|
Name |
Accession |
Description |
Interval |
E-value |
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-380 |
3.34e-173 |
|
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: 487.39 E-value: 3.34e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 4 FYQPSRINFGQGTLSELPRIIGKYGKKCLLVTTPNVEPLDKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAK 83
Cdd:cd08185 1 YYQPTRILFGAGKLNELGEEALRPGKKALIVTGKGSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 84 KESVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYMFSTYTNPfkiydKVSEKELPLIAVSTTSGTGSQVTQAAVISRG- 162
Cdd:cd08185 81 EEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYIFGGTGKG-----PPPEKALPIIAIPTTAGTGSEVDPWAVITNPe 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 163 -SEKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKNN 241
Cdd:cd08185 156 tKEKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 242 IEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVT-HIPHGEALAIVFPKFAEKFYKDNIEKFAKVARMlnqELEKVE 320
Cdd:cd08185 236 LEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVARA---EASGLS 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489535278 321 DDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQITSCP--VLGFL----P-FGKKEDLVEILE 380
Cdd:cd08185 313 DAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAmeTMGGLfannPvELTEEDIVEIYE 379
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
7-358 |
4.00e-127 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 370.01 E-value: 4.00e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGKYGKKCLLVTTPNVEPLDkLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKKES 86
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLKSG-LLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 87 VDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYMFStytnpfkiyDKVSEKELPLIAVSTTSGTGSQVTQAAVISR--GSE 164
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGG---------KPLTKPALPLIAIPTTAGTGSEVTPLAVITDteTGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 165 KNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKNNIEY 244
Cdd:pfam00465 151 KLGIFSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 245 RTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKVARMLNQElekvEDDEA 324
Cdd:pfam00465 231 RENMLLASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGED----SDEEA 306
|
330 340 350
....*....|....*....|....*....|....
gi 489535278 325 AKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQI 358
Cdd:pfam00465 307 AEEAIEALRELLRELGLPTTLSELGVTEEDLDAL 340
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-383 |
4.60e-125 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 365.21 E-value: 4.60e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 1 MINFYQPSRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVEPLDkLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGF 79
Cdd:COG1454 2 MFTFRLPTRIVFGAGALAELGEELKRLGaKRALIVTDPGLAKLG-LLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 80 ELAKKESVDVVLAVGGGSSIDTAKVLALTfglekidwdymfstYTNPFKIYD-----KVSEKELPLIAVSTTSGTGSQVT 154
Cdd:COG1454 81 AAAREFGADVVIALGGGSAIDAAKAIALL--------------ATNPGDLEDylgikKVPGPPLPLIAIPTTAGTGSEVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 155 QAAVISRGS--EKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYL 232
Cdd:COG1454 147 PFAVITDPEtgVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 233 PKVMEDKNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKVARML 312
Cdd:COG1454 227 PRAVADGDDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARAL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489535278 313 NQELEKvEDDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQI------TSCpvLGFLPFG-KKEDLVEILEKSY 383
Cdd:COG1454 307 GLDVGL-SDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELaelalaDRC--LANNPRPlTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
7-358 |
1.31e-118 |
|
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: 348.67 E-value: 1.31e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVEPLDkLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKKE 85
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGgKKVLLVTDPGLVKAG-LLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 86 SVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYMfstytnpfkIYDKVSEKELPLIAVSTTSGTGSQVTQAAVISRGSE- 164
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYE---------GIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 165 -KNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKNNIE 243
Cdd:cd08551 151 rKMGIVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 244 YRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPkFAEKFYKD-NIEKFAKVARMLNQELEKVEDD 322
Cdd:cd08551 231 AREAMLLASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLP-YVMEFNLPaCPEKYAEIAEALGEDVEGLSDE 309
|
330 340 350
....*....|....*....|....*....|....*.
gi 489535278 323 EAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQI 358
Cdd:cd08551 310 EAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPEL 345
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-383 |
4.24e-109 |
|
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: 324.87 E-value: 4.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 3 NFYQPSRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVEPLDkLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFEL 81
Cdd:cd14863 1 TYSQLTPVIFGAGAVEQIGELLKELGcKKVLLVTDKGLKKAG-IVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 82 AKKESVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYmfstYTNPFKIYDKVsekeLPLIAVSTTSGTGSQVTQAAVISR 161
Cdd:cd14863 80 AREEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDY----ALAGPPVPKPG----IPLIAIPTTAGTGSEVTPIAVITD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 162 GSE--KNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDK 239
Cdd:cd14863 152 EENgvKKSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 240 NNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFP---KFAEKFYkdnIEKFAKVARMLNQEL 316
Cdd:cd14863 232 DNLEARENMLLASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPvvlEFNAEAY---PEKVKKIAKALGVSF 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489535278 317 EKVEDDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQIT----SCPVLGFLPFG-KKEDLVEILEKSY 383
Cdd:cd14863 309 PGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAeavlKDPFAMFNPRPiTEEEVAEILEAIY 380
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
3-380 |
5.53e-95 |
|
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: 288.56 E-value: 5.53e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 3 NFYQPSRINFGQGTLSELPRIIGKYGKKCLLVTtpnveplDK-------LYKRVTLNLIEKGIEVVHFDRVEPNPTVELI 75
Cdd:cd08187 3 TFYNPTKIIFGKGAIEELGEEIKKYGKKVLLVY-------GGgsikkngLYDRVVASLKEAGIEVVEFGGVEPNPRLETV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 76 NEGFELAKKESVDVVLAVGGGSSIDTAKVLALTFGLEkID-WDYMFstytnpfkiYDKVSEKELPLIAVSTTSGTGSQVT 154
Cdd:cd08187 76 REGIELAREENVDFILAVGGGSVIDAAKAIAAGAKYD-GDvWDFFT---------GKAPPEKALPVGTVLTLAATGSEMN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 155 QAAVISRGS--EKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYI-NPNANDFTEIMSEKSMELVINY 231
Cdd:cd08187 146 GGAVITNEEtkEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFtGTEDAPLQDRLAEGLLRTVIEN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 232 LPKVMEDKNNIEYRTKLAVADTLGGSSLANAGAA---APHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKV 308
Cdd:cd08187 226 GPKALKDPDDYEARANLMWAATLALNGLLGAGRGgdwATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQF 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489535278 309 A-RMLNQELEKVEDDEAAKTLgNEIESFLKRVGLKTKMSEFNVTKEQLEQIT-SCPVLGFLPFGKK----EDLVEILE 380
Cdd:cd08187 306 ArRVFGIDPGGDDEETALEGI-EALEEFFKSIGLPTTLSELGIDEEDIEEMAeKAVRGGGLGGGFKpltrEDIEEILK 382
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-358 |
1.93e-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: 341475 [Multi-domain] Cd Length: 367 Bit Score: 274.07 E-value: 1.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 3 NFYQPSRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVEPlDKLYKRVTLNLIEKGIEVvhFDRVEPNPTVELINEGFEL 81
Cdd:cd08196 2 SYYQPVKIIFGEGILKELPDIIKELGgKRGLLVTDPSFIK-SGLAKRIVESLKGRIVAV--FSDVEPNPTVENVDKCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 82 AKKESVDVVLAVGGGSSIDTAKVLAltfglekidwdymfSTYTNPFKIYD------KVSEKELPLIAVSTTSGTGSQVTQ 155
Cdd:cd08196 79 ARENGADFVIAIGGGSVLDTAKAAA--------------CLAKTDGSIEDylegkkKIPKKGLPLIAIPTTAGTGSEVTP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 156 AAVISrGSEKN---TIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYL 232
Cdd:cd08196 145 VAVLT-DKEKGkkaPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 233 PKVMEDKNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKVARML 312
Cdd:cd08196 224 EKAYNNPNDKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQL 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489535278 313 NqelekVEDDEAAKtlgNEIESFLKRVGLKTKMSEFNVTKEQLEQI 358
Cdd:cd08196 304 G-----FKDAEELA---DKIEELKKRIGLRTRLSELGITEEDLEEI 341
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-357 |
5.16e-88 |
|
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: 270.56 E-value: 5.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGK-YGKKCLLVTTPNVEPLDkLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKKE 85
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASlGGKRALIVTDKVMVKLG-LVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 86 SVDVVLAVGGGSSIDTAKVLAL--TFGlEKIDwDYMFstytnpfkiYDKVSEKELPLIAVSTTSGTGSQVTQAAVI--SR 161
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAIAVlaTNG-GPIR-DYMG---------PRKVDKPGLPLIAIPTTAGTGSEVTRFTVItdTE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 162 GSEKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKNN 241
Cdd:cd08194 149 TDVKMLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 242 IEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKVARMLNQELEKVED 321
Cdd:cd08194 229 LEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSD 308
|
330 340 350
....*....|....*....|....*....|....*.
gi 489535278 322 DEAAKTLGNEIESFLKRVGLKTkMSEFNVTKEQLEQ 357
Cdd:cd08194 309 EEAAEKLVEALERLCADLEIPT-LREYGIDEEEFEA 343
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
3-356 |
1.93e-85 |
|
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: 263.99 E-value: 1.93e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 3 NFYQPSRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVEPLDkLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFEL 81
Cdd:cd08188 2 RFYIPPVNLFGPGCLKEIGDELKKLGgKKALIVTDKGLVKLG-LVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 82 AKKESVDVVLAVGGGSSIDTAK---VLAltfglekidwdymfstyTNPFKIYD-----KVSEKELPLIAVSTTSGTGSQV 153
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKaigILA-----------------TNGGEIEDyegvdKSKKPGLPLIAINTTAGTASEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 154 TQAAVI--SRGSEKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINY 231
Cdd:cd08188 144 TRFAVItdEERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAEN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 232 LPKVMEDKNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPkFAEKFYKD-NIEKFAKVAR 310
Cdd:cd08188 224 LPKAVANGKDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLP-HVMEFNLPaCPERFADIAR 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489535278 311 MLNQELEKVEDDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLE 356
Cdd:cd08188 303 ALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFP 348
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
8-383 |
2.03e-85 |
|
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: 265.18 E-value: 2.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 8 SRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVEPLDkLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKKES 86
Cdd:cd08190 2 SNIRFGPGATRELGMDLKRLGaKKVLVVTDPGLAKLG-LVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 87 VDVVLAVGGGSSIDTAKVLALtfglekidwdymFSTYTNPFKIY--------DKVSEKELPLIAVSTTSGTGSQVTQAAV 158
Cdd:cd08190 81 FDAFVAVGGGSVIDTAKAANL------------YATHPGDFLDYvnapigkgKPVPGPLKPLIAIPTTAGTGSETTGVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 159 ISRGSE--KNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYI-----------NPN-------ANDFTE 218
Cdd:cd08190 149 FDLEELkvKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTarpynarprpaNPDerpayqgSNPISD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 219 IMSEKSMELVINYLPKVMEDKNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGV-------------THIPHGEA 285
Cdd:cd08190 229 VWAEKAIELIGKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLvkdyrppgypvdhPHVPHGLS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 286 LAIVFPKFAEKFYKDNIEKFAKVARMLNQELEKVEDDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQItscpVLG 365
Cdd:cd08190 309 VALTAPAVFRFTAPACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPAL----VEG 384
|
410 420
....*....|....*....|....*...
gi 489535278 366 FLPF----------GKKEDLVEILEKSY 383
Cdd:cd08190 385 TLPQqrllklnprpVTEEDLEEIFEDAL 412
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
1-383 |
2.26e-83 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 259.23 E-value: 2.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 1 MINF--YQPSRINFGQGTLSELPRIIGKYGKKCLLVTtpnveplDK-------LYKRVTLNLIEKGIEVVHFDRVEPNPT 71
Cdd:COG1979 1 MNNFtfYNPTKIIFGKGQIAKLGEEIPKYGKKVLLVY-------GGgsikkngLYDQVKAALKEAGIEVVEFGGVEPNPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 72 VELINEGFELAKKESVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYmfstYTNPFKIydkvsEKELPLIAVSTTSGTGS 151
Cdd:COG1979 74 LETVRKGVELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDI----LTGKAPV-----EKALPLGTVLTLPATGS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 152 QVTQAAVISR--GSEKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYI-NPNANDFTEIMSEKSMELV 228
Cdd:COG1979 145 EMNSGSVITNeeTKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFtYPVDAPLQDRFAEGLLRTL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 229 INYLPKVMEDKNNIEYRTKLAVADTLGGSSLANAGAA---APHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKF 305
Cdd:COG1979 225 IEEGPKALKDPEDYDARANLMWAATLALNGLIGAGVPqdwATHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKF 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 306 AKVA-RMLNqeLEKVEDDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQIT-SCPVLGFLPFG-----KKEDLVEI 378
Cdd:COG1979 305 AQYAeRVWG--ITEGDDEERALEGIEATEEFFESLGLPTRLSEYGIDEEDIEEMAeKATAHGMTALGefkdlTPEDVREI 382
|
....*
gi 489535278 379 LEKSY 383
Cdd:COG1979 383 LELAL 387
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
7-359 |
3.46e-83 |
|
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: 258.25 E-value: 3.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVEPLdKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKKE 85
Cdd:cd08176 6 NPTSYFGWGAIEEIGEEAKKRGfKKALIVTDKGLVKF-GIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 86 SVDVVLAVGGGSSIDTAKVLALTfglekidwdymfstYTNPFKI------YDKVSEKELPLIAVSTTSGTGSQVTQAAVI 159
Cdd:cd08176 85 GADGIIAVGGGSSIDTAKAIGII--------------VANPGADvrslegVAPTKNPAVPIIAVPTTAGTGSEVTINYVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 160 SRGSE--KNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVME 237
Cdd:cd08176 151 TDTEKkrKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 238 DKNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKfAEKFYKD-NIEKFAKVARMLNQEL 316
Cdd:cd08176 231 NPNNVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPY-VMEFNAPaTGEKYRDIARAMGVDT 309
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489535278 317 EKVEDDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQIT 359
Cdd:cd08176 310 TGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALA 352
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
7-360 |
5.29e-82 |
|
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.
Pssm-ID: 341461 [Multi-domain] Cd Length: 370 Bit Score: 254.84 E-value: 5.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGKYG-KKCLLVTTPnvEPLDKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKKE 85
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLGaRRVLLVTGP--SAVRESGAADILDALGGRIPVVVFSDFSPNPDLEDLERGIELFRES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 86 SVDVVLAVGGGSSIDTAKVLALTFGLEKidwdymFSTYTNPFKIYdKVSEKELPLIAVSTTSGTGSQVTQAAVISRGSE- 164
Cdd:cd08182 79 GPDVIIAVGGGSVIDTAKAIAALLGSPG------ENLLLLRTGEK-APEENALPLIAIPTTAGTGSEVTPFATIWDEAEg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 165 -KNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKNNIE 243
Cdd:cd08182 152 kKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 244 YRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPkfaeKFYKDNIEKFAK-----VARMLNQELEK 318
Cdd:cd08182 232 AREAMAEASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLP----AVLRYNAGADDEcdddpRGREILLALGA 307
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489535278 319 VEDDEAAKTlgneIESFLKRVGLKTKMSEFNVTKEQLEQITS 360
Cdd:cd08182 308 SDPAEAAER----LRALLESLGLPTRLSEYGVTAEDLEALAA 345
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
4-358 |
2.95e-81 |
|
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: 252.51 E-value: 2.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 4 FYQPSRINFGQGTLSELPRIIGKYGKKCLLVTTPNVEPLDKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAK 83
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELAALGKKALIVTGKHSAKKNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 84 KESVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYMFSTYTNPFkiydkvsekeLPLIAVSTTSGTGSQVTQAAVISR-- 161
Cdd:cd08181 81 KEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDLFQNGKYNPP----------LPIVAIPTTAGTGSEVTPYSILTDhe 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 162 -GSEKNtIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKN 240
Cdd:cd08181 151 kGTKKS-FGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 241 NIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEK------------FAKV 308
Cdd:cd08181 230 DEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKvdkilkllgfgsIEEF 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489535278 309 ARMLNQELEKVEDDEAAktlgnEIESFLKRVgLKTKMSE---FNVTKEQLEQI 358
Cdd:cd08181 310 QKFLNRLLGKKEELSEE-----ELEKYADEA-MKAKNKKntpGNVTKEDILRI 356
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
13-381 |
2.97e-81 |
|
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: 253.16 E-value: 2.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 13 GQGTLSELPRIIGKYG-KKCLLVTTPNVEPLdKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKKESVDVVL 91
Cdd:cd08189 11 GAGSLLQLPEALKKLGiKRVLIVTDKGLVKL-GLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAII 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 92 AVGGGSSIDTAKVLALTFglekidwdymfstyTNPFK-IYD-----KVSEKELPLIAVSTTSGTGSQVTQAAVIS--RGS 163
Cdd:cd08189 90 AIGGGSVIDCAKVIAARA--------------ANPKKsVRKlkgllKVRKKLPPLIAVPTTAGTGSEATIAAVITdpETH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 164 EKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKNNIE 243
Cdd:cd08189 156 EKYAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 244 YRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEkFYKDNIE-KFAKVARMLNQELEKVEDD 322
Cdd:cd08189 236 ARENMLLASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLE-FYGPAAEkRLAELADAAGLGDSGESDS 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489535278 323 EAAKTLGNEIESFLKRVGLKTKMSEFNvtKEQLEQIT---------SCPVLGFLpfgKKEDLVEILEK 381
Cdd:cd08189 315 EKAEAFIAAIRELNRRMGIPTTLEELK--EEDIPEIAkralkeanpLYPVPRIM---DRKDCEELLRK 377
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
1-357 |
2.67e-80 |
|
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: 250.99 E-value: 2.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 1 MINFYQPsRINFGQGTLSELPRIIGKygkKCLLVTTPNVEPLDKLyKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFE 80
Cdd:cd14862 1 MWYFSSP-KIVFGEDALSHLEQLSGK---RALIVTDKVLVKLGLL-KKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 81 LAKKESVDVVLAVGGGSSIDTAKVLALTFglEKIDWDymfSTYTNPFKIYDKvsEKELPLIAVSTTSGTGSQVTQAAVIS 160
Cdd:cd14862 76 AMREFEPDLIIALGGGSVMDAAKAAWVLY--ERPDLD---PEDISPLDLLGL--RKKAKLIAIPTTSGTGSEATWAIVLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 161 RGSE--KNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMED 238
Cdd:cd14862 149 DTEEprKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 239 KNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKVARmlnQELEK 318
Cdd:cd14862 229 GDDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKL---LGIEA 305
|
330 340 350
....*....|....*....|....*....|....*....
gi 489535278 319 VEDDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQ 357
Cdd:cd14862 306 RDEEEALKKLVEAIRELYKEVGQPLSIKDLGISEEEFEE 344
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-358 |
2.74e-80 |
|
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: 250.88 E-value: 2.74e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGKYGKKCLLVTTPNVEPLDkLYKRVTLNLIEKGIEVVHFDrVEPNPTVELINEGFELAKKES 86
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKRALLVTGRSSLRSG-RLARLLEALEAAGIEVALFS-VSGEPTVETVDAAVALAREAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 87 VDVVLAVGGGSSIDTAKVLAltfGLekidwdymfstYTNPFKIYD---------KVSEKELPLIAVSTTSGTGSQVTQAA 157
Cdd:cd08183 79 CDVVIAIGGGSVIDAAKAIA---AL-----------LTNEGSVLDylevvgkgrPLTEPPLPFIAIPTTAGTGSEVTKNA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 158 VISRGSE--KNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKV 235
Cdd:cd08183 145 VLSSPEHgvKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 236 MEDKNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFP-------KFAEKFYKDN--IEKFA 306
Cdd:cd08183 225 YEDGEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPpvleanlRALREREPDSpaLARYR 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489535278 307 KVARMLNQelekvEDDEAAKTLGNEIESFLKRVGLKtKMSEFNVTKEQLEQI 358
Cdd:cd08183 305 ELAGILTG-----DPDAAAEDGVEWLEELCEELGIP-RLSEYGLTEEDFPEI 350
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-383 |
2.19e-79 |
|
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: 248.61 E-value: 2.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 4 FYQPSRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVEPLdKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELA 82
Cdd:cd14865 3 FFNPTKIVSGAGALENLPAELARLGaRRPLIVTDKGLAAA-GLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 83 KKESVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYmfstytnpFKIYDKVSEKELPLIAVSTTSGTGSQVTQAAVIS-- 160
Cdd:cd14865 82 REAGADGIIAVGGGSVIDTAKGVNILLSEGGDDLDD--------YGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKde 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 161 RGSEKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKN 240
Cdd:cd14865 154 EKKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 241 NIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEkFYKDNI-EKFAKVARMLNQELEKV 319
Cdd:cd14865 234 DLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMR-YNLDAAaERYAELALALAYGVTPA 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489535278 320 EDD--EAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQIT----SCPVLGFLP-FGKKEDLVEILEKSY 383
Cdd:cd14865 313 GRRaeEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAelalNDGAILFNPrEVDPEDILAILEAAY 383
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
4-359 |
3.09e-74 |
|
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: 235.16 E-value: 3.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 4 FYQPSRINFGQGTLSELPRIigkYGKKCLLVTTPNVEPLDKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAK 83
Cdd:cd08179 2 FFVPRDIYFGEGALEYLKTL---KGKRAFIVTGGGSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 84 KESVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYMFSTYTNPfkiydkVSEKELPLIAVSTTSGTGSQVTQAAVISRGS 163
Cdd:cd08179 79 EFEPDWIIAIGGGSVIDAAKAMWVFYEYPELTFEDALVPFPLP------ELRKKARFIAIPSTSGTGSEVTRASVITDTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 164 E--KNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKNN 241
Cdd:cd08179 153 KgiKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 242 IEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDniekfAKVARMLNQELEKVED 321
Cdd:cd08179 233 LEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKD-----PEARARYAALLIGLTD 307
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489535278 322 DEAAKTLGNEIESFLKRVGLKTKMSEFNVT----KEQLEQIT 359
Cdd:cd08179 308 EELVEDLIEAIEELNKKLGIPLSFKEAGIDedefFAKLDEMA 349
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-358 |
1.07e-70 |
|
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: 226.73 E-value: 1.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 4 FYQPSRINFGQGTLSELPRIIGKYGKKCLLVTTPNVEPLDkLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAK 83
Cdd:cd08191 1 LRSPSRLLFGPGARRALGRVAARLGSRVLIVTDPRLASTP-LVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 84 KESVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYmFStytnpfkiYDKVSEKELPLIAVSTTSGTGSQVTQAAVIS--- 160
Cdd:cd08191 80 AFDPDVVIGLGGGSNMDLAKVVALLLAHGGDPRDY-YG--------EDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTdpa 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 161 RGSeKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPN---------------ANDFTEIMSEKSM 225
Cdd:cd08191 151 RGM-KVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDfppfprldpdpvyvgKNPLTDLLALEAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 226 ELVINYLPKVMEDKNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPkFAEKFYKDNI-EK 304
Cdd:cd08191 230 RLIGRHLPRAVRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLP-YVMRFNRPARaAE 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489535278 305 FAKVARMLNQELEKVEDDEAAKTLgNEIESFLKRVGLKTKMSEFNVTKEQLEQI 358
Cdd:cd08191 309 LAEIARALGVTTAGTSEEAADRAI-ERVEELLARIGIPTTLADLGVTEADLPGL 361
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
7-358 |
2.42e-69 |
|
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: 222.39 E-value: 2.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVEPLDkLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKKE 85
Cdd:cd14861 3 PTRIRFGAGAIAELPEELKALGiRRPLLVTDPGLAALG-IVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 86 SVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYmFSTYTNPFKIYDKVSekelPLIAVSTTSGTGSQVTQAAVIS--RGS 163
Cdd:cd14861 82 GCDGIIALGGGSAIDAAKAIALMATHPGPLWDY-EDGEGGPAAITPAVP----PLIAIPTTAGTGSEVGRAAVITddDTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 164 EKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKNNIE 243
Cdd:cd14861 157 RKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 244 YRTKLAVADTLGGSSLANA-GAAapHPLSEIIGGVTHIPHGEALAIVFPkFAEKFYKDNIE-KFAKVARMLNQELEKVED 321
Cdd:cd14861 237 ARGEMMMAALMGAVAFQKGlGAV--HALAHALGALYGLHHGLLNAILLP-YVLRFNRPAVEdKLARLARALGLGLGGFDD 313
|
330 340 350
....*....|....*....|....*....|....*..
gi 489535278 322 deaaktLGNEIESFLKRVGLKTKMSEFNVTKEQLEQI 358
Cdd:cd14861 314 ------FIAWVEDLNERLGLPATLSELGVTEDDLDEL 344
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-360 |
3.93e-69 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 222.03 E-value: 3.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 12 FGQGTLSElpriIGKY-----GKKCLLVTTPNVEpldK--LYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKK 84
Cdd:cd17814 9 FGVGARKL----AGRYaknlgARKVLVVTDPGVI---KagWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 85 ESVDVVLAVGGGSSIDTAK---VLAltfglekidwdymfstyTNPFKIY-----DKVSEKELPLIAVSTTSGTGSQVTQA 156
Cdd:cd17814 82 EGCDGIVAVGGGSPIDCAKgigIVV-----------------SNGGHILdyegvDKVRRPLPPLICIPTTAGSSADVSQF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 157 AVI--SRGSEKNTIFhqncfSKE-----CIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVI 229
Cdd:cd17814 145 AIItdTERRVKMAII-----SKTlvpdvSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLIS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 230 NYLPKVMEDKNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKVA 309
Cdd:cd17814 220 ENLPKAVADPDDLEAREKMMLASLQAGLAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIA 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489535278 310 RMLNQELEKVEDDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQITS 360
Cdd:cd17814 300 EAMGLDVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAK 350
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-382 |
3.44e-68 |
|
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: 219.83 E-value: 3.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 10 INFGQGTLSELPRIIGKYGKKC-LLVTTPNVEPLDKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKKESVD 88
Cdd:cd08186 4 LYFGVGAIAKIKDILKDLGIDKvIIVTGRSSYKKSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 89 VVLAVGGGSSIDTAKVLALTfglekidwdyMFSTYTNPFKIYDK--VSEKELPLIAVSTTSGTGSQVTQAAVIS---RGs 163
Cdd:cd08186 84 AVIAIGGGSPIDTAKSVAVL----------LAYGGKTARDLYGFrfAPERALPLVAINLTHGTGSEVDRFAVATipeKG- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 164 EKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKNNIE 243
Cdd:cd08186 153 YKPGIAYDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 244 YRTKLAVADTLGGSSLANAGA----AAPHPLSEIiggVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKVARMLNQELEKV 319
Cdd:cd08186 233 ARYWLLYASMIAGIAIDNGLLhlthALEHPLSGL---KPELPHGLGLALLGPAVVKYIYKAVPETLADILRPIVPGLKGT 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489535278 320 EDDeaAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQIT----SCPVLGFL----PFGKKEDLV-EILEKS 382
Cdd:cd08186 310 PDE--AEKAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVelafTTPSLDLLlslaPVEVTEEVVrEIYEES 379
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-383 |
3.80e-67 |
|
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: 216.78 E-value: 3.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 4 FYQPSRINFGQGTLSELPRIIGKYGKKCLLVTTPNVEPlDKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAK 83
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVKEYGSRFLLITDPVLKE-SGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 84 KESVDVVLAVGGGSSIDTAKVLALTfglekidwdymfstYTNPFKIYD-----KVSEKELPLIAVSTTSGTGSQVTQAAV 158
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAIL--------------ANNDGGAYDflegaKPKKKPLPLIAVPTTPRSGFEFSDRFP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 159 I--SRGSEKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVM 236
Cdd:cd14864 146 VvdSRSREVKLLKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 237 EDKNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKVARMLNQEL 316
Cdd:cd14864 226 ADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDV 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489535278 317 EKVEDDEAAKTLGNEIESFLKRVGLKTKMSEFNV--TKEQL-EQITSCPVLGFLPFG-KKEDLVEILEKSY 383
Cdd:cd14864 306 EGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLDLasSLEQLaAIAEDAPKLNGLPRSmSSDDIFDILKAAF 376
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
4-356 |
4.07e-65 |
|
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: 211.60 E-value: 4.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 4 FYQPSRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVEPLdKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELA 82
Cdd:cd08193 1 FQTVPRIICGAGAAARLGELLRELGaRRVLLVTDPGLVKA-GLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 83 KKESVDVVLAVGGGSSIDTAKVLA-LTFGLEKIDwdymfstytnpfKIY--DKVSEKELPLIAVSTTSGTGSQVTQAAVI 159
Cdd:cd08193 80 REAGADGVIGFGGGSSMDVAKLVAlLAGSDQPLD------------DIYgvGKATGPRLPLILVPTTAGTGSEVTPISIV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 160 SRGS-EKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINP-NANDFTEIMSEKSMELVINYLPKVME 237
Cdd:cd08193 148 TTGEtEKKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRhKKNPISDALAREALRLLGANLRRAVE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 238 DKNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFP---KF----AEKFYkdniekfAKVAR 310
Cdd:cd08193 228 DGSDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPhvlRFnlpaAEALY-------AELAR 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489535278 311 MLNQELEKVEDDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLE 356
Cdd:cd08193 301 ALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLP 346
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
4-358 |
1.22e-64 |
|
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: 208.89 E-value: 1.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 4 FYQPSRINFGQGTLSELPRIIGKygkKCLLVTTPNVEPLDKLyKRVTlNLIEKGIEVVHFDRVEPNPTVELINEGFELAK 83
Cdd:cd08180 1 FSLKTKIYSGEDSLERLKELKGK---RVFIVTDPFMVKSGMV-DKVT-DELDKSNEVEIFSDVVPDPSIEVVAKGLAKIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 84 KESVDVVLAVGGGSSIDTAKVlALTFGLEkidwdymfsTYTNPFKIYdkvsekelpLIAVSTTSGTGSQVTQAAVISrGS 163
Cdd:cd08180 76 EFKPDTIIALGGGSAIDAAKA-IIYFALK---------QKGNIKKPL---------FIAIPTTSGTGSEVTSFAVIT-DP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 164 EKNT---IFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKN 240
Cdd:cd08180 136 EKGIkypLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 241 NIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFaekfykdnIEKFAKVARMLNQELE--- 317
Cdd:cd08180 216 DLEAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYV--------IEFLIAAIRRLNKKLGips 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489535278 318 KVEDdeaaktLGNEIESFLKRvglKTKMSEF------------NVTKEQLEQI 358
Cdd:cd08180 288 TLKE------LGIDEEEFEKA---IDEMAEAaladrctatnprKPTAEDLIEL 331
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
7-357 |
1.57e-63 |
|
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: 208.19 E-value: 1.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELpRIIGKYGKKCLLVTTPNVEPLDKLyKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKKES 86
Cdd:cd08178 3 PPKIYFEPGCLPYL-LLELPGVKRAFIVTDRVLYKLGYV-DKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 87 VDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYMFSTYTNPFKIYDKVSE--KELPLIAVSTTSGTGSQVTQAAVIS--RG 162
Cdd:cd08178 81 PDVIIALGGGSAMDAAKIMWLFYEHPETKFEDLAQRFMDIRKRVYKFPKlgKKAKLVAIPTTSGTGSEVTPFAVITddKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 163 SEKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKNNI 242
Cdd:cd08178 161 GKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGNDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 243 EYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFP------------KFA----EKFYKDnIEKFA 306
Cdd:cd08178 241 EAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPhvirynatdpptKQAafpqYKYYVA-KERYA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489535278 307 KVARMLnqELEKVEDDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQ 357
Cdd:cd08178 320 EIADLL--GLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADFLA 368
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
7-356 |
1.51e-52 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 187.31 E-value: 1.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLS----ELPRIigkygKKCLLVTTPnvePLDKL-Y-KRVT--LNLIEKGIEVVHFDRVEPNPTVELINEG 78
Cdd:PRK13805 460 PKKIYFERGSLPylldELDGK-----KRAFIVTDR---FMVELgYvDKVTdvLKKRENGVEYEVFSEVEPDPTLSTVRKG 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 79 FELAKKESVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYMFSTYTNPFK-IYD--KVSEKELpLIAVSTTSGTGSQVTQ 155
Cdd:PRK13805 532 AELMRSFKPDTIIALGGGSPMDAAKIMWLFYEHPETDFEDLAQKFMDIRKrIYKfpKLGKKAK-LVAIPTTSGTGSEVTP 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 156 AAVISrgSEKNTIfhqncfsKE-----------CIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKS 224
Cdd:PRK13805 611 FAVIT--DDKTGV-------KYpladyeltpdvAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQA 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 225 MELVINYLPK-VMEDKNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFP---KF----AEK 296
Cdd:PRK13805 682 IKLVFEYLPRsYKNGAKDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPhviRYnatdPPK 761
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489535278 297 F-------YKDNIEKFAKVARMLNqeLEKVEDDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLE 356
Cdd:PRK13805 762 QaafpqyeYPRADERYAEIARHLG--LPGSTTEEKVESLIKAIEELKAELGIPMSIKEAGVDEADFL 826
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
12-358 |
5.69e-50 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 172.49 E-value: 5.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 12 FGQGTLSELPRIIGKYG-KKCLLVTTPNvepLDK--LYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKKESVD 88
Cdd:PRK10624 13 FGRGAIGALTDEVKRRGfKKALIVTDKT---LVKcgVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 89 VVLAVGGGSSIDTAKVLALTFglekidwdymfstyTNPfKIYDKVS--------EKELPLIAVSTTSGTGSQVTQAAVIS 160
Cdd:PRK10624 90 YLIAIGGGSPQDTCKAIGIIS--------------NNP-EFADVRSlegvaptkKPSVPIIAIPTTAGTAAEVTINYVIT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 161 rGSEKNTIF---HQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVME 237
Cdd:PRK10624 155 -DEEKRRKFvcvDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 238 dkNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEkFYKD-NIEKFAKVARMLNQEL 316
Cdd:PRK10624 234 --GDKEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVME-YNADfTGEKYRDIARAMGVKV 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489535278 317 EKVEDDEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQI 358
Cdd:PRK10624 311 EGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPAL 352
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
70-359 |
1.45e-46 |
|
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: 163.16 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 70 PTVELINEGFELAKKESVDVVLAVGGGSSIDTAKVLALtfglekidwdymfSTYTNPFKIYDKVSE--KELPLIAVSTTS 147
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLAL-------------KGISPVLDLFDGKIPliKEKELIIVPTTC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 148 GTGSQVTQAAVISRGSE--KNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSM 225
Cdd:cd14860 129 GTGSEVTNISIVELTSLgtKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 226 ELVINYLPKVMEDKNniEYRTKL----AVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDN 301
Cdd:cd14860 209 EMILEGYQEIAEKGE--EARFPLlgdfLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQEKN 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 489535278 302 IE-KFAKVARMLNQELEKVEDDeaaktLGNEIESFLKRVGLKTKMSEFNVTKEQLEQIT 359
Cdd:cd14860 287 PDgEIKKLNEFLAKILGCDEED-----VYDELEELLNKILPKKPLHEYGMKEEEIDEFA 340
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
4-360 |
5.14e-44 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 156.65 E-value: 5.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 4 FYQPSRINFGQGTLSELPRIIGKYGKKCLLVTTPNVEPLDKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAK 83
Cdd:PRK09860 6 FFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 84 KESVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYmfstytnpfKIYDKVSEKELPLIAVSTTSGTGSQVTQAAVISRGS 163
Cdd:PRK09860 86 ENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDY---------EGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 164 E--KNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKNN 241
Cdd:PRK09860 157 RhiKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 242 IEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKVARMLNQELEKVED 321
Cdd:PRK09860 237 AKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKND 316
|
330 340 350
....*....|....*....|....*....|....*....
gi 489535278 322 DEAAKTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQITS 360
Cdd:PRK09860 317 AEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLAT 355
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
7-358 |
1.23e-40 |
|
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: 146.50 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVEPLdklYKRVTLNLieKGIEVVHFDRVEPNPTVELINEGFELAKKE 85
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLGaRRALVLSTPRQRAL---AERVAALL--GDRVAGVFDGAVMHVPVEVAERALAAAREA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 86 SVDVVLAVGGGSSIDTAKVLALTFGLekidwdymfstytnpfkiydkvsekelPLIAVSTTSgTGSQVTQAAVISRGSEK 165
Cdd:cd08177 76 GADGLVAIGGGSAIGLAKAIALRTGL---------------------------PIVAVPTTY-AGSEMTPIWGETEDGVK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 166 NTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKNNIEYR 245
Cdd:cd08177 128 TTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEAR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 246 TKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPkFAEKFykdniekfakVARMLNQELEKVEDDEAA 325
Cdd:cd08177 208 SDALYGAWLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLP-HVLAY----------NAPAAPDAMARLARALGG 276
|
330 340 350
....*....|....*....|....*....|...
gi 489535278 326 KTLGNEIESFLKRVGLKTKMSEFNVTKEQLEQI 358
Cdd:cd08177 277 GDAAGGLYDLARRLGAPTSLRDLGMPEDDIDRA 309
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-380 |
1.15e-38 |
|
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: 142.39 E-value: 1.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 9 RINFGQGTLSELPRIIGKYG-KKCLLVT-------TPNVEPLDKLykrvtlnLiekGIEVV-HFDRVEPNPTVELINEGF 79
Cdd:cd08192 3 RVSYGPGAVEALLHELATLGaSRVFIVTskslatkTDVIKRLEEA-------L---GDRHVgVFSGVRQHTPREDVLEAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 80 ELAKKESVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYMFSTYTNPfKIYDKVSEKELPLIAVSTT-SGtgSQVTQAA- 157
Cdd:cd08192 73 RAVREAGADLLVSLGGGSPIDAAKAVALALAEDVTDVDQLDALEDGK-RIDPNVTGPTLPHIAIPTTlSG--AEFTAGAg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 158 -VISRGSEKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVM 236
Cdd:cd08192 150 aTDDDTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 237 EDKNNIEYRTK--LAVADTLGGsSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKVARMLNQ 314
Cdd:cd08192 230 ADPEDLEARLKcqLAAWLSLFG-LGSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALGL 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489535278 315 ELEKVEDDEAAktLGNEIESFLKRVGLKTKMSEFNVTKEQLEQITS------CPVLGFLPFGKKEDLVEILE 380
Cdd:cd08192 309 VTGGLGREAAD--AADAIDALIRELGLPRTLRDVGVGRDQLEKIAEnaltdvWCRTNPRPITDKDDVLEILE 378
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-358 |
7.68e-33 |
|
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: 126.58 E-value: 7.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 4 FYQPSRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVepldkLYKRVTLNLIEKGI--EVVH-FDRVEPNPTVELINEGF 79
Cdd:cd14866 2 DYPPLRLFSGRGALARLGRELDRLGaRRALVVCGSSV-----GANPDLMDPVRAALgdRLAGvFDGVRPHSPLETVEAAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 80 ELAKKESVDVVLAVGGGSSIDTAKVLALTFGLEKIDWDYMFSTYTNPFKIYDKVSEKELPLIAVSTTSGTGSQVTQAAVI 159
Cdd:cd14866 77 EALREADADAVVAVGGGSAIVTARAASILLAEDRDVRELCTRRAEDGLMVSPRLDAPKLPIFVVPTTPTTADVKAGSAVT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 160 SRGS-EKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKvMED 238
Cdd:cd14866 157 DPPAgQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPR-LAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 239 KNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKVARMLNQELEK 318
Cdd:cd14866 236 DDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGVADAG 315
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489535278 319 VEDDEAAktLGNEIESFLKRVGLKTKMSEFNVTKEQLEQI 358
Cdd:cd14866 316 DEASAAA--VVDAVEALLDALGVPTRLRDLGVSREDLPAI 353
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
88-354 |
2.08e-32 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 125.53 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 88 DVVLAVGGGSSIDTAKVLALTFglekidwdymfstyTNPFKIYDKVSEK-----ELPLIAVSTTSGTGSQVTQAAVI--S 160
Cdd:PRK15454 108 DGVIAFGGGSVLDAAKAVALLV--------------TNPDSTLAEMSETsvlqpRLPLIAIPTTAGTGSETTNVTVIidA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 161 RGSEKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKVMEDKN 240
Cdd:PRK15454 174 VSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGH 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 241 NIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFAEKFYKDNIEKFAKVARMLNQelEKVE 320
Cdd:PRK15454 254 DLAARESMLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRALRT--KKSD 331
|
250 260 270
....*....|....*....|....*....|....
gi 489535278 321 DDEAAktlgNEIESFLKRVGLKTKMSEFNVTKEQ 354
Cdd:PRK15454 332 DRDAI----NAVSELIAEVGIGKRLGDVGATSAH 361
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
1-350 |
3.64e-30 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 119.13 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 1 MINF--YQPSRINFGQGTLSEL-------PRIIGKYGKKCllVTTPNVepLDKLYKRVtlnlieKGIEVVHFDRVEPNPT 71
Cdd:PRK15138 1 MNNFnlHTPTRILFGKGAIAGLreqipadARVLITYGGGS--VKKTGV--LDQVLDAL------KGMDVLEFGGIEPNPT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 72 VELINEGFELAKKESVDVVLAVGGGSSIDTAKVLALTFGlekidwdymFSTYTNPFKIYDKVS---EKELPLIAVSTTSG 148
Cdd:PRK15138 71 YETLMKAVKLVREEKITFLLAVGGGSVLDGTKFIAAAAN---------YPENIDPWHILETGGkeiKSAIPMGSVLTLPA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 149 TGSQVTQAAVISRGS--EKNTIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFESYIN-PNANDFTEIMSEKSM 225
Cdd:PRK15138 142 TGSESNAGAVISRKTtgDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTyPVDAKIQDRFAEGIL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 226 ELVINYLPKVMEDKNNIEYRTKLAVADTLGGSSLANAGAA---APHPLSEIIGGVTHIPHGEALAIVFPKFAekfykdNI 302
Cdd:PRK15138 222 LTLIEEGPKALKEPENYDVRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAMHGLDHAQTLAIVLPALW------NE 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489535278 303 EKFAKVARMLnQELEKV------EDDEAAKTLGNEIESFLKRVGLKTKMSEFNV 350
Cdd:PRK15138 296 KRDTKRAKLL-QYAERVwnitegSDDERIDAAIAATRNFFEQMGVPTRLSDYGL 348
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
7-358 |
4.51e-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: 113.61 E-value: 4.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGKYGKKCLLVTTPNVeplDKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFELAKKES 86
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGV---VKGVGEKVADSLKKGLAVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 87 VDVVLAVGGGSSIDTAKVLALTfglekidwdymfstytnpfkiydkvSEKELPLIAVSTTSGTGSQVTQAAVISRGSEKN 166
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAAL-------------------------LNRGIPFIIVPTTASTDSEVSPKSVITDKGGKN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 167 TIFHQNCFSKECIVDPELMLTLPERITASTAFDAFTHAFEsyinpnandfteimseksmelvinylpkvmedknnieyRT 246
Cdd:cd07766 133 KQVGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE--------------------------------------LE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 247 KLAVADTLGGSSLANAGA-AAPHPLSEIIGGVTHIPHGEALAIVFPkfaekfYKDNIEKfaKVARMLNQELEkveddeaa 325
Cdd:cd07766 175 KVVEAATLAGMGLFESPGlGLAHAIGHALTAFEGIPHGEAVAVGLP------YVLKVAN--DMNPEPEAAIE-------- 238
|
330 340 350
....*....|....*....|....*....|...
gi 489535278 326 ktlgnEIESFLKRVGLKTKMSEFNVTKEQLEQI 358
Cdd:cd07766 239 -----AVFKFLEDLGLPTHLADLGVSKEDIPKL 266
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
7-331 |
8.48e-29 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 114.67 E-value: 8.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGKYGKKcllVTTPNVEPLDKLYKRVTL--NLIEKGIEVVHFDRVEPNPTVELINEGFELAKK 84
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERRKS---NNDYVVFFIDDVFKGKPLldRLPLQNGDLLIFVDTTDEPKTDQIDALRAQIRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 85 ESV---DVVLAVGGGSSIDTAKVLALTfglekidwdymfstYTNP-----FKIYDKVSEKELPLIAVSTTSGTGSQVTQA 156
Cdd:cd08184 78 ENDklpAAVVGIGGGSTMDIAKAVSNM--------------LTNPgsaadYQGWDLVKNPGIYKIGVPTLSGTGAEASRT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 157 AVIsRGSEKN-------TIFHQncfskeCIVDPELMLTLPERITASTAFDAFTHAFES----YINPNANDFteimSEKSM 225
Cdd:cd08184 144 AVL-TGPEKKlginsdyTVFDQ------VILDPELIATVPRDQYFYTGMDCYIHCVESlngtYRNAFGDAY----AEKAL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 226 ELVINYLPKvmEDKNNIEYRTKLAVADTLGGSSLANAGAAAPHPLSEIIGGVTHIPHGEALAIVFPKFaEKFYKDNIEKF 305
Cdd:cd08184 213 ELCRDVFLS--DDMMSPENREKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCIVFNVL-EEFYPEGVKEF 289
|
330 340 350
....*....|....*....|....*....|....*
gi 489535278 306 AKVARMLNQELEK-----VEDDEAAK----TLGNE 331
Cdd:cd08184 290 REMLEKQNITLPKgickdLTDEQYEKmvavTLIHE 324
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
7-358 |
2.96e-19 |
|
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: 87.91 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGKYGKKCLLVTTPNVepLDKLYKRVTLNLIEKGIEVVHFdRVEPNPTVELINEGFELAKKES 86
Cdd:COG0371 6 PRRYVQGEGALDELGEYLADLGKRALIITGPTA--LKAAGDRLEESLEDAGIEVEVE-VFGGECSEEEIERLAEEAKEQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 87 VDVVLAVGGGSSIDTAKVLAltfglekidwdymfsTYTNpfkiydkvsekeLPLIAVSTTSGTGSQVTQAAVI--SRGSE 164
Cdd:COG0371 83 ADVIIGVGGGKALDTAKAVA---------------YRLG------------LPVVSVPTIASTDAPASPLSVIytEDGAF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 165 KNTIFHQNCfSKECIVDPELMLTLPERITAS---------TAFDAFTHAFESYINPNANDFTEIMSEKSMELVINYLPKV 235
Cdd:COG0371 136 DGYSFLAKN-PDLVLVDTDIIAKAPVRLLAAgigdalakwYEARDWSLAHRDLAGEYYTEAAVALARLCAETLLEYGEAA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 236 MEDKNNIEYRTKLA--VADTLGGSSLA------NAGAAAPHPLSEiigGVTHIP------HGE--ALAIVFpkfaekfyk 299
Cdd:COG0371 215 IKAVEAGVVTPALErvVEANLLLSGLAmgigssRPGSGAAHAIHN---GLTALPethhalHGEkvAFGTLV--------- 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 489535278 300 dniekfakvarMLnqELEkvEDDEAAKtlgnEIESFLKRVGLKTKMSEFNVTKEQLEQI 358
Cdd:COG0371 283 -----------QL--VLE--GRPEEIE----ELLDFLRSVGLPTTLADLGLDDETEEEL 322
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
15-357 |
2.56e-16 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 79.12 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 15 GTLSELPRIIGKYGKKCLLVTTPNVepLDKLYKRVTLNLIEKGI--EVVHFdrvEPNPTVELINEGFELAKKESVDVVLA 92
Cdd:cd08550 9 GILAKAGEYIAPLGKKALIIGGKTA--LEAVGEKLEKSLEEAGIdyEVEVF---GGECTEENIERLAEKAKEEGADVIIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 93 VGGGSSIDTAKVLAltfglEKIDwdymfstytnpfkiydkvsekeLPLIAVSTTSGTGSQVTQAAVIsrgSEKNTIFHQN 172
Cdd:cd08550 84 IGGGKVLDTAKAVA-----DRLG----------------------LPVVTVPTIAATCAAWSALSVL---YDEEGEFLGY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 173 CFSKEC----IVDPELMLTLPERITASTAFDAFTHAFE-SYINPNAND--FTEI---MSEKSMELVINYLPKVMEDKNNI 242
Cdd:cd08550 134 SLLKRSpdlvLVDTDIIAAAPVRYLAAGIGDTLAKWYEaRPSSRGGPDdlALQAavqLAKLAYDLLLEYGVQAVEDVRQG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 243 EyRTKL--AVADT---LGG--SSLANAG--AAAPHPLSEiigGVTHIP------HGE--ALAIVFPKFAEKFYKDNIEKF 305
Cdd:cd08550 214 K-VTPAleDVVDAiilLAGlvGSLGGGGcrTAAAHAIHN---GLTKLPethgtlHGEkvAFGLLVQLALEGRSEEEIEEL 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489535278 306 AKVARMLN-----QELE-KVEDDEAAKtlgneIESFLKRVGLKTKMSEFNVTKEQLEQ 357
Cdd:cd08550 290 IEFLRRLGlpvtlEDLGlELTEEELRK-----IAEYACDPPDMAHMLPFPVTPEMLAE 342
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
13-111 |
1.33e-11 |
|
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: 65.13 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 13 GQGTLSELPRIIGKYGKKCLLVTTPNVepLDKLYKRVTLNLIEKGIEVvHFDRVEPNPTVELINEGFELAKKESVDVVLA 92
Cdd:cd08170 7 GPGALDRLGEYLAPLGKKALVIADPFV--LDLVGERLEESLEKAGLEV-VFEVFGGECSREEIERLAAIARANGADVVIG 83
|
90
....*....|....*....
gi 489535278 93 VGGGSSIDTAKVLALTFGL 111
Cdd:cd08170 84 IGGGKTIDTAKAVADYLGL 102
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
7-260 |
4.13e-10 |
|
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: 60.64 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGK--YGKKCLLVTTPNVepLDKLYKRVTLNLIEKGIEVVHFDrvepNPTVELINEGFELAKK 84
Cdd:cd08173 2 PRNVVVGHGAINKIGEVLKKllLGKRALIITGPNT--YKIAGKRVEDLLESSGVEVVIVD----IATIEEAAEVEKVKKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 85 ---ESVDVVLAVGGGSSIDTAKVLAltfglekidwdymfstytnpfkiydkvSEKELPLIAVSTTSGTGSQVTQAAVIsR 161
Cdd:cd08173 76 ikeSKADFIIGVGGGKVIDVAKYAA---------------------------YKLNLPFISIPTSASHDGIASPFASI-K 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 162 GSEKNTIFHQNcfSKECIV-DPELMLTLPERITASTAFD-------------AFTHAFESYinpnaNDFTEIMSEKSMEL 227
Cdd:cd08173 128 GGDKPYSIKAK--APIAIIaDTEIISKAPKRLLAAGCGDlisnitavkdwrlAHRLKGEYY-----SEYAASLALMSAKL 200
|
250 260 270
....*....|....*....|....*....|...
gi 489535278 228 VINYLPKVmedKNNIEYRTKLAVaDTLGGSSLA 260
Cdd:cd08173 201 IIENADLI---KPGLEEGVRTVV-KALISSGVA 229
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
7-106 |
1.88e-09 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 58.67 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGKYGKKCLLVTTPNVepLDKLYKRVTLNLIEKGIEVvHFDRVEPNPTVELINEGFELAKKES 86
Cdd:PRK09423 8 PSKYVQGKGALARLGEYLKPLGKRALVIADEFV--LGIVGDRVEASLKEAGLTV-VFEVFNGECSDNEIDRLVAIAEENG 84
|
90 100
....*....|....*....|
gi 489535278 87 VDVVLAVGGGSSIDTAKVLA 106
Cdd:PRK09423 85 CDVVIGIGGGKTLDTAKAVA 104
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
7-358 |
7.13e-09 |
|
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: 56.76 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIG---KYGKKCLLVTTPNVeplDKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEGFelaK 83
Cdd:cd08174 1 PLILKIEEGALEHLGKYLAdrnQGFGKVAIVTGEGI---DELLGEDILESLEEAGEIVTVEENTDNSAEELAEKAF---S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 84 KESVDVVLAVGGGSSIDTAKVLAltfglekidwdymfstytnpfkiydkvSEKELPLIAVSTT---SGTGSQVtqaAVI- 159
Cdd:cd08174 75 LPKVDAIVGIGGGKVLDVAKYAA---------------------------FLSKLPFISVPTSlsnDGIASPV---AVLk 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 160 ---SRGSEKNTIfhqncfSKECIVDPELMLTLPERITAS---------TA-FD---AFTHAFESYinpnaNDFTEIMSEK 223
Cdd:cd08174 125 vdgKRKSLGAKM------PYGVIVDLDVIKSAPRRLILAgigdlisniTAlYDwklAEEKGGEPV-----DDFAYLLSRT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 224 SMELVINYLPKVMEDKNNIeyrTKLAVADTLGGSSLANAGAAAP---------HPLSEIIGGVThiPHGE--ALAIVfpk 292
Cdd:cd08174 194 AADSLLNTPGKDIKDDEFL---KELAESLVLSGIAMEIAGSSRPasgsehlisHALDKLFPGPA--LHGIqvGLGTY--- 265
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489535278 293 FAEKFYKDNIEKFAKVarmlnqeLEKVEDDEAAKTLGNEIESFLKRVGLKTKM--------SEFNVTKEQLEQI 358
Cdd:cd08174 266 FMSFLQGQRYEEIRDV-------LKRTGFPLNPSDLGLTKEEFIEAVKLAPSTrpgrytilEELDLSEERLKEI 332
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
7-106 |
5.22e-08 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 54.13 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIG--KYGKKCLLVTTPNvePLDKLYKRVTLNLIEKG-IEVVhfdrVEPNPTVELINEGFELAK 83
Cdd:PRK00843 11 PRDVVVGHGVLDDIGDVCSdlKLTGRALIVTGPT--TKKIAGDRVEENLEDAGdVEVV----IVDEATMEEVEKVEEKAK 84
|
90 100
....*....|....*....|...
gi 489535278 84 KESVDVVLAVGGGSSIDTAKVLA 106
Cdd:PRK00843 85 DVNAGFLIGVGGGKVIDVAKLAA 107
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
7-357 |
9.27e-08 |
|
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: 53.34 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 7 PSRINFGQGTLSELPRIIGKYG-KKCLLVTTPNVEpldKLYKRVTLNLIEKGIEVVHFDrvepnptvELINEGFELAKKE 85
Cdd:cd08549 1 PRYTIVGDGAINKIEEILKKLNlKRVLIITGKNTK---AKYCRFFYDQLKTVCDIVYYD--------NIDNLEDELKKYT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 86 SVDVVLAVGGGSSIDTAKVLALTFGlekidwdymfstytnpfkiydkvsekeLPLIAVSTTSGTGSQVTQAAVISRGSEK 165
Cdd:cd08549 70 FYDCVIGIGGGRSIDTGKYLAYKLK---------------------------IPFISVPTSASNDGIASPIVSLRIPGVK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 166 NTIFHQNCFSkeCIVDPELMLTLPERITAS---------TAFDAFTHAFESYINPnANDFTEIMSEKSMELVINYLPKVM 236
Cdd:cd08549 123 KTFMADAPIA--IIADTEIIKKSPRRLLSAgigdlvsniTAVLDWKLAHKEKGEK-YSEFAAILSKTSAKELVSYVLKAS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 237 EDKnniEYRTKLavADTLGGSSLANAGAAAPHPLSeiiGGVTHIPHgealaiVFPKFAEKFYKDNIEKFAKVArMLNQEL 316
Cdd:cd08549 200 DLE---EYHRVL--VKALVGSGIAMAIAGSSRPAS---GSEHLFSH------ALDKLKEEYLNINVLHGEQVG-VGTIIM 264
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489535278 317 EKVEDDEAAKTLGNE--IESFLKRVGLKTKMSEFNVTKEQLEQ 357
Cdd:cd08549 265 SYLHEKENKKLSGLHerIKMILKKVGAPTTAKQLGIDEDLIIE 307
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
19-106 |
1.45e-06 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341450 Cd Length: 345 Bit Score: 49.44 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 19 ELPRIIGKYGKKCLLVTTPNVepLDKLYKRVTLNLIEKGIEVVHFDRVEPNPTVELINEgfeLAKKESV---DVVLAVGG 95
Cdd:cd08171 13 AIPKICSPYGKKVVVIGGKKA--LAAAKPKLRAALEGSGLEITDFIWYGGEATYENVEK---LKANPEVqeaDMIFAVGG 87
|
90
....*....|.
gi 489535278 96 GSSIDTAKVLA 106
Cdd:cd08171 88 GKAIDTVKVLA 98
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
13-106 |
5.20e-04 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 41.73 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535278 13 GQGTLSELPRIIGKYG-KKCLLVTTPN----VEP-LDKLYkrvtlnliEKGIEVVHFDRvepNPTVELINEGFELAKKES 86
Cdd:cd08172 7 EEGALKELPELLSEFGiKRPLIIHGEKswqaAKPyLPKLF--------EIEYPVLRYDG---ECSYEEIDRLAEEAKEHQ 75
|
90 100
....*....|....*....|
gi 489535278 87 VDVVLAVGGGSSIDTAKVLA 106
Cdd:cd08172 76 ADVIIGIGGGKVLDTAKAVA 95
|
|
| |
