A0A246BDP2 · A0A246BDP2_9FLAO
- ProteinFused isobutyryl-CoA mutase
- GeneicmF
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1120 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly.
Catalytic activity
- 2-methylpropanoyl-CoA = butanoyl-CoA
- GTP + H2O = GDP + phosphate + H+
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 24 | Co (UniProtKB | ChEBI) of adenosylcob(III)alamin (UniProtKB | ChEBI); axial binding residue | |||
Binding site | 206-211 | GTP (UniProtKB | ChEBI) | |||
Binding site | 210 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 234 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 235 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 248 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 248 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 251 | GTP (UniProtKB | ChEBI) | |||
Binding site | 296 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 296 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 297 | Mg2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 343-346 | GTP (UniProtKB | ChEBI) | |||
Binding site | 570 | substrate | |||
Binding site | 605 | substrate | |||
Binding site | 755 | substrate | |||
Binding site | 799 | substrate | |||
Binding site | 848 | substrate | |||
Binding site | 883 | substrate | |||
Binding site | 888 | substrate | |||
Binding site | 1000 | GTP (UniProtKB | ChEBI) | |||
Binding site | 1119 | GTP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | cobalamin binding | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | isobutyryl-CoA mutase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | methylmalonyl-CoA mutase activity | |
Molecular Function | pivalyl-CoA mutase activity | |
Biological Process | acyl-CoA metabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameFused isobutyryl-CoA mutase
Including 2 domains:
- Recommended nameIsobutyryl-CoA mutase
- EC number
- Short namesICM
- Recommended nameP-loop GTPase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Weeksellaceae > Chryseobacterium group > Kaistella
Accessions
- Primary accessionA0A246BDP2
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 11-145 | B12-binding | |||
Domain
Is composed of four functional domains: the N-terminal 5'-deoxyadenosylcobalamin binding region that is homologous to the small subunit of ICM (IcmB), a middle P-loop GTPase domain (MeaI) that likely acts as a chaperone for ICM, a structured linker region involved in dimer formation, and a C-terminal part that is homologous to the large substrate-binding subunit of ICM (IcmA).
Sequence similarities
Belongs to the IcmF family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,120
- Mass (Da)126,082
- Last updated2017-10-25 v1
- MD5 Checksum7E728B043EE384C658508C0262CE3395
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JASZ02000001 EMBL· GenBank· DDBJ | OWK99489.1 EMBL· GenBank· DDBJ | Genomic DNA |