Reviewed,
UniProtKB/Swiss-Prot P22949 (MCRB_METTE)
Last modified
September 22, 2009.
Version 37.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Methyl-coenzyme M reductase subunit beta EC=2.8.4.1 Alternative name(s): Coenzyme-B sulfoethylthiotransferase beta |
| Organism | Methanosarcina thermophila |
| Taxonomic identifier | 2210 [NCBI] |
| Taxonomic lineage | Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina |
Protein attributes
| Sequence length | 18 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| 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 | 2-(methylthio)ethanesulfonate (methyl-CoM) + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) = 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 process | Methanogenesis |
| 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)
Sequences
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
Entry information
| Entry name | MCRB_METTE | ||||||||
| Accession | Primary (citable) accession number: P22949 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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