A0A0L0K4U2 · A0A0L0K4U2_9ACTN
- ProteinFused isobutyryl-CoA mutase
- GeneicmF
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1074 (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 + H+ + phosphate
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 23 | Co (UniProtKB | ChEBI) of adenosylcob(III)alamin (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 200-205 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GSGKSS | ||||||
Binding site | 204 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: S | ||||||
Binding site | 229 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 230 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 243 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 243 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 246 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 290 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 290 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 291 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 337-340 | GTP (UniProtKB | ChEBI) | ||||
Sequence: NKFE | ||||||
Binding site | 567 | substrate | ||||
Sequence: F | ||||||
Binding site | 602 | substrate | ||||
Sequence: R | ||||||
Binding site | 708 | substrate | ||||
Sequence: R | ||||||
Binding site | 752 | substrate | ||||
Sequence: Y | ||||||
Binding site | 801 | substrate | ||||
Sequence: S | ||||||
Binding site | 836 | substrate | ||||
Sequence: R | ||||||
Binding site | 841 | substrate | ||||
Sequence: K | ||||||
Binding site | 953 | GTP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1073 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N |
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 > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A0L0K4U2
Proteomes
Interaction
Subunit
Heterodimer of an alpha and a beta chain.
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-147 | B12-binding | ||||
Sequence: PVRLVTASALFDGHDASINIMRRIFQAQGAEVIHLGHNRSVREVVDAALEEDAHGVAVSSYQGGHVEYFEYLVESLREQGADHVRVVGGGGGVIVPEEITRLRASGVTIFSPEDGQRMGLAGMINSVVRDCDFDLWDG | ||||||
Region | 398-559 | Linker | ||||
Sequence: KGLPLGEGALAHVDVRYSSGIRQVVPAERVRYLAEITDTVRAYHAQTLQLADAARRLQRLEAVEEELADAGSDAANLVPLIKNARRDLPGDVADQIANWPAVVASYSGDEQVVTVRGKELRTRLTRESLSGNKIPRVALPRFVDHGELVSFWRRENLPGQFP |
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,074
- Mass (Da)118,333
- Last updated2015-11-11 v1
- ChecksumF405A01C58E834AA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JPPY01000132 EMBL· GenBank· DDBJ | KND32833.1 EMBL· GenBank· DDBJ | Genomic DNA |