PROSITE documentation PDOC51819Vicinal 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.
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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). | |
| PubMed ID | 10082363 | |
| DOI | 10.1002/pro.5560070801 |
| 2 | Authors | Armstrong R.N. |
| Title | Mechanistic diversity in a metalloenzyme superfamily. | |
| Source | Biochemistry 39:13625-13632(2000). | |
| PubMed ID | 11076500 |
| 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). | |
| PubMed ID | 21820381 | |
| DOI | 10.1016/j.jinorgbio.2011.06.006 |
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