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 489497996   6 SRMLLRPADYQRSLSFYRDQIGLAIAREYGAGTV--FFAGQSLLELAGYGEPDHSRGP----FPGALWLQVRDLEATQTE 79
Cdd:cd07264    2 AYIVLYVDDFAASLRFYRDVLGLPPRFLHEEGEYaeFDTGETKLALFSRKEMARSGGPdrrgSAFELGFEVDDVEATVEE 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489497996  80 LVSRGVSIAREPRREPWGLHEMHVTDPDGITLIFVE 115
Cdd:cd07264   82 LVERGAEFVREPANKPWGQTVAYVRDPDGNLIEICE 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 489497996   6 SRMLLRPADYQRSLSFYRDQIGLAIAREYGAGTV--FFAGQSLLELAGYGEPDHSRGP----FPGALWLQVRDLEATQTE 79
Cdd:cd07264    2 AYIVLYVDDFAASLRFYRDVLGLPPRFLHEEGEYaeFDTGETKLALFSRKEMARSGGPdrrgSAFELGFEVDDVEATVEE 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489497996  80 LVSRGVSIAREPRREPWGLHEMHVTDPDGITLIFVE 115
Cdd:cd07264   82 LVERGAEFVREPANKPWGQTVAYVRDPDGNLIEICE 117

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 489497996  13 ADYQRSLSFYRDQIGLAIAREY-----GAGTVFFA--GQSLLELAGY--GEPDHSRGPFpGALWLQVRDLEATQTELVSR 83
Cdd:COG0346   11 SDLEASLAFYTDVLGLELVKRTdfgdgGFGHAFLRlgDGTELELFEApgAAPAPGGGGL-HHLAFRVDDLDAAYARLRAA 89

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489497996  84 GVSIAREPRREPWGLHEMHVTDPDGITLIFVEVPEG 119
Cdd:COG0346   90 GVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPPG 125

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 489497996   6 SRMLLRPADYQRSLSFYRDQIGLAIAREYGAGTV--FFAGQSLLELAGYGEPDHSRGP----FPGALWLQVRDLEATQTE 79
Cdd:cd07264    2 AYIVLYVDDFAASLRFYRDVLGLPPRFLHEEGEYaeFDTGETKLALFSRKEMARSGGPdrrgSAFELGFEVDDVEATVEE 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489497996  80 LVSRGVSIAREPRREPWGLHEMHVTDPDGITLIFVE 115
Cdd:cd07264   82 LVERGAEFVREPANKPWGQTVAYVRDPDGNLIEICE 117

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 489497996  13 ADYQRSLSFYRDQIGLAIAREY-----GAGTVFFA--GQSLLELAGY--GEPDHSRGPFpGALWLQVRDLEATQTELVSR 83
Cdd:COG0346   11 SDLEASLAFYTDVLGLELVKRTdfgdgGFGHAFLRlgDGTELELFEApgAAPAPGGGGL-HHLAFRVDDLDAAYARLRAA 89

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489497996  84 GVSIAREPRREPWGLHEMHVTDPDGITLIFVEVPEG 119
Cdd:COG0346   90 GVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPPG 125

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 489497996  10 LRPADYQRSLSFYRDQIGLAIAREYGAGTVFFAGQSLLELAGYGEPDHSRGPFPGALWLQVRDLEATQTELVSRGVSIAR 89
Cdd:cd08349    4 LPVRDIDKTLAFYVDVLGFEVDYERPPPGYAILSRGGVELHLFEHPGLDPAGSGVAAYIRVEDIDALHAELKAAGLPLFG 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489497996  90 EPRR-----EPWGLHEMHVTDPDGITLIFVE 115
Cdd:cd08349   84 IPRItpiedKPWGMREFAVVDPDGNLLRFGQ 114

uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; 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 489497996  14 DYQRSLSFYRDQIGLAIAREYGAGTVFFA-----GQSLLELAGyGEPDHSRGPFPGAL-----WLQV--RDLEATQTELV 81
Cdd:cd16355    9 DIPASFAWFEKVLGFQKDWDWGDPPTFGSvgsgeCEIFLCQGG-QGGSLRLGPCGDALpsygaWMSVwvDDVDALHRECR 87

                         90       100
                 ....*....|....*....|....*..
gi 489497996  82 SRGVSIAREPRREPWGLHEMHVTDPDG 108
Cdd:cd16355   88 ARGADIRQPPTDMPWGMREMHVRHPDG 114

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 489497996  13 ADYQRSLSFYRDQIGLAIAREYGAGTVFF---AGQSLLELAGYGEPDHSRGPFPGALWLQVRDLEATQTELVSRGV--SI 87
Cdd:cd06587    7 PDLDASVAFYEEVLGFEVVSRNEGGGFAFlrlGPGLRLALLEGPEPERPGGGGLFHLAFEVDDVDEVDERLREAGAegEL 86

                         90       100
                 ....*....|....*....|....*.
gi 489497996  88 AREPRREPWGLHEMHVTDPDGITLIF 113
Cdd:cd06587   87 VAPPVDDPWGGRSFYFRDPDGNLIEF 112

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Vibrio cholerae VCA0619 and similar proteins. The 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 489497996  12 PA-DYQRSLSFYRDqIGLAIAREYGAGTVFFAGQSLLELAGYGEPDHSRGpfpGALWLQVRDLEATQTELVSRGVS---- 86
Cdd:cd08356    8 PAkDFELSKAFYQA-LGFELASEEGGVAYFRLGDCSFLLQDFYEKEHAEN---FMMHLLVEDVDAWHQHVKTLGLAeryg 83

                         90       100
                 ....*....|....*....|....
gi 489497996  87 -IAREPRREPWGLHEMHVTDPDGI 109
Cdd:cd08356   84 vKVTDPTDQPWGMRDFVLTDPSGV 107

vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Bacillus subtilis YwkD and similar proteins. 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 489497996  14 DYQRSLSFYRDQIGLAIAREY---GAGTVFF---AGQSLLELAGYGEPDhSRGPFPGALWL-----QVRDLEATQTELVS 82
Cdd:cd08352   12 DYEKSKDFYVDKLGFEIIREHyrpERNDIKLdlaLGGYQLELFIKPDAP-ARPSYPEALGLrhlafKVEDVEATVAELKS 90

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489497996  83 RGvsIAREPRR--EPWGLHEMHVTDPDGITLIFVE 115
Cdd:cd08352   91 LG--IETEPIRvdDFTGKKFTFFFDPDGLPLELYE 123

Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497996   9 LLRPADYQRSLSFYRDQIGLAIAR--EYGAG--TVFFAG------QSLLELA-GYGEPDHSRGPFPGALWLQVRDLEATQ 77
Cdd:cd16358    5 MLRVGDLDRSIKFYTEVLGMKLLRkrDYPEGkyTLAFVGygdedeNTVLELTyNWGVDKYDLGTAYGHIAIGVEDVYETC 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489497996  78 TELVSRGVSIAREPRREPWGLHEM-HVTDPDG--ITLI 112
Cdd:cd16358   85 ERIRKKGGKVTREPGPMKGGTTVIaFVEDPDGykIELI 122

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489497996  54 EPDHSRGPF-----PGALW--LQVRDLEATQTELVSRGVSIAREPRREPWGLHEMHVTDPDGiTLIFV 114
Cdd:cd08359   51 DGQHGAVPAasqtqSSGLIinFEVDDADAEYERLTQAGLEFLEPPRDEPWGQRRFIVRDPNG-VLIDV 117