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        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117249   11 IPVLKINNRKNNLAFYCQTLGMKNLLEEGAFVSLGDQ-TKVEKLQLEESPSMRTRKVVGTKKLAKIVIKVADSREIEALL 89
Cdd:pfam14506   2 IPVLRVNNRKLNIDFYQETLGFKLLSEENALAVFGDWqTGLSLFVIEESPSYRTRAVEGTKKLAKIIVKVSNPLEIEGLL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 489117249   90 ARGSKVDYLYQGDNGYAFEATSPEGDTFLLHSEEDWTTLQRV 131
Cdd:pfam14506  82 ANGDQAHRVYKGQNGYAFETISPEDDLILIHAEDDLSTLVEV 123

CppA N-terminal; This is the N-terminal domain of the CppA protein found in species of Streptococcus. CppA is a putative C3-glycoprotein degrading proteinase, involved in pathogenicity. It is often found associated with pfam14507.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117249   11 IPVLKINNRKNNLAFYCQTLGMKNLLEEGAFVSLGDQ-TKVEKLQLEESPSMRTRKVVGTKKLAKIVIKVADSREIEALL 89
Cdd:pfam14506   2 IPVLRVNNRKLNIDFYQETLGFKLLSEENALAVFGDWqTGLSLFVIEESPSYRTRAVEGTKKLAKIIVKVSNPLEIEGLL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 489117249   90 ARGSKVDYLYQGDNGYAFEATSPEGDTFLLHSEEDWTTLQRV 131
Cdd:pfam14506  82 ANGDQAHRVYKGQNGYAFETISPEDDLILIHAEDDLSTLVEV 123

N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. 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        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117249  14 LKINNRKNNLAFYCQTLGMKNLLEEGAFVSLGDQTKVEKLQLEESPSMRtRKVVGTKKLAKIVIKVADSREIEALLARGS 93
Cdd:cd07255    8 LKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAV-LAPRSTTGLYHFAILLPDRKALGRALAHLA 86

                         90       100
                 ....*....|....*....|....
gi 489117249  94 KVDYLY-QGDNGY--AFEATSPEG 114
Cdd:cd07255   87 EHGPLIgAADHGVseAIYLSDPEG 110

CppA N-terminal; This is the N-terminal domain of the CppA protein found in species of Streptococcus. CppA is a putative C3-glycoprotein degrading proteinase, involved in pathogenicity. It is often found associated with pfam14507.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117249   11 IPVLKINNRKNNLAFYCQTLGMKNLLEEGAFVSLGDQ-TKVEKLQLEESPSMRTRKVVGTKKLAKIVIKVADSREIEALL 89
Cdd:pfam14506   2 IPVLRVNNRKLNIDFYQETLGFKLLSEENALAVFGDWqTGLSLFVIEESPSYRTRAVEGTKKLAKIIVKVSNPLEIEGLL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 489117249   90 ARGSKVDYLYQGDNGYAFEATSPEGDTFLLHSEEDWTTLQRV 131
Cdd:pfam14506  82 ANGDQAHRVYKGQNGYAFETISPEDDLILIHAEDDLSTLVEV 123

N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. 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        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489117249  14 LKINNRKNNLAFYCQTLGMKNLLEEGAFVSLGDQTKVEKLQLEESPSMRtRKVVGTKKLAKIVIKVADSREIEALLARGS 93
Cdd:cd07255    8 LKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAV-LAPRSTTGLYHFAILLPDRKALGRALAHLA 86

                         90       100
                 ....*....|....*....|....
gi 489117249  94 KVDYLY-QGDNGY--AFEATSPEG 114
Cdd:cd07255   87 EHGPLIgAADHGVseAIYLSDPEG 110