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Enzyme Nomenclature
Information on EC 1.8.98.4 - coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase
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EC Tree
1.8.98.4 coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductaseIUBMB Comments
The enzyme, characterized from the archaeon Methanosarcina acetivorans, catalyses the reduction of CoB-CoM heterodisulfide back to CoB and CoM. The enzyme consists of three components, HdrA, HdrB and HdrC, all of which contain [4Fe-4S] clusters. Electrons enter at HdrA, which also contains FAD, and are transferred via HdrC to the catalytic component, HdrB. During methanogenesis from acetate the enzyme catalyses the activity of EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase. However, it can also use electron bifurcation to direct electron pairs from reduced coenzyme F420 towards the reduction of both ferredoxin and CoB-CoM heterodisulfide. This activity is proposed to take place during Fe(III)-dependent anaerobic methane oxidation. cf. EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
2
+
2
+
+
+
2
=
2
+
2
+
2
+
2
reduced ferredoxin [iron-sulfur] cluster
+
+
+
2
=
2
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
hdrA2B2C2
hdrA2B2C2
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
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SYSTEMATIC NAME
IUBMB Comments
CoB,CoM,ferredoxin:coenzyme F420 oxidoreductase
The enzyme, characterized from the archaeon Methanosarcina acetivorans, catalyses the reduction of CoB-CoM heterodisulfide back to CoB and CoM. The enzyme consists of three components, HdrA, HdrB and HdrC, all of which contain [4Fe-4S] clusters. Electrons enter at HdrA, which also contains FAD, and are transferred via HdrC to the catalytic component, HdrB. During methanogenesis from acetate the enzyme catalyses the activity of EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase. However, it can also use electron bifurcation to direct electron pairs from reduced coenzyme F420 towards the reduction of both ferredoxin and CoB-CoM heterodisulfide. This activity is proposed to take place during Fe(III)-dependent anaerobic methane oxidation. cf. EC 1.8.98.5, H2:CoB-CoM heterodisulfide,ferredoxin reductase, EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
oxidized coenzyme F420 + reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
reduced coenzyme F420 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
Methanosarcina barkeri MS DSM 800
-
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
oxidized coenzyme F420 + reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
reduced coenzyme F420 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 oxidized coenzyme F420 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced coenzyme F420 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
Methanosarcina barkeri MS DSM 800
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
coenzyme F420
-
reduced F420 is a direct electron donor in the carbon dioxide reduction pathway and also serves as the electron donor for the proposed HdrABC-catalyzed electron bifurcation reaction in which reduced ferredoxin (also required for carbon dioxide reduction) is generated with simultaneous reduction of CoM-S-S-CoB
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
coculture of Methanosarcina barkeri with Geobacter metallireducens, transcriptome analysis, overview. Out of the 3809 predicted protein-coding genes in the Methanosarcina barkeri MS genome, 1912 and 1909 genes have expression levels that are higher than the median in DIET-grown cells, respectively
brenda
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coculture of Methanosarcina barkeri with Geobacter metallireducens, transcriptome analysis, overview. Out of the 3809 predicted protein-coding genes in the Methanosarcina barkeri MS genome, 1912 and 1909 genes have expression levels that are higher than the median in DIET-grown cells, respectively
-
brenda
-
coculture of Methanosarcina barkeri with Geobacter metallireducens, transcriptome analysis, overview. Out of the 3809 predicted protein-coding genes in the Methanosarcina barkeri MS genome, 1912 and 1909 genes have expression levels that are higher than the median in DIET-grown cells, respectively
-
brenda
Methanosarcina barkeri MS DSM 800
-
coculture of Methanosarcina barkeri with Geobacter metallireducens, transcriptome analysis, overview. Out of the 3809 predicted protein-coding genes in the Methanosarcina barkeri MS genome, 1912 and 1909 genes have expression levels that are higher than the median in DIET-grown cells, respectively
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
-
generalized model for electron and proton flux during hydrogen interspecies electron transfer (HIT) and direct interspecies electron transfer (DIET) with growth on ethanol as an example, overview. Electron and protons are transported by different mechanisms during DIET. Electron transfer is direct, through e-pili and other electrical contacts. Protons move by diffusion creating a positive proton pressure outside the cell. A mechanism for proton translocation into the cell is required for charge balance in the cytoplasm when cytoplasmic electron acceptors (EA) are reduced and to prevent acidification of the external space between cells. The transcriptome reflects faster growth during HIT and possible greater importance of membrane and outer-surface proteins during DIET. Model for electron and proton flux for carbon dioxide reduction to methane in Methanosarcina barkeri during DIET-based growth, overview
metabolism
-
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase or formate dehydrogenase generates reduced ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, three-fourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. When switched from growth with methanol to growth with acetate, Methanosarcina acetivorans upregulates an electron bifurcating heterodisulfide reductase (HdrA2B2C2) that oxidizes F420H2 and reduces Fdx driven by reduction of CoMS-SCoB. A role has been proposed for sHdrA2B2C2 dependent on reduction of NAD-like coenzyme F420 (F420) by the Rnf complex analogous to Fdx-dependent reduction of NADC by homologous Rnf complexes from the domain Bacteria. In this way, Fdx reduced by HdrA2B2C2 is re-oxidized by Rnf thereby supplementing the translocation of Na+. HdrA2B2C2 is involved in reverse methanogenesis
metabolism
-
generalized model for electron and proton flux during hydrogen interspecies electron transfer (HIT) and direct interspecies electron transfer (DIET) with growth on ethanol as an example, overview. Electron and protons are transported by different mechanisms during DIET. Electron transfer is direct, through e-pili and other electrical contacts. Protons move by diffusion creating a positive proton pressure outside the cell. A mechanism for proton translocation into the cell is required for charge balance in the cytoplasm when cytoplasmic electron acceptors (EA) are reduced and to prevent acidification of the external space between cells. The transcriptome reflects faster growth during HIT and possible greater importance of membrane and outer-surface proteins during DIET. Model for electron and proton flux for carbon dioxide reduction to methane in Methanosarcina barkeri during DIET-based growth, overview
-
metabolism
-
generalized model for electron and proton flux during hydrogen interspecies electron transfer (HIT) and direct interspecies electron transfer (DIET) with growth on ethanol as an example, overview. Electron and protons are transported by different mechanisms during DIET. Electron transfer is direct, through e-pili and other electrical contacts. Protons move by diffusion creating a positive proton pressure outside the cell. A mechanism for proton translocation into the cell is required for charge balance in the cytoplasm when cytoplasmic electron acceptors (EA) are reduced and to prevent acidification of the external space between cells. The transcriptome reflects faster growth during HIT and possible greater importance of membrane and outer-surface proteins during DIET. Model for electron and proton flux for carbon dioxide reduction to methane in Methanosarcina barkeri during DIET-based growth, overview
-
metabolism
Methanosarcina barkeri MS DSM 800
-
generalized model for electron and proton flux during hydrogen interspecies electron transfer (HIT) and direct interspecies electron transfer (DIET) with growth on ethanol as an example, overview. Electron and protons are transported by different mechanisms during DIET. Electron transfer is direct, through e-pili and other electrical contacts. Protons move by diffusion creating a positive proton pressure outside the cell. A mechanism for proton translocation into the cell is required for charge balance in the cytoplasm when cytoplasmic electron acceptors (EA) are reduced and to prevent acidification of the external space between cells. The transcriptome reflects faster growth during HIT and possible greater importance of membrane and outer-surface proteins during DIET. Model for electron and proton flux for carbon dioxide reduction to methane in Methanosarcina barkeri during DIET-based growth, overview
-
physiological function
-
direct interspecies electron transfer (DIET) is important in diverse methanogenic environments. In DIET, electrically conductive pili [e-pili] and associated electron transport proteins deliver electrons to cytoplasmic electron acceptors. Protons have to be translocated into the cytoplasm for charge balance. The transcriptome of Methanosarcina barkeri grown via DIET in co-culture with Geobacter metallireducens compared with its transcriptome when grown via H2 interspecies transfer (HIT) with Pelobacter carbinolicus shows that transcripts for the F420H2 dehydrogenase (Fpo) and the heterodisulfide reductase, HdrABC, are more abundant during growth on DIET. Electrons delivered to methanophenazine in the cell membrane are transferred to Fpo (cf. EC 1.8.98.1). The external proton gradient necessary to drive the otherwise thermodynamically unfavorable reverse electron transport for Fpo-catalyzed F420 reduction is derived from protons released from Geobacter metallireducens metabolism. Reduced F420 is a direct electron donor in the carbon dioxide reduction pathway and also serves as the electron donor for the proposed HdrABC-catalyzed electron bifurcation reaction in which reduced ferredoxin (also required for carbon dioxide reduction) is generated with simultaneous reduction of CoM-S-S-CoB
physiological function
-
The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, three-fourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB. When switched from growth with methanol to growth with acetate, Methanosarcina acetivorans upregulates an electron bifurcating heterodisulfide reductase (HdrA2B2C2) that oxidizes F420H2 and reduces Fdx driven by reduction of CoMS-SCoB. A role has been proposed for HdrA2B2C2 dependent on reduction of NAD-like coenzyme F420 (F420) by the Rnf complex analogous to Fdx-dependent reduction of NADC by homologous Rnf complexes from the domain Bacteria
physiological function
-
direct interspecies electron transfer (DIET) is important in diverse methanogenic environments. In DIET, electrically conductive pili [e-pili] and associated electron transport proteins deliver electrons to cytoplasmic electron acceptors. Protons have to be translocated into the cytoplasm for charge balance. The transcriptome of Methanosarcina barkeri grown via DIET in co-culture with Geobacter metallireducens compared with its transcriptome when grown via H2 interspecies transfer (HIT) with Pelobacter carbinolicus shows that transcripts for the F420H2 dehydrogenase (Fpo) and the heterodisulfide reductase, HdrABC, are more abundant during growth on DIET. Electrons delivered to methanophenazine in the cell membrane are transferred to Fpo (cf. EC 1.8.98.1). The external proton gradient necessary to drive the otherwise thermodynamically unfavorable reverse electron transport for Fpo-catalyzed F420 reduction is derived from protons released from Geobacter metallireducens metabolism. Reduced F420 is a direct electron donor in the carbon dioxide reduction pathway and also serves as the electron donor for the proposed HdrABC-catalyzed electron bifurcation reaction in which reduced ferredoxin (also required for carbon dioxide reduction) is generated with simultaneous reduction of CoM-S-S-CoB
-
physiological function
-
direct interspecies electron transfer (DIET) is important in diverse methanogenic environments. In DIET, electrically conductive pili [e-pili] and associated electron transport proteins deliver electrons to cytoplasmic electron acceptors. Protons have to be translocated into the cytoplasm for charge balance. The transcriptome of Methanosarcina barkeri grown via DIET in co-culture with Geobacter metallireducens compared with its transcriptome when grown via H2 interspecies transfer (HIT) with Pelobacter carbinolicus shows that transcripts for the F420H2 dehydrogenase (Fpo) and the heterodisulfide reductase, HdrABC, are more abundant during growth on DIET. Electrons delivered to methanophenazine in the cell membrane are transferred to Fpo (cf. EC 1.8.98.1). The external proton gradient necessary to drive the otherwise thermodynamically unfavorable reverse electron transport for Fpo-catalyzed F420 reduction is derived from protons released from Geobacter metallireducens metabolism. Reduced F420 is a direct electron donor in the carbon dioxide reduction pathway and also serves as the electron donor for the proposed HdrABC-catalyzed electron bifurcation reaction in which reduced ferredoxin (also required for carbon dioxide reduction) is generated with simultaneous reduction of CoM-S-S-CoB
-
physiological function
Methanosarcina barkeri MS DSM 800
-
direct interspecies electron transfer (DIET) is important in diverse methanogenic environments. In DIET, electrically conductive pili [e-pili] and associated electron transport proteins deliver electrons to cytoplasmic electron acceptors. Protons have to be translocated into the cytoplasm for charge balance. The transcriptome of Methanosarcina barkeri grown via DIET in co-culture with Geobacter metallireducens compared with its transcriptome when grown via H2 interspecies transfer (HIT) with Pelobacter carbinolicus shows that transcripts for the F420H2 dehydrogenase (Fpo) and the heterodisulfide reductase, HdrABC, are more abundant during growth on DIET. Electrons delivered to methanophenazine in the cell membrane are transferred to Fpo (cf. EC 1.8.98.1). The external proton gradient necessary to drive the otherwise thermodynamically unfavorable reverse electron transport for Fpo-catalyzed F420 reduction is derived from protons released from Geobacter metallireducens metabolism. Reduced F420 is a direct electron donor in the carbon dioxide reduction pathway and also serves as the electron donor for the proposed HdrABC-catalyzed electron bifurcation reaction in which reduced ferredoxin (also required for carbon dioxide reduction) is generated with simultaneous reduction of CoM-S-S-CoB
-
additional information
-
physiological studies of direct interspecies electron transfer (DIET) require defined co-cultures. Geobacter metallireducens is an environmentally relevant pure culture model for electron-donating partners for DIET because Geobacter species function as the electron-donating partner in important methanogenic environments such as anaerobic digesters and terrestrial wetlands. Studies with defined co-cultures in which Geobacter metallireducens is the electron-donating partner for DIET have suggested that c-type cytochromes and electrically conductive pili [e-pili] facilitate electron transport from Geobacter metallireducens to the electron accepting partner. However, Methanosarcina barkeri, a methanogen shown to participate in DIET, does not possess outer-surface c-type cytochromes or e-pili
additional information
-
physiological studies of direct interspecies electron transfer (DIET) require defined co-cultures. Geobacter metallireducens is an environmentally relevant pure culture model for electron-donating partners for DIET because Geobacter species function as the electron-donating partner in important methanogenic environments such as anaerobic digesters and terrestrial wetlands. Studies with defined co-cultures in which Geobacter metallireducens is the electron-donating partner for DIET have suggested that c-type cytochromes and electrically conductive pili [e-pili] facilitate electron transport from Geobacter metallireducens to the electron accepting partner. However, Methanosarcina barkeri, a methanogen shown to participate in DIET, does not possess outer-surface c-type cytochromes or e-pili
-
additional information
-
physiological studies of direct interspecies electron transfer (DIET) require defined co-cultures. Geobacter metallireducens is an environmentally relevant pure culture model for electron-donating partners for DIET because Geobacter species function as the electron-donating partner in important methanogenic environments such as anaerobic digesters and terrestrial wetlands. Studies with defined co-cultures in which Geobacter metallireducens is the electron-donating partner for DIET have suggested that c-type cytochromes and electrically conductive pili [e-pili] facilitate electron transport from Geobacter metallireducens to the electron accepting partner. However, Methanosarcina barkeri, a methanogen shown to participate in DIET, does not possess outer-surface c-type cytochromes or e-pili
-
additional information
Methanosarcina barkeri MS DSM 800
-
physiological studies of direct interspecies electron transfer (DIET) require defined co-cultures. Geobacter metallireducens is an environmentally relevant pure culture model for electron-donating partners for DIET because Geobacter species function as the electron-donating partner in important methanogenic environments such as anaerobic digesters and terrestrial wetlands. Studies with defined co-cultures in which Geobacter metallireducens is the electron-donating partner for DIET have suggested that c-type cytochromes and electrically conductive pili [e-pili] facilitate electron transport from Geobacter metallireducens to the electron accepting partner. However, Methanosarcina barkeri, a methanogen shown to participate in DIET, does not possess outer-surface c-type cytochromes or e-pili
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HDRA2_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
793
0
86918
Swiss-Prot
-
HDRB2_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
300
0
32819
Swiss-Prot
-
HDRC2_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
161
0
18150
Swiss-Prot
-
A0A8B6SDK1_9EURY
441
0
49666
TrEMBL
-
A0A8B3S144_9EURY
198
0
22644
TrEMBL
-
A0A8B3S0M9_9EURY
755
0
82703
TrEMBL
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yan, Z.; Wang, M.; Ferry, J.G.
A ferredoxin- and F420H2-dependent, electron-bifurcating, heterodisulfide reductase with homologs in the domains Bacteria and Archaea
mBio
8
e02285-16
2017
Methanosarcina acetivorans
brenda
Yan, Z.; Ferry, J.
Electron bifurcation and confurcation in methanogenesis and reverse methanogenesis
Front. Microbiol.
9
1322
2018
Methanosarcina acetivorans
brenda
Holmes, D.; Rotaru, A.; Ueki, T.; Shrestha, P.; Ferry, J.; Lovley, D.
Electron and proton flux for carbon dioxide reduction in Methanosarcina barkeri during direct interspecies electron transfer
Front. Microbiol.
9
3109
2018
Methanosarcina barkeri, Methanosarcina barkeri MS, Methanosarcina barkeri DSM 800
brenda
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Release 2023.1 (January 2023)
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