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InterPro: IPR012775 Gamma-butyrobetaine,2-oxoglutarate dioxygenase

Protein matchesHelp
UniProtKB
Matches:
23 proteins
AccessionHelp IPR012775 2-oxoglut_dOase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR003819 Taurine catabolism dioxygenase TauD/TfdA
GO Term annotationHelp
Process GO:0045329 carnitine biosynthetic process
GO:0055114 oxidation reduction
Function GO:0005506 iron ion binding
GO:0016706 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Members of this protein family are gamma-butyrobetaine hydroxylase, both bacterial and eukaryotic. This enzyme catalyzes the last step in the conversion of lysine to carnitine. Carnitine can serve as a compatible solvent in bacteria and also participates in fatty acid metabolism.

Database linksHelp
Enzyme: EC:1.14.11.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR012775 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O75936 Gamma-butyrobetaine dioxygenase

P80193 Gamma-butyrobetaine dioxygenase

Q19000 Probable gamma-butyrobetaine dioxygenase

Q5R5D8 Gamma-butyrobetaine dioxygenase

Q924Y0 Gamma-butyrobetaine dioxygenase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR003819 Taurine catabolism dioxygenase TauD/TfdA
IPR012775 Gamma-butyrobetaine,2-oxoglutarate dioxygenase
SWISS-MODEL
ModBase

PublicationsHelp

Additional ReadingHelp
Ruetschi U, Nordin I, Odelhog B, Jornvall H, Lindstedt S.
gamma-Butyrobetaine hydroxylase. Structural characterization of the Pseudomonas enzyme.
Eur. J. Biochem. 213 1993 1075-80 [PubMed: 8504802]
http://dx.doi.org/10.1111/j.1432-1033.1993.tb17855.x
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InterPro 23.1