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Protein

Methyl-coenzyme M reductase subunit beta

Gene
N/A
Organism
Methanosarcina thermophila
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. coenzyme-B sulfoethylthiotransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. methanogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Methanogenesis

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-coenzyme M reductase subunit beta (EC:2.8.4.1)
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase beta
OrganismiMethanosarcina thermophila
Taxonomic identifieri2210 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›18›18Methyl-coenzyme M reductase subunit betaPRO_0000147470Add
BLAST

Interactioni

Subunit structurei

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

Sequencei

Sequence statusi: Fragment.

P22949-1 [UniParc]FASTAAdd to Basket

« Hide

        10 
SDTVDIYDAG KILERVII
Length:18
Mass (Da):2,020
Last modified:August 1, 1991 - v1
Checksum:i3783D55E2C6E369D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei18 – 181

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00646; UER00699.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  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 nameiMCRB_METTE
AccessioniPrimary (citable) accession number: P22949
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 1, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Reduced ferredoxin could reductively reactivate the enzyme.

Keywords - Technical termi

Direct protein sequencing

Documents

  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.