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InterPro: IPR017678 CoB--CoM heterodisulphide reductase, subunit B

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UniProtKB
Matches:
38 proteins
AccessionHelp IPR017678 CoB/CoM_hetero-S_Rdtase_bsu
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR004017 Cysteine-rich domain
GO Term annotationHelp
Process GO:0015948 methanogenesis
GO:0051186 cofactor metabolic process
GO:0055114 oxidation reduction
Function GO:0051912 CoB--CoM heterodisulfide reductase activity
InterPro annotation
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AbstractHelp

This entry represents subunit B (HdrB) from CoB--CoM heterodisulphide reductase (or heterodisulphide reductase; Hdr; EC:1.8.98.1), an iron-sulphur protein found in methanogenic archaea [1]. Hdr catalyses the reversible reduction of the heterodisulphide (CoM-S-S-CoB) to the thiol-coenzymes: coenzyme M (H-S-CoM) and coenzyme B (H-S-CoB). Hdr is composed of three subunits: hdrA (subunit A), hdrB (subunit B) and hdrC (subunit C). Hdr forms a complex with the F420-non-reducing hydrogenase (Mvh), which provides the reducing equivalents to the heterodisulphide reductase.

All processes in methanogenesis lead to the formation of a mixed disulphide bond between coenzyme-M and coenzyme-B, by a reaction in which coenzyme B reduces methyl-CoM, leading to formation of methane and a CoB-CoM heterodisulphide [2]. There are two different systems that are capable of reducing the CoB-CoM heterodisulphide, using either H2 or a reduced cofactor F420 as electron donors [3].

HdrB may have a function in energy transduction. Some archaea species have two copies, HdrB1 and HdrB2.

Database linksHelp
Enzyme: EC:1.8.98.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR017678 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O27907 CoB--CoM heterodisulfide reductase subunit B

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Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR017678 CoB--CoM heterodisulphide reductase, subunit B
IPR004017 Cysteine-rich domain

PublicationsHelp
1. Madadi-Kahkesh S, Duin EC, Heim S, Albracht SP, Johnson MK, Hedderich R.
A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea.
Eur. J. Biochem. 268 2566-77 2001 [PubMed: 11322875]
http://dx.doi.org/10.1046/j.1432-1327.2001.02141.x
2. Deppenmeier U.
The unique biochemistry of methanogenesis.
Prog. Nucleic Acid Res. Mol. Biol. 71 223-83 2002 [PubMed: 12102556]
http://dx.doi.org/10.1016/S0079-6603(02)71045-3
3. Deppenmeier U.
The membrane-bound electron transport system of Methanosarcina species.
J. Bioenerg. Biomembr. 36 55-64 2004 [PubMed: 15168610]
http://dx.doi.org/10.1023/B:JOBB.0000019598.64642.97

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InterPro 23.1