|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
5-251 |
0e+00 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 512.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 5 ISFTLKVWRQKGPKAKGAFETYQMKDIPGDTSFLEMLDILNEQLISEGKEPVVFDHDCREGICGMCSLYINGHPHGPATG 84
Cdd:PRK07570 1 MKLTLKIWRQKGPDDKGKFETYEVDDISPDMSFLEMLDVLNEQLIEKGEEPVAFDHDCREGICGMCGLVINGRPHGPDRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 85 ATTCQIYMRRFNDGDTITVEPWRSAGFPVIKDLMVDRTAYDKIMQAGGYVSVRTGAPQDANAILIPKPIADEAMDAASCI 164
Cdd:PRK07570 81 TTTCQLHMRSFKDGDTITIEPWRAAAFPVIKDLVVDRSALDRIIQAGGYVSVNTGGAPDANAIPVPKEDADRAFDAAACI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 165 GCGACVAACKNGSAMLFVSAKVSQLNLLPQGKPEALRRAKAMLSKMDELGFGNCTNTRACEAECPKNVSISNIARLNRDF 244
Cdd:PRK07570 161 GCGACVAACPNGSAMLFTGAKVSHLALLPQGQPERARRVRAMVAQMDEEGFGNCTNTGECEAVCPKGISLENIARMNREY 240
|
....*..
gi 492395712 245 IIAKLKD 251
Cdd:PRK07570 241 LRASFRG 247
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
7-247 |
3.89e-88 |
|
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440247 [Multi-domain] Cd Length: 230 Bit Score: 260.83 E-value: 3.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 7 FTLKVWRQKGPK-AKGAFETYQMkDIPGDTSFLEMLDILNEqlisEGKEPVVFDHDCREGICGMCSLYINGHPhgpatgA 85
Cdd:COG0479 3 VTLKIWRQDPETdSKPRFQTYEV-PVSPGMTVLDALDYIKE----EQDPTLAFRRSCREGICGSCAMVINGRP------R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 86 TTCQIYMRRFNdgDTITVEPWRsaGFPVIKDLMVDRTA-YDKIMQAGGYVSVRTGAPQdaNAILIPKPIADEAMDAASCI 164
Cdd:COG0479 72 LACQTHVRDLK--DTITIEPLR--NFPVIKDLVVDRSAfFDKLKKVKPYLSPDGPAPD--NERLQSPEDREKADDLAECI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 165 GCGACVAACKNGSAML-FVSAKVS----QLNLLPQGKpEALRRAKAMlskMDELGFGNCTNTRACEAECPKNVSIS-NIA 238
Cdd:COG0479 146 LCGACVAACPNVWANPdFLGPAALaqayRFALDPRDE-ETEERLEAL---EDEEGVWRCTTCGNCTEVCPKGIPPTkAIA 221
|
....*....
gi 492395712 239 RLNRDFIIA 247
Cdd:COG0479 222 KLKREALKR 230
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
8-124 |
6.00e-29 |
|
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.
Pssm-ID: 432963 [Multi-domain] Cd Length: 107 Bit Score: 105.40 E-value: 6.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 8 TLKVWRQKGPKAKGA--FETYQMKDIPGDTsFLEMLDILNEQLisegKEPVVFDHDCREGICGMCSLYINGHPhgpatgA 85
Cdd:pfam13085 1 TLRVFRYDPRVDRDEpyYQEYEVPYEEGMT-VLDALNKIKEEQ----DPTLAFRRSCREGICGSCAMNINGKP------R 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 492395712 86 TTCQIYMRRFNDGDtITVEPWrsAGFPVIKDLMVDRTAY 124
Cdd:pfam13085 70 LACKTLIDDLLGQD-ITLEPL--PGFPVIRDLVVDRSAF 105
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
24-232 |
6.21e-19 |
|
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]
Pssm-ID: 273049 [Multi-domain] Cd Length: 220 Bit Score: 82.48 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 24 ETYQMKDIPGdTSFLEMLDILNEQLISEgkepVVFDHDCREGICGMCSLYINGHPhgpaTGATTCQIymrRFNDGDTITV 103
Cdd:TIGR00384 15 QSYEVPADEG-MTVLDALNYIKDEQDPS----LAFRRSCRNGICGSCAMNVNGKP----VLACKTKV---EDLGQPVMKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 104 EPWrsAGFPVIKDLMVDRTA-YDKIMQAGGYVSvRTGAPQDANAILIpKPIADEAMDAAS-CIGCGACVAAC----KN-- 175
Cdd:TIGR00384 83 EPL--PNLPVIKDLVVDMGPfYAKLEAIKPYLI-RKSQPEPEGEFLQ-TPEQREKLDQLSgCILCGCCYSSCpafwWNpe 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492395712 176 --GSAMLfvsAKVSQLNLLPQGKPEALRraKAMLSkmDELGFGNCTNTRACEAECPKNV 232
Cdd:TIGR00384 159 flGPAAL---TAAYRFLIDSRDHATKDR--LEGLN--DKNGVWRCTTCMNCSEVCPKGV 210
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
148-245 |
2.06e-06 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 48.17 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 148 LIPKPIADEAMD-AASCIGCGACVAACKNGsamLFVsakvsqlnllpqgkPEALRRAKAM-LSKMDELgFGNCTNTRACE 225
Cdd:cd01916 351 EKKLPTDEEFQElAAKCTDCGWCTRACPNS---LRI--------------KEAMEAAKEGdFSGLADL-FDQCVGCGRCE 412
|
90 100
....*....|....*....|.
gi 492395712 226 AECPKNVSISN-IARLNRDFI 245
Cdd:cd01916 413 QECPKEIPIINmIEKAARERI 433
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07570 |
PRK07570 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated |
5-251 |
0e+00 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated
Pssm-ID: 181038 [Multi-domain] Cd Length: 250 Bit Score: 512.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 5 ISFTLKVWRQKGPKAKGAFETYQMKDIPGDTSFLEMLDILNEQLISEGKEPVVFDHDCREGICGMCSLYINGHPHGPATG 84
Cdd:PRK07570 1 MKLTLKIWRQKGPDDKGKFETYEVDDISPDMSFLEMLDVLNEQLIEKGEEPVAFDHDCREGICGMCGLVINGRPHGPDRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 85 ATTCQIYMRRFNDGDTITVEPWRSAGFPVIKDLMVDRTAYDKIMQAGGYVSVRTGAPQDANAILIPKPIADEAMDAASCI 164
Cdd:PRK07570 81 TTTCQLHMRSFKDGDTITIEPWRAAAFPVIKDLVVDRSALDRIIQAGGYVSVNTGGAPDANAIPVPKEDADRAFDAAACI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 165 GCGACVAACKNGSAMLFVSAKVSQLNLLPQGKPEALRRAKAMLSKMDELGFGNCTNTRACEAECPKNVSISNIARLNRDF 244
Cdd:PRK07570 161 GCGACVAACPNGSAMLFTGAKVSHLALLPQGQPERARRVRAMVAQMDEEGFGNCTNTGECEAVCPKGISLENIARMNREY 240
|
....*..
gi 492395712 245 IIAKLKD 251
Cdd:PRK07570 241 LRASFRG 247
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
7-247 |
3.89e-88 |
|
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440247 [Multi-domain] Cd Length: 230 Bit Score: 260.83 E-value: 3.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 7 FTLKVWRQKGPK-AKGAFETYQMkDIPGDTSFLEMLDILNEqlisEGKEPVVFDHDCREGICGMCSLYINGHPhgpatgA 85
Cdd:COG0479 3 VTLKIWRQDPETdSKPRFQTYEV-PVSPGMTVLDALDYIKE----EQDPTLAFRRSCREGICGSCAMVINGRP------R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 86 TTCQIYMRRFNdgDTITVEPWRsaGFPVIKDLMVDRTA-YDKIMQAGGYVSVRTGAPQdaNAILIPKPIADEAMDAASCI 164
Cdd:COG0479 72 LACQTHVRDLK--DTITIEPLR--NFPVIKDLVVDRSAfFDKLKKVKPYLSPDGPAPD--NERLQSPEDREKADDLAECI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 165 GCGACVAACKNGSAML-FVSAKVS----QLNLLPQGKpEALRRAKAMlskMDELGFGNCTNTRACEAECPKNVSIS-NIA 238
Cdd:COG0479 146 LCGACVAACPNVWANPdFLGPAALaqayRFALDPRDE-ETEERLEAL---EDEEGVWRCTTCGNCTEVCPKGIPPTkAIA 221
|
....*....
gi 492395712 239 RLNRDFIIA 247
Cdd:COG0479 222 KLKREALKR 230
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
8-124 |
6.00e-29 |
|
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.
Pssm-ID: 432963 [Multi-domain] Cd Length: 107 Bit Score: 105.40 E-value: 6.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 8 TLKVWRQKGPKAKGA--FETYQMKDIPGDTsFLEMLDILNEQLisegKEPVVFDHDCREGICGMCSLYINGHPhgpatgA 85
Cdd:pfam13085 1 TLRVFRYDPRVDRDEpyYQEYEVPYEEGMT-VLDALNKIKEEQ----DPTLAFRRSCREGICGSCAMNINGKP------R 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 492395712 86 TTCQIYMRRFNDGDtITVEPWrsAGFPVIKDLMVDRTAY 124
Cdd:pfam13085 70 LACKTLIDDLLGQD-ITLEPL--PGFPVIRDLVVDRSAF 105
|
|
| sdhB |
PRK08640 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
1-251 |
5.54e-24 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 181515 [Multi-domain] Cd Length: 249 Bit Score: 96.60 E-value: 5.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 1 MDKNIsfTLKVWRQKGPKAKGAFETYQMKDIPGDTSFLEMLDILNEQLISEGKE--PVVFDHDCREGICGMCSLYINGHP 78
Cdd:PRK08640 2 SEKTV--RLIIKRQDGPDSKPYWEEFEIPYRPNMNVISALMEIRRNPVNAKGEKttPVVWDMNCLEEVCGACSMVINGKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 79 HGPATgATTCQIymrrfndGDTITVEPWRSagFPVIKDLMVDRT-AYDKIMQAGGYVsvrtgaPQDANAILIPKP-IADE 156
Cdd:PRK08640 80 RQACT-ALIDQL-------EQPIRLEPMST--FPVVRDLQVDRSrMFDNLKRVKAWI------PIDGTYDLGPGPrMPEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 157 ----AMDAASCIGCGACVAACKN-GSAMLFVS-AKVSQ---LNLLPQGKPEALRRAKAMlskMDELGFGNCTNTRACEAE 227
Cdd:PRK08640 144 krqwAYELSKCMTCGCCLEACPNvNEKSDFIGpAAISQvrlFNAHPTGEMHKEERLRAL---MGDGGIADCGNAQNCVRV 220
|
250 260
....*....|....*....|....*
gi 492395712 228 CPKNVSIS-NIARLNRDFIIAKLKD 251
Cdd:PRK08640 221 CPKGIPLTtSIAAMNRETTKQSFKS 245
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
7-234 |
9.91e-20 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 87.75 E-value: 9.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 7 FTLKVWRQKGPKAKGAFETYQMKDIPGDTsFLEMLDILNEQLISEgkepVVFDHDCREGICGMCSLYINGHPhgpatgAT 86
Cdd:PRK06259 4 ITITVKRFDPEKDEPHFESYEVPVKEGMT-VLDALEYINKTYDAN----IAFRSSCRAGQCGSCAVTINGEP------VL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 87 TCqiyMRRFNDGDTItvEPWRsagFPVIKDLMVDRTAYD-KIMQAGGYVSVRTGAPQDANAILIPKPIADeamdaasCIG 165
Cdd:PRK06259 73 AC---KTEVEDGMII--EPLD---FPVIKDLIVDREPYYkKLKSLRNYLQRKNEKITYPEDIEDIKKLRG-------CIE 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492395712 166 CGACVAACKNGSAMLF----VSAKVSQLNLLPQGKPEALRRAkamlskMDElGFGNCTNTRACEAECPKNVSI 234
Cdd:PRK06259 138 CLSCVSTCPARKVSDYpgptFMRQLARFAFDPRDEGDREKEA------FDE-GLYNCTTCGKCVEVCPKEIDI 203
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
24-232 |
6.21e-19 |
|
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]
Pssm-ID: 273049 [Multi-domain] Cd Length: 220 Bit Score: 82.48 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 24 ETYQMKDIPGdTSFLEMLDILNEQLISEgkepVVFDHDCREGICGMCSLYINGHPhgpaTGATTCQIymrRFNDGDTITV 103
Cdd:TIGR00384 15 QSYEVPADEG-MTVLDALNYIKDEQDPS----LAFRRSCRNGICGSCAMNVNGKP----VLACKTKV---EDLGQPVMKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 104 EPWrsAGFPVIKDLMVDRTA-YDKIMQAGGYVSvRTGAPQDANAILIpKPIADEAMDAAS-CIGCGACVAAC----KN-- 175
Cdd:TIGR00384 83 EPL--PNLPVIKDLVVDMGPfYAKLEAIKPYLI-RKSQPEPEGEFLQ-TPEQREKLDQLSgCILCGCCYSSCpafwWNpe 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492395712 176 --GSAMLfvsAKVSQLNLLPQGKPEALRraKAMLSkmDELGFGNCTNTRACEAECPKNV 232
Cdd:TIGR00384 159 flGPAAL---TAAYRFLIDSRDHATKDR--LEGLN--DKNGVWRCTTCMNCSEVCPKGV 210
|
|
| PRK12577 |
PRK12577 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
8-233 |
3.88e-17 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183605 [Multi-domain] Cd Length: 329 Bit Score: 79.35 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 8 TLKVWRQKGPKAKgAFETYQMKDIPGDTsfleMLDILNeQLISEGKEPVVFDHDCREGICGMCSLYINGHphgpatGATT 87
Cdd:PRK12577 4 LFKILRQKQNSAP-YVQTYTLEVEPGNT----ILDCLN-RIKWEQDGSLAFRKNCRNTICGSCAMRINGR------SALA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 88 CQ----IYMRRFNDGD-----TITVEPWrsAGFPVIKDLMVDRTAY-DKIMQAGGYVSvrTGAPQDANAILIPKPIADEA 157
Cdd:PRK12577 72 CKenvgSELARLSDSNsgaipEITIAPL--GNMPVIKDLVVDMSSFwQNLEAVDPYVS--TAARQVPEREFLQTPEERSK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 158 MDAA-SCIGCGACVAACK----NGSamlFVSakvsqlnllpqgkPEALRRAKAMLS--------------KMDELGFGNC 218
Cdd:PRK12577 148 LDQTgNCILCGACYSECNarevNPE---FVG-------------PHALAKAQRMVAdsrdtateqrlelyNQGTAGVWGC 211
|
250
....*....|....*
gi 492395712 219 TNTRACEAECPKNVS 233
Cdd:PRK12577 212 TRCYYCNSVCPMEVA 226
|
|
| frdB |
PRK13552 |
fumarate reductase iron-sulfur subunit; Provisional |
8-248 |
1.43e-15 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 184136 [Multi-domain] Cd Length: 239 Bit Score: 73.44 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 8 TLKVWRQKgPKAKGA---FETYQMKDIPGDTSFLEmldiLNEqlISEGKEP-VVFDHDCREGICGMCSLYINGHPhgpat 83
Cdd:PRK13552 6 TFNIFRYN-PQDPGSkphMVTYQLEETPGMTLFIA----LNR--IREEQDPsLQFDFVCRAGICGSCAMVINGRP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 84 gATTCQIYMRRFNDGDtITVEPWrsAGFPVIKDLMVDRTAYDKIMQAGGYVSVRTGAPQDANAILIP--KPIADEAMDAA 161
Cdd:PRK13552 74 -TLACRTLTSDYPDGV-ITLMPL--PVFKLIGDLSVNTGKWFREMSERVESWIHTDKEFDIHRLEERmePEEADEIYELD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 162 SCIGCGACVAACknGSAML---FVSAkvSQLNllpqgkpealRRAKAMLSKMDE---------LG-----FGnCTNTRAC 224
Cdd:PRK13552 150 RCIECGCCVAAC--GTKQMredFVGA--VGLN----------RIARFELDPRDErtdedfyelIGnddgvFG-CMSLLGC 214
|
250 260
....*....|....*....|....*
gi 492395712 225 EAECPKNVSI-SNIARLNRDFIIAK 248
Cdd:PRK13552 215 EDNCPKDLPLqQQIAYLRRKMAATG 239
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
37-232 |
2.63e-15 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 73.24 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 37 FLEMLDILneQLISEGKEP-VVFDHDCREGICGMCSLYINGHPhgpatgATTCQIYMRRF--NDGDTITVEPWRSagFPV 113
Cdd:PRK12576 34 FTQVTEAL--RRIKEEQDPtLSYRASCHMAVCGSCGMKINGEP------RLACKTLVLDVakKYNSVITIEPMDY--FKV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 114 IKDLMVDRTA-YDKIMQAGGYVsVRTGAPQDANAILIPKPiaDEAMD---AASCIGCGACVAACKngsamlfvSAKVSQL 189
Cdd:PRK12576 104 VKDLIVDFDEfYERMFKVKPRL-YRAKEVLEGKAEHRLKP--EDQKElwkFAQCIWCGLCVSACP--------VVAIDPE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492395712 190 NLLPQGKPEALR---------RAKAMLSKMDelGFGNCTNTRACEAECPKNV 232
Cdd:PRK12576 173 FLGPAAHAKGYRfladprdtiTEERMKILID--SSWRCTYCYSCSNVCPRDI 222
|
|
| PRK12385 |
PRK12385 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
23-250 |
1.24e-13 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 183490 [Multi-domain] Cd Length: 244 Bit Score: 68.19 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 23 FETYQmkdIPGD--TSFLEMLDILNEQLISEgkepVVFDHDCREGICGMCSLYINGHPhgpatgATTCQIYMRRFNDGdt 100
Cdd:PRK12385 24 SQTYE---VPYDetTSLLDALGYIKDNLAPD----LSYRWSCRMAICGSCGMMVNNVP------KLACKTFLRDYTGG-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 101 ITVEPWrsAGFPVIKDLMVDRTAY-DKIMQAGGYVSVRTGAPQDANAILIPKPIADEAmDAASCIGCGACVAACKN---- 175
Cdd:PRK12385 89 MKVEAL--ANFPIERDLVVDMTHFiESLEAIKPYIIGNDRTPDDGPNKQTPAQMAKYH-QFSGCINCGLCYAACPQfgln 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 176 ----GSAMLFVSAKVSQLNlLPQGKPEalrRAKAMLSkmdELGFGNCTNTRACEAECPKNVSISNIARLNR-----DFII 246
Cdd:PRK12385 166 pefiGPAAITLAHRYNLDS-RDHGKKE---RMKQLNG---QNGVWSCTFVGYCSEVCPKHVDPAAAIQQGKvesakDFLI 238
|
....
gi 492395712 247 AKLK 250
Cdd:PRK12385 239 AMLK 242
|
|
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
8-173 |
2.59e-13 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 67.13 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 8 TLKVWR---QKGPKAKgaFETYQM-KDIPGDTsfleMLDILNeqLISEGKEP-VVFDHDCREGICGMCSLYINGHPhGPA 82
Cdd:PRK05950 1 TFKIYRynpDVDANPR--MQTYEVdVDECGPM----VLDALI--KIKNEIDPtLTFRRSCREGVCGSDAMNINGKN-GLA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 83 tgattCQIYMRRFnDGDTITVEPWRsaGFPVIKDLMVDRT----AYDKIMQaggYVsVRTGAPQDANAILIPkpiADEAM 158
Cdd:PRK05950 72 -----CITPISDL-KKGKIVIRPLP--GLPVIKDLVVDMTqfyaQYRSIKP---YL-INDTPPPARERLQSP---EDREK 136
|
170
....*....|....*..
gi 492395712 159 --DAASCIGCGACVAAC 173
Cdd:PRK05950 137 ldGLYECILCACCSTSC 153
|
|
| PRK12386 |
PRK12386 |
fumarate reductase iron-sulfur subunit; Provisional |
8-238 |
7.47e-12 |
|
fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 237086 [Multi-domain] Cd Length: 251 Bit Score: 63.18 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 8 TLKVWRqkGPKAKGAFETYQMKDIPGDTsfleMLDILNeQLISEGKEPVVFDHDCREGICGMCSLYINGHPHgpatgaTT 87
Cdd:PRK12386 6 KFRVWR--GDASGGELQDYTVEVNEGEV----VLDVIH-RLQATQAPDLAVRWNCKAGKCGSCSAEINGRPR------LM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 88 CQIYMRRFNDGDTITVEPWRSagFPVIKDLMVDRT-AYDKIMQaggyVSVRTGAPQDANAILIPKPI-ADEAMDAASCIG 165
Cdd:PRK12386 73 CMTRMSTFDEDETVTVTPMRT--FPVIRDLVTDVSfNYEKARE----IPSFTPPKDLQPGEYRMQQVdVERSQEFRKCIE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 166 CGACVAAC-------KNGSAM----LFVsaKVSQLNLLPQGkpEALRRAKAmlskMDELGFGNCTNTRACEAECPKNVSI 234
Cdd:PRK12386 147 CFLCQNVChvvrdheENKPAFagprFLM--RIAELEMHPLD--TADRRAEA----QEEHGLGYCNITKCCTEVCPEHIKI 218
|
....
gi 492395712 235 SNIA 238
Cdd:PRK12386 219 TDNA 222
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
8-237 |
9.29e-10 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 57.28 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 8 TLKVWR-QKGPKAKGAFETYQMKDIPGDTSFLEMLDILNEQlisegKEPVVFDHDCREGICGMCSLYINGhphgpaTGAT 86
Cdd:PRK12575 6 ILHIYRyDPDDDAAPRMQRYEIAPRAEDRMLLDVLGRVKAQ-----DETLSYRRSCREGICGSDAMNING------RNGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 87 TCQIYMRRFNdgDTITVEPWrsAGFPVIKDLMVDRTAYdkimqAGGYVSVRtgaPQDANAILIPK------PIADEAMDA 160
Cdd:PRK12575 75 ACLTNMQALP--REIVLRPL--PGLPVVRDLIVDMTDF-----FNQYHSIR---PYLINDTVPPErerlqtPQEREQLDG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 161 A-SCIGCGACVAACKN--GSAMLFVSakvsqlnllPQGKPEALR-----RAKAMLSKMDELG----FGNCTNTRACEAEC 228
Cdd:PRK12575 143 LyECILCACCSTACPSywWNPDKFVG---------PAGLLQAYRfiadsRDDATAARLDDLEdpyrLFRCRTIMNCVDVC 213
|
250
....*....|...
gi 492395712 229 PKNV----SISNI 237
Cdd:PRK12575 214 PKGLnparAIGQI 226
|
|
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
40-250 |
3.01e-07 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 50.17 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 40 MLDIL----NEQLISegkepVVFDHDCREGICGMCSLYINGhphgpaTGATTCQIYMRRfNDGDTITVEPwrsagFP--- 112
Cdd:PLN00129 75 VLDVLikikNEQDPS-----LTFRRSCREGICGSCAMNIDG------KNTLACLTKIDR-DESGPTTITP-----LPhmf 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 113 VIKDLMVDRTA-YDKIMQAGGYVSVRTGAPQDANAILIPKpiADEA-MDAA-SCIGCGACVAACK----NGSAMLfvsak 185
Cdd:PLN00129 138 VIKDLVVDMTNfYQQYKSIEPWLKTKKPPEDGQKEHLQSK--EDRAkLDGMyECILCACCSTSCPsywwNPEKFL----- 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492395712 186 vsqlnllpqgKPEALRRAKAMLSKM-------------DELGFGNCTNTRACEAECPKNvsisniarLNRDFIIAKLK 250
Cdd:PLN00129 211 ----------GPAALLHAYRWISDSrdeytkerlealdDEFKLYRCHTIRNCSNACPKG--------LNPAKAIAKIK 270
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
148-244 |
4.53e-07 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 50.08 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 148 LIPKPIADEAMDAA-SCIGCGACVAACKngsamlfvSAKVSQ-LNLLPQGKPEALRRA-----KAMLSKMDELGFGNCTN 220
Cdd:COG0247 64 NLKTLPWKELLDALdACVGCGFCRAMCP--------SYKATGdEKDSPRGRINLLREVlegelPLDLSEEVYEVLDLCLT 135
|
90 100
....*....|....*....|....
gi 492395712 221 TRACEAECPKNVsisNIARLNRDF 244
Cdd:COG0247 136 CKACETACPSGV---DIADLIAEA 156
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
148-245 |
2.06e-06 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 48.17 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 148 LIPKPIADEAMD-AASCIGCGACVAACKNGsamLFVsakvsqlnllpqgkPEALRRAKAM-LSKMDELgFGNCTNTRACE 225
Cdd:cd01916 351 EKKLPTDEEFQElAAKCTDCGWCTRACPNS---LRI--------------KEAMEAAKEGdFSGLADL-FDQCVGCGRCE 412
|
90 100
....*....|....*....|.
gi 492395712 226 AECPKNVSISN-IARLNRDFI 245
Cdd:cd01916 413 QECPKEIPIINmIEKAARERI 433
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
163-232 |
4.22e-05 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 433017 [Multi-domain] Cd Length: 64 Bit Score: 40.37 E-value: 4.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 163 CIGCGACVAACkngsamLFVSAKVSQLNLLPQGKPEALRRAKAMLSKMDElGFGNCTNTRACEAECPKNV 232
Cdd:pfam13183 2 CIRCGACLAAC------PVYLVTGGRFPGDPRGGAAALLGRLEALEGLAE-GLWLCTLCGACTEVCPVGI 64
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
163-232 |
1.22e-04 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 38.66 E-value: 1.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 163 CIGCGACVAACKNGSAMLFVSAKvsqlnllPQGKPEAlrrakamlskmdELGFGNCTNTRACEAECPKNV 232
Cdd:pfam12838 1 CIGCGACVAACPVGAITLDEVGE-------KKGTKTV------------VIDPERCVGCGACVAVCPTGA 51
|
|
| glpC |
PRK11168 |
anaerobic glycerol-3-phosphate dehydrogenase subunit C; |
158-247 |
2.98e-04 |
|
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
Pssm-ID: 236869 [Multi-domain] Cd Length: 396 Bit Score: 41.39 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 158 MDAASCIGCGACVAACKngsamlfVsAKVSQLNLLP-QGKPEALR-RAKAMLSKMDELGFgnCTNTRACEAECPKNVSIS 235
Cdd:PRK11168 4 TSFDSCIKCTVCTTACP-------V-ARVNPLYPGPkQAGPDGERlRLKDGALYDESLKY--CSNCKRCEVACPSGVKIG 73
|
90 100
....*....|....*....|....
gi 492395712 236 NI---ARLN---------RDFIIA 247
Cdd:PRK11168 74 DIiqrARAKyvtergpplRDRILS 97
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
159-229 |
1.47e-03 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 36.07 E-value: 1.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492395712 159 DAASCIGCGACVAACkngsamlfvsakvsqlnllPQGKPEALRRAKAMLSKMDELGFGNCTNTRACEAECP 229
Cdd:pfam13237 5 DPDKCIGCGRCTAAC-------------------PAGLTRVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
|
|
| PRK10882 |
PRK10882 |
hydrogenase 2 operon protein HybA; |
119-174 |
3.03e-03 |
|
hydrogenase 2 operon protein HybA;
Pssm-ID: 236786 [Multi-domain] Cd Length: 328 Bit Score: 38.11 E-value: 3.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 119 VDRTAYDKIMQAGGYVSvrTGAPQDANAILIPKPIADEAM----DAASCIGCGACVAACK 174
Cdd:PRK10882 1 MNRRNFLKAASAGALLA--GALPSVSHAAAENRPPIPGALgmlyDSTLCVGCQACVTKCQ 58
|
|
| DMSOR_beta_like |
cd16371 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
158-175 |
4.09e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319893 [Multi-domain] Cd Length: 140 Bit Score: 36.39 E-value: 4.09e-03
|
| PsrB |
cd10551 |
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ... |
157-175 |
5.56e-03 |
|
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.
Pssm-ID: 319873 [Multi-domain] Cd Length: 185 Bit Score: 36.74 E-value: 5.56e-03
|
| RnfC |
COG4656 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ... |
145-251 |
6.66e-03 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 443694 [Multi-domain] Cd Length: 451 Bit Score: 37.43 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395712 145 NAILIPKPIADEAMDAASCIGCGACVAACKngsamlfvsakvsqLNLLPQgkpEALRRAKA-MLSKMDELGFGNCTNTRA 223
Cdd:COG4656 348 NGILALTKEEVPPPEEQPCIRCGRCVDACP--------------MGLLPQ---QLYWYARAgDFDKAEEYNLMDCIECGC 410
|
90 100
....*....|....*....|....*...
gi 492395712 224 CEAECPKNVSISNIARLNRDFIIAKLKD 251
Cdd:COG4656 411 CSYVCPSKIPLVQYIRLAKAEIRARRRE 438
|
|
| HybA_like |
cd10561 |
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ... |
158-174 |
7.11e-03 |
|
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.
Pssm-ID: 319883 [Multi-domain] Cd Length: 196 Bit Score: 36.42 E-value: 7.11e-03
|
| |
