{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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