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 2050364036  13 HSLTPHLICDGAAAAIEFYKKAFDAVEISRLPSRDaGRLMHAAVRIGDSTLMLVDEMGQCGALSPKALKGSPVFIHLYVP 92
Cdd:cd07246     1 TTVSPYLVVEDAAAAIAFYKKAFGAEELGRTTQED-GRVGHAELRIGGTVVMVADENPERGALSPTKLGGTPVIFHLYVE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2050364036  93 DVDAVIARAVEAGAKLTMPPADMFWGDRYGQLEDPFGHRWSVATH 137
Cdd:cd07246    80 DVDATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 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 2050364036  13 HSLTPHLICDGAAAAIEFYKKAFDAVEISRLPSRDaGRLMHAAVRIGDSTLMLVDEMGQCGALSPKALKGSPVFIHLYVP 92
Cdd:cd07246     1 TTVSPYLVVEDAAAAIAFYKKAFGAEELGRTTQED-GRVGHAELRIGGTVVMVADENPERGALSPTKLGGTPVIFHLYVE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2050364036  93 DVDAVIARAVEAGAKLTMPPADMFWGDRYGQLEDPFGHRWSVATH 137
Cdd:cd07246    80 DVDATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 124

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050364036  19 LICDGAAAAIEFYKKAFDAVEISRLPSRDAGRLMHAAVRIGDSTLMLVDEMGqcgALSPKALKGSPVFIHLY--VPDVDA 96
Cdd:pfam00903   7 LRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNET---PPPAAAGFGGHHIAFIAfsVDDVDA 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2050364036  97 VIARAVEAGAKLTMPPADMFWGDRYGQLEDPFGHRW 132
Cdd:pfam00903  84 AYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLI 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 2050364036  13 HSLTPHLICDGAAAAIEFYKKAFDAVEISRLPSRDaGRLMHAAVRIGDSTLMLVDEMGQCGALSPKALKGSPVFIHLYVP 92
Cdd:cd07246     1 TTVSPYLVVEDAAAAIAFYKKAFGAEELGRTTQED-GRVGHAELRIGGTVVMVADENPERGALSPTKLGGTPVIFHLYVE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2050364036  93 DVDAVIARAVEAGAKLTMPPADMFWGDRYGQLEDPFGHRWSVATH 137
Cdd:cd07246    80 DVDATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLATP 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 2050364036  15 LTPHLICDGAAAAIEFYKKAFDAVEISRLPsRDAGRLMHAAVRIGDSTLMLVDEMGQCGALSPKALKGS-PVFIHLYVPD 93
Cdd:cd08355     1 VVPTLRYRDAVAAIDWLVEAFGFEERMVVP-GDEGTIHHAELTFGGGGVMVGSVRDEARPDRPADAGGHgTQSVYVAVAD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2050364036  94 VDAVIARAVEAGAKLTMPPADMFWGDRYGQLEDPFGHRWSVATH 137
Cdd:cd08355    80 PDAHYERARAAGAEIVMEPTDTDYGSRDYSARDPEGHLWSFGTY 123

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 2050364036  19 LICDGAAAAIEFYKKAFDAVEISRLPSRDaGRLMHAAVRIGDSTLMlvdEMGQCGALSPKALKGSPVFIHLYVPDVDAVI 98
Cdd:COG0346     8 LRVSDLEASLAFYTDVLGLELVKRTDFGD-GGFGHAFLRLGDGTEL---ELFEAPGAAPAPGGGGLHHLAFRVDDLDAAY 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2050364036  99 ARAVEAGAKLTMPPADMFWGDRYGQLEDPFGHRWSVATHRQD 140
Cdd:COG0346    84 ARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPPG 125

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050364036  25 AAAIEFYKKAFDAVeisrlPSRDAGRLMHAAvrigdstlMLVDEMGQCGALSPKALKGSPVFIHLY--VPDVDAVIARAV 102
Cdd:COG3324    16 ERAKAFYEEVFGWT-----FEDDAGPGGDYA--------EFDTDGGQVGGLMPGAEEPGGPGWLLYfaVDDLDAAVARVE 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2050364036 103 EAGAKLTMPPADMFWGDRYGQLEDPFGHRWSVATHRQ 139
Cdd:COG3324    83 AAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGLWQPAA 119

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 2050364036  19 LICDGAAAAIEFYKKAFDaVEISRLPSRDAGrlmHAAVRIGDSTLMLVDEMGQCGALSPkalkgSPVFIHLYVPDVDAVI 98
Cdd:cd07247     6 LPTTDLERAKAFYGAVFG-WTFEDEGDGGGD---YALFTAGGGAVGGLMRAPEEVAGAP-----PGWLIYFAVDDLDAAL 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2050364036  99 ARAVEAGAKLTMPPADMFWGDRYGQLEDPFGHRWSV 134
Cdd:cd07247    77 ARVEAAGGKVVVPPTDIPGGGRFAVFADPEGNRFGL 112

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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2050364036  77 PKALKGSPVFIHLYVPDVDAVIARAVEAGAKLTMPPADMFWGDRYGQLEDPFGHRWSVA 135
Cdd:cd16355    62 GDALPSYGAWMSVWVDDVDALHRECRARGADIRQPPTDMPWGMREMHVRHPDGHRFRVG 120

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 2050364036  18 HLICDGAAAAIEFYKKAFDAVEISRLPSRDagrlmHAAVRIGD-STLMLVDemgqcGALSPKALKGSPVFIHLYVPDVDA 96
Cdd:cd06587     3 ALRVPDLDASVAFYEEVLGFEVVSRNEGGG-----FAFLRLGPgLRLALLE-----GPEPERPGGGGLFHLAFEVDDVDE 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2050364036  97 VIARAVEAGAK--LTMPPADMFWGDRYGQLEDPFGHRW 132
Cdd:cd06587    73 VDERLREAGAEgeLVAPPVDDPWGGRSFYFRDPDGNLI 110

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 2050364036  19 LICDGAAAAIEFYKKAFDaVEISRL-PSRDAGRLMHAAVRIGdstLMLVDEMGQcgaLSPKALKGSPVFIHLYVPDVDAV 97
Cdd:cd07264     6 LYVDDFAASLRFYRDVLG-LPPRFLhEEGEYAEFDTGETKLA---LFSRKEMAR---SGGPDRRGSAFELGFEVDDVEAT 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2050364036  98 IARAVEAGAKLTMPPADMFWGDRYGQLEDPFGH 130
Cdd:cd07264    79 VEELVERGAEFVREPANKPWGQTVAYVRDPDGN 111

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 2050364036  21 CDGAAAAIEFYKKAFDAVEISRLPSRDAGrlmHAAVRIGDSTLML----VDEmgqcgalsPKALKGsPVFIHLYVPDVDA 96
Cdd:pfam18029   6 CADPAALAAFWSAALGWEVVPDDTALPDP---DGGGPIGGGGPRLlfqrVPE--------PKPGKN-RVHLDLAVDDLEA 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2050364036  97 VIARAVEAGAKLTMPPADMFWGDRYgqLEDPFGHRWSV 134
Cdd:pfam18029  74 AVARLVALGATVLDDGDDPDGGRWV--LADPEGNEFCL 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
                  ....*....|....*....|....*....|....*...
gi 2050364036  93 DVDAVIARAVEAGAKLTMPPADMFWGDRYGQLEDPFGH 130
Cdd:cd07235    80 EVDAKYAELTGAGYEGHLKPWNAPWGQRYAIVKDPDGN 117

Bleomycin N-Acetyltransferase and similar proteins; BlmB, encodes a bleomycin N-acetyltransferase, designated BAT, which inactivates Bm using acetyl-coenzyme A (AcCoA). BAT forms a dimer structure via interaction of its C-terminal domains in the monomers. The N-terminal domain of BAT has a tunnel with two entrances: a wide entrance that accommodates the metal-binding domain of Bm and a narrow entrance that accommodates acetyl-CoA (AcCoA). A groove formed on the dimer interface of two BAT C-terminal domains forms the DNA-binding domain of Bm. In a ternary complex of BAT, BmA(2), and CoA, a thiol group of CoA is positioned near the primary amine of Bm at the midpoint of the tunnel and ensures efficient transfer of an acetyl group from AcCoA to the primary amine of Bm. BAT 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 thiocoraline, 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 2050364036  83 SPVFIHLYV-PDVDAVIARAVEAGAKLTMPPADMFWGDRYGQLEDPFGHRWSVAT 136
Cdd:cd16354    60 APVTLHLDAgVEFDSLHRRALAAGARVDGPPVRQPWGRREFVLRLPEGHRLVVSG 114