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 1852544737   6 LDHVQLAMPagREDEARSFYGGLLGFAEQAKPANLaARGGCWFSRGSI-KLHLGVEQDF-------RPAKKAHPAFLVDD 77
Cdd:cd07245     1 LDHVALACP--DLERARRFYTDVLGLEEVPRPPFL-KFGGAWLYLGGGqQIHLVVEQNPselprpeHPGRDRHPSFSVPD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1852544737  78 MATLRKTLETAGCHVVEDE-PLEGYHRFYVHDPFGNRIEM 116
Cdd:cd07245    78 LDALKQRLKEAGIPYTESTsPGGGVTQLFFRDPDGNRLEF 117

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        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852544737   6 LDHVQLAMPagREDEARSFYGGLLGFAEQAKPANLaARGGCWFSRGSI-KLHLGVEQDF-------RPAKKAHPAFLVDD 77
Cdd:cd07245     1 LDHVALACP--DLERARRFYTDVLGLEEVPRPPFL-KFGGAWLYLGGGqQIHLVVEQNPselprpeHPGRDRHPSFSVPD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1852544737  78 MATLRKTLETAGCHVVEDE-PLEGYHRFYVHDPFGNRIEM 116
Cdd:cd07245    78 LDALKQRLKEAGIPYTESTsPGGGVTQLFFRDPDGNRLEF 117

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852544737   6 LDHVqlAMPAGREDEARSFYGGLLGF--AEQAKPANLAARGGCWFSRGSIKLHL----GVEQDFRPAKKAHPAFLVDDMA 79
Cdd:pfam00903   2 IDHV--ALRVGDLEKSLDFYTDVLGFklVEETDAGEEGGLRSAFFLAGGRVLELllneTPPPAAAGFGGHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1852544737  80 TLRKT---LETAGCHVVEDEPLEGYHR--FYVHDPFGNRIEM 116
Cdd:pfam00903  80 DVDAAydrLKAAGVEIVREPGRHGWGGrySYFRDPDGNLIEL 121

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        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852544737   6 LDHVQLAMPagREDEARSFYGGLLGFAEQAKPANLaARGGCWFSRGSI-KLHLGVEQDF-------RPAKKAHPAFLVDD 77
Cdd:cd07245     1 LDHVALACP--DLERARRFYTDVLGLEEVPRPPFL-KFGGAWLYLGGGqQIHLVVEQNPselprpeHPGRDRHPSFSVPD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1852544737  78 MATLRKTLETAGCHVVEDE-PLEGYHRFYVHDPFGNRIEM 116
Cdd:cd07245    78 LDALKQRLKEAGIPYTESTsPGGGVTQLFFRDPDGNRLEF 117

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852544737  19 DEARSFYGGLLGFaEQAKPANLAARGGCWFSRGSIKLHLGVEQDFRPAKKAHPAFLVDDMATLRKTLETAGCHVV---ED 95
Cdd:COG3324    16 ERAKAFYEEVFGW-TFEDDAGPGGDYAEFDTDGGQVGGLMPGAEEPGGPGWLLYFAVDDLDAAVARVEAAGGTVLrppTD 94

                          90       100
                  ....*....|....*....|....*.
gi 1852544737  96 EPLEGYhRFYVHDPFGNRIEMMQPLE 121
Cdd:COG3324    95 IPPWGR-FAVFRDPEGNRFGLWQPAA 119

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 1852544737  19 DEARSFYGGLLGFAEQAKPANlaaRGGCWFSRGS-IKLHLGVEQDFRPAKKA---HPAFLVDDMATLRKTLETAGCHVVE 94
Cdd:cd06587    10 DASVAFYEEVLGFEVVSRNEG---GGFAFLRLGPgLRLALLEGPEPERPGGGglfHLAFEVDDVDEVDERLREAGAEGEL 86

                          90       100
                  ....*....|....*....|....*
gi 1852544737  95 DEPLE----GYHRFYVHDPFGNRIE 115
Cdd:cd06587    87 VAPPVddpwGGRSFYFRDPDGNLIE 111

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. As for the larger superfamily, this family contains members with or without domain swapping.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852544737  13 MPAGREDEARSFYGGLLGFAEQAKPANlaaRGGCWFSRGSIKLHLGVEQDFRPAKKAHPAFL-VDDMATLRKTLETAGC- 90
Cdd:cd08349     4 LPVRDIDKTLAFYVDVLGFEVDYERPP---PGYAILSRGGVELHLFEHPGLDPAGSGVAAYIrVEDIDALHAELKAAGLp 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1852544737  91 -------HVVEDEPLeGYHRFYVHDPFGNRI 114
Cdd:cd08349    81 lfgipriTPIEDKPW-GMREFAVVDPDGNLL 110

vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; This subfamily of vicinal oxygen chelate (VOC) family protein includes Streptomyces hygroscopicus ValD protein and similar proteins. ValD protein functions in validamycin biosynthetic pathway. 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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1852544737  70 HPAFLVDDMATLRKTLETAGCHVV-------EDEPLEGYHRFYVHDPFGNRIEMMQ 118
Cdd:cd16361    93 HFALQVDDVEAAAERLAAAGGKVLmgpreipDGGPGKGNRMVYLRDPWGTLIELVS 148

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 1852544737  22 RSFYGGLLGFA---EQAKPANLAARGGcwfsRGSIKLHLGVEQDFRPAKKA---HPAFLVDDmatlRKTLETAGCHVVED 95
Cdd:cd07255    17 SAFYQNVIGLSvlkQNASRAYLGVDGK----QVLLVLEAIPDAVLAPRSTTglyHFAILLPD----RKALGRALAHLAEH 88

                          90       100
                  ....*....|....*....|....*..
gi 1852544737  96 EPLEGY--H----RFYVHDPFGNRIEM 116
Cdd:cd07255    89 GPLIGAadHgvseAIYLSDPEGNGIEI 115

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

                          10        20        30
                  ....*....|....*....|....*....|....
gi 1852544737   1 MAILALDHVQLAMPAGREDEARSFYGGLLGFAEQ 34
Cdd:COG3185   142 AGLTRIDHIGIAVPRGDLDEWVLFYEDVLGFEEI 175

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 1852544737  19 DEARSFYGGLLGFAEQAkPANLAARGGCWFSRGSIKLHLGVEQ--DFRPAK-KAHPAFLVDDMATLRKTLETAGCHVVED 95
Cdd:pfam18029  10 AALAAFWSAALGWEVVP-DDTALPDPDGGGPIGGGGPRLLFQRvpEPKPGKnRVHLDLAVDDLEAAVARLVALGATVLDD 88

                          90
                  ....*....|....*...
gi 1852544737  96 EPLEGYHRFYVHDPFGNR 113
Cdd:pfam18029  89 GDDPDGGRWVLADPEGNE 106