Q1QYU7 · GBMOO_CHRSD

Function

function

Involved in degradation of glycine betaine (PubMed:29703733).
Part of a Rieske-type oxygenase system that catalyzes the conversion of glycine betaine (GB) to dimethylglycine (DMG) (PubMed:29703733).
This subunit is the terminal oxygenase component of the system (PubMed:29703733).
Is specific for GB, and does not show any activity on choline, L-carnitine, stachydrine, dimethylglycine or sarcosine (PubMed:29703733).
Activity is strictly dependent on NADH (PubMed:29703733).

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

Note: Binds 1 [2Fe-2S] cluster per subunit.
Fe cation (UniProtKB | Rhea| CHEBI:24875 )

Note: Binds 1 Fe cation per subunit.

Activity regulation

Activity is absolutely dependent on the presence of BmoB (PubMed:29703733).
Glycine betaine monooxygenase activity is significantly enhanced by Fe2+ and severely inhibited by heavy-metal ions, including Co2+, Mn2+, Zn2+, Cu2+ and Ag+ (PubMed:29703733).
Severely inhibited by EDTA (PubMed:29703733).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
1.2 mMglycine betaine
kcat is 0.65 sec-1 with glycine betaine as substrate.

pH Dependence

Optimum pH is 7.5.

Temperature Dependence

Optimum temperature is 30 degrees Celsius.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site115[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site117[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site135[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site138[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site234Fe cation (UniProtKB | ChEBI)
Binding site239Fe cation (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Functioniron ion binding
Molecular Functionmonooxygenase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glycine betaine monooxygenase oxygenase subunit
  • EC number
  • Short names
    BMO oxygenase subunit
    ; GB monooxygenase oxygenase subunit
  • Alternative names
    • BMO Rieske-type oxygenase component

Gene names

    • Name
      bmoA
    • Ordered locus names
      Csal_1004

Organism names

Accessions

  • Primary accession
    Q1QYU7

Proteomes

Phenotypes & Variants

Disruption phenotype

Can use glucose or dimethylglycine as the sole carbon source, but is incapable of growth on glycine betaine as the sole source of carbon.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004590921-445Glycine betaine monooxygenase oxygenase subunit

Interaction

Subunit

Homotrimer (PubMed:29703733).
The system is composed of an oxygenase subunit (BmoA) and a reductase subunit (BmoB) (PubMed:29703733).
Maximal specific activity is obtained when the ratio of BmoA to BmoB is 5:1 (PubMed:29703733).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain73-180Rieske

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    445
  • Mass (Da)
    50,393
  • Last updated
    2006-05-16 v1
  • Checksum
    7895449E58193642
MSLAPSVIEPAHEEDAFMDLLATSALDDPLAAARDATADMLRQRQGDHSLPQPFYNDPRVFALEMREIFEHEWLFVGMTCEIPAKGNYLTVQIGDNPIIVVRGDQGTIHAFHNVCRHRGSRLCTQAKGKVAKLVCPYHQWTYELDGRLLFAGQDMGEDFDLGAHGLKPVAVTHAGGFLFVSLADQPPAIDDFLATLDDYLAPYEMDNVKVAAESNIVEQANWKLVIENNRECYHCNGAHPELLNSLIEYDDTDDPRATPAYRDLVARQQAHWEQQQVPWALKRFGKRNRLTRTPMIEGVVSMTMDGRPASQRLMGRLPNPDMGSLRILHLPNSWNHFMGDHAVVFRVLPLGPQQTLVTTKWLVHRDAQEGVDYDPEWMRKVWDATTDQDRQLAEENQRGINSVAYQPGPYSRTYEFGVIDFVDWYSDTMLSRLDAEAPSLHIVQG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000285
EMBL· GenBank· DDBJ
ABE58361.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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