Vicinal oxygen chelate (VOC) domain (IPR037523)

Short name: VOC

Overlapping homologous superfamilies

Domain relationships



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 centre 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 Beta-Alpha-Beta-Beta-Beta units that form an incompletely closed barrel of beta-sheet about the metal ion [PMID: 21820381].

Members of this family include the glyoxalases I (GLO), 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 [PMID: 10082363, PMID: 11076500, PMID: 21820381].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles