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 1400899763  15 VIPRLVCRDPTAAIDFCARTFDAVELNRRPGPDGKVAHALMTIGPAMIMIEAEWPTLPSRAPTPDGSSPVVIFVYVEDAD 94
Cdd:cd07246     3 VSPYLVVEDAAAAIAFYKKAFGAEELGRTTQEDGRVGHAELRIGGTVVMVADENPERGALSPTKLGGTPVIFHLYVEDVD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1400899763  95 KTVERAIANGAQVLVPLQNQFWGDRIAWIMDPSGHVWTVATR 136
Cdd:cd07246    83 ATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 124

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 1400899763  15 VIPRLVCRDPTAAIDFCARTFDAVELNRRPGPDGKVAHALMTIGPAMIMIEAEWPTLPSRAPTPDGSSPVVIFVYVEDAD 94
Cdd:cd07246     3 VSPYLVVEDAAAAIAFYKKAFGAEELGRTTQEDGRVGHAELRIGGTVVMVADENPERGALSPTKLGGTPVIFHLYVEDVD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1400899763  95 KTVERAIANGAQVLVPLQNQFWGDRIAWIMDPSGHVWTVATR 136
Cdd:cd07246    83 ATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 124

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400899763  19 LVCRDPTAAIDFCARTFDAVELNRRP-GPDGKVAHALMTIGPAMIMIEAEWPTLPSRAPtPDGSSPVVIFVYVEDADKTV 97
Cdd:pfam00903   7 LRVGDLEKSLDFYTDVLGFKLVEETDaGEEGGLRSAFFLAGGRVLELLLNETPPPAAAG-FGGHHIAFIAFSVDDVDAAY 85

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1400899763  98 ERAIANGAQVLVPLQNQFWGDRIAWIMDPSGHVW 131
Cdd:pfam00903  86 DRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLI 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 1400899763  15 VIPRLVCRDPTAAIDFCARTFDAVELNRRPGPDGKVAHALMTIGPAMIMIEAEWPTLPSRAPTPDGSSPVVIFVYVEDAD 94
Cdd:cd07246     3 VSPYLVVEDAAAAIAFYKKAFGAEELGRTTQEDGRVGHAELRIGGTVVMVADENPERGALSPTKLGGTPVIFHLYVEDVD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1400899763  95 KTVERAIANGAQVLVPLQNQFWGDRIAWIMDPSGHVWTVATR 136
Cdd:cd07246    83 ATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 124

Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of the thiocoraline biosynthetic gene cluster. Thiocoraline is a thiodepsipeptide with potent antitumor activity. TioX may be involved in thiocoraline resistance or secretion. TioX belongs to vicinal oxygen chelate (VOC) superfamily that 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 1400899763  15 VIPRLVCRDPTAAIDFCARTFDAVELNRRPGPDGKVAHALMTIGPAMIMIEAEwpTLPSRAPTPDGSSPVV---IFVYVE 91
Cdd:cd08355     1 VVPTLRYRDAVAAIDWLVEAFGFEERMVVPGDEGTIHHAELTFGGGGVMVGSV--RDEARPDRPADAGGHGtqsVYVAVA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1400899763  92 DADKTVERAIANGAQVLVPLQNQFWGDRIAWIMDPSGHVWTVAT 135
Cdd:cd08355    79 DPDAHYERARAAGAEIVMEPTDTDYGSRDYSARDPEGHLWSFGT 122

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 1400899763  19 LVCRDPTAAIDFCARTFDAVELNRRPGPDGKVAHALMTIGPAMIMIEAEWPtlpSRAPTPDGSSPVVIFVYVEDADKTVE 98
Cdd:COG0346     8 LRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAP---GAAPAPGGGGLHHLAFRVDDLDAAYA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1400899763  99 RAIANGAQVLVPLQNQFWGDRIAWIMDPSGHVWTVATRIEE 139
Cdd:COG0346    85 RLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPPG 125

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 1400899763  19 LVCRDPTAAIDFCARTFDAvelNRRPGPDGKVAHALMTIGPAMIMieaewPTLPSRAPTPDGSSPVVIFVYVEDADKTVE 98
Cdd:cd07247     6 LPTTDLERAKAFYGAVFGW---TFEDEGDGGGDYALFTAGGGAVG-----GLMRAPEEVAGAPPGWLIYFAVDDLDAALA 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1400899763  99 RAIANGAQVLVPLQNQFWGDRIAWIMDPSGHVWTV 133
Cdd:cd07247    78 RVEAAGGKVVVPPTDIPGGGRFAVFADPEGNRFGL 112

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 1400899763  19 LVCRDPTAAIDFCARTFDAVELNRRPGPDgkvaHALMTIGPAmIMIEaewPTLPSRAPTPDGSSPVVIFVYVEDADKTVE 98
Cdd:cd06587     4 LRVPDLDASVAFYEEVLGFEVVSRNEGGG----FAFLRLGPG-LRLA---LLEGPEPERPGGGGLFHLAFEVDDVDEVDE 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1400899763  99 RAIANGAQVLV--PLQNQFWGDRIAWIMDPSGHVWTV 133
Cdd:cd06587    76 RLREAGAEGELvaPPVDDPWGGRSFYFRDPDGNLIEF 112

Escherichia coli PhnB and similar proteins; The Escherichia coli phnB gene is found next to an operon of fourteen genes (phnC-to-phnP) related to the cleavage of carbon-phosphorus (C-P) bonds in unactivated alkylphosphonates, supporting bacterial growth on alkylphosphonates as the sole phosphorus source. It was originally considered part of that operon. PhnB appears to play no direct catalytic role in the usage of alkylphosphonate. Although many of the proteins in this family have been annotated as 3-demethylubiquinone-9 3-methyltransferase enzymes by automatic annotation programs, the experimental evidence for this assignment is lacking. In Escherichia coli, the gene coding 3-demethylubiquinone-9 3-methyltransferase enzyme is ubiG, which belongs to the AdoMet-MTase protein family. PhnB-like proteins adopt a structural fold similar to bleomycin resistance proteins, glyoxalase I, and type I extradiol dioxygenases.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1400899763  27 AIDFCARTFDAVELNRR-----------PGPDGKVAHALMTI-GPAMIMIEAewptLPSRAPTPD-GSSPVVIFVYVEDA 93
Cdd:cd06588    14 ALEFYAEVFPGGEILSLtrygegppdfpEGDEGKVMHAEFTLgGQTLMASDD----GPGFPFTFGnAISLSVDCDSQEEA 89

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1400899763  94 DKTVERAIANGaQVLVPLQNQFWGDRIAWIMDPSGHVW 131
Cdd:cd06588    90 DRLFEKLSEGG-EVLMPLQETFWGARYGWVKDKFGVSW 126

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 1400899763  16 IPRLVCRDPTAAIDFCART--FDAVelNRRPGPDgkvaHALMTIGPAMIMIEAEwptlPSRAPTPDGSSpvvIFVYVEDA 93
Cdd:cd08349     1 IPILPVRDIDKTLAFYVDVlgFEVD--YERPPPG----YAILSRGGVELHLFEH----PGLDPAGSGVA---AYIRVEDI 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1400899763  94 DKTVERAIANG-----AQVLVPLQNQFWGDRIAWIMDPSGH 129
Cdd:cd08349    68 DALHAELKAAGlplfgIPRITPIEDKPWGMREFAVVDPDGN 108

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1400899763  91 EDADKTVERAIANGAQVLVPLQNQFWGdRIAWIMDPSGHVWTVA 134
Cdd:COG3607    83 EEVDALVAKALAAGGTVLKPPQDVGGM-YSGYFADPDGHLWEVA 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 1400899763  19 LVCRDPTAAIDFCARTFDAVELNRRPGPDGKVahalMTIGP------AMIMIEAEWPTLPSRAPTPDGSSPVVIFvYVED 92
Cdd:cd07263     4 LYVDDQDKALDFYVEKLGFEVVEDVPMGGMRW----VTVAPpgspgtSLLLEPKAHPAQMPQSPEAAGGTPGILL-ATDD 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1400899763  93 ADKTVERAIANGAQVLVPLQNQFWGdRIAWIMDPSGHVW 131
Cdd:cd07263    79 IDATYERLTAAGVTFVQEPTQMGGG-RVANFRDPDGNLF 116