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 788198506  19 LTPHLTVKNVADSKHFYTEVFGFQV--RHENlKEGVPVHVEMSYhNELAIMFVPENvANSGTLAPASFTDAkqrTAYQYI 96
Cdd:cd07246    3 VSPYLVVEDAAAAIAFYKKAFGAEElgRTTQ-EDGRVGHAELRI-GGTVVMVADEN-PERGALSPTKLGGT---PVIFHL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 788198506  97 YVNNVDATVKRAQALGATVLQQPYDAPWGDRFTLMVDINGYHWGIAQ 143
Cdd:cd07246   77 YVEDVDATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLAT 123

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 788198506  23 LTVKNVADSKHFYTEVFGFQVRHEnlkegvpVHVEMSYHnelaimFVPENVANSGTLAPASFTDAKQRTAYqYIYVNNVD 102
Cdd:COG3324   10 LPVDDLERAKAFYEEVFGWTFEDD-------AGPGGDYA------EFDTDGGQVGGLMPGAEEPGGPGWLL-YFAVDDLD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 788198506 103 ATVKRAQALGATVLQQPYDAPWGDRFTLMVDINGYHWGIAQ 143
Cdd:COG3324   76 AAVARVEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGLWQ 116

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 788198506  23 LTVKNVADSKHFYTEVFGFQVRHENLKEGvpvhvemSYHnelaiMFVPENVANSGTLAPASFTDAKQRTAYQYIYVNNVD 102
Cdd:cd07247    6 LPTTDLERAKAFYGAVFGWTFEDEGDGGG-------DYA-----LFTAGGGAVGGLMRAPEEVAGAPPGWLIYFAVDDLD 73

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 788198506 103 ATVKRAQALGATVLQQPYDAPWGDRFTLMVDINGYHWGI 141
Cdd:cd07247   74 AALARVEAAGGKVVVPPTDIPGGGRFAVFADPEGNRFGL 112

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 788198506  19 LTPHLTVKNVADSKHFYTEVFGF--QVRHENlKEGVPVHVEMSYHNElAIMFvpeNVANSGTLAPASFTDAKQRTAYQYI 96
Cdd:cd08355    1 VVPTLRYRDAVAAIDWLVEAFGFeeRMVVPG-DEGTIHHAELTFGGG-GVMV---GSVRDEARPDRPADAGGHGTQSVYV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 788198506  97 YVNNVDATVKRAQALGATVLQQPYDAPWGDRFTLMVDINGYHWGIAQT 144
Cdd:cd08355   76 AVADPDAHYERARAAGAEIVMEPTDTDYGSRDYSARDPEGHLWSFGTY 123

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 788198506  16 SRLLTPHLTVKNVADSKHFYTEvFGFQVRHENLKEGVpvhVEMSYHNELAIMFVPE-------NVANSGTLAPASFT--- 85
Cdd:COG3607    2 PRIIFVNLPVADLERSRAFYEA-LGFTFNPQFSDEGA---ACFVLGEGIVLMLLPRekfatftGKPIADATGFTEVLlal 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 788198506  86 DAKQRTAyqyiyvnnVDATVKRAQALGATVLQQPYDAPWGDRFTLmVDINGYHWGIAQ 143
Cdd:COG3607   78 NVESREE--------VDALVAKALAAGGTVLKPPQDVGGMYSGYF-ADPDGHLWEVAW 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 788198506  22 HLTVKNVADSKHFYTEVFGFQVRHENLKEGVpVHVEMSYHNELAIMFVPENVANSGTlapasftdakqRTAYQYIYVNNV 101
Cdd:cd06587    3 ALRVPDLDASVAFYEEVLGFEVVSRNEGGGF-AFLRLGPGLRLALLEGPEPERPGGG-----------GLFHLAFEVDDV 70

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 788198506 102 DATVKRAQALGATVLQQ--PYDAPWGDRFTLMVDINGY 137
Cdd:cd06587   71 DEVDERLREAGAEGELVapPVDDPWGGRSFYFRDPDGN 108

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 788198506  20 TPHLTVKNVADSKHFYTEVFGFQVRHEnlkegvpvHVEMSY----HNELAIMFvpenvansgTLAPAsfTDAKQRTAYQY 95
Cdd:cd08349    1 IPILPVRDIDKTLAFYVDVLGFEVDYE--------RPPPGYailsRGGVELHL---------FEHPG--LDPAGSGVAAY 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 788198506  96 IYVNNVDATVKRAQALGATV-----LQQPYDAPWGDRFTLMVDINGY 137
Cdd:cd08349   62 IRVEDIDALHAELKAAGLPLfgiprITPIEDKPWGMREFAVVDPDGN 108

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 788198506  19 LTPHLTVKNVADSKHFYTEVFGFQVRHENlkeGVPVHVEMSYHN--ELAIMfvpENVANSGTLAPASFTDAkqrtAYQYI 96
Cdd:cd08359    3 LGPVIVTEDVAATAAFYVKHFGFRVIFDS---DWYVSLRRAERHgfELAIM---DGQHGAVPAASQTQSSG----LIINF 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 788198506  97 YVNNVDATVKRAQALGATVLQQPYDAPWGDRFTLMVDING 136
Cdd:cd08359   73 EVDDADAEYERLTQAGLEFLEPPRDEPWGQRRFIVRDPNG 112

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 788198506  23 LTVKNVADSKHFYTEVfGFQVRHENLKEGV----PVHVEMSYHNELaimFVPENVANSGTLAPASFTdakqrTAYQYIYV 98
Cdd:cd07251    4 LGVRDLERSARFYEAL-GWKPNLDPNDGVVffqlGGTVLALYPRDA---LAEDAGVSVTGAGFSGVT-----LAHNVRSR 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 788198506  99 NNVDATVKRAQALGATVLQQPYDAPWGDRFTLMVDINGYHWGIA 142
Cdd:cd07251   75 EEVDQLLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVA 118

Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];

                         10        20
                 ....*....|....*....|....*
gi 788198506  22 HLTVKNVADSKHFYTEVFGFQVRHE 46
Cdd:COG2514    8 TLRVRDLERSAAFYTDVLGLEVVER 32

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 788198506   34 FYTEVFGFQVRHENLKEGVPVHVEMSYHNELAIMF--VPENVAnsgtlapasftdAKQRtAYQYIYVNNVDATVKRAQAL 111
Cdd:pfam18029  15 FWSAALGWEVVPDDTALPDPDGGGPIGGGGPRLLFqrVPEPKP------------GKNR-VHLDLAVDDLEAAVARLVAL 81

                          90
                  ....*....|....*.
gi 788198506  112 GATVLQQPYDAPWGDR 127
Cdd:pfam18029  82 GATVLDDGDDPDGGRW 97