A0A2E0F649 · A0A2E0F649_9FLAO
- ProteinKetol-acid reductoisomerase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids472 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Cofactor
Pathway
Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4.
Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 217 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 217 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 221 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 389 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 393 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 414 | substrate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | isomerase activity | |
Molecular Function | ketol-acid reductoisomerase activity | |
Molecular Function | metal ion binding | |
Biological Process | isoleucine biosynthetic process | |
Biological Process | valine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKetol-acid reductoisomerase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae
Accessions
- Primary accessionA0A2E0F649
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-208 | KARI N-terminal Rossmann | ||||
Sequence: LNMCRFMNNDEFSDGVNALLGKKIVIVGCGAQGLNQGLNMRDSGLDISYVLRQSSIDSKKESYLNAKENNFNVGNFEDLIPEADIVINLTPDKNHTNVVSNVVPLMKKNSVLSFSHGFNIVEEGTIVRNDITVIMVAPKCPGTEVREEYLRGFGVPTLIAVHPENDPHNNGLELAKAYAVATGGHRAGVLES | ||||||
Domain | 209-343 | KARI C-terminal knotted | ||||
Sequence: SFVAEVKSDLMGEQTILCGVLQTGSLLCFEKMLSLGFDKSFSVKLIQFGWETITEELKHNGITGMINRLDDKSRYAVHELSEQLKDIMTPLFNKHMNDILDGTFSTGMMKDWENDDHNLLKWREETGDTLFEKTP | ||||||
Domain | 345-472 | KARI C-terminal knotted | ||||
Sequence: GSENISNQDFFDKGILMIAFVKSGVELAFETMVNNGIIDESAYYESLHELPLIANLVARKKLYEMNRIISDTAEYGCYLFNHECLPLLKGFMNELERGFIGENIPNSYTFNEEKLNEYDNLTSSHPIE |
Sequence similarities
Belongs to the ketol-acid reductoisomerase family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length472
- Mass (Da)53,038
- Last updated2018-04-25 v1
- Checksum8A49A313010B6023
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 472 | |||||
Sequence: E |