H7CHY2 · H7CHY2_METWO
- Proteincoenzyme-B sulfoethylthiotransferase
- GenemrtA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids381 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
Catalytic activity
- coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B heterodisulfide + methaneThis reaction proceeds in the forward direction.
Cofactor
Pathway
One-carbon metabolism; methyl-coenzyme M reduction; methane from methyl-coenzyme M: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 54 | coenzyme F430 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 55 | coenzyme F430 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 56 | coenzyme F430 (UniProtKB | ChEBI); covalent | ||||
Sequence: Q | ||||||
Binding site | 134 | coenzyme B (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 165 | coenzyme B (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 179 | coenzyme B (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 236 | coenzyme F430 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 237 | coenzyme F430 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 240 | coenzyme F430 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 241 | coenzyme F430 (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | coenzyme-B sulfoethylthiotransferase activity | |
Molecular Function | metal ion binding | |
Biological Process | methanogenesis |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namecoenzyme-B sulfoethylthiotransferase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Methanomada group > Methanobacteria > Methanobacteriales > Methanobacteriaceae > Methanothermobacter
Accessions
- Primary accessionH7CHY2
PTM/Processing
Keywords
- PTM
Interaction
Subunit
MCR is a hexamer of two alpha, two beta, and two gamma chains, forming a dimer of heterotrimers.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-177 | Methyl-coenzyme M reductase alpha subunit N-terminal | ||||
Sequence: AAIQQMVDDIKRTVIVGMDTAHAVLEKRLGVEVTPETINEYMEVINHALPGGAVVQEHMVEVHPGIVEDCYAKVFTGDDNLADELDKRILIDINKEFPEEQAEQLKSYIGNRTYQVNRVPTIVVRACDGGTVSRWSAMQIGMSFISAYKLCAGEAAIADFSFAAKHADVIEMGTIMP | ||||||
Domain | 224-349 | Methyl-coenzyme M reductase alpha subunit C-terminal | ||||
Sequence: DQVWLGSYMSGGVGFTQYATAAYTDDILDDFLYYGMEYVEDKFGICGSEPTMDVVRDISTEVTLYSLEQYEEYPTLLEDHFGGSQRAAVAAAAAGCSTAFATGNSNAGVNGWYLSQILHKEAHSRL |
Sequence similarities
Belongs to the methyl-coenzyme M reductase alpha subunit family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length381
- Mass (Da)41,335
- Last updated2012-05-16 v1
- ChecksumBFEBA56BD2CDA97F
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: A | ||||||
Non-terminal residue | 381 | |||||
Sequence: P |
Keywords
- Technical term