Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Methyl-coenzyme M reductase subunit beta

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.


Reduced ferredoxin could reductively reactivate the enzyme.

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


Molecular functionTransferase
Biological processMethanogenesis

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001474701 – ›18Methyl-coenzyme M reductase subunit betaAdd BLAST›18


Subunit structurei

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


Sequence statusi: Fragment.

P22949-1 [UniParc]FASTAAdd to basket

« Hide

Mass (Da):2,020
Last modified:August 1, 1991 - v1

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei181

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 one 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.

Entry informationi

Entry nameiMCRB_METTE
AccessioniPrimary (citable) accession number: P22949
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: March 15, 2017
This is version 48 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program


Keywords - Technical termi

Direct protein sequencing


  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways