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Methyl-coenzyme M reductase subunit gamma

Methanosarcina thermophila
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli


Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide.

Catalytic activityi

Methyl-CoM + CoB = CoM-S-S-CoB + methane.

Temperature dependencei

Optimum temperature is 60 degrees Celsius.

Pathwayi: methyl-coenzyme M reduction

This protein is involved in step 1 of the subpathway that synthesizes methane from methyl-coenzyme M.
Proteins known to be involved in this subpathway in this organism are:
  1. Methyl-coenzyme M reductase subunit beta, Methyl-coenzyme M reductase subunit alpha, Methyl-coenzyme M reductase subunit gamma
This subpathway is part of the pathway methyl-coenzyme M reduction, which is itself part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes methane from methyl-coenzyme M, the pathway methyl-coenzyme M reduction and in One-carbon metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni


Keywords - Biological processi


Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-coenzyme M reductase subunit gamma (EC:
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase gamma
OrganismiMethanosarcina thermophila
Taxonomic identifieri2210 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›20›20Methyl-coenzyme M reductase subunit gammaPRO_0000147482Add


Subunit structurei

Heterotrimer composed of an alpha, a beta, and a gamma subunit.


Sequence statusi: Fragment.

P22950-1 [UniParc]FASTAAdd to basket

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        10         20
Mass (Da):2,224
Last modified:August 1, 1991 - v1

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei20 – 201


3D structure databases


Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.

Family and domain databases



  1. "Purification and properties of methyl coenzyme M methylreductase from acetate-grown Methanosarcina thermophila."
    Jablonski P.E., Ferry J.G.
    J. Bacteriol. 173:2481-2487(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: DSM 1825 / TM-1.

Entry informationi

Entry nameiMCRG_METTE
AccessioniPrimary (citable) accession number: P22950
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 1, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program



Reduced ferredoxin could reductively reactivate the enzyme.

Keywords - Technical termi

Direct protein sequencing


  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.