A0A2I6QLJ4 · A0A2I6QLJ4_9BACT
- Protein3-methyl-2-oxobutanoate hydroxymethyltransferase
- GenepanB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids235 (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; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 8 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 8-9 | 3-methyl-2-oxobutanoate (UniProtKB | ChEBI) | ||||
Sequence: DS | ||||||
Binding site | 47 | 3-methyl-2-oxobutanoate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 47 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 77 | 3-methyl-2-oxobutanoate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 79 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 147 | Proton acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-methyl-2-oxobutanoate hydroxymethyltransferase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | methyltransferase activity | |
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
- Organism
- Taxonomic lineageBacteria > environmental samples
Accessions
- Primary accessionA0A2I6QLJ4
Subcellular Location
Interaction
Subunit
Homodecamer; pentamer of dimers.
Structure
Sequence
- Sequence statusComplete
- Length235
- Mass (Da)25,402
- Last updated2018-03-28 v1
- Checksum26173C1A4FEB3A21