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 115285570   4 TIFINLPVADLPRATAFYVALGFEVVPAYTTEQGACIRISDAIFVMLLVRPFFQTFTGKTI-VEPATHVQVLPCLSCDSR 82
Cdd:cd09012    1 MIFINLPVTDLEASTAFYEALGFKKNPQFSDEHASCMVVSDNIFVMLLAHDRFKTFIPEPIaVDAKKSTEVLLTLSAKSR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 115285570  83 AEVDAVVAKARAAGGTVPRQ--AQEYPGMYSHDFADPDGHEWGLVF 126
Cdd:cd09012   81 QEVDAFVDKAVEAGGKADPYvnGGDEGFMYGRSFEDLDGHLWEVVW 126

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 115285570   4 TIFINLPVADLPRATAFYVALGFEVVPAYTTEQGACIRISDAIFVMLLVRPFFQTFTGKTI-VEPATHVQVLPCLSCDSR 82
Cdd:cd09012    1 MIFINLPVTDLEASTAFYEALGFKKNPQFSDEHASCMVVSDNIFVMLLAHDRFKTFIPEPIaVDAKKSTEVLLTLSAKSR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 115285570  83 AEVDAVVAKARAAGGTVPRQ--AQEYPGMYSHDFADPDGHEWGLVF 126
Cdd:cd09012   81 QEVDAFVDKAVEAGGKADPYvnGGDEGFMYGRSFEDLDGHLWEVVW 126

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 115285570   7 INLPVADLPRATAFYV-ALGFEVVPAYTTEQGACIRISDAIFVMLLVRPFFQTFTGKTIvepaTHVqvlpCLSCDSRAEV 85
Cdd:cd06587    2 VALRVPDLDASVAFYEeVLGFEVVSRNEGGGFAFLRLGPGLRLALLEGPEPERPGGGGL----FHL----AFEVDDVDEV 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 115285570  86 DAVVAKARAAGGTVPRQAQEYPGMYSHDFADPDGHEW 122
Cdd:cd06587   74 DERLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLI 110

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115285570   7 INLPVADLPRATAFYV-ALGFEVVPAYTTEQGAC----IRISDAIFVMLLVRPFFQTFTGKTivePATHVqvlpCLSCDs 81
Cdd:COG0346    6 VTLRVSDLEASLAFYTdVLGLELVKRTDFGDGGFghafLRLGDGTELELFEAPGAAPAPGGG---GLHHL----AFRVD- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 115285570  82 raEVDAVVAKARAAGGTVPRQAQEYP-GMYSHDFADPDGHEWGLV 125
Cdd:COG0346   78 --DLDAAYARLRAAGVEIEGEPRDRAyGYRSAYFRDPDGNLIELV 120

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115285570    7 INLPVADLPRATAFYV-ALGFEVV-----PAYTTEQGACIRISDAIFVMLLVRPffqtfTGKTIVEPAT-HVQVLpclsC 79
Cdd:pfam00903   5 VALRVGDLEKSLDFYTdVLGFKLVeetdaGEEGGLRSAFFLAGGRVLELLLNET-----PPPAAAGFGGhHIAFI----A 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 115285570   80 DSRAEVDAVVAKARAAGGTV--PRQAQEYPGMYSHdFADPDGHEW 122
Cdd:pfam00903  76 FSVDDVDAAYDRLKAAGVEIvrEPGRHGWGGRYSY-FRDPDGNLI 119

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 115285570  11 VADLPRATAFYVAL--GFEVVPAYTTEQGACIRISDAIFVMLlvrpfFQTFTGK-TIVEPATHVqvlpCLSCDSRAEVDA 87
Cdd:cd07262    8 VNDLERSRAFYDAAlaPLGYKRGFEDGGRVGYGLEGGPDFWV-----TEPFDGEpATAGNGTHV----AFAAPSRAAVDA 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 115285570  88 VVAKARAAGGT---VPRQAQEYPGMYSHDFA-DPDGH 120
Cdd:cd07262   79 FHAAALAAGGTdngAPGLRPHYHPGYYAAYVrDPDGN 115

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 115285570   3 KTIFINLPVADLPRATAFYV-ALGFEVVPAYTTEQG----ACIRISDAIFVMLLVRPFFQTFTGKTivEPAThvqvlPCL 77
Cdd:cd07246    1 TTVSPYLVVEDAAAAIAFYKkAFGAEELGRTTQEDGrvghAELRIGGTVVMVADENPERGALSPTK--LGGT-----PVI 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 115285570  78 SCDSRAEVDAVVAKARAAGGTV--PRQAQEYPGMYSHdFADPDGHEWGLV 125
Cdd:cd07246   74 FHLYVEDVDATFARAVAAGAVVvePVEDQFWGDRVGK-VKDPFGHVWWLA 122

N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Rhodococcus rhodochrous K37, and similar proteins; 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). The enzyme contains a N-terminal and a C-terminal domain of similar structure fold, resulting from an ancient gene duplication. BphC belongs to the type I extradiol dioxygenase family, which requires a metal in the active site for its catalytic activity. Polychlorinated biphenyl degrading bacteria demonstrate multiplicity of BphCs. Bacterium Rhodococcus rhodochrous K37 has eight genes encoding BphC enzymes. This family includes the N-terminal domain of BphC5-RrK37. The crystal structure of the protein from Novosphingobium aromaticivorans has a Mn(II)in the active site, although most proteins of type I extradiol dioxygenases are activated by Fe(II).

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 115285570  76 CLSCDSRAEVDAVVAKARAAGGTV---PRQAQEYPGMYSHDFADPDG 119
Cdd:cd08362   63 AFAAATRADVDALAARLAAAGVRIlsePGPLDDPGGGYGFRFFDPDG 109

Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, and antitumor agent used in the treatment of cancer. Its antitumor activity is exerted primarily through monofunctional and bifunctional alkylation of DNA. MRD binds to MC and functions as a component of the MC exporting system. MC is bound to MRD by a stacking interaction between a His and a Trp. MRD adopts a structural fold similar to bleomycin resistance protein, glyoxalase I, and extradiol dioxygenases; and it has binding sites at an identical location to binding sites in these evolutionarily related enzymes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115285570   7 INLPVADLPRATAFYVALGFEVV----PAYTTEQG--ACIRIS-DAIFVMLLVRPFFQTFTGKTIVEPAthvqvlpcLSC 79
Cdd:cd07235    4 IAIVVEDMAKSLEFYRKLGFEVPeeadSAPHTEAAlpGGIRLAlDTEETIRSYDPGWQAPTGGGRFAIA--------FLC 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 115285570  80 DSRAEVDAVVAKARAAGGTVPRQAQEYP-GMYSHDFADPDGH 120
Cdd:cd07235   76 PTPAEVDAKYAELTGAGYEGHLKPWNAPwGQRYAIVKDPDGN 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 115285570   9 LPVADLPRATAFYV-ALGFEVVPAytTEQGACIRISDAifvMLLVrpFFQTFTGKTIVEPA-----THVQVLPCLSCDSr 82
Cdd:cd08354    6 LYADDLDAAEAFYEdVLGLKPMLR--SGRHAFFRLGPQ---VLLV--FDPGATSKDVRTGEvpghgASGHGHFAFAVPT- 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 115285570  83 AEVDAVVAKARAAGGTVPRQAQEYPGMYSHDFADPDGH 120
Cdd:cd08354   78 EELAAWEARLEAKGVPIESYTQWPEGGKSLYFRDPAGN 115