08184 236 ASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCIVFNVLEEFYPEGVKEFREM-LEKQNITlpkgICKDLTDEQYE 314
|
250 260 270
....*....|....*....|....*....|....
gi 373228229 321 KAAVDAVK--KLSEDVGIPaNLKDIVKKEDIRFL 352
Cdd:cd08184 315 KMVAVTLIheKPLTNALGP-DWKDILTPEKVTKL 347
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
12-374 |
3.84e-18 |
|
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: 84.83 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIVTEVKGRGfKKAFLCSDPdlVKFGVTG-KVTSILDEANLSYELYTnIKANPTIENVKSGVEAYKKSGADY 90
Cdd:COG0371 10 VQGEGALDELGEYLADLG-KRALIITGP--TALKAAGdRLEESLEDAGIEVEVEV-FGGECSEEEIERLAEEAKEQGADV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 91 IIAVGGGSSMDTAKAIGIIINnkefedvvslegvaptknksVPIIAVPTTAGTAAEVTINYVITDVEKnrKFVCVDTH-D 169
Cdd:COG0371 86 IIGVGGGKALDTAKAVAYRLG--------------------LPVVSVPTIASTDAPASPLSVIYTEDG--AFDGYSFLaK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 170 IPVVAIIDPEMMQSMPKGLTAAtGM-DAL-------------THAIEGYITGAAWEM----TDMFHLKAIELISKHLRGA 231
Cdd:COG0371 144 NPDLVLVDTDIIAKAPVRLLAA-GIgDALakwyeardwslahRDLAGEYYTEAAVALarlcAETLLEYGEAAIKAVEAGV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 232 VenTPEGR----EGMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTP---HG--VANAIIlptVMEYnaeetgdkykyi 302
Cdd:COG0371 223 V--TPALErvveANLLLSGLAMGIGSSRPGSGAAHAIHNGLTALPETHhalHGekVAFGTL---VQLV------------ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 303 aaamgVENtenmtveeyRKAAVDAVKKLSEDVGIPANLKDI----VKKEDIRFLAESayndACRPG-----NPMETSVED 373
Cdd:COG0371 286 -----LEG---------RPEEIEELLDFLRSVGLPTTLADLglddETEEELLTVAEA----ARPERytilnLPFEVTPEA 347
|
.
gi 373228229 374 I 374
Cdd:COG0371 348 V 348
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
41-342 |
3.44e-17 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 82.15 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 41 LVKFGVTGKVTSILdeANLSYELYTNIKANPTIENVKSGVEAYKKSGADYIIAVGGGSSMDTAKAIGIIINNKEFEDVVS 120
Cdd:PRK15138 41 VKKTGVLDQVLDAL--KGMDVLEFGGIEPNPTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKFIAAAANYPENIDPWH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 121 -LEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIPVVAIIDPEMMQSMPKGLTAATGMDALTH 199
Cdd:PRK15138 119 iLETGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 200 AIEGYITGAA-WEMTDMFH----LKAIELISKHLrgaveNTPEGREGMALGQYIAGMGFSN-VGLGI-----VHSMAHSL 268
Cdd:PRK15138 199 TVEQYVTYPVdAKIQDRFAegilLTLIEEGPKAL-----KEPENYDVRANVMWAATQALNGlIGAGVpqdwaTHMLGHEL 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 373228229 269 GAVYDTPHGVANAIILPTVMeyNAEETGDKYKYIAAAMGVENTENMTVEEYRKAAVDAVKKLSEDVGIPANLKD 342
Cdd:PRK15138 274 TAMHGLDHAQTLAIVLPALW--NEKRDTKRAKLLQYAERVWNITEGSDDERIDAAIAATRNFFEQMGVPTRLSD 345
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
13-375 |
3.49e-16 |
|
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: 78.73 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 13 HGAGAIKEIVTEVKGRGfKKAFLCSDPDLVKfGVTGKVTSILDEANLSYELYTNiKANPTIENVKSGVEAYKKSGADYII 92
Cdd:cd08550 6 QEPGILAKAGEYIAPLG-KKALIIGGKTALE-AVGEKLEKSLEEAGIDYEVEVF-GGECTEENIERLAEKAKEEGADVII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 93 AVGGGSSMDTAKAIGIIINnkefedvvslegvaptknksVPIIAVPTTAGTAAEVTINYVITDveKNRKFVCVDTHD-IP 171
Cdd:cd08550 83 GIGGGKVLDTAKAVADRLG--------------------LPVVTVPTIAATCAAWSALSVLYD--EEGEFLGYSLLKrSP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 172 VVAIIDPEMMQSMPKGLTAAtGM-DALTHAIEGYITGAAWEMTDMFHLK------AIELISKHLRGAVENTPEGREGMAL 244
Cdd:cd08550 141 DLVLVDTDIIAAAPVRYLAA-GIgDTLAKWYEARPSSRGGPDDLALQAAvqlaklAYDLLLEYGVQAVEDVRQGKVTPAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 245 GQ------YIAGMGFS----NVGLGIVHSMAHSLGAVYDTP---HG--VANAIILptvmeynaeetgdkykyiaaamgve 309
Cdd:cd08550 220 EDvvdaiiLLAGLVGSlgggGCRTAAAHAIHNGLTKLPETHgtlHGekVAFGLLV------------------------- 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 310 nteNMTVEEYRKAAVDAVKKLSEDVGIPANLKDI---VKKEDIRFLAESAYNDA-CRPGNPMETSVEDII 375
Cdd:cd08550 275 ---QLALEGRSEEEIEELIEFLRRLGLPVTLEDLgleLTEEELRKIAEYACDPPdMAHMLPFPVTPEMLA 341
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
14-375 |
8.37e-14 |
|
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: 71.67 E-value: 8.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGfKKAFLCSDPDLVKFgVTGKVTSILDEANLSYELYT-NIKAnpTIENVKSGVEAYKKSGADYII 92
Cdd:cd08170 7 GPGALDRLGEYLAPLG-KKALVIADPFVLDL-VGERLEESLEKAGLEVVFEVfGGEC--SREEIERLAAIARANGADVVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 93 AVGGGSSMDTAKAIGIIINnkefedvvslegvaptknksVPIIAVPTTAGTAAEVTINYVI-TDvekNRKFVCVDTHDI- 170
Cdd:cd08170 83 GIGGGKTIDTAKAVADYLG--------------------LPVVIVPTIASTDAPCSALSVIyTE---DGEFDEYLFLPRn 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 171 PVVAIIDPEMMQSMPKGLTAAtGM-DALTHAIE--------------GYITGAAWEMTD------MFH-LKAIELISKHL 228
Cdd:cd08170 140 PDLVLVDTEIIAKAPVRFLVA-GMgDALATYFEaracarsgapnmagGRPTLAALALAElcydtlLEYgVAAKAAVEAGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 229 RG-AVE-----NTpegregmalgqYIAGMGFSNVGLGIVHSMAH---SLGAVYDTPHG--VANAIILPTVMEyNAEEtgd 297
Cdd:cd08170 219 VTpALEavieaNT-----------LLSGLGFESGGLAAAHAIHNgltALPETHHLLHGekVAFGTLVQLVLE-GRPD--- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 298 kykyiaaamgventenmtvEEyrkaaVDAVKKLSEDVGIPANLKDI----VKKEDIRFLAESayndACRPG-----NPME 368
Cdd:cd08170 284 -------------------EE-----IEEVIRFCRSVGLPVTLADLgledVTDEELRKVAEA----ACAPGetihnMPFP 335
|
....*..
gi 373228229 369 TSVEDII 375
Cdd:cd08170 336 VTPEDVV 342
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
14-374 |
3.84e-12 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 66.76 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGfKKAFLCSDPDLVKFgVTGKVTSILDEANLSYElYTNIKANPTIENVKSGVEAYKKSGADYIIA 93
Cdd:PRK09423 14 GKGALARLGEYLKPLG-KRALVIADEFVLGI-VGDRVEASLKEAGLTVV-FEVFNGECSDNEIDRLVAIAEENGCDVVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 94 VGGGSSMDTAKAIGIIINnkefedvvslegvaptknksVPIIAVPTTAGTAAEVTINYVI-TD---------VEKNRKFV 163
Cdd:PRK09423 91 IGGGKTLDTAKAVADYLG--------------------VPVVIVPTIASTDAPTSALSVIyTEegeferylfLPKNPDLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 164 CVDTHdipVVAiidpemmqSMPKGLTAAtGM-DALTHAIE--------------GYITGAA-------WEmTDMFH-LKA 220
Cdd:PRK09423 151 LVDTA---IIA--------KAPARFLAA-GIgDALATWFEaracsrsggttmagGKPTLAAlalaelcYE-TLLEDgLKA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 221 IELISKHL-RGAVENTPEGRegmalgQYIAGMGFSNVGLGIVHSMAHSLGAVYDTP---HG--VANAIILPTVMEyNAEe 294
Cdd:PRK09423 218 KLAVEAKVvTPALENVIEAN------TLLSGLGFESGGLAAAHAIHNGLTALEDTHhltHGekVAFGTLTQLVLE-NRP- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 295 tgdkykyiaaamgventenmtveeyrKAAVDAVKKLSEDVGIPANLKDI----VKKEDIRFLAESayndACRPGN----- 365
Cdd:PRK09423 290 --------------------------KEEIEEVIDFCHAVGLPTTLADLglkeDSDEELRKVAEA----ACAEGEtihnm 339
|
....*....
gi 373228229 366 PMETSVEDI 374
Cdd:PRK09423 340 PFKVTPEDV 348
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
12-186 |
4.29e-08 |
|
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: 54.45 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 12 YHGAGAIKEIVTEVKGRGFKKAFLcsdpdlvkfgVTGKvTSI---------LDEANLSYELYTNikaNPTIENVKSGVEA 82
Cdd:cd08172 5 ICEEGALKELPELLSEFGIKRPLI----------IHGE-KSWqaakpylpkLFEIEYPVLRYDG---ECSYEEIDRLAEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 83 YKKSGADYIIAVGGGSSMDTAKAIGIIINnkefedvvslegvaptknksVPIIAVPTTAGTAAEVT---INYviTDvekN 159
Cdd:cd08172 71 AKEHQADVIIGIGGGKVLDTAKAVADKLN--------------------IPLILIPTLASNCAAWTplsVIY--DE---D 125
|
170 180
....*....|....*....|....*...
gi 373228229 160 RKFVCVDTHDIPVVA-IIDPEMMQSMPK 186
Cdd:cd08172 126 GEFIGYDYFPRSAYLvLVDPRLLLDSPK 153
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
14-141 |
1.56e-07 |
|
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: 52.56 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEV-KGRGFKKAFLCSDPDLVKfgVTGKVTSILDEANLSYELYTNIKANPTIENVKSGVEAYKKSGADYII 92
Cdd:cd08173 8 GHGAINKIGEVLkKLLLGKRALIITGPNTYK--IAGKRVEDLLESSGVEVVIVDIATIEEAAEVEKVKKLIKESKADFII 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 373228229 93 AVGGGSSMDTAKAIgiiinnkefedvvslegvapTKNKSVPIIAVPTTA 141
Cdd:cd08173 86 GVGGGKVIDVAKYA--------------------AYKLNLPFISIPTSA 114
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
14-191 |
1.73e-06 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 49.51 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGRGFKKAFLCsdpdlvkfgVTGKVT------SILDEANLSYELYTNIKANPTIENVKSGVEAYKKSG 87
Cdd:PRK00843 17 GHGVLDDIGDVCSDLKLTGRALI---------VTGPTTkkiagdRVEENLEDAGDVEVVIVDEATMEEVEKVEEKAKDVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 88 ADYIIAVGGGSSMDTAKaigiiinnkefedvvslegVAPTKNkSVPIIAVPTTAGTAAEVTINYVITDVEKNrkfVCVDT 167
Cdd:PRK00843 88 AGFLIGVGGGKVIDVAK-------------------LAAYRL-GIPFISVPTAASHDGIASPRASIKGGGKP---VSVKA 144
|
170 180
....*....|....*....|....*
gi 373228229 168 HdiPVVAII-DPEMMQSMPKGLTAA 191
Cdd:PRK00843 145 K--PPLAVIaDTEIIAKAPYRLLAA 167
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
14-191 |
6.79e-06 |
|
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: 47.52 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 14 GAGAIKEIVTEVKGR--GFKKAFLCSDPDlVKFGVTGKVTSILDEANLSYELYTNikANPTIENVKSgvEAYKKSGADYI 91
Cdd:cd08174 7 EEGALEHLGKYLADRnqGFGKVAIVTGEG-IDELLGEDILESLEEAGEIVTVEEN--TDNSAEELAE--KAFSLPKVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373228229 92 IAVGGGSSMDTAKaigiiinnkefedvvslegVAPTKNKsVPIIAVPTTA---GTAAEVTinyVITDVEKNRKFVCVdth 168
Cdd:cd08174 82 VGIGGGKVLDVAK-------------------YAAFLSK-LPFISVPTSLsndGIASPVA---VLKVDGKRKSLGAK--- 135
|
170 180
....*....|....*....|...
gi 373228229 169 dIPVVAIIDPEMMQSMPKGLTAA 191
Cdd:cd08174 136 -MPYGVIVDLDVIKSAPRRLILA 157
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
72-148 |
1.27e-04 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341450 Cd Length: 345 Bit Score: 43.66 E-value: 1.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 373228229 72 TIENVKSGVEAYKKSGADYIIAVGGGSSMDTAKAIGIIINnkefedvvslegvaptknksVPIIAVPTTAGTAAEVT 148
Cdd:cd08171 63 TYENVEKLKANPEVQEADMIFAVGGGKAIDTVKVLADRLN--------------------KPVFTFPTIASNCAAVT 119
|
|
| |
