A0A218P1F2 · A0A218P1F2_THECE
- Protein3-methyl-2-oxobutanoate hydroxymethyltransferase
- GenepanB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids285 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic activity
- (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Cofactor biosynthesis; coenzyme A biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 44 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 44-45 | 3-methyl-2-oxobutanoate (UniProtKB | ChEBI) | ||||
Sequence: DS | ||||||
Binding site | 83 | 3-methyl-2-oxobutanoate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 83 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 112 | 3-methyl-2-oxobutanoate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 114 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 181 | Proton acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-methyl-2-oxobutanoate hydroxymethyltransferase activity | |
Molecular Function | metal ion binding | |
Molecular Function | methyltransferase activity | |
Biological Process | coenzyme A biosynthetic process | |
Biological Process | methylation | |
Biological Process | pantothenate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-methyl-2-oxobutanoate hydroxymethyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Thermococci > Thermococcales > Thermococcaceae > Thermococcus
Accessions
- Primary accessionA0A218P1F2
Proteomes
Subcellular Location
Interaction
Subunit
Homodecamer; pentamer of dimers.
Structure
Sequence
- Sequence statusComplete
- Length285
- Mass (Da)31,952
- Last updated2017-09-27 v1
- Checksum8E118F4D7677CC26
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP014854 EMBL· GenBank· DDBJ | ASI98741.1 EMBL· GenBank· DDBJ | Genomic DNA |