1.8.7.3: ferredoxin:CoB-CoM heterodisulfide reductase
This is an abbreviated version!
For detailed information about ferredoxin:CoB-CoM heterodisulfide reductase, go to the full flat file.
Reaction
2 oxidized ferredoxin [iron-sulfur] cluster + + = 2 reduced ferredoxin [iron-sulfur] cluster + + 2 H+
Synonyms
CoB-CoM heterodisulfide reductase, CoB-CoM heterodisulfide reductase iron-sulfur subunit A, CoB-S-S-CoM reductase, Coenzyme B-Coenzyme M heterodisulfide reductase, ferredoxin:heterodisulfide oxidoreductase, HDR, hdrA1B1C1, hdrA2B2C2, HdrABC, HdrB, HdrB2, HdrB2C2, HdrD, heterodisulfide reductase, Mhun_1838, More
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Cofactor
Cofactor on EC 1.8.7.3 - ferredoxin:CoB-CoM heterodisulfide reductase
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FAD
required for activity. Conformational changes within the HdrA subunit provide a conformationally gated pathway for electrons to and from the bifurcating flavin adenine dinucleotide (FAD)
FAD
the enzyme is an iron-sulfur subunit A of the HdrABC complex and contains [4 Fe-4S] clusters
FAD
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the multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached
FAD
the multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached
FAD
P60200; Q58153; Q58273; Q58154; Q58274
the multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached
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subunits HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters used for reduction activity. The two noncubane [4Fe-4S] clusters are composed of fused [3Fe-4S]-[2Fe-2S] units sharing 1 iron (Fe) and 1 sulfur (S), which are coordinated at the CCG motifs. The N-terminal domain has a fold similar to MvhD but contains, instead of a [2Fe-2S] cluster, a [4Fe-4S] cluster (HA3) that is unusually ligated by five cysteines
Fe-S center
subunits HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters used for reduction activity. The two noncubane [4Fe-4S] clusters are composed of fused [3Fe-4S]-[2Fe-2S] units sharing 1 iron (Fe) and 1 sulfur (S), which are coordinated at the CCG motifs. The N-terminal domain has a fold similar to MvhD but contains, instead of a [2Fe-2S] cluster, a [4Fe-4S] cluster (HA3) that is unusually ligated by five cysteines
Fe-S center
P60200; Q58153; Q58273; Q58154; Q58274
subunits HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters used for reduction activity. The two noncubane [4Fe-4S] clusters are composed of fused [3Fe-4S]-[2Fe-2S] units sharing 1 iron and 1 sulfur, which are coordinated at the CCG motifs. The N-terminal domain has a fold similar to MvhD but contains, instead of a [2Fe-2S] cluster, a [4Fe-4S] cluster (HA3) that is unusually ligated by five cysteines
the enzyme contains (4Fe-4S)clusters
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additional information
the HdrABC·MvhAGD (see also EC 1.8.98.1) complex is abundant in iron-sulfur cofactors, with 11 [4 Fe-4S] clusters, one [2 Fe-2S], a Ni-Fe site for H2 catalysis, and two noncubane iron-sulfur clusters
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additional information
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the thioredoxin reductase domain of HdrA (145 to 236 and 315 to 567) resembles thioredoxin reductase in the fold and geometry of the FAD-binding site but forms a completely different dimer interface, owing to the perpendicular position of the respective two-fold axes. The thioredoxin-reductase domain of HdrA has, in addition, a [4Fe-4S] cluster (HA4) that is surrounded by several basic residues and coordinated with a Cys386, Cys399, Cys403, and Cys404 sequence motif (consensus sequence CX10-16-Y/W/H/F-C-S/A/C-X2-3CC)
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additional information
the thioredoxin reductase domain of HdrA (145 to 236 and 315 to 567) resembles thioredoxin reductase in the fold and geometry of the FAD-binding site but forms a completely different dimer interface, owing to the perpendicular position of the respective two-fold axes. The thioredoxin-reductase domain of HdrA has, in addition, a [4Fe-4S] cluster (HA4) that is surrounded by several basic residues and coordinated with a Cys386, Cys399, Cys403, and Cys404 sequence motif (consensus sequence CX10-16-Y/W/H/F-C-S/A/C-X2-3CC)
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additional information
P60200; Q58153; Q58273; Q58154; Q58274
the thioredoxin reductase domain of HdrA (145 to 236 and 315 to 567) resembles thioredoxin reductase in the fold and geometry of the FAD-binding site but forms a completely different dimer interface, owing to the perpendicular position of the respective two-fold axes. The thioredoxin-reductase domain of HdrA has, in addition, a [4Fe-4S] cluster (HA4) that is surrounded by several basic residues and coordinated with a Cys386, Cys399, Cys403, and Cys404 sequence motif (consensus sequence CX10-16-Y/W/H/F-C-S/A/C-X2-3CC)
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