Q1QYU7 · GBMOO_CHRSD
- ProteinGlycine betaine monooxygenase oxygenase subunit
- GenebmoA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids445 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- glycine betaine + H+ + NADH + O2 = formaldehyde + H2O + N,N-dimethylglycine + NAD+This reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [2Fe-2S] cluster per subunit.
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).
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 mM | glycine 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 115 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 117 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 135 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 138 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 234 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 239 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | iron ion binding | |
Molecular Function | monooxygenase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycine betaine monooxygenase oxygenase subunit
- EC number
- Short namesBMO oxygenase subunit ; GB monooxygenase oxygenase subunit
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Oceanospirillales > Halomonadaceae > Chromohalobacter
Accessions
- Primary accessionQ1QYU7
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000459092 | 1-445 | Glycine betaine monooxygenase oxygenase subunit | |||
Sequence: MSLAPSVIEPAHEEDAFMDLLATSALDDPLAAARDATADMLRQRQGDHSLPQPFYNDPRVFALEMREIFEHEWLFVGMTCEIPAKGNYLTVQIGDNPIIVVRGDQGTIHAFHNVCRHRGSRLCTQAKGKVAKLVCPYHQWTYELDGRLLFAGQDMGEDFDLGAHGLKPVAVTHAGGFLFVSLADQPPAIDDFLATLDDYLAPYEMDNVKVAAESNIVEQANWKLVIENNRECYHCNGAHPELLNSLIEYDDTDDPRATPAYRDLVARQQAHWEQQQVPWALKRFGKRNRLTRTPMIEGVVSMTMDGRPASQRLMGRLPNPDMGSLRILHLPNSWNHFMGDHAVVFRVLPLGPQQTLVTTKWLVHRDAQEGVDYDPEWMRKVWDATTDQDRQLAEENQRGINSVAYQPGPYSRTYEFGVIDFVDWYSDTMLSRLDAEAPSLHIVQG |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 73-180 | Rieske | ||||
Sequence: WLFVGMTCEIPAKGNYLTVQIGDNPIIVVRGDQGTIHAFHNVCRHRGSRLCTQAKGKVAKLVCPYHQWTYELDGRLLFAGQDMGEDFDLGAHGLKPVAVTHAGGFLFV |
Sequence similarities
Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length445
- Mass (Da)50,393
- Last updated2006-05-16 v1
- Checksum7895449E58193642
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000285 EMBL· GenBank· DDBJ | ABE58361.1 EMBL· GenBank· DDBJ | Genomic DNA |