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P22950 (MCRG_METTE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methyl-coenzyme M reductase subunit gamma

EC=2.8.4.1
Alternative name(s):
Coenzyme-B sulfoethylthiotransferase gamma
OrganismMethanosarcina thermophila
Taxonomic identifier2210 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length20 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 2 coenzyme F430 noncovalently per hexamer. Coenzyme F430 is a yellow nickel porphinoid Potential.

Pathway

One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1.

Subunit structure

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

Miscellaneous

Reduced ferredoxin could reductively reactivate the enzyme.

Biophysicochemical properties

Temperature dependence:

Optimum temperature is 60 degrees Celsius.

Ontologies

Keywords
   Biological processMethanogenesis
   Molecular functionTransferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processmethanogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncoenzyme-B sulfoethylthiotransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›20›20Methyl-coenzyme M reductase subunit gamma
PRO_0000147482

Experimental info

Non-terminal residue201

Sequences

Sequence LengthMass (Da)Tools
P22950 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: D1AACAAA6D653658

FASTA202,224
        10         20 
AYERQFYPGA TSVAENNIGH 

« Hide

References

[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.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00646; UER00699.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameMCRG_METTE
AccessionPrimary (citable) accession number: P22950
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 16, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways