P22948 (MCRA_METTE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Methyl-coenzyme M reductase subunit alpha EC=2.8.4.1 Alternative name(s): Coenzyme-B sulfoethylthiotransferase alpha
Organism	Methanosarcina thermophila
Taxonomic identifier	2210 [NCBI]
Taxonomic lineage	Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	15 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and an 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 By similarity.
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 process	Methanogenesis
Ligand	Nickel
Molecular function	Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	methanogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	coenzyme-B sulfoethylthiotransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›15	›15	Methyl-coenzyme M reductase subunit alpha		PRO_0000147459
Experimental info
	Non-terminal residue	15	1

Sequences

	Sequence		Length	Mass (Da)
	P22948 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: D5D59892FCA5F63C	FASTA	15	1,686
	10 AADIFAKFKT SMEVK

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: 2013570] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: DSM 1825 / TM-1.

Cross-references

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

MCRA_METTE

Accession

Primary (citable) accession number: P22948

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program