A0A8T6ZFB0 · A0A8T6ZFB0_9BURK

  • Protein
    Carnitine monooxygenase oxygenase subunit
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Converts carnitine to trimethylamine and malic semialdehyde.

Caution

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:
Fe cation (UniProtKB | Rhea| CHEBI:24875 )

Note: Binds 1 Fe cation per subunit.
[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

Note: Binds 1 [2Fe-2S] cluster per subunit.

Pathway

Amine and polyamine metabolism; carnitine metabolism.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site96[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site98[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site116[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site119[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site218Fe cation (UniProtKB | ChEBI)
Binding site223Fe cation (UniProtKB | ChEBI)
Binding site333Fe cation (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Functioniron ion binding
Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
Biological Processcarnitine metabolic process
Biological Processcatabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Carnitine monooxygenase oxygenase subunit
  • EC number
  • Alternative names
    • Carnitine monooxygenase alpha subunit

Gene names

    • ORF names
      NH14_017460

Organism names

  • Taxonomic identifier
  • Strain
    • LMG 19450
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Paraburkholderia

Accessions

  • Primary accession
    A0A8T6ZFB0

Proteomes

Interaction

Subunit

Composed of an oxygenase subunit and a reductase subunit.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain54-162Rieske

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    382
  • Mass (Da)
    43,471
  • Last updated
    2022-10-12 v1
  • Checksum
    F4638BAA9F7039E4
MTYLPIEFHKKPELPKLPADFCANPELAWTIPASYYTSESVYKAEEKKIFENAWICVAHRSELAETNAYVTREVVGESILLVRGKDKVLRAFYNVCPHRGHQLLEGSGKAKNVITCPYHAWAFKLDGALAHANNCDHVESFDKENSTLVPVRVEEYAGFVFINLNPDAEGVEAQLPGLEASLRKACPVIDDLKLAARFVTETPANWKSIVDNYLECYHCGPAHPGFSDSVKIDQYTHTLHGNWTVQFGHAQSSERSFKLDPSIKDPSFSGYWAWPCTMFNVPPGGDFMTVIYEFPMSAEVTLQHYDIYFLNDEPTEEQQKLIEWYRTVFRPEDLRLVESVQKGLKSRGYRGQGRIMVDKQRSGVSEHGIAHFHNLLAQQYQD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JTDB02000004
EMBL· GenBank· DDBJ
NLP62924.1
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.
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