Protein Domain : Vicinal oxygen chelate (VOC) domain IPR037523

Type	Domain
Description	The vicinal oxygen chelate (VOC) family of enzymes catalyzes a highly diverse set of chemistries that derives from one common mechanistic trait: bidentatecoordination to a divalent metal centre by a substrate or intermediate or transition state through vicinal oxygen atoms. The array of reactionscatalyzed by this family is mediated structurally by a common fold and protein-chelating residues that secure and localize a metal ion. The commonfold has topological symmetry being comprised of two Beta-α-β-β-β units that form an incompletely closed barrel of β-sheet about the metalion [ ]. Members of this family include the glyoxalases I (GLO), the extradiol dioxygenases (DHBD), the bleomycin resistance proteins, the fosfomycin resistance proteins, and the methylmalonyl-CoAepimerases (MMCE) involved in the epimerization of (2S)-methylmalonyl-CoA to its (2R)-stereoisomer. The bleomycin resistance proteins are unique in thatthey do not possess a metal binding site and are not enzymes. They bind and sequester bleomycin and related compounds without degrading or transformingthem [ , , ].
Short Name	VOC