PROSITE documentation PDOC51819
Vicinal oxygen chelate (VOC) domain profile


The vicinal oxygen chelate (VOC) family of enzymes catalyzes a highly diverse set of chemistries that derives from one common mechanistic trait: bidentate coordination to a divalent metal center by a substrate or intermediate or transition state through vicinal oxygen atoms. The array of reactions catalyzed by this family is mediated structurally by a common fold and protein-chelating residues that secure and localize a metal ion. The common fold has topological symmetry being comprised of two βαβββ units that form an incompletely closed barrel of β-sheet about the metal ion (see <PDB:1F9Z>). Members of this family include the glyoxalases I (GLO) (see <PDOC00720>), the extradiol dioxygenases (DHBD), the bleomycin resistance proteins, the fosfomycin resistance proteins, and the methylmalonyl-CoA epimerases (MMCE) involved in the epimerization of (2S)-methylmalonyl-CoA to its (2R)-stereoisomer. The bleomycin resistance proteins are unique in that they do not possess a metal binding site and are not enzymes. They bind and sequester bleomycin and related compounds without degrading or transforming them [1,2,3].

The profile we developed covers the entire VOC domain.

Last update:

November 2016 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

VOC, PS51819; Vicinal oxygen chelate (VOC) domain profile  (MATRIX)


1AuthorsBergdoll M. Eltis L.D. Cameron A.D. Dumas P. Bolin J.T.
TitleAll in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly.
SourceProtein Sci. 7:1661-1670(1998).
PubMed ID10082363

2AuthorsArmstrong R.N.
TitleMechanistic diversity in a metalloenzyme superfamily.
SourceBiochemistry 39:13625-13632(2000).
PubMed ID11076500

3AuthorsHe P. Moran G.R.
TitleStructural and mechanistic comparisons of the metal-binding members of the vicinal oxygen chelate (VOC) superfamily.
SourceJ. Inorg. Biochem. 105:1259-1272(2011).
PubMed ID21820381

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)