A0A246BDP2 · A0A246BDP2_9FLAO

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 site24Co (UniProtKB | ChEBI) of adenosylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site206-211GTP (UniProtKB | ChEBI)
Binding site210Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site234Mg2+ 2 (UniProtKB | ChEBI)
Binding site235Mg2+ 2 (UniProtKB | ChEBI)
Binding site248Mg2+ 2 (UniProtKB | ChEBI)
Binding site248Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site251GTP (UniProtKB | ChEBI)
Binding site296Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site296Mg2+ 2 (UniProtKB | ChEBI)
Binding site297Mg2+ 2 (UniProtKB | ChEBI)
Binding site343-346GTP (UniProtKB | ChEBI)
Binding site570substrate
Binding site605substrate
Binding site755substrate
Binding site799substrate
Binding site848substrate
Binding site883substrate
Binding site888substrate
Binding site1000GTP (UniProtKB | ChEBI)
Binding site1119GTP (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
      AP75_00660

Organism names

  • Taxonomic identifier
  • Strain
    • DSM 19056
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Weeksellaceae > Chryseobacterium group > Kaistella

Accessions

  • Primary accession
    A0A246BDP2

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-145B12-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 status
    Complete
  • Length
    1,120
  • Mass (Da)
    126,082
  • Last updated
    2017-10-25 v1
  • MD5 Checksum
    7E728B043EE384C658508C0262CE3395
MEIQKYSPKNKIRIVTAAALFDGHDAAINIMRRVIQGTGVEVIHLGHDKSAEEVVNCAVQEDANAIALTSYQGGHNEYFKYIYDLLKEKNASHIKIFGGGGGVILPEEIKDLMDYGVTRIYSPDDGRELGLQGMIDDLVQKSDFPTGEKITVQDLDKIKFEDSKSIAEVISAVENFSETKPDLVKEIEQRSKDSHIPIIGITGTGGAGKSSLTDELVRRFLRSNPEKKIAIISIDPSKKKTGGALLGDRIRMNSINDPRVYMRSMATRENNVSVSPHIHSALNILKIAKPDVIVLETSGIGQSGSEITDIADVSMYVMTPEYGASTQLEKIDMLDYADLVALNKSDKRGALDALQAVKKQFQRNHLLFEQPLEEMPVYSTKASQFNDWGTTELYNELIKKLNEKFDGLNLSGYIEQNVSEETTIIPPKRVRYLSEIVENNRAYDKDVVDQALIARKLYQLQGAKNILEDDVNSQEILEKRYQKIKKDLSQENIYFLNGWHDFKLKHEADEYIYLVRGKEIKVQTKSETLSHLKIPKIALPKFQDWGDLIRWKGQENVPGAFPFTAGIYPFKRTGEDPTRMFAGEGGPERTNRRFHYVSAEMDAKRLSTAFDSVTLYGQDPAFPPDIYGKIGNAGVSIATLDDAKKLYSGFDLVNAMTSVSMTINGPAPMLLAFFMNAAIDQNCEKYIEENNLWDKVEARLKEKFDDKGLSRPTYSGDLPPSNNGLGLKLLGLTGDEILDEETYAKIKAETIATVRGTVQADILKEDQAQNTCIFSTEFALRLMGDVQEYFIKEKVRNFYSVSISGYHIAEAGANPISQLAFTLANGFTYVEYYLSRGMDINDFAPNLSFFFSNGIDPEYAVIGRVARRIWAKAMREKYNANERSQMLKYHIQTSGRSLHAQEIDFNDIRTTLQALYAIYDNCNSLHTNAYDEAITTPTEESVRRAMAIQLIINKELGLAKNENPLQGSFIIEELTDLVEEAVYAEFDRITERGGVLGAMETMYQRSKIQEESMHYEWLKHTGEYPIVGVNTFLGKDGSPTVLPGEVIRSTEEEKQQQIKNLETYQIANKAHTQKILEELQHAAINQKNLFEVMMEAVKFCSLGQITNALFEVGGKYRRNM

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JASZ02000001
EMBL· GenBank· DDBJ
OWK99489.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help