A0A0L0K4U2 · A0A0L0K4U2_9ACTN

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

adenosylcob(III)alamin (UniProtKB | Rhea| CHEBI:18408 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site23Co (UniProtKB | ChEBI) of adenosylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site200-205GTP (UniProtKB | ChEBI)
Binding site204Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site229Mg2+ 2 (UniProtKB | ChEBI)
Binding site230Mg2+ 2 (UniProtKB | ChEBI)
Binding site243Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site243Mg2+ 2 (UniProtKB | ChEBI)
Binding site246GTP (UniProtKB | ChEBI)
Binding site290Mg2+ 2 (UniProtKB | ChEBI)
Binding site290Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site291Mg2+ 2 (UniProtKB | ChEBI)
Binding site337-340GTP (UniProtKB | ChEBI)
Binding site567substrate
Binding site602substrate
Binding site708substrate
Binding site752substrate
Binding site801substrate
Binding site836substrate
Binding site841substrate
Binding site953GTP (UniProtKB | ChEBI)
Binding site1073GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functioncobalamin binding
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functionisobutyryl-CoA mutase activity
Molecular Functionmagnesium ion binding
Molecular Functionmethylmalonyl-CoA mutase activity
Molecular Functionpivalyl-CoA mutase activity
Biological Processacyl-CoA metabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Fused isobutyryl-CoA mutase

Including 2 domains:

  • Recommended name
    Isobutyryl-CoA mutase
  • EC number
  • Short names
    ICM
  • Recommended name
    P-loop GTPase
  • EC number
  • Alternative names
    • G-protein chaperone

Gene names

    • Name
      icmF
    • ORF names
      IQ63_22045

Organism names

  • Taxonomic identifier
  • Strain
    • NCPPB 4445
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A0L0K4U2

Proteomes

Interaction

Subunit

Heterodimer of an alpha and a beta chain.
Homodimer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain10-147B12-binding
Region398-559Linker

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 status
    Complete
  • Length
    1,074
  • Mass (Da)
    118,333
  • Last updated
    2015-11-11 v1
  • Checksum
    F405A01C58E834AA
MSELHRPTHPVRLVTASALFDGHDASINIMRRIFQAQGAEVIHLGHNRSVREVVDAALEEDAHGVAVSSYQGGHVEYFEYLVESLREQGADHVRVVGGGGGVIVPEEITRLRASGVTIFSPEDGQRMGLAGMINSVVRDCDFDLWDGRPADVDAVLAGDRFAVARAVTGAELGKLPREFMETLRGTTRTVPVLGITGTGGSGKSSLTDELVRRFRVDQQDKLRIAVIAVDPTRRRGGGALLGDRIRMNSLDGNRVFFRSLATRGSRELPEHLADVIDVVKAAGFDLVIVETPGIGQGDAAIVPFVDTSLYVMTPEFGAASQLEKIDMLDFADTVAINKFERRGAKDALRDVGRQLVRNREEFGKKPEDMPVYGTSAATFNDDGVTALYQHLRGELADKGLPLGEGALAHVDVRYSSGIRQVVPAERVRYLAEITDTVRAYHAQTLQLADAARRLQRLEAVEEELADAGSDAANLVPLIKNARRDLPGDVADQIANWPAVVASYSGDEQVVTVRGKELRTRLTRESLSGNKIPRVALPRFVDHGELVSFWRRENLPGQFPFTAGVFPFKRDGEDPARMFAGEGDPFRTNRRFKLLSEGQPATRLSTAFDSVTLYGRDPDERPDIYGKVGTSGVSVATLDDMKALYDGFDLVAPTTSVSMTINGPAPTVLAFFLNTVMDQRTDAFRSAEGREPSPEEAEGLRAEALASVRGTVQADILKEDQGQNTCLFSTEFSLRMMADIQEWFIRQQVRNFYSVSISGYHIAEAGANPISQLAFTLANGFTYVEAYLARGMDIDDFAPNLSFFFSNGMDPEYAVLGRVARRIWAVAMKEKYGANERSQKLKYHVQTSGRSLHAQEMDFNDIRTTLQALIALYDNCNSLHTNAYDEAVTTPTEDSVRRALAIQLIINREWGLAMNENPLQGSYVIDELTDLVEEAVLTEFERISERGGVLGAMETGYQRGRIQDESMLYEQRKHDGTLPIVGVNTFRNPHADTAAPGPVELARATEKEKRSQLERVVEFRTHHRSEAHEALAALKEAAIGDGNVFAVLMEAARVCTLQQITEAFFEVGGQYRRNV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JPPY01000132
EMBL· GenBank· DDBJ
KND32833.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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