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 297840067  15 DVPKAARFYEKGLDFSVN--VVTLRWAELHSGPLKLALMqCPSEHMPSEKGYSS----LLSFTVTDINTTISKLMELGAE 88
Cdd:cd07264   10 DFAASLRFYRDVLGLPPRflHEEGEYAEFDTGETKLALF-SRKEMARSGGPDRRgsafELGFEVDDVEATVEELVERGAE 88

                         90       100       110
                 ....*....|....*....|....*....|
gi 297840067  89 LDGSIKYEVHG-KVASVRCLDGHVLGLYEP 117
Cdd:cd07264   89 FVREPANKPWGqTVAYVRDPDGNLIEICEP 118

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 297840067  15 DVPKAARFYEKGLDFSVN--VVTLRWAELHSGPLKLALMqCPSEHMPSEKGYSS----LLSFTVTDINTTISKLMELGAE 88
Cdd:cd07264   10 DFAASLRFYRDVLGLPPRflHEEGEYAEFDTGETKLALF-SRKEMARSGGPDRRgsafELGFEVDDVEATVEELVERGAE 88

                         90       100       110
                 ....*....|....*....|....*....|
gi 297840067  89 LDGSIKYEVHG-KVASVRCLDGHVLGLYEP 117
Cdd:cd07264   89 FVREPANKPWGqTVAYVRDPDGNLIEICEP 118

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 297840067  14 RDVPKAARFYEKGLDFSV--NVVTLRWAELHSGP-LKLALMQcPSEHMPSEKGYSSLLSFTVTDINTTISKLMELGAELD 90
Cdd:cd06587    7 PDLDASVAFYEEVLGFEVvsRNEGGGFAFLRLGPgLRLALLE-GPEPERPGGGGLFHLAFEVDDVDEVDERLREAGAEGE 85

                         90       100
                 ....*....|....*....|....*
gi 297840067  91 GSIKYEV-HGKVASVRCLD--GHVL 112
Cdd:cd06587   86 LVAPPVDdPWGGRSFYFRDpdGNLI 110

N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297840067  14 RDVPKAARFYEKGLDFSVNVVTLRWAE----LHSGPLKLALMQCPSEHMPSEKGYssLLSFTVTDINTTISKLMELGAE- 88
Cdd:cd07247    9 TDLERAKAFYGAVFGWTFEDEGDGGGDyalfTAGGGAVGGLMRAPEEVAGAPPGW--LIYFAVDDLDAALARVEAAGGKv 86

                         90       100
                 ....*....|....*....|....*...
gi 297840067  89 LDGSIKYEVHGKVASVRCLDGHVLGLYE 116
Cdd:cd07247   87 VVPPTDIPGGGRFAVFADPEGNRFGLWS 114