Glyoxalase-like domain; This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764347   10 QITFDCHDPSKLAKFWSAATGCEIAADY-------GDFVMVDSTPALGFQRVEEPTPGKNRMHVDVGGAERETLIERLKD 82
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDDtalpdpdGGGPIGGGGPRLLFQRVPEPKPGKNRVHLDLAVDDLEAAVARLVA 80

                          90       100
                  ....*....|....*....|....*....
gi 552764347   83 LGATELTTHEAPGLVWTVMQDPEGNEFCV 111
Cdd:pfam18029  81 LGATVLDDGDDPDGGRWVLADPEGNEFCL 109

Glyoxalase-like domain; This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764347   10 QITFDCHDPSKLAKFWSAATGCEIAADY-------GDFVMVDSTPALGFQRVEEPTPGKNRMHVDVGGAERETLIERLKD 82
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDDtalpdpdGGGPIGGGGPRLLFQRVPEPKPGKNRVHLDLAVDDLEAAVARLVA 80

                          90       100
                  ....*....|....*....|....*....
gi 552764347   83 LGATELTTHEAPGLVWTVMQDPEGNEFCV 111
Cdd:pfam18029  81 LGATVLDDGDDPDGGRWVLADPEGNEFCL 109

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 552764347  11 ITFDCHDPSKLAKFWSAATGCEIA--ADYGDFVMVDSTPALGFQRVEEPTP------GKNRMHVDVGGAERetLIERLKD 82
Cdd:cd06587    2 VALRVPDLDASVAFYEEVLGFEVVsrNEGGGFAFLRLGPGLRLALLEGPEPerpgggGLFHLAFEVDDVDE--VDERLRE 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 552764347  83 LGATELTTHEAPGLVWTV----MQDPEGNEFCV 111
Cdd:cd06587   80 AGAEGELVAPPVDDPWGGrsfyFRDPDGNLIEF 112

Glyoxalase-like domain; This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552764347   10 QITFDCHDPSKLAKFWSAATGCEIAADY-------GDFVMVDSTPALGFQRVEEPTPGKNRMHVDVGGAERETLIERLKD 82
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDDtalpdpdGGGPIGGGGPRLLFQRVPEPKPGKNRVHLDLAVDDLEAAVARLVA 80

                          90       100
                  ....*....|....*....|....*....
gi 552764347   83 LGATELTTHEAPGLVWTVMQDPEGNEFCV 111
Cdd:pfam18029  81 LGATVLDDGDDPDGGRWVLADPEGNEFCL 109

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 552764347  11 ITFDCHDPSKLAKFWSAATGCEIA--ADYGDFVMVDSTPALGFQRVEEPTP------GKNRMHVDVGGAERetLIERLKD 82
Cdd:cd06587    2 VALRVPDLDASVAFYEEVLGFEVVsrNEGGGFAFLRLGPGLRLALLEGPEPerpgggGLFHLAFEVDDVDE--VDERLRE 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 552764347  83 LGATELTTHEAPGLVWTV----MQDPEGNEFCV 111
Cdd:cd06587   80 AGAEGELVAPPVDDPWGGrsfyFRDPDGNLIEF 112