|
Name |
Accession |
Description |
Interval |
E-value |
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
10-378 |
2.68e-149 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and 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: 426.92 E-value: 2.68e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 10 PANIRFGRGQAESAAPWLAQQGGPILLVHGASPQ---RAAFLRQQLETLQLAVTTLAISREPWLSDIEQGVQLAREKGIR 86
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKRALLVTGRSSLrsgRLARLLEALEAAGIEVALFSVSGEPTVETVDAAVALAREAGCD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 87 AVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEVVGTGRQLEASPLPFVAIPTTAGTGAEATKNAVINVPEQQRKVSLRDD 166
Cdd:cd08183 81 VVIAIGGGSVIDAAKAIAALLTNEGSVLDYLEVVGKGRPLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLRSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 167 RMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRALKILMEQ-ECPASRDEMAWV 245
Cdd:cd08183 161 SMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDgEDLEAREDMALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 246 SLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALN-----ESQINDPGLRqRVNDVRRWLADGLDVPVD 320
Cdd:cd08183 241 SLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANlralrEREPDSPALA-RYRELAGILTGDPDAAAE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 490253424 321 RVWDSLREWSHRAGLGTLRDLGVARDALEPAALAASTSSSMKANPVSLSGEQLLEMLE 378
Cdd:cd08183 320 DGVEWLEELCEELGIPRLSEYGLTEEDFPEIVEKARGSSSMKGNPIELSDEELLEILE 377
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
3-381 |
2.86e-106 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 317.45 E-value: 2.86e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 3 TPFTVLMPANIRFGRGQAESAAPWLAQQGG-PILLVHGASPQRAAF---LRQQLETLQLAVTTLA-ISREPWLSDIEQGV 77
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLGAkRALIVTDPGLAKLGLldrVLDALEAAGIEVVVFDdVEPNPTVETVEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 78 QLAREKGIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEVvgtgRQLEASPLPFVAIPTTAGTGAEATKNAVINVPEQ 157
Cdd:COG1454 81 AAAREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGI----KKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 158 QRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRALKILMEQ-ECP 236
Cdd:COG1454 157 GVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADgDDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 237 ASRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQIndpglRQRVNDVRRWL--ADG 314
Cdd:COG1454 237 EAREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAA-----PERYAEIARALglDVG 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 315 LDVP--VDRVWDSLREWSHRAGL-GTLRDLGVARDALEPAALAASTSSSMKANPVSLSGEQLLEMLEAAW 381
Cdd:COG1454 312 LSDEeaAEALIEAIRELLRDLGIpTRLSELGVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
10-373 |
6.20e-95 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 287.96 E-value: 6.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 10 PANIRFGRGQAESAAPWLAQQGGPILLVHGASPQRAAF---LRQQLETLQLAVTTLA-ISREPWLSDIEQGVQLAREKGI 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLKSGLldkVLASLEEAGIEVVVFDgVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 86 RAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEvvgtGRQLEASPLPFVAIPTTAGTGAEATKNAVINVPEQQRKVSLRD 165
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLG----GKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 166 DRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRALKILMEQ-ECPASRDEMAW 244
Cdd:pfam00465 157 PKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADgEDLEARENMLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 245 VSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQINDpglrqRVNDVRRWLADGLDVP-VDRVW 323
Cdd:pfam00465 237 ASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPE-----KLAQLARALGEDSDEEaAEEAI 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 490253424 324 DSLREWSHRAGL-GTLRDLGVARDALEPAALAASTSSSMKANPVSLSGEQL 373
Cdd:pfam00465 312 EALRELLRELGLpTTLSELGVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
10-349 |
8.50e-82 |
|
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: 254.29 E-value: 8.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 10 PANIRFGRGQAESAAPWLAQQGG-PILLVHGASPQRAAFL---RQQLETLQLAVTTLA-ISREPWLSDIEQGVQLAREKG 84
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGGkKVLLVTDPGLVKAGLLdkvLESLKAAGIEVEVFDdVEPNPTVETVEAAAELAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 85 IRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEVvgtgRQLEASPLPFVAIPTTAGTGAEATKNAVINVPEQQRKVSLR 164
Cdd:cd08551 81 ADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGI----GKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 165 DDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRAL-KILMEQECPASRDEMA 243
Cdd:cd08551 157 SPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLrRAVADGSDLEAREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 244 WVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQIndPGLRQRVNDVRRWLADGLDV--PVDR 321
Cdd:cd08551 237 LASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPAC--PEKYAEIAEALGEDVEGLSDeeAAEA 314
|
330 340
....*....|....*....|....*....
gi 490253424 322 VWDSLREWSHRAGL-GTLRDLGVARDALE 349
Cdd:cd08551 315 AVEAVRELLRDLGIpTSLSELGVTEEDIP 343
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-378 |
7.12e-65 |
|
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: 211.20 E-value: 7.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 9 MPANIRFGRGQAESAAPWLAQQGGPILLV--HGASPQRA--AFLRQQLETLQLAVTTLA-ISREPWLSDIEQGVQLAREK 83
Cdd:cd08185 3 QPTRILFGAGKLNELGEEALRPGKKALIVtgKGSSKKTGllDRVKKLLEKAGVEVVVFDkVEPNPLTTTVMEGAALAKEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 84 GIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEVVGTGRQLEASPLPFVAIPTTAGTGAEATKNAVINVPEQQRKVSL 163
Cdd:cd08185 83 GCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYIFGGTGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKKGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 164 RDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRALKILMEQ-ECPASRDEM 242
Cdd:cd08185 163 GHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDgSDLEAREKM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 243 AWVSLCGGLALANAGLGVIHGLAGPLGGL-SRASHGAlcgSLLPFGLALNESQIndPGLRQRVNDVRRWLADGLDVPVD- 320
Cdd:cd08185 243 AWASTLAGIVIANSGTTLPHGLEHPLSGYhPNIPHGA---GLAALYPAYFEFTI--EKAPEKFAFVARAEASGLSDAKAa 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490253424 321 -RVWDSLREWSHRAGL-GTLRDLGVARDALE--PAALAASTSSSMKANPVSLSGEQLLEMLE 378
Cdd:cd08185 318 eDFIEALRKLLKDIGLdDLLSDLGVTEEDIPwlAENAMETMGGLFANNPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-377 |
3.95e-64 |
|
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: 208.59 E-value: 3.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 5 FTVLMPANIRFGRGQAESAAPWLAQQGGP-ILLVHGASPQRAAFLRQQLETLQLAVTTL--AISREPWLSDIEQGVQLAR 81
Cdd:cd08196 1 WSYYQPVKIIFGEGILKELPDIIKELGGKrGLLVTDPSFIKSGLAKRIVESLKGRIVAVfsDVEPNPTVENVDKCARLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 82 EKGIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEvvgTGRQLEASPLPFVAIPTTAGTGAEATKNAVINVPEQQRKV 161
Cdd:cd08196 81 ENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYLE---GKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 162 SLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRALKILMEQECPA-SRD 240
Cdd:cd08196 158 PLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPNDKeARE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 241 EMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLalnesQINDPGLRQRVNDvrrwLADGLDVP-V 319
Cdd:cd08196 238 KMALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFI-----RLNAEALPGRLDE----LAKQLGFKdA 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 490253424 320 DRVWDSLREWSHRAGLGT-LRDLGVARDALEPAALAASTSSSMKANPVSLSGEQLLEML 377
Cdd:cd08196 309 EELADKIEELKKRIGLRTrLSELGITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
73-381 |
5.16e-61 |
|
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: 201.23 E-value: 5.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 73 IEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEVVGTgrqLEASPLPFVAIPTTAGTGAEATKNAVI 152
Cdd:cd14865 74 VNEAAARAREAGADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGGANR---LTRPLKPLIAIPTTAGTGSEVTLVAVI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 153 NVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIpRGIRA--LKIL 230
Cdd:cd14865 151 KDEEKKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAI-RLISEnlPKAV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 231 MEQECPASRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQINDpglrqRVNDVRRW 310
Cdd:cd14865 230 KNGKDLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAE-----RYAELALA 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490253424 311 LADGLDVPVDR-------VWDSLREWSHRAGL-GTLRDLGVARDALEPAALAASTSSSMKANPVSLSGEQLLEMLEAAW 381
Cdd:cd14865 305 LAYGVTPAGRRaeeaieaAIDLVRRLHELCGLpTRLRDVGVPEEQLEAIAELALNDGAILFNPREVDPEDILAILEAAY 383
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
10-378 |
5.40e-59 |
|
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: 195.52 E-value: 5.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 10 PANIRFGRGQAESAAPWLAQQGGP-ILLVHGASPQRAAFLRQQLETLQLAVTTLAISRE---PWLSDIEQGVQLAREKGI 85
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLGARrVLLVTGPSAVRESGAADILDALGGRIPVVVFSDFspnPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 86 RAVVSLGGGAVIDAGKAIAALvpAAGPVIDYLEVVGTGRQLEASPLPFVAIPTTAGTGAEATKNAVINVPEQQRKVSLRD 165
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAAL--LGSPGENLLLLRTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 166 DRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRALKILMEQEC-PASRDEMAW 244
Cdd:cd08182 159 PSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPnLEAREAMAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 245 VSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQINDpglRQRVNDVRRWLADGLDVPVDRVWD 324
Cdd:cd08182 239 ASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDE---CDDDPRGREILLALGASDPAEAAE 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 490253424 325 SLREWSHRAGLGT-LRDLGVARDALEPAALAASTSSSMKANPVSLSGEQLLEMLE 378
Cdd:cd08182 316 RLRALLESLGLPTrLSEYGVTAEDLEALAASVNTPERLKNNPVRLSEEDLLRLLE 370
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
67-381 |
2.76e-58 |
|
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: 193.91 E-value: 2.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 67 EPWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLevvGTGRQLEASPLPFVAIPTTAGTGAEA 146
Cdd:cd14863 67 DPPDEIVDEAAEIAREEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDYA---LAGPPVPKPGIPLIAIPTTAGTGSEV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 147 TKNAVINVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRA 226
Cdd:cd14863 144 TPIAVITDEENGVKKSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKN 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 227 LKILMEQecPAS---RDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNEsqindPGLRQR 303
Cdd:cd14863 224 LPRAVKD--GDNleaRENMLLASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNA-----EAYPEK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 304 VNDVRRWLadGLDVP-------VDRVWDSLREWSHRAGLGT-LRDLGVARDALEPAALAASTSSSMKANPVSLSGEQLLE 375
Cdd:cd14863 297 VKKIAKAL--GVSFPgesdeelGEAVADAIREFMKELGIPSlFEDYGIDKEDLDKIAEAVLKDPFAMFNPRPITEEEVAE 374
|
....*.
gi 490253424 376 MLEAAW 381
Cdd:cd14863 375 ILEAIY 380
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
10-285 |
6.83e-58 |
|
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: 192.75 E-value: 6.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 10 PANIRFGRGQAESAAPWLAQQGGP-ILLVHGASPQRAAFLRQQLETLQLAVTTLA----ISREPWLSDIEQGVQLAREKG 84
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLGGKrALIVTDKVMVKLGLVDKVTQLLAEAGIAYAvfddVVSEPTDEMVEEGLALYKEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 85 IRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYlevvGTGRQLEASPLPFVAIPTTAGTGAEATKNAVINVPEQQRKVSLR 164
Cdd:cd08194 81 CDFIVALGGGSPIDTAKAIAVLATNGGPIRDY----MGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 165 DDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRALKILMEQecP---ASRDE 241
Cdd:cd08194 157 GPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYAD--GddlEAREA 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490253424 242 MAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLP 285
Cdd:cd08194 235 MMLAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLP 278
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
5-349 |
3.32e-57 |
|
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: 191.19 E-value: 3.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 5 FTVLMPANIRFGRGQAESAAPWLAQQGG-PILLVHGASPQRAAFLRQQLETLQLAVTTLAISRE----PWLSDIEQGVQL 79
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGGkKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGvqpnPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 80 AREKGIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEVvgtgRQLEASPLPFVAIPTTAGTGAEATKNAVINVPEQQR 159
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDYEGV----DKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 160 KVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAI-------PRGIRALKILMe 232
Cdd:cd08188 157 KMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIrliaenlPKAVANGKDLE- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 233 qecpaSRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQINdpglrQRVNDVrrWLA 312
Cdd:cd08188 236 -----ARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACP-----ERFADI--ARA 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 490253424 313 DGLDVP-------VDRVWDSLREWSHRAGLGT-LRDLGVARDALE 349
Cdd:cd08188 304 LGENTEglsdeeaAEAAIEAIRKLSRRVGIPSgLKELGVKEEDFP 348
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
10-381 |
5.53e-56 |
|
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: 187.72 E-value: 5.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 10 PANIRFGRGQAESAAPWLAQQGG--PiLLVHGASPQRAAFLRQQLETLQLAVTTLA----ISREPWLSDIEQGVQLAREK 83
Cdd:cd14861 3 PTRIRFGAGAIAELPEELKALGIrrP-LLVTDPGLAALGIVDRVLEALGAAGLSPAvfsdVPPNPTEADVEAGVAAYREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 84 GIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEVVGTGRQLEASPLPFVAIPTTAGTGAEATKNAVINVPEQQRKVSL 163
Cdd:cd14861 82 GCDGIIALGGGSAIDAAKAIALMATHPGPLWDYEDGEGGPAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 164 RDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRALKILMEQ-ECPASRDEM 242
Cdd:cd14861 162 FSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADgSDLEARGEM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 243 AWVSLCGGLALANaGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQINDpglrqRVNDVRRWLADGLDvPVDRV 322
Cdd:cd14861 242 MMAALMGAVAFQK-GLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVED-----KLARLARALGLGLG-GFDDF 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 323 WDSLREWSHRAGL-GTLRDLGVARDALEPAALAASTSSSMKANPVSLSGEQLLEMLEAAW 381
Cdd:cd14861 315 IAWVEDLNERLGLpATLSELGVTEDDLDELAELALADPCHATNPRPVTAEDYRALLREAL 374
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
9-294 |
6.00e-56 |
|
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: 187.41 E-value: 6.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 9 MPANIRFGRGQAESAAPWLAQQGGPILLVHGA-SPQRAAFLRQQLETLQLAVTTLAISRE----PWLSDIEQGVQLAREK 83
Cdd:cd08181 3 MPTKVYFGKNCVEKHADELAALGKKALIVTGKhSAKKNGSLDDVTEALEENGIEYFIFDEveenPSIETVEKGAELARKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 84 GIRAVVSLGGGAVIDAGKAIAALvpAAGPVIDYLEVVGTgrqLEASPLPFVAIPTTAGTGAEATKNAVINVPEQQRKVSL 163
Cdd:cd08181 83 GADFVIGIGGGSPLDAAKAIALL--AANKDGDEDLFQNG---KYNPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 164 RDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRALKILMEQEC-PASRDEM 242
Cdd:cd08181 158 GNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDELdEEDREKL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 490253424 243 AWVSLCGGLALANAGLGVIHGLAGPL---GGLsraSHGALCGSLLPFGLALNESQ 294
Cdd:cd08181 238 MYASTLAGMVIAQTGTTLPHGLGYPLtyfKGI---PHGRANGILLPAYLKLCEKQ 289
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
10-381 |
4.83e-55 |
|
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: 185.89 E-value: 4.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 10 PANIRFGRGQAESAAPWLAQQGGPILLVH----GASPQRAAfLRQQLETLQLAVTTLAISR-EPWLSDIEQGVQLAREKG 84
Cdd:cd08191 4 PSRLLFGPGARRALGRVAARLGSRVLIVTdprlASTPLVAE-LLAALTAAGVAVEVFDGGQpELPVSTVADAAAAARAFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 85 IRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYL-EVVGTGRqleasPLPFVAIPTTAGTGAEATKNAVINVPEQQRKVSL 163
Cdd:cd08191 83 PDVVIGLGGGSNMDLAKVVALLLAHGGDPRDYYgEDRVPGP-----VLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 164 RDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSR---------------ATPFTDALCQQAIPRGIRALK 228
Cdd:cd08191 158 SSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDfppfprldpdpvyvgKNPLTDLLALEAIRLIGRHLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 229 ILMEQecPAS---RDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQIndpglRQRVN 305
Cdd:cd08191 238 RAVRD--GDDleaRSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPAR-----AAELA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 306 DVRRWL----ADGLDVPVDRVWDSLREWSHRAGL-GTLRDLGVARDALEPAALAASTSS-SMKANPVSLSGEQLLEMLEA 379
Cdd:cd08191 311 EIARALgvttAGTSEEAADRAIERVEELLARIGIpTTLADLGVTEADLPGLAEKALSVTrLIANNPRPPTEEDLLRILRA 390
|
..
gi 490253424 380 AW 381
Cdd:cd08191 391 AF 392
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
10-382 |
7.64e-53 |
|
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: 179.69 E-value: 7.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 10 PANIRFGRGQAESaapwLAQQGG--PILLVHGASPQRAAFLRQQLETLQLA-VTTLAIS---REPWLSDIEQGVQLAREK 83
Cdd:cd08179 5 PRDIYFGEGALEY----LKTLKGkrAFIVTGGGSMKRNGFLDKVEDYLKEAgMEVKVFEgvePDPSVETVEKGAEAMREF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 84 GIRAVVSLGGGAVIDAGKAIAALVPAagPVIDYLEVVgtgRQLEASPLP----FVAIPTTAGTGAEATKNAVINVPEQQR 159
Cdd:cd08179 81 EPDWIIAIGGGSVIDAAKAMWVFYEY--PELTFEDAL---VPFPLPELRkkarFIAIPSTSGTGSEVTRASVITDTEKGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 160 KVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRALKI------LMEq 233
Cdd:cd08179 156 KYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKsynggkDLE- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 234 ecpaSRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESqinDPGLRQRVNDVRRWLAD 313
Cdd:cd08179 235 ----AREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSK---DPEARARYAALLIGLTD 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490253424 314 GLDVP--VDRVWDSLREwshragLG---TLRDLGVARDA----LEPAALAASTSSSMKANPVSLSGEQLLEMLEAAWE 382
Cdd:cd08179 308 EELVEdlIEAIEELNKK------LGiplSFKEAGIDEDEffakLDEMAENAMNDACTGTNPRKPTVEEMKELLKAAYY 379
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
73-291 |
4.57e-49 |
|
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: 169.65 E-value: 4.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 73 IEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEVVGTgrqLEASPLPFVAIPTTAGTGAEATKNAVI 152
Cdd:cd08176 74 VMAGVAAYKESGADGIIAVGGGSSIDTAKAIGIIVANPGADVRSLEGVAP---TKNPAVPIIAVPTTAGTGSEVTINYVI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 153 NVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRALKI-LM 231
Cdd:cd08176 151 TDTEKKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKaVA 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 232 EQECPASRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALN 291
Cdd:cd08176 231 NPNNVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFN 290
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
67-285 |
3.20e-48 |
|
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: 166.13 E-value: 3.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 67 EPWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALvpaagpvidYLEVVGTGRQLEasplpFVAIPTTAGTGAEA 146
Cdd:cd08180 61 DPSIEVVAKGLAKILEFKPDTIIALGGGSAIDAAKAIIYF---------ALKQKGNIKKPL-----FIAIPTTSGTGSEV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 147 TKNAVINVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIprgira 226
Cdd:cd08180 127 TSFAVITDPEKGIKYPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAI------ 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490253424 227 lKILMEQ--------ECPASRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLP 285
Cdd:cd08180 201 -KLVFENlprayrdgDDLEAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLP 266
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
68-285 |
7.05e-48 |
|
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: 166.49 E-value: 7.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 68 PWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALvpAAGPVIDYLEVVGTGRQLEAsPLPFVAIPTTAGTGAEAT 147
Cdd:cd08189 68 PTIDNVEEGLALYKENGCDAIIAIGGGSVIDCAKVIAAR--AANPKKSVRKLKGLLKVRKK-LPPLIAVPTTAGTGSEAT 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 148 KNAVINVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRAL 227
Cdd:cd08189 145 IAAVITDPETHEKYAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENL 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490253424 228 KILMEQ----EcpaSRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLP 285
Cdd:cd08189 225 PKAYEDgsdlE---ARENMLLASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLP 283
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
12-285 |
2.88e-45 |
|
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: 160.40 E-value: 2.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 12 NIRFGRGQAESAAPWLAQQGGP-ILLVHGASPQRAAFLRQQLETLQLAVTTLAI----SREPWLSDIEQGVQLAREKGIR 86
Cdd:cd08190 3 NIRFGPGATRELGMDLKRLGAKkVLVVTDPGLAKLGLVERVLESLEKAGIEVVVydgvRVEPTDESFEEAIEFAKEGDFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 87 AVVSLGGGAVIDAGKAIAALVPAAGPVIDYL-EVVGTGRQLEASPLPFVAIPTTAGTGAEATKNAVINVPEQQRKVSLRD 165
Cdd:cd08190 83 AFVAVGGGSVIDTAKAANLYATHPGDFLDYVnAPIGKGKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 166 DRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLC----SR--------------ATPFTDALCQQAIPRGIRAL 227
Cdd:cd08190 163 RYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTArpynARprpanpderpayqgSNPISDVWAEKAIELIGKYL 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490253424 228 K--ILMEQECPAsRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSR-------------ASHGALCGSLLP 285
Cdd:cd08190 243 RraVNDGDDLEA-RSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKdyrppgypvdhphVPHGLSVALTAP 314
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
73-348 |
3.28e-43 |
|
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: 154.24 E-value: 3.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 73 IEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYlevVGTGRQLEASPlPFVAIPTTAGTGAEATKNAVI 152
Cdd:cd17814 72 VMEGAELYREEGCDGIVAVGGGSPIDCAKGIGIVVSNGGHILDY---EGVDKVRRPLP-PLICIPTTAGSSADVSQFAII 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 153 NVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRAL-KILM 231
Cdd:cd17814 148 TDTERRVKMAIISKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLpKAVA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 232 EQECPASRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQINDpglrqRVNDVrrwl 311
Cdd:cd17814 228 DPDDLEAREKMMLASLQAGLAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPE-----RYRKI---- 298
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490253424 312 ADGLDVPVD---------RVWDSLREWSHRAGL-GTLRDLGVARDAL 348
Cdd:cd17814 299 AEAMGLDVDglddeevaeRLIEAIRDLREDLGIpETLSELGVDEEDI 345
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
5-289 |
8.52e-43 |
|
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: 153.36 E-value: 8.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 5 FTVLMPANIRFGRGQAESAAPWLAQQGGPILLVHGASP-------QRaafLRQQLETLQLAVTTLA-ISREPWLSDIEQG 76
Cdd:cd08187 2 FTFYNPTKIIFGKGAIEELGEEIKKYGKKVLLVYGGGSikknglyDR---VVASLKEAGIEVVEFGgVEPNPRLETVREG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 77 VQLAREKGIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLevvgTGRQLEASPLPFVAIPTTAGTGAEATKNAVINVPE 156
Cdd:cd08187 79 IELAREENVDFILAVGGGSVIDAAKAIAAGAKYDGDVWDFF----TGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 157 QQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLC-SRATPFTDALCqQAIPRG-IRALKILMEQe 234
Cdd:cd08187 155 TKEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTgTEDAPLQDRLA-EGLLRTvIENGPKALKD- 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490253424 235 cPAS---RDEMAWvslCGGLALAN-AGLGV-----IHGLAGPLGGLSRASHGAlcgsllpfGLA 289
Cdd:cd08187 233 -PDDyeaRANLMW---AATLALNGlLGAGRggdwaTHAIEHELSALYDITHGA--------GLA 284
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
67-349 |
1.68e-42 |
|
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: 152.38 E-value: 1.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 67 EPWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALVPAagPVIDYLEVvgtgrqleaSPLP---------FVAIP 137
Cdd:cd14862 64 EPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAKAAWVLYER--PDLDPEDI---------SPLDllglrkkakLIAIP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 138 TTAGTGAEATKNAVINVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQ 217
Cdd:cd14862 133 TTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALAL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 218 QAIpRGI-----RALKILMEQEcpaSRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNe 292
Cdd:cd14862 213 KAI-ELIfkylpRAYKDGDDLE---AREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFY- 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490253424 293 sqindpglrQRVNDVRRWLADGLDVPV-------DRVWDSLREWSHRAGL-GTLRDLGVARDALE 349
Cdd:cd14862 288 ---------AKVTDERYDLLKLLGIEArdeeealKKLVEAIRELYKEVGQpLSIKDLGISEEEFE 343
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
68-381 |
7.74e-41 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 148.22 E-value: 7.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 68 PWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALVpaAGPviDYLEVvgtgRQLE-ASP-----LPFVAIPTTAG 141
Cdd:PRK10624 71 PTIEVVKEGVEVFKASGADYLIAIGGGSPQDTCKAIGIIS--NNP--EFADV----RSLEgVAPtkkpsVPIIAIPTTAG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 142 TGAEATKNAVINVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIP 221
Cdd:PRK10624 143 TAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 222 RGIRALKILMEQEcPASRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNesqindpglR 301
Cdd:PRK10624 223 IIAGALRGAVAGD-KEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYN---------A 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 302 QRVNDVRRWLADGLDVPVDRV---------WDSLREWSHRAGL-GTLRDLGVARDALEPAALAASTSSSMKANPVSLSGE 371
Cdd:PRK10624 293 DFTGEKYRDIARAMGVKVEGMsleearnaaVEAVKALNRDVGIpPHLRDVGVKEEDIPALAQAAFDDVCTGGNPREATLE 372
|
330
....*....|
gi 490253424 372 QLLEMLEAAW 381
Cdd:PRK10624 373 DIVELYKKAW 382
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
68-380 |
8.29e-40 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 145.48 E-value: 8.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 68 PWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYlevvgTGRQLEASP-LPFVAIPTTAGTGAEA 146
Cdd:PRK09860 72 PTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDY-----EGVDRSAKPqLPMIAINTTAGTASEM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 147 TKNAVINVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRA 226
Cdd:PRK09860 147 TRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAEN 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 227 LKILMEQ-ECPASRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNeSQINDPGLRQ--- 302
Cdd:PRK09860 227 LPLAVEDgSNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFN-SKVAAARLRDcaa 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 303 --RVNDVRRWLADGLDVPVDRVWDSLREWSHRAGlgtLRDLGVARDALEPAALAASTSSSMKANPVSLSGEQLLEMLEAA 380
Cdd:PRK09860 306 amGVNVTGKNDAEGAEACINAIRELAKKVDIPAG---LRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAA 382
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-381 |
4.84e-39 |
|
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: 143.21 E-value: 4.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 9 MPANIRFGRGQAESAAPWLAQQGGPILLVHG---ASPQRAAFLRQQLETLQLAVTTLA-ISREPWLSDIEQGVQLAREKG 84
Cdd:cd14864 3 IPPNIVFGADSLERIGEEVKEYGSRFLLITDpvlKESGLADKIVSSLEKAGISVIVFDeIPASATSDTIDEAAELARKAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 85 IRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEvvgtGRQLEASPLPFVAIPTTAGTGAEATKNAVInVPEQQRKVSL- 163
Cdd:cd14864 83 ADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLE----GAKPKKKPLPLIAVPTTPRSGFEFSDRFPV-VDSRSREVKLl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 164 RDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALcqqaiprGIRALKILMEQECPASRDE-- 241
Cdd:cd14864 158 KAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDAL-------ALKAIELVSENLDGALADPkn 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 242 ------MAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALN-ESQINDPGLRQRVNDVRRWLADG 314
Cdd:cd14864 231 tpaeelLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAaTSAPDKYAKIARALGEDVEGASP 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490253424 315 LDVpVDRVWDSLREWSHRAGL-GTLRDLGVArDALEPAALAASTSSSMKANPVSLSGEQLLEMLEAAW 381
Cdd:cd14864 311 EEA-AIAAVEGVRRLIAQLNLpTRLKDLDLA-SSLEQLAAIAEDAPKLNGLPRSMSSDDIFDILKAAF 376
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
67-291 |
1.59e-37 |
|
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: 139.63 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 67 EPWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALVPAagPVIDYLEVVGT-----GRqleASPLP-------FV 134
Cdd:cd08178 63 DPTLSTVRKGLEAMNAFKPDVIIALGGGSAMDAAKIMWLFYEH--PETKFEDLAQRfmdirKR---VYKFPklgkkakLV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 135 AIPTTAGTGAEATKNAVINVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDA 214
Cdd:cd08178 138 AIPTTSGTGSEVTPFAVITDDKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 215 LCQQAI-------PRGIRalkilmEQECPASRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFG 287
Cdd:cd08178 218 LALQAIklifeylPRSYN------NGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHV 291
|
....
gi 490253424 288 LALN 291
Cdd:cd08178 292 IRYN 295
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
67-380 |
3.04e-37 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 138.62 E-value: 3.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 67 EPWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLevvgTGRQLEASPLPFVAIPTTAGTGAEA 146
Cdd:PRK15454 89 EPCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEM----SETSVLQPRLPLIAIPTTAGTGSET 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 147 TKNAVINVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRA 226
Cdd:PRK15454 165 TNVTVIIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 227 L-KILMEQECPASRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQIndpglRQRVN 305
Cdd:PRK15454 245 LpKAVGYGHDLAARESMLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVC-----RERFS 319
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490253424 306 DVRRWLADGLDVPVDRVwDSLREWSHRAGLGT-LRDLGVARDALEPAALAASTSSSMKANPVSLSGEQLLEMLEAA 380
Cdd:PRK15454 320 QIGRALRTKKSDDRDAI-NAVSELIAEVGIGKrLGDVGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLYAAA 394
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
10-381 |
7.57e-36 |
|
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: 134.67 E-value: 7.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 10 PANIRFGRGQAESAAPWLAQQGGP-ILLVHGASPQRAAFLRQQLETL---QLAVTTLAISREPWLSDIEQGVQLAREKGI 85
Cdd:cd14866 5 PLRLFSGRGALARLGRELDRLGARrALVVCGSSVGANPDLMDPVRAAlgdRLAGVFDGVRPHSPLETVEAAAEALREADA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 86 RAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEVVGTGRQ-----LEASPLPFVAIPTTAgTGAEATKNAVINVPEQQRK 160
Cdd:cd14866 85 DAVVAVGGGSAIVTARAASILLAEDRDVRELCTRRAEDGLmvsprLDAPKLPIFVVPTTP-TTADVKAGSAVTDPPAGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 161 VSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRALKILMEQECPASRD 240
Cdd:cd14866 164 LALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLADDDDPAARA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 241 EMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQIndPGLRQRVNDVRRWLADGLDVPVD 320
Cdd:cd14866 244 DLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPAT--DGRLDRLAEALGVADAGDEASAA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490253424 321 RVWDSLREWshRAGLG---TLRDLGVARDALEPAALAASTSSSMKANPVSL-SGEQLLEMLEAAW 381
Cdd:cd14866 322 AVVDAVEAL--LDALGvptRLRDLGVSREDLPAIAEAAMDDWFMDNNPRPVpTAEELEALLEAAW 384
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
10-381 |
2.73e-35 |
|
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: 132.24 E-value: 2.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 10 PANIRFGRGQAESAAPWLAQQGG--PILLVHGASPQRAAFLRQQLETLQLAVTTLAISREPWlSDIEQGVQLAREKGIRA 87
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLGArrALVLSTPRQRALAERVAALLGDRVAGVFDGAVMHVPV-EVAERALAAAREAGADG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 88 VVSLGGGAVIDAGKAIAAlvpaagpvidylevvgtgrqleASPLPFVAIPTTAgTGAEATknAVINVPEQQRKVSLRDDR 167
Cdd:cd08177 80 LVAIGGGSAIGLAKAIAL----------------------RTGLPIVAVPTTY-AGSEMT--PIWGETEDGVKTTGRDPR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 168 MLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRAL-KILMEQECPASRDEMAWVS 246
Cdd:cd08177 135 VLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALpRLVADPSDLEARSDALYGA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 247 LCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQIndPGLRQRVNDvrrwlADGLDVPVDRVWDSL 326
Cdd:cd08177 215 WLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAA--PDAMARLAR-----ALGGGDAAGGLYDLA 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490253424 327 RewshRAGLGT-LRDLGVARDALEPAALAASTSSSmkANPVSLSGEQLLEMLEAAW 381
Cdd:cd08177 288 R----RLGAPTsLRDLGMPEDDIDRAADLALANPY--PNPRPVERDALRALLERAW 337
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
48-285 |
1.85e-33 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 131.85 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 48 LRQQLETLQLAVTTLAIS---REPWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALVPAagPVIDYLEVV---- 120
Cdd:PRK13805 500 VTDVLKKRENGVEYEVFSevePDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMWLFYEH--PETDFEDLAqkfm 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 121 ------------GTGRQleasplpFVAIPTTAGTGAEATKNAVINVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSIT 188
Cdd:PRK13805 578 dirkriykfpklGKKAK-------LVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLT 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 189 LSSGLDALTQVIEPWLCSRATPFTDALCQQAIprgiralKILME---------QECPASRDEMAWVSLCGGLALANAGLG 259
Cdd:PRK13805 651 ADTGIDALTHALEAYVSVMASDYTDGLALQAI-------KLVFEylprsykngAKDPEAREKMHNASTIAGMAFANAFLG 723
|
250 260
....*....|....*....|....*.
gi 490253424 260 VIHGLAGPLGGLSRASHGALCGSLLP 285
Cdd:PRK13805 724 ICHSMAHKLGAEFHIPHGRANAILLP 749
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
13-380 |
1.43e-32 |
|
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: 125.82 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 13 IRFGRGQAESAAPWLAQQGGP-ILLVHGASPQRAAFLRQQLETLQ----LAVTTLAISREPWlSDIEQGVQLAREKGIRA 87
Cdd:cd08192 4 VSYGPGAVEALLHELATLGASrVFIVTSKSLATKTDVIKRLEEALgdrhVGVFSGVRQHTPR-EDVLEAARAVREAGADL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 88 VVSLGGGAVIDAGKAI----AALVPAAGPVIDYLEVVGTGRQLEASPLPFVAIPTTAgTGAEATKNAVINVPEQQRKVSL 163
Cdd:cd08192 83 LVSLGGGSPIDAAKAValalAEDVTDVDQLDALEDGKRIDPNVTGPTLPHIAIPTTL-SGAEFTAGAGATDDDTGHKQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 164 RDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPwLCS-RATPFTDALCQQAIPRGIRALKILME-QECPASRDE 241
Cdd:cd08192 162 AHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVET-LCSpQATPFVDALALKALRLLFEGLPRSKAdPEDLEARLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 242 M---AWvsLCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESqiNDPGLRQRVNDVRRWLADGLDVP 318
Cdd:cd08192 241 CqlaAW--LSLFGLGSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAP--VNAERQRLIARALGLVTGGLGRE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490253424 319 VDRVWDSLREWSHRAGLG-TLRDLGVARDALEPAALAASTSSSMKANPVSL-SGEQLLEMLEAA 380
Cdd:cd08192 317 AADAADAIDALIRELGLPrTLRDVGVGRDQLEKIAENALTDVWCRTNPRPItDKDDVLEILESA 380
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
5-349 |
6.40e-32 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 124.03 E-value: 6.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 5 FTVLMPANIRFGRGQAESAAPWLAQQGGPILLVHGA-SPQRAAFL---RQQLETLQLAVTTLA-ISREPWLSDIEQGVQL 79
Cdd:COG1979 4 FTFYNPTKIIFGKGQIAKLGEEIPKYGKKVLLVYGGgSIKKNGLYdqvKAALKEAGIEVVEFGgVEPNPRLETVRKGVEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 80 AREKGIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEvvgTGRQLEaSPLPFVAIPTTAGTGAEATKNAVINVPEQQR 159
Cdd:COG1979 84 CKEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDILT---GKAPVE-KALPLGTVLTLPATGSEMNSGSVITNEETKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 160 KVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCS-RATPFTDALCQqaiprGIraLKILMEqECP-- 236
Cdd:COG1979 160 KLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYpVDAPLQDRFAE-----GL--LRTLIE-EGPka 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 237 -------ASRDEMAWvslCGGLALaN--AGLGV-----IHGLAGPLGGLSRASHGAlcgsllpfGLAlnesqINDPGL-- 300
Cdd:COG1979 232 lkdpedyDARANLMW---AATLAL-NglIGAGVpqdwaTHMIEHELSALYDIDHGA--------GLA-----IVLPAWmr 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490253424 301 RQRVNDVRRWLADGldvpvDRVW---------------DSLREWSHRAGLGT-LRDLGVARDALE 349
Cdd:COG1979 295 YVLEEKPEKFAQYA-----ERVWgitegddeeralegiEATEEFFESLGLPTrLSEYGIDEEDIE 354
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
10-381 |
7.09e-31 |
|
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: 121.08 E-value: 7.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 10 PANIRFGRGQAESAAPWLAQQGGP-ILLVHGASPQRAAFLRQQLETLQ---LAVTTL-AISREPWLSDIEQGVQLAREKG 84
Cdd:cd08193 4 VPRIICGAGAAARLGELLRELGARrVLLVTDPGLVKAGLADPALAALEaagIAVTVFdDVVADPPEAVVEAAVEQAREAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 85 IRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEV--VGTGRqleaspLPFVAIPTTAGTGAEATKNAVINVPEQQRK-- 160
Cdd:cd08193 84 ADGVIGFGGGSSMDVAKLVALLAGSDQPLDDIYGVgkATGPR------LPLILVPTTAGTGSEVTPISIVTTGETEKKgv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 161 VSlrdDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLC-SRATPFTDALcqqaiprGIRALKIL---MEQEC- 235
Cdd:cd08193 158 VS---PQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDAL-------AREALRLLganLRRAVe 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 236 ----PASRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHGaLCGSL-LPFGLALNES----------QINDPGL 300
Cdd:cd08193 228 dgsdLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHG-LSNALvLPHVLRFNLPaaealyaelaRALLPGL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 301 RQRVNDVRrwlADGLdvpVDRvwdsLREWSHRAGL-GTLRDLGVARDALEpaalaASTSSSMK------ANPVSLSGEQL 373
Cdd:cd08193 307 AFGSDAAA---AEAF---IDA----LEELVEASGLpTRLRDVGVTEEDLP-----MLAEDAMKqtrllvNNPREVTEEDA 371
|
....*...
gi 490253424 374 LEMLEAAW 381
Cdd:cd08193 372 LAIYQAAL 379
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
68-285 |
2.53e-30 |
|
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: 119.68 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 68 PWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALVPAAGPVIDYLEvvgTGRQLEASPLPFVAIPTTAGTGAEAT 147
Cdd:cd08186 65 PTVDQADEAAKLARDFGADAVIAIGGGSPIDTAKSVAVLLAYGGKTARDLY---GFRFAPERALPLVAINLTHGTGSEVD 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 148 KNAVINVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIPRGIRAL 227
Cdd:cd08186 142 RFAVATIPEKGYKPGIAYDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYL 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 228 KILM-EQECPASRDEMAWVSLCGGLALANAGLGVIHGLAGPLGGLS-RASHGALCGSLLP 285
Cdd:cd08186 222 PRALaNPKDLEARYWLLYASMIAGIAIDNGLLHLTHALEHPLSGLKpELPHGLGLALLGP 281
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
67-375 |
5.72e-28 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 112.69 E-value: 5.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 67 EPwlSD--IEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAalVPAAGPVIDYLEvvgtGRQLEASPLPFVAIPTTAGTGA 144
Cdd:cd14860 61 EP--SDemVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLA--LKGISPVLDLFD----GKIPLIKEKELIIVPTTCGTGS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 145 EATKNAVINVPEQQRKVSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIpRGI 224
Cdd:cd14860 133 EVTNISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAI-EMI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 225 RALKILMEQECPASR----DEMAWVSLCGGLALANAGLGVIHGLAGPLGGLSRASHG----ALCGSLLPfglalNESQIN 296
Cdd:cd14860 212 LEGYQEIAEKGEEARfpllGDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGeanyAVFTGVLK-----NYQEKN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 297 DPGlrqRVNDVRRWLADGLDVPVDRVWDSLREWshragLGT------LRDLGVARDALE--PAALAASTSSSMKANPVSL 368
Cdd:cd14860 287 PDG---EIKKLNEFLAKILGCDEEDVYDELEEL-----LNKilpkkpLHEYGMKEEEIDefADSVMENQQRLLANNYVPL 358
|
....*..
gi 490253424 369 SGEQLLE 375
Cdd:cd14860 359 DREDVAE 365
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
67-350 |
1.04e-21 |
|
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: 93.58 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 67 EPWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALVPAAgpvidylevvgtgrqleaspLPFVAIPTTAGTGAEA 146
Cdd:cd07766 60 NPTFEEVKNAVERARAAEADAVIAVGGGSTLDTAKAVAALLNRG--------------------IPFIIVPTTASTDSEV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 147 TKNAVINVPEQQRKvsLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEpwlcsratpftdalcqqaiprgira 226
Cdd:cd07766 120 SPKSVITDKGGKNK--QVGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE------------------------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 227 lkilmeqecpasRDEMAWVS-LCGGLALANAGLGVIHGLAGPLGGLSRASHGALCGSLLPFGLALNESQINDPGlrQRVN 305
Cdd:cd07766 173 ------------LEKVVEAAtLAGMGLFESPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPEPE--AAIE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490253424 306 DVRRWLADgLDVPVDrvwdslrewshraglgtLRDLGVARDALEP 350
Cdd:cd07766 239 AVFKFLED-LGLPTH-----------------LADLGVSKEDIPK 265
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
86-272 |
3.95e-21 |
|
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: 93.10 E-value: 3.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 86 RAVVSLGGGAVIDAGKAIAALVPAAGPVIDYlevvgTGRQLEASP-LPFVAIPTTAGTGAEATKNAVINVPEqqRKVSLR 164
Cdd:cd08184 84 AAVVGIGGGSTMDIAKAVSNMLTNPGSAADY-----QGWDLVKNPgIYKIGVPTLSGTGAEASRTAVLTGPE--KKLGIN 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 165 DDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATPFTDALCQQAIP--RGIRALKILMEqecPASRDEM 242
Cdd:cd08184 157 SDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALElcRDVFLSDDMMS---PENREKL 233
|
170 180 190
....*....|....*....|....*....|
gi 490253424 243 AWVSLCGGLALANAGLGVIHGLAgplGGLS 272
Cdd:cd08184 234 MVASYLGGSSIANSQVGVCHALS---YGLS 260
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
6-196 |
2.13e-14 |
|
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: 73.66 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 6 TVLMPANIRFGRGQAESAAPWLAQQGGPILLVHGASPQRAA--FLRQQLETLQLAVTTLAISREPWLSDIEQGVQLAREK 83
Cdd:COG0371 2 VIILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAgdRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAKEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 84 GIRAVVSLGGGAVIDAGKAIAalvpaagpviDYLEvvgtgrqleaspLPFVAIPTTAGTGAEATKNAVINVPEQQRKVSL 163
Cdd:COG0371 82 GADVIIGVGGGKALDTAKAVA----------YRLG------------LPVVSVPTIASTDAPASPLSVIYTEDGAFDGYS 139
|
170 180 190
....*....|....*....|....*....|....
gi 490253424 164 RDDRMlPDLAIVDPALTDNAPRSiTLSSGL-DAL 196
Cdd:COG0371 140 FLAKN-PDLVLVDTDIIAKAPVR-LLAAGIgDAL 171
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
5-244 |
1.31e-12 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 68.28 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 5 FTVLMPANIRFGRGQAESAAPWLAQQGGPILLVHGASPQRAAFLRQQLETLQ-LAVTTLA-ISREPWLSDIEQGVQLARE 82
Cdd:PRK15138 4 FNLHTPTRILFGKGAIAGLREQIPADARVLITYGGGSVKKTGVLDQVLDALKgMDVLEFGgIEPNPTYETLMKAVKLVRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 83 KGIRAVVSLGGGAVIDAGKAIAALV--PAAgpvIDYLEVVGTGRQLEASPLPFVAIPTTAGTGAEATKNAVINVPEQQRK 160
Cdd:PRK15138 84 EKITFLLAVGGGSVLDGTKFIAAAAnyPEN---IDPWHILETGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 161 VSLRDDRMLPDLAIVDPALTDNAPRSITLSSGLDALTQVIEPWLCSRATP-----FTDALCQQAIPRGIRALKilmEQEC 235
Cdd:PRK15138 161 QAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAkiqdrFAEGILLTLIEEGPKALK---EPEN 237
|
....*....
gi 490253424 236 PASRDEMAW 244
Cdd:PRK15138 238 YDVRANVMW 246
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
14-281 |
1.10e-11 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 64.25 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 14 RFGRGQAESAAPWLAQQGGP-ILLVHGASPQRAAF--LRQQLETLQLAVTTLA-ISREPWLSDIEQGVQLAREKGIRAVV 89
Cdd:pfam13685 1 VIGPGALGRLGEYLAELGFRrVALVADANTYAAAGrkVAESLKRAGIEVETRLeVAGNADMETAEKLVGALRERDADAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 90 SLGGGAVIDAGKAIAALVpaagpvidylevvgtgrqleasPLPFVAIPTTAGTGAEATKNAVINVpeQQRKVSLRddRML 169
Cdd:pfam13685 81 GVGGGTVIDLAKYAAFKL----------------------GKPFISVPTAASNDGFASPGASLTV--DGKKRSIP--AAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 170 PDLAIVDPALTDNAPRSITLSSGLDALTQVIEP--WLCSRATPFTDALCQQAI-------------PRGIRALKILMEQe 234
Cdd:pfam13685 135 PFGVIADTDVIAAAPRRLLASGVGDLLAKITAVadWELAHAEEVAAPLALLSAamvmnfadrplrdPGDIEALAELLSA- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490253424 235 cpasrdemawvSLCGGLALANAGLGVIHGLAGPLGGLS--RASHGALCG 281
Cdd:pfam13685 214 -----------LAMGGAGSSRPASGSEHLISHALDMIApkQALHGEQVG 251
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
10-196 |
1.93e-08 |
|
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: 55.62 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 10 PANIRFGRGQAESAAPWLAQQGGPILLVHGASPQRAAflRQQLET-LQLAVTTLAI---SREPWLSDIEQGVQLAREKGI 85
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAV--GEKLEKsLEEAGIDYEVevfGGECTEENIERLAEKAKEEGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 86 RAVVSLGGGAVIDAGKAIAALvpaAGpvidylevvgtgrqleaspLPFVAIPTTAGTGAEATKNAVINVPEQQRKVSLRD 165
Cdd:cd08550 79 DVIIGIGGGKVLDTAKAVADR---LG-------------------LPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLL 136
|
170 180 190
....*....|....*....|....*....|..
gi 490253424 166 DRMlPDLAIVDPALTDNAPRSiTLSSG-LDAL 196
Cdd:cd08550 137 KRS-PDLVLVDTDIIAAAPVR-YLAAGiGDTL 166
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
48-196 |
1.95e-08 |
|
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: 55.50 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 48 LRQQLETLQLAVTTLAISREPWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAalvpaagpviDYLEvvgtgrqle 127
Cdd:cd08170 41 LEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADVVIGIGGGKTIDTAKAVA----------DYLG--------- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490253424 128 aspLPFVAIPTTAGTGAEATKNAVINVPEQqrkvSLRDDRML---PDLAIVDPALTDNAPRSiTLSSGL-DAL 196
Cdd:cd08170 102 ---LPVVIVPTIASTDAPCSALSVIYTEDG----EFDEYLFLprnPDLVLVDTEIIAKAPVR-FLVAGMgDAL 166
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
73-208 |
2.58e-06 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 49.04 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 73 IEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAalvpaagpviDYLEVvgtgrqleasplPFVAIPTTAGTGAEATKNAVI 152
Cdd:PRK09423 73 IDRLVAIAEENGCDVVIGIGGGKTLDTAKAVA----------DYLGV------------PVVIVPTIASTDAPTSALSVI 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 153 NVPEQqrkvSLRDDRML---PDLAIVDPALTDNAPRSItLSSGL-DALTQVIEPWLCSRA 208
Cdd:PRK09423 131 YTEEG----EFERYLFLpknPDLVLVDTAIIAKAPARF-LAAGIgDALATWFEARACSRS 185
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
31-185 |
2.93e-04 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 42.57 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 31 GGPILLVHGASPQRAA--FLRQQLETLqlAVTTLAISREPWLSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAalvp 108
Cdd:PRK00843 34 TGRALIVTGPTTKKIAgdRVEENLEDA--GDVEVVIVDEATMEEVEKVEEKAKDVNAGFLIGVGGGKVIDVAKLAA---- 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490253424 109 aagpviDYLEVvgtgrqleasplPFVAIPTTAGTGAEATKNAVInvPEQQRKVSLRDDrmlPDLAIV-DPALTDNAPR 185
Cdd:PRK00843 108 ------YRLGI------------PFISVPTAASHDGIASPRASI--KGGGKPVSVKAK---PPLAVIaDTEIIAKAPY 162
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
70-185 |
6.07e-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: 41.35 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 70 LSDIEQGVQLAREKGIRAVVSLGGGAVIDAGKAIAALvpaagpvidylevvgtgrqleaSPLPFVAIPTTAGTGAEATKN 149
Cdd:cd08172 61 YEEIDRLAEEAKEHQADVIIGIGGGKVLDTAKAVADK----------------------LNIPLILIPTLASNCAAWTPL 118
|
90 100 110
....*....|....*....|....*....|....*.
gi 490253424 150 AVINVPEQQRKVSLRDDRMlPDLAIVDPALTDNAPR 185
Cdd:cd08172 119 SVIYDEDGEFIGYDYFPRS-AYLVLVDPRLLLDSPK 153
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
66-190 |
7.95e-04 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 40.97 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253424 66 REPWLSDIEQGVQLAR-EKGIRAVVSLGGGAVIDAGKAIAALvpaagpvidylevvgtgrqleaSPLPFVAIPTTAGTGA 144
Cdd:cd08174 58 EENTDNSAEELAEKAFsLPKVDAIVGIGGGKVLDVAKYAAFL----------------------SKLPFISVPTSLSNDG 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 490253424 145 EATKNAVINVpeQQRKVSLRdDRMlPDLAIVDPALTDNAPRSITLS 190
Cdd:cd08174 116 IASPVAVLKV--DGKRKSLG-AKM-PYGVIVDLDVIKSAPRRLILA 157
|
|
| |
