{PDOC51819}
{PS51819; VOC}
{BEGIN}
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* Vicinal oxygen chelate (VOC) domain profile *
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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 BetaAlphaBetaBetaBeta
units that form an incompletely closed barrel of beta-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.
-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 2016 / First entry.
[ 1] Bergdoll M., Eltis L.D., Cameron A.D., Dumas P., Bolin J.T.
"All in the family: structural and evolutionary relationships among
three modular proteins with diverse functions and variable
assembly."
Protein Sci. 7:1661-1670(1998).
PubMed=10082363; DOI=10.1002/pro.5560070801
[ 2] Armstrong R.N.
"Mechanistic diversity in a metalloenzyme superfamily."
Biochemistry 39:13625-13632(2000).
PubMed=11076500
[ 3] He P., Moran G.R.
"Structural and mechanistic comparisons of the metal-binding members
of the vicinal oxygen chelate (VOC) superfamily."
J. Inorg. Biochem. 105:1259-1272(2011).
PubMed=21820381; DOI=10.1016/j.jinorgbio.2011.06.006
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