vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.

                          10        20
                  ....*....|....*....|....
gi 1933716685   5 LNHLTLAVSNLQTSLTFWRDLLGL 28
Cdd:cd07244     2 INHITLAVSDLERSLAFYVDLLGF 25

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.

                          10        20
                  ....*....|....*....|....
gi 1933716685   5 LNHLTLAVSNLQTSLTFWRDLLGL 28
Cdd:cd07244     2 INHITLAVSDLERSLAFYVDLLGF 25

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];

                          10        20
                  ....*....|....*....|....*.
gi 1933716685   5 LNHLTLAVSNLQTSLTFWRDLLGLHV 30
Cdd:COG0346     3 LHHVTLRVSDLEASLAFYTDVLGLEL 28

Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1933716685   1 MLQSLNHLTLAVSNLQTSLTFWRDLLGLHVGDLASrlaqcREKPYAGMRFGHG 53
Cdd:COG3324     1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAG-----PGGDYAEFDTDGG 48

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.

                          10        20
                  ....*....|....*....|....
gi 1933716685   5 LNHLTLAVSNLQTSLTFWRDLLGL 28
Cdd:cd07244     2 INHITLAVSDLERSLAFYVDLLGF 25

C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.

                          10        20
                  ....*....|....*....|....
gi 1933716685   7 HLTLAVSNLQTSLTFWRDLLGLHV 30
Cdd:cd16357     1 KVSLAVSDLEKSIDYWSDLLGMKV 24

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20
                  ....*....|....*....|....*..
gi 1933716685   4 SLNHLTLAVSNLQTSLTFWRDLLGLHV 30
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKL 27

fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin resistant protein. FosB is a Mg(2+)-dependent L-cysteine thiol transferase. Fosfomycin inhibits the enzyme UDP-nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosB catalyzes the Mg(II) dependent addition of L-cysteine to the epoxide ring of fosfomycin, (1R,2S)-epoxypropylphosphonic acid, rendering it inactive. FosB is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.

                          10        20
                  ....*....|....*....|...
gi 1933716685   5 LNHLTLAVSNLQTSLTFWRDLLG 27
Cdd:cd08363     1 INHITFSVSNLNKSIAFYKDVLD 23

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.

                          10        20
                  ....*....|....*....|....*...
gi 1933716685   5 LNHLTLAVSNLQTSLTFWRDLLGLHVGD 32
Cdd:cd07245     1 LDHVALACPDLERARRFYTDVLGLEEVP 28

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1933716685   1 MLQSLNHLTLAVS--NLQTSLTFWRDLLGLHV 30
Cdd:COG3185   143 GLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEE 174