|PROSITE documentation PDOC51819 [for PROSITE entry PS51819]|
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.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Bergdoll M. Eltis L.D. Cameron A.D. Dumas P. Bolin J.T.|
|Title||All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly.|
|Source||Protein Sci. 7:1661-1670(1998).|
|Title||Mechanistic diversity in a metalloenzyme superfamily.|
|3||Authors||He P. Moran G.R.|
|Title||Structural and mechanistic comparisons of the metal-binding members of the vicinal oxygen chelate (VOC) superfamily.|
|Source||J. Inorg. Biochem. 105:1259-1272(2011).|