|
Name |
Accession |
Description |
Interval |
E-value |
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
24-399 |
0e+00 |
|
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: 549.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 24 MPSLAYMAFNGQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQ 103
Cdd:cd08189 1 LPWPEPELFEGAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 104 QQHKCDAVLAIGGGSSIDCAKTIASAATNGR-DGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFL 182
Cdd:cd08189 81 KENGCDAIIAIGGGSVIDCAKVIAARAANPKkSVRKLKGLLKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 183 ADPKMLPKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQM 262
Cdd:cd08189 161 NDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 263 ALAAYYAGMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKF 342
Cdd:cd08189 241 LLASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGDSGESDSEKAEAF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2524884235 343 IDAVADLNTRLGVPDVLDTLREEDIAAIAADAVKEGAG-YPVPVLMSRKECQAILRTL 399
Cdd:cd08189 321 IAAIRELNRRMGIPTTLEELKEEDIPEIAKRALKEANPlYPVPRIMDRKDCEELLRKV 378
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
34-400 |
3.12e-144 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 415.29 E-value: 3.12e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:COG1454 14 GAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAAREFGADVVIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAVA 193
Cdd:COG1454 94 LGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVKKGIADPELLPDVAI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 194 LDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMAI 273
Cdd:COG1454 174 LDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLEAREKMALASLLAGMAF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 274 NDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTgDAQAAEKFIDAVADLNTRL 353
Cdd:COG1454 254 ANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARALGLDVGLS-DEEAAEALIEAIRELLRDL 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524884235 354 GVP----------DVLDTLreediaaiAADAVKEGAGYPVPVLMSRKECQAILRTLL 400
Cdd:COG1454 333 GIPtrlselgvteEDLPEL--------AELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
34-356 |
9.88e-139 |
|
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: 401.06 E-value: 9.88e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd08551 7 GAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGADLVIA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAVA 193
Cdd:cd08551 87 VGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLLPDVAI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 194 LDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMAI 273
Cdd:cd08551 167 LDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLASLLAGIAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 274 NDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKFIDAVADLNTRL 353
Cdd:cd08551 247 GNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELLRDL 326
|
...
gi 2524884235 354 GVP 356
Cdd:cd08551 327 GIP 329
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
23-362 |
2.98e-131 |
|
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: 382.25 E-value: 2.98e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 23 LMPSLAYMafnGQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLAL 102
Cdd:cd08188 4 YIPPVNLF---GPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 103 QQQHKCDAVLAIGGGSSIDCAKTIASAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFL 182
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 183 ADPKMLPKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQM 262
Cdd:cd08188 161 VDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKDLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 263 ALAAYYAGMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKF 342
Cdd:cd08188 241 AYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGENTEGLSDEEAAEAA 320
|
330 340
....*....|....*....|
gi 2524884235 343 IDAVADLNTRLGVPDVLDTL 362
Cdd:cd08188 321 IEAIRKLSRRVGIPSGLKEL 340
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
34-356 |
1.01e-122 |
|
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: 360.31 E-value: 1.01e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd08194 7 GGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGCDFIVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAVA 193
Cdd:cd08194 87 LGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPALLPAVAI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 194 LDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMAI 273
Cdd:cd08194 167 VDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAALEAGIAF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 274 NDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKFIDAVADLNTRL 353
Cdd:cd08194 247 SNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALERLCADL 326
|
...
gi 2524884235 354 GVP 356
Cdd:cd08194 327 EIP 329
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
34-356 |
8.28e-122 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 357.30 E-value: 8.28e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAqRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:pfam00465 7 GAGALAELGEELKRLGA-RALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGADVIIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAVA 193
Cdd:pfam00465 86 VGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKLLPDLAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 194 LDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMAI 273
Cdd:pfam00465 166 LDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLASTLAGLAF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 274 NDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADastgDAQAAEKFIDAVADLNTRL 353
Cdd:pfam00465 246 SNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGEDS----DEEAAEEAIEALRELLREL 321
|
...
gi 2524884235 354 GVP 356
Cdd:pfam00465 322 GLP 324
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
34-400 |
1.85e-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: 354.53 E-value: 1.85e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd14863 11 GAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRDGRKLEGYFK-VKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAV 192
Cdd:cd14863 91 IGGGSVLDTAKAIAVLLTNPGPIIDYALAGPpVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVPDLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 193 ALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMA 272
Cdd:cd14863 171 ILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENMLLASNLAGIA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 273 INDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKFIDAVADLNTR 352
Cdd:cd14863 251 FNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREFMKE 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2524884235 353 LGVPDVLDTLR--EEDIAAIAADAVKEGAGYPVPVLMSRKECQAILRTLL 400
Cdd:cd14863 331 LGIPSLFEDYGidKEDLDKIAEAVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
34-359 |
2.18e-120 |
|
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: 354.55 E-value: 2.18e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd08176 12 GWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKESGADGIIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATN-GRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAV 192
Cdd:cd08176 92 VGGGSSIDTAKAIGIIVANpGADVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKRKFVCVDPHDIPTVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 193 ALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMA 272
Cdd:cd08176 172 IVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNVEARENMALAQYIAGMA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 273 INDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKFIDAVADLNTR 352
Cdd:cd08176 252 FSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKD 331
|
....*..
gi 2524884235 353 LGVPDVL 359
Cdd:cd08176 332 VGIPQKL 338
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
34-356 |
1.37e-107 |
|
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: 321.80 E-value: 1.37e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd14865 12 GAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAGADGIIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIA-SAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAV 192
Cdd:cd14865 92 VGGGSVIDTAKGVNiLLSEGGDDLDDYGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVSPFLLPDVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 193 ALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMA 272
Cdd:cd14865 172 ILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGKDLEARLALAIAATMAGIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 273 INDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRL--IGVADASTGDAQAAEKFIDAVADLN 350
Cdd:cd14865 252 FSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALAlaYGVTPAGRRAEEAIEAAIDLVRRLH 331
|
....*.
gi 2524884235 351 TRLGVP 356
Cdd:cd14865 332 ELCGLP 337
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
34-359 |
1.74e-103 |
|
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: 310.98 E-value: 1.74e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd14861 9 GAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDGIIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRDGRKLE---GYFKVKTMPL-PLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLP 189
Cdd:cd14861 89 LGGGSAIDAAKAIALMATHPGPLWDYEdgeGGPAAITPAVpPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSPKLLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 190 KAVALDADLLLGMPAPITAATGMDALTHAVETYislwgteSSNGY-----GYA--AVKMIFDYLPRAYRDGNDAEAREQM 262
Cdd:cd14861 169 KVAICDPELTLGLPPRLTAATGMDALTHCIEAY-------LSPGFhpmadGIAleGLRLISEWLPRAVADGSDLEARGEM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 263 ALAAYYAGMAInDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEkplaelGRLIGVADASTGDAQAAEKF 342
Cdd:cd14861 242 MMAALMGAVAF-QKGLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVE------DKLARLARALGLGLGGFDDF 314
|
330
....*....|....*..
gi 2524884235 343 IDAVADLNTRLGVPDVL 359
Cdd:cd14861 315 IAWVEDLNERLGLPATL 331
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
31-362 |
1.36e-97 |
|
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: 296.27 E-value: 1.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 31 AFNGQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDA 110
Cdd:TIGR02638 10 SYFGAGAIEDIVDEVKRRGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVAAFKASGADY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 111 VLAIGGGSSIDCAKTIASAATNGR--DGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKML 188
Cdd:TIGR02638 90 LIAIGGGSPIDTAKAIGIISNNPEfaDVRSLEGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEENKRKFVCVDPHDI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 189 PKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYY 268
Cdd:TIGR02638 170 PDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGGKDLEAREQMALGQYV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 269 AGMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKFIDAVAD 348
Cdd:TIGR02638 250 AGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAEFTGEKYREIAKAMGVKTEGMSDEEARDAAVEAVKT 329
|
330
....*....|....
gi 2524884235 349 LNTRLGVPDVLDTL 362
Cdd:TIGR02638 330 LSKRVGIPEGLSEL 343
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
33-356 |
2.85e-96 |
|
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: 292.88 E-value: 2.85e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 33 NGQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVL 112
Cdd:cd08193 9 CGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAGADGVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 113 AIGGGSSIDCAKTIASAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPaSHEKCFLADPKMLPKAV 192
Cdd:cd08193 89 GFGGGSSMDVAKLVALLAGSDQPLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIVTTG-ETEKKGVVSPQLLPDVA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 193 ALDADLLLGMPAPITAATGMDALTHAVETYIS-LWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGM 271
Cdd:cd08193 168 LLDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDALAREALRLLGANLRRAVEDGSDLEAREAMLLGSMLAGQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 272 AINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKFIDAVADLNT 351
Cdd:cd08193 248 AFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVE 327
|
....*
gi 2524884235 352 RLGVP 356
Cdd:cd08193 328 ASGLP 332
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
34-359 |
9.27e-96 |
|
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: 291.71 E-value: 9.27e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLcRHIARQGAQRVLIVSDKI-LVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVL 112
Cdd:cd08185 10 GAGKLNEL-GEEALRPGKKALIVTGKGsSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGCDFVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 113 AIGGGSSIDCAKTIASAATNGRD------GRKleGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPK 186
Cdd:cd08185 89 GLGGGSSMDAAKAIAFMATNPGDiwdyifGGT--GKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKKGIGHPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 187 MLPKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAA 266
Cdd:cd08185 167 LFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEAREKMAWAS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 267 YYAGMAINDAGVGNVHAIAHQLGRHYG-TPHGLANALVMPEVLRFMAKASEKPLAELGRligVADASTGDAQAAEKFIDA 345
Cdd:cd08185 247 TLAGIVIANSGTTLPHGLEHPLSGYHPnIPHGAGLAALYPAYFEFTIEKAPEKFAFVAR---AEASGLSDAKAAEDFIEA 323
|
330
....*....|....
gi 2524884235 346 VADLNTRLGVPDVL 359
Cdd:cd08185 324 LRKLLKDIGLDDLL 337
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
51-348 |
1.25e-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: 284.39 E-value: 1.25e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 51 QRVLIVSDKILVELGIVGKAVDVLKEeGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLAIGGGSSIDCAKTIasaa 130
Cdd:cd08180 23 KRVFIVTDPFMVKSGMVDKVTDELDK-SNEVEIFSDVVPDPSIEVVAKGLAKILEFKPDTIIALGGGSAIDAAKAI---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 131 tngrdgrKLEGYFKVKTMPLPLF-ALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAVALDADLLLGMPAPITAA 209
Cdd:cd08180 98 -------IYFALKQKGNIKKPLFiAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSMLPDIAILDPELVKSVPPKVTAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 210 TGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMAINDAGVGNVHAIAHQLG 289
Cdd:cd08180 171 TGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNASCMAGIAFNNAGLGINHSLAHALG 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2524884235 290 RHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTgDAQAAEKFIDAVAD 348
Cdd:cd08180 251 GRFHIPHGRANAILLPYVIEFLIAAIRRLNKKLGIPSTLKELGI-DEEEFEKAIDEMAE 308
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
34-357 |
6.30e-93 |
|
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: 284.39 E-value: 6.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGaQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGIlPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd08183 7 GRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVS-GEPTVETVDAAVALAREAGCDVVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRD-GRKLEGY---FKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLP 189
Cdd:cd08183 85 IGGGSVIDAAKAIAALLTNEGSvLDYLEVVgkgRPLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLRSPSMLP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 190 KAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYA 269
Cdd:cd08183 165 DVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 270 GMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIG---VADASTGDAQA-AEKFIDA 345
Cdd:cd08183 245 GLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRALREREPDSPALARyreLAGILTGDPDAaAEDGVEW 324
|
330
....*....|..
gi 2524884235 346 VADLNTRLGVPD 357
Cdd:cd08183 325 LEELCEELGIPR 336
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
23-356 |
3.57e-92 |
|
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: 282.19 E-value: 3.57e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 23 LMPSLAYmafnGQGSTAQLCRHIARqgaqRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLAL 102
Cdd:cd14862 5 SSPKIVF----GEDALSHLEQLSGK----RALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 103 QQQHKCDAVLAIGGGSSIDCAKtiASAATNGRDGRKLE-------GYFKVKTMplpLFALPTTSGTGSEATIAAVVSDPA 175
Cdd:cd14862 77 MREFEPDLIIALGGGSVMDAAK--AAWVLYERPDLDPEdispldlLGLRKKAK---LIAIPTTSGTGSEATWAIVLTDTE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 176 SHEKCFLADPKMLPKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGND 255
Cdd:cd14862 152 EPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 256 AEAREQMALAAYYAGMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADAstgD 335
Cdd:cd14862 232 LEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKLLGIEARD---E 308
|
330 340
....*....|....*....|.
gi 2524884235 336 AQAAEKFIDAVADLNTRLGVP 356
Cdd:cd14862 309 EEALKKLVEAIRELYKEVGQP 329
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
34-356 |
3.66e-90 |
|
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: 277.15 E-value: 3.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTaqlcRHIARQGAQRVLIVSDK-ILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVL 112
Cdd:cd08179 11 GEGAL----EYLKTLKGKRAFIVTGGgSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDWII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 113 AIGGGSSIDCAKTIASAATNgrDGRKLEGYFKVKTMPLP-----LFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKM 187
Cdd:cd08179 87 AIGGGSVIDAAKAMWVFYEY--PELTFEDALVPFPLPELrkkarFIAIPSTSGTGSEVTRASVITDTEKGIKYPLASFEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 188 LPKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAY 267
Cdd:cd08179 165 TPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKDLEAREKMHNASC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 268 YAGMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVAdastgDAQAAEKFIDAVA 347
Cdd:cd08179 245 LAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAALLIGLT-----DEELVEDLIEAIE 319
|
....*....
gi 2524884235 348 DLNTRLGVP 356
Cdd:cd08179 320 ELNKKLGIP 328
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
34-356 |
4.11e-90 |
|
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: 276.77 E-value: 4.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVEcvIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd08196 12 GEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVA--VFSDVEPNPTVENVDKCARLARENGADFVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRDGRK-LEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAV 192
Cdd:cd08196 90 IGGGSVLDTAKAAACLAKTDGSIEDyLEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLVSPGFYPDIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 193 ALDADLLLGMPAPITAATGMDALTHAVETYislWGTES---SNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYA 269
Cdd:cd08196 170 IVDPELTYSMPPKVTASTGIDALCHAIEAY---WSINHqpiSDALALEAAKLVLENLEKAYNNPNDKEAREKMALASLLA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 270 GMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADastgdaqaAEKFIDAVADL 349
Cdd:cd08196 247 GLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQLGFKD--------AEELADKIEEL 318
|
....*..
gi 2524884235 350 NTRLGVP 356
Cdd:cd08196 319 KKRIGLR 325
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
31-359 |
2.28e-89 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 275.34 E-value: 2.28e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 31 AFNGQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDA 110
Cdd:PRK10624 11 AYFGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 111 VLAIGGGSSIDCAKTIASAATNGR--DGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKML 188
Cdd:PRK10624 91 LIAIGGGSPQDTCKAIGIISNNPEfaDVRSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 189 PKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRdgNDAEAREQMALAAYY 268
Cdd:PRK10624 171 PQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVA--GDKEAGEGMALGQYI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 269 AGMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKFIDAVAD 348
Cdd:PRK10624 249 AGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVKVEGMSLEEARNAAVEAVKA 328
|
330
....*....|.
gi 2524884235 349 LNTRLGVPDVL 359
Cdd:PRK10624 329 LNRDVGIPPHL 339
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
34-359 |
2.45e-89 |
|
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: 274.81 E-value: 2.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd17814 10 GVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRDGRKLEGYFKVkTMPL-PLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAV 192
Cdd:cd17814 90 VGGGSPIDCAKGIGIVVSNGGHILDYEGVDKV-RRPLpPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 193 ALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMA 272
Cdd:cd17814 169 LIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMMLASLQAGLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 273 INDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKFIDAVADLNTR 352
Cdd:cd17814 249 FSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLRED 328
|
....*..
gi 2524884235 353 LGVPDVL 359
Cdd:cd17814 329 LGIPETL 335
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
34-362 |
2.60e-88 |
|
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: 272.95 E-value: 2.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGaQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd08191 10 GPGARRALGRVAARLG-SRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDPDVVIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAVA 193
Cdd:cd08191 89 LGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRPAVAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 194 LDADLLLGMPAPITAATGMDALTHAVETYISL---WGTESSNGYGYA------------AVKMIFDYLPRAYRDGNDAEA 258
Cdd:cd08191 169 VDPELTLTCPPGVTADSGIDALTHAIESYTARdfpPFPRLDPDPVYVgknpltdllaleAIRLIGRHLPRAVRDGDDLEA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 259 REQMALAAYYAGMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAqA 338
Cdd:cd08191 249 RSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVTTAGTSEE-A 327
|
330 340
....*....|....*....|....
gi 2524884235 339 AEKFIDAVADLNTRLGVPDVLDTL 362
Cdd:cd08191 328 ADRAIERVEELLARIGIPTTLADL 351
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
49-356 |
2.31e-86 |
|
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: 268.29 E-value: 2.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 49 GAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLAIGGGSSIDCAKTI-- 126
Cdd:cd08178 22 GVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFKPDVIIALGGGSAMDAAKIMwl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 127 ---------ASAATNGRDGRKLegYFKVKTMPLP--LFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAVALD 195
Cdd:cd08178 102 fyehpetkfEDLAQRFMDIRKR--VYKFPKLGKKakLVAIPTTSGTGSEVTPFAVITDDKTGKKYPLADYALTPDMAIVD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 196 ADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMAIND 275
Cdd:cd08178 180 PELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGNDIEAREKMHNAATIAGMAFAN 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 276 AGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKA----------SEKPLA-----ELGRLIGVADAStgDAQAAE 340
Cdd:cd08178 260 AFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDpptkqaafpqYKYYVAkeryaEIADLLGLGGKT--PEEKVE 337
|
330
....*....|....*.
gi 2524884235 341 KFIDAVADLNTRLGVP 356
Cdd:cd08178 338 SLIKAIEDLKKDLGIP 353
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
34-356 |
4.66e-86 |
|
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: 266.40 E-value: 4.66e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEgVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd08182 7 GPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDALGGR-IPVVVFSDFSPNPDLEDLERGIELFRESGPDVIIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRD--GRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKA 191
Cdd:cd08182 86 VGGGSVIDTAKAIAALLGSPGEnlLLLRTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPSLYPDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 192 VALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGM 271
Cdd:cd08182 166 AILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEASLLAGL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 272 AINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKFIDAvadLNT 351
Cdd:cd08182 246 AISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDECDDDPRGREILLALGASDPAEAAERLRA---LLE 322
|
....*
gi 2524884235 352 RLGVP 356
Cdd:cd08182 323 SLGLP 327
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
34-397 |
8.73e-86 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 266.05 E-value: 8.73e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:PRK09860 15 GADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVIS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAVA 193
Cdd:PRK09860 95 LGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 194 LDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMAI 273
Cdd:PRK09860 175 NDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAGMAF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 274 NDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKFIDAVADLNTRL 353
Cdd:PRK09860 255 NNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKV 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2524884235 354 GVPDVLDTLREEDI--AAIAADAVKEGAGYPVPVLMSRKECQAILR 397
Cdd:PRK09860 335 DIPAGLRDLNVKEEdfAVLATNALKDACGFTNPIQATHEEIVAIYR 380
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
34-362 |
8.73e-84 |
|
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: 262.10 E-value: 8.73e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd08190 7 GPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRD-----------GRKLEGYFKvktmplPLFALPTTSGTGSEATIAAVVSDPASHEKCFL 182
Cdd:cd08190 87 VGGGSVIDTAKAANLYATHPGDfldyvnapigkGKPVPGPLK------PLIAIPTTAGTGSETTGVAIFDLEELKVKTGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 183 ADPKMLPKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTES------------------SNGYGYAAVKMIFD 244
Cdd:cd08190 161 SSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNARprpanpderpayqgsnpiSDVWAEKAIELIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 245 YLPRAYRDGNDAEAREQMALAAYYAGMAINDAGVGNVHAIAHQLG-------------RHYGTPHGLANALVMPEVLRFM 311
Cdd:cd08190 241 YLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAglvkdyrppgypvDHPHVPHGLSVALTAPAVFRFT 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2524884235 312 AKASEKPLAELGRLIGVADASTGDAQAAEKFIDAVADLNTRLGVPDVLDTL 362
Cdd:cd08190 321 APACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSAL 371
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
49-356 |
2.09e-81 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 267.05 E-value: 2.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 49 GAQRVLIVSDKILVELGIVGKAVDVLK--EEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLAIGGGSSIDCAKTI 126
Cdd:PRK13805 479 GKKRAFIVTDRFMVELGYVDKVTDVLKkrENGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIM 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 127 -----------ASAATNGRDGRKLegYFKVKTMP--LPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAVA 193
Cdd:PRK13805 559 wlfyehpetdfEDLAQKFMDIRKR--IYKFPKLGkkAKLVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDVAI 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 194 LDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDG-NDAEAREQMALAAYYAGMA 272
Cdd:PRK13805 637 VDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGaKDPEAREKMHNASTIAGMA 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 273 INDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKP--------------LAELGRLIGVAdASTgDAQA 338
Cdd:PRK13805 717 FANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDPPKQaafpqyeypraderYAEIARHLGLP-GST-TEEK 794
|
330
....*....|....*...
gi 2524884235 339 AEKFIDAVADLNTRLGVP 356
Cdd:PRK13805 795 VESLIKAIEELKAELGIP 812
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
34-356 |
1.15e-69 |
|
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: 224.62 E-value: 1.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGaQRVLIVSDK--IlVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAV 111
Cdd:cd08187 13 GKGAIEELGEEIKKYG-KKVLLVYGGgsI-KKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVDFI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 112 LAIGGGSSIDCAKTIASAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKA 191
Cdd:cd08187 91 LAVGGGSVIDAAKAIAAGAKYDGDVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLRPKF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 192 VALDADLLLGMPAPITAATGMDALTHAVETYISL-WGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYyag 270
Cdd:cd08187 171 SILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGtEDAPLQDRLAEGLLRTVIENGPKALKDPDDYEARANLMWAAT--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 271 MAIND---AGVGN---VHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLI-GVaDASTGDAQAAEKFI 343
Cdd:cd08187 248 LALNGllgAGRGGdwaTHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRVfGI-DPGGDDEETALEGI 326
|
330
....*....|...
gi 2524884235 344 DAVADLNTRLGVP 356
Cdd:cd08187 327 EALEEFFKSIGLP 339
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
24-330 |
1.24e-64 |
|
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: 210.52 E-value: 1.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 24 MPSLAYMafnGQGSTAQLCRHIARQGaQRVLIV----SDKilvELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEG 99
Cdd:cd08181 3 MPTKVYF---GKNCVEKHADELAALG-KKALIVtgkhSAK---KNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 100 LALQQQHKCDAVLAIGGGSSIDCAKTIASAATNGRDGRKLegYFKVKTM-PLPLFALPTTSGTGSEATIAAVVSDPASHE 178
Cdd:cd08181 76 AELARKEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDL--FQNGKYNpPLPIVAIPTTAGTGSEVTPYSILTDHEKGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 179 KCFLADPKMLPKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEA 258
Cdd:cd08181 154 KKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDELDEED 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524884235 259 REQMALAAYYAGMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVAD 330
Cdd:cd08181 234 REKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLGFGS 305
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
34-354 |
2.22e-53 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 182.53 E-value: 2.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:PRK15454 33 GPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAVA 193
Cdd:PRK15454 113 FGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASLMPDVAI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 194 LDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMAI 273
Cdd:PRK15454 193 LDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESMLLASCMAGMAF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 274 NDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKFIDAVADLNTRL 353
Cdd:PRK15454 273 SSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRALRTKKSDDRDAINAVSELIAEVGIGKRL 352
|
.
gi 2524884235 354 G 354
Cdd:PRK15454 353 G 353
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
46-356 |
3.20e-52 |
|
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: 179.03 E-value: 3.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 46 ARQGAQRVLIVSDKILVELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLAIGGGSSIDCAKT 125
Cdd:cd14864 21 VKEYGSRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAGADGIIAVGGGKVLDTAKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 126 IASAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLPKAVALDADLLLGMPAP 205
Cdd:cd14864 101 VAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKAQPGLPKAVIVDPNLMASLTGN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 206 ITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYYAGMAINDAGVGNVHAIA 285
Cdd:cd14864 181 QTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEELLAQAGCLAGLAASSSSPGLATALA 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524884235 286 HQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADASTGDAQAAEKFIDAVADLNTRLGVP 356
Cdd:cd14864 261 LAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLP 331
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
34-356 |
5.50e-52 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 178.34 E-value: 5.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAqRVLIV----SDKilvELGIVGKAVDVLKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCD 109
Cdd:COG1979 15 GKGQIAKLGEEIPKYGK-KVLLVygggSIK---KNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGID 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 110 AVLAIGGGSSIDCAKTIASAATNGRDgrkLEGYFKVKTMP---LPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPK 186
Cdd:COG1979 91 FILAVGGGSVIDGAKAIAAGAKYDGD---PWDILTGKAPVekaLPLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 187 MLPKAVALDADLLLGMPAPITAATGMDALTHAVETYISL-WGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALA 265
Cdd:COG1979 168 VFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYpVDAPLQDRFAEGLLRTLIEEGPKALKDPEDYDARANLMWA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 266 AYyagMAIND---AGVGN---VHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLI-GVADAStgDAQA 338
Cdd:COG1979 248 AT---LALNGligAGVPQdwaTHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAERVwGITEGD--DEER 322
|
330
....*....|....*...
gi 2524884235 339 AEKFIDAVADLNTRLGVP 356
Cdd:COG1979 323 ALEGIEATEEFFESLGLP 340
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
34-359 |
7.41e-51 |
|
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: 175.51 E-value: 7.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVEL-GIVGKAVDVLKEEGVEcvIYDGILPDPTFAMVDEGLALQQQHKCDAVL 112
Cdd:cd08192 7 GPGAVEALLHELATLGASRVFIVTSKSLATKtDVIKRLEEALGDRHVG--VFSGVRQHTPREDVLEAARAVREAGADLLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 113 AIGGGSSIDCAKTIASA-ATNGRDGRKLEGYF-------KVKTMPLPLFALPTT-SGtgSEATIAAVVSDPASHEKCFLA 183
Cdd:cd08192 85 SLGGGSPIDAAKAVALAlAEDVTDVDQLDALEdgkridpNVTGPTLPHIAIPTTlSG--AEFTAGAGATDDDTGHKQGFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 184 DPKMLPKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMA 263
Cdd:cd08192 163 HPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADPEDLEARLKCQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 264 LAAYYAGMA-INDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGvaDASTGDAQAAEKF 342
Cdd:cd08192 243 LAAWLSLFGlGSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALG--LVTGGLGREAADA 320
|
330
....*....|....*..
gi 2524884235 343 IDAVADLNTRLGVPDVL 359
Cdd:cd08192 321 ADAIDALIRELGLPRTL 337
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
34-359 |
8.67e-51 |
|
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: 175.15 E-value: 8.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILvelGIVGKAVDV----LKEEGVECVIYDGILPDPTFAMVDEGLALQQQHKCD 109
Cdd:cd08186 7 GVGAIAKIKDILKDLGIDKVIIVTGRSS---YKKSGAWDDvekaLEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 110 AVLAIGGGSSIDCAKTIAS-AATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKML 188
Cdd:cd08186 84 AVIAIGGGSPIDTAKSVAVlLAYGGKTARDLYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 189 PKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYY 268
Cdd:cd08186 164 PLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYASMI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 269 AGMAINDAGVGNVHAIAHQL-GRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIgvADASTGDAQAAEKFIDAVA 347
Cdd:cd08186 244 AGIAIDNGLLHLTHALEHPLsGLKPELPHGLGLALLGPAVVKYIYKAVPETLADILRPI--VPGLKGTPDEAEKAARGVE 321
|
330
....*....|..
gi 2524884235 348 DLNTRLGVPDVL 359
Cdd:cd08186 322 EFLFSVGFTEKL 333
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
32-359 |
6.39e-50 |
|
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: 172.80 E-value: 6.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 32 FNGQGSTAQLCRHIARQGAQRVLIVSDKilvELGIVGKAVDVLKEE-GVECV-IYDGILPDPTFAMVDEGLALQQQHKCD 109
Cdd:cd14866 9 FSGRGALARLGRELDRLGARRALVVCGS---SVGANPDLMDPVRAAlGDRLAgVFDGVRPHSPLETVEAAAEALREADAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 110 AVLAIGGGSSIDCAKTIASAATNGRDGRKL------EGYFKVKTMP---LPLFALPTTSGTGSEATIAAVvSDPASHEKC 180
Cdd:cd14866 86 AVVAVGGGSAIVTARAASILLAEDRDVRELctrraeDGLMVSPRLDapkLPIFVVPTTPTTADVKAGSAV-TDPPAGQRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 181 FLADPKMLPKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYLPRAyRDGNDAEARE 260
Cdd:cd14866 165 ALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRL-ADDDDPAARA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 261 QMALAAYYAGMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADAstGDAQAAE 340
Cdd:cd14866 244 DLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGVADA--GDEASAA 321
|
330
....*....|....*....
gi 2524884235 341 KFIDAVADLNTRLGVPDVL 359
Cdd:cd14866 322 AVVDAVEALLDALGVPTRL 340
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
34-362 |
1.06e-46 |
|
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: 163.06 E-value: 1.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELgivgkAVDVLKEEGVECV-IYDGILPDPTFAMVDEGLALQQQHKCDAVL 112
Cdd:cd08177 7 GAGTLAELAEELERLGARRALVLSTPRQRAL-----AERVAALLGDRVAgVFDGAVMHVPVEVAERALAAAREAGADGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 113 AIGGGSSIDCAKTIAsaatngrdgrklegyfkvKTMPLPLFALPTTSgTGSEAT-IAAVVSDpasHEKCFLADPKMLPKA 191
Cdd:cd08177 82 AIGGGSAIGLAKAIA------------------LRTGLPIVAVPTTY-AGSEMTpIWGETED---GVKTTGRDPRVLPRT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 192 VALDADLLLGMPAPITAATGMDALTHAVEtyiSLWGTESS---NGYGYAAVKMIFDYLPRAYRDGNDAEAREQMALAAYY 268
Cdd:cd08177 140 VIYDPDLTLGLPAALSVASGLNALAHAVE---ALYAPDANpitSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 269 AGMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLIGVADAstgdaqaaekfIDAVAD 348
Cdd:cd08177 217 AGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGGGDA-----------AGGLYD 285
|
330
....*....|....
gi 2524884235 349 LNTRLGVPDVLDTL 362
Cdd:cd08177 286 LARRLGAPTSLRDL 299
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
91-327 |
1.03e-43 |
|
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: 156.22 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 91 PTFAMVDEGLALQQQHKCDAVLAIGGGSSIDCAKTIASaatngRDGRKLEGYFKVKtMPL----PLFALPTTSGTGSEAT 166
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLAL-----KGISPVLDLFDGK-IPLikekELIIVPTTCGTGSEVT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 167 IAAVVSDPASHEKCFLADPKMLPKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTESSNGYGYAAVKMIFDYL 246
Cdd:cd14860 136 NISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEGY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 247 PRAYRDGNDA--EAREQMALAAYYAGMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRF-MAKASEKPLAELG 323
Cdd:cd14860 216 QEIAEKGEEArfPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNyQEKNPDGEIKKLN 295
|
....
gi 2524884235 324 RLIG 327
Cdd:cd14860 296 EFLA 299
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
34-326 |
1.94e-29 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 115.15 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLcRHIARQGAQRVLIVSDKILVElGIVGKAVDVLKEeGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:cd07766 7 GEGAIAKL-GEIKRRGFDRALVVSDEGVVK-GVGEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAEADAVIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIASAATNGrdgrklegyfkvktmpLPLFALPTTSGTGSEATIAAVVSDPASHEKcfLADPKMLPKAVA 193
Cdd:cd07766 84 VGGGSTLDTAKAVAALLNRG----------------IPFIIVPTTASTDSEVSPKSVITDKGGKNK--QVGPHYNPDVVF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 194 LDADLLLGMPAPITAATGMDALTHAVEtyislwgtessngygyaavkmifdylprayrdgndaeaREQMALAAYYAGMAI 273
Cdd:cd07766 146 VDTDITKGLPPRQVASGGVDALAHAVE--------------------------------------LEKVVEAATLAGMGL 187
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2524884235 274 -NDAGVGNVHAIAHQLGRHYGTPHGLANALVMPEVLRFMAKASEKPLAELGRLI 326
Cdd:cd07766 188 fESPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPEPEAAIEAVF 241
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
34-312 |
3.52e-27 |
|
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: 110.82 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQR---VLIVSDKILVELGIVgkavDVLKEEGVECVIYDGILPDPTFAMVDEGLA--LQQQHKC 108
Cdd:cd08184 7 GRGSFDQLGELLAERRKSNndyVVFFIDDVFKGKPLL----DRLPLQNGDLLIFVDTTDEPKTDQIDALRAqiRAENDKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 109 -DAVLAIGGGSSIDCAKTIASAATNGRDGRKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPAshEKCFLADPKM 187
Cdd:cd08184 83 pAAVVGIGGGSTMDIAKAVSNMLTNPGSAADYQGWDLVKNPGIYKIGVPTLSGTGAEASRTAVLTGPE--KKLGINSDYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 188 LPKAVALDADLLLGMPAPITAATGMDALTHAVEtyiSLWGT---ESSNGYGYAAVKMIFD-YLpraYRDGNDAEAREQMA 263
Cdd:cd08184 161 VFDQVILDPELIATVPRDQYFYTGMDCYIHCVE---SLNGTyrnAFGDAYAEKALELCRDvFL---SDDMMSPENREKLM 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2524884235 264 LAAYYAGMAINDAGVGNVHAIAHQLGRHYGTPHGLANALVM--------PEVLRFMA 312
Cdd:cd08184 235 VASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCIVFnvleefypEGVKEFRE 291
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
34-356 |
2.91e-18 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 85.62 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGaqRVLIV-SDKILVELGIVGKAVDVLKeeGVECVIYDGILPDPTFAMVDEGLALQQQHKCDAVL 112
Cdd:PRK15138 15 GKGAIAGLREQIPADA--RVLITyGGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPTYETLMKAVKLVREEKITFLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 113 AIGGGSSIDCAKTIASAA--TNGRDG-RKLEGYFKVKTMPLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMLP 189
Cdd:PRK15138 91 AVGGGSVLDGTKFIAAAAnyPENIDPwHILETGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGDKQAFHSPHVQP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 190 KAVALDADLLLGMPAPITAATGMDALTHAVETYIslwgTESSNG-----YGYAAVKMIFDYLPRAYRDGNDAEAREQMAL 264
Cdd:PRK15138 171 VFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYV----TYPVDAkiqdrFAEGILLTLIEEGPKALKEPENYDVRANVMW 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 265 AAYYAGMAINDAGVGN---VHAIAHQLGRHYGTPHGLANALVMPEVLRFM-AKASEKPLAELGRLIGVADAStgDAQAAE 340
Cdd:PRK15138 247 AATQALNGLIGAGVPQdwaTHMLGHELTAMHGLDHAQTLAIVLPALWNEKrDTKRAKLLQYAERVWNITEGS--DDERID 324
|
330
....*....|....*.
gi 2524884235 341 KFIDAVADLNTRLGVP 356
Cdd:PRK15138 325 AAIAATRNFFEQMGVP 340
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
34-298 |
3.01e-13 |
|
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: 70.20 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGaQRVLIVSDKILveLGIVGKAV-DVLKEEGVE--CVIYDGilpDPTFAMVDEGLALQQQHKCDA 110
Cdd:COG0371 12 GEGALDELGEYLADLG-KRALIITGPTA--LKAAGDRLeESLEDAGIEveVEVFGG---ECSEEEIERLAEEAKEQGADV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 111 VLAIGGGSSIDCAKTIAsaatngrdgrklegyFKVKtmpLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMlPK 190
Cdd:COG0371 86 IIGVGGGKALDTAKAVA---------------YRLG---LPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKN-PD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 191 AVALDADLLLGMPAPITAAtGM-DALthAVETYISLW-------GTESSNGYGYAAVKM----IFDYLPRAYRD---GND 255
Cdd:COG0371 147 LVLVDTDIIAKAPVRLLAA-GIgDAL--AKWYEARDWslahrdlAGEYYTEAAVALARLcaetLLEYGEAAIKAveaGVV 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2524884235 256 AEAREQMALAA-YYAGMAIN----DAGVGNVHAIAHQLGRHYGTPHGL 298
Cdd:COG0371 224 TPALERVVEANlLLSGLAMGigssRPGSGAAHAIHNGLTALPETHHAL 271
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
32-286 |
3.50e-09 |
|
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: 57.93 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 32 FNGQGSTAQLCRHIARQGaQRVLIVSDKIlvELGIVGKAV-DVLKEEGV--ECVIYDGilpDPTFAMVDEGLALQQQHKC 108
Cdd:cd08550 5 IQEPGILAKAGEYIAPLG-KKALIIGGKT--ALEAVGEKLeKSLEEAGIdyEVEVFGG---ECTEENIERLAEKAKEEGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 109 DAVLAIGGGSSIDCAKTIASAATngrdgrklegyfkvktmpLPLFALPTTSGTGSEATIAAVVSDPASHEKCFLADPKMl 188
Cdd:cd08550 79 DVIIGIGGGKVLDTAKAVADRLG------------------LPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRS- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 189 PKAVALDADLLLGMPAPITAATGMDALTHAVETYISLWGTEsSNGYGYAAVKM-------IFDYLPRAYRD---GNDAEA 258
Cdd:cd08550 140 PDLVLVDTDIIAAAPVRYLAAGIGDTLAKWYEARPSSRGGP-DDLALQAAVQLaklaydlLLEYGVQAVEDvrqGKVTPA 218
|
250 260 270
....*....|....*....|....*....|
gi 2524884235 259 REQMALAA-YYAGMaINDAGVGNVH-AIAH 286
Cdd:cd08550 219 LEDVVDAIiLLAGL-VGSLGGGGCRtAAAH 247
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
24-128 |
1.51e-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: 52.94 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 24 MPSLAYMAFNGQGSTAQLCRHIarQGAQRVLIVSDKILVElgIVGKAV-DVLKEEGVECVIYDGILPDpTFAMVDEGLAL 102
Cdd:cd08173 1 LPRNVVVGHGAINKIGEVLKKL--LLGKRALIITGPNTYK--IAGKRVeDLLESSGVEVVIVDIATIE-EAAEVEKVKKL 75
|
90 100
....*....|....*....|....*.
gi 2524884235 103 QQQHKCDAVLAIGGGSSIDCAKTIAS 128
Cdd:cd08173 76 IKESKADFIIGVGGGKVIDVAKYAAY 101
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
69-265 |
1.68e-05 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341450 Cd Length: 345 Bit Score: 46.36 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 69 KAVDVLKE--EGVECVIYDGIL--PDPTFAMVDEGLALQQQHKCDAVLAIGGGSSIDCAKTIAsaatnGRDGRklegyfk 144
Cdd:cd08171 36 AAKPKLRAalEGSGLEITDFIWygGEATYENVEKLKANPEVQEADMIFAVGGGKAIDTVKVLA-----DRLNK------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 145 vktmplPLFALPTTSGTGSEATIAAVVSDPaSHEKCFLADPKMLPKAVALDADLLLGMPAPITAAtGM-DALTHAVETYI 223
Cdd:cd08171 104 ------PVFTFPTIASNCAAVTAVSVMYNP-DGSFKEYYFLKRPPVHTFIDTEIIAEAPEKYLWA-GIgDTLAKYYEVEF 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2524884235 224 SLWGTES--SNGYGYAAVKM----IFDYLPRAYRD---GNDAEAREQMALA 265
Cdd:cd08171 176 SARGDELdhTNALGVAISKMcsepLLKYGVQALEDcraNKVSDALEQVVLD 226
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
34-127 |
2.73e-05 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 45.96 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGaQRVLIVSDKILveLGIVGKAVD-VLKEEGVECVI--YDGilpDPTFAMVDEGLALQQQHKCDA 110
Cdd:PRK09423 14 GKGALARLGEYLKPLG-KRALVIADEFV--LGIVGDRVEaSLKEAGLTVVFevFNG---ECSDNEIDRLVAIAEENGCDV 87
|
90
....*....|....*..
gi 2524884235 111 VLAIGGGSSIDCAKTIA 127
Cdd:PRK09423 88 VIGIGGGKTLDTAKAVA 104
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
34-127 |
4.97e-05 |
|
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: 45.09 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGaQRVLIVSDKILveLGIVGKAV-DVLKEEGVEC--VIYDGILpdpTFAMVDEGLALQQQHKCDA 110
Cdd:cd08170 7 GPGALDRLGEYLAPLG-KKALVIADPFV--LDLVGERLeESLEKAGLEVvfEVFGGEC---SREEIERLAAIARANGADV 80
|
90
....*....|....*..
gi 2524884235 111 VLAIGGGSSIDCAKTIA 127
Cdd:cd08170 81 VIGIGGGKTIDTAKAVA 97
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
36-127 |
9.00e-05 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 44.11 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 36 GSTAQLCRHIARQGaqRVLIVSDKILVElgIVGKAV-DVLKEEG-VECVIYDgilpDPTFAMVDEGLALQQQHKCDAVLA 113
Cdd:PRK00843 22 DDIGDVCSDLKLTG--RALIVTGPTTKK--IAGDRVeENLEDAGdVEVVIVD----EATMEEVEKVEEKAKDVNAGFLIG 93
|
90
....*....|....
gi 2524884235 114 IGGGSSIDCAKTIA 127
Cdd:PRK00843 94 VGGGKVIDVAKLAA 107
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
34-225 |
6.86e-04 |
|
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with 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. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.
Pssm-ID: 341479 [Multi-domain] Cd Length: 331 Bit Score: 41.40 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 34 GQGSTAQLCRHIARQGAQRVLIVSDKILVELgiVGKAVDVLKEEGVECVIYDGILpdptfAMVDEglaLQQQHKCDAVLA 113
Cdd:cd08549 7 GDGAINKIEEILKKLNLKRVLIITGKNTKAK--YCRFFYDQLKTVCDIVYYDNID-----NLEDE---LKKYTFYDCVIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 114 IGGGSSIDCAKTIAsaatngrdgrklegyFKVKtmpLPLFALPTTSGTGSEATIAAVVSDPaSHEKCFLADPkmlPKAVA 193
Cdd:cd08549 77 IGGGRSIDTGKYLA---------------YKLK---IPFISVPTSASNDGIASPIVSLRIP-GVKKTFMADA---PIAII 134
|
170 180 190
....*....|....*....|....*....|..
gi 2524884235 194 LDADLLLGMPAPITAAtGMDALthaVETYISL 225
Cdd:cd08549 135 ADTEIIKKSPRRLLSA-GIGDL---VSNITAV 162
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
46-130 |
2.28e-03 |
|
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: 39.81 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 46 ARQGAQRVLIVSDKILVELgIVGKAVDVLKEEGVECVIYDGilpdpTFAMVDE-GLALQQQHKCDAVLAIGGGSSIDCAK 124
Cdd:cd08174 21 RNQGFGKVAIVTGEGIDEL-LGEDILESLEEAGEIVTVEEN-----TDNSAEElAEKAFSLPKVDAIVGIGGGKVLDVAK 94
|
....*.
gi 2524884235 125 TIASAA 130
Cdd:cd08174 95 YAAFLS 100
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
32-127 |
7.54e-03 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 38.27 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524884235 32 FNGQGSTAQLCRHIARQGAQRVLIVSDKILVElgIVGKAVDVLKEEGVECVIYDGILpdpTFAMVDEgLALQ-QQHKCDA 110
Cdd:cd08172 5 ICEEGALKELPELLSEFGIKRPLIIHGEKSWQ--AAKPYLPKLFEIEYPVLRYDGEC---SYEEIDR-LAEEaKEHQADV 78
|
90
....*....|....*..
gi 2524884235 111 VLAIGGGSSIDCAKTIA 127
Cdd:cd08172 79 IIGIGGGKVLDTAKAVA 95
|
|
| |
