Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 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 15596077   3 IDRLDHLVLTVRDIDASIDFYTRVLGMRAVTFGAGRKALAFGAQKINLHQAGGEFEPKAERPTPGSADLCFIVATPLEAV 82
Cdd:cd07253   1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15596077  83 AEQLRQQAVEILEGPVQRTGAGGPILSLYLRDPDLNLIELSNP 125
Cdd:cd07253  81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 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 15596077   3 IDRLDHLVLTVRDIDASIDFYTRVLGMRAVTFGAGRKALAFGAQKINLHQAGGEFEPKAERPTPGSADLCFIVATPLEAV 82
Cdd:cd07253   1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15596077  83 AEQLRQQAVEILEGPVQRTGAGGPILSLYLRDPDLNLIELSNP 125
Cdd:cd07253  81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596077     5 RLDHLVLTVRDIDASIDFYTRVLGMRAV-----TFGAGRKALAF--GAQKINLHQAGGefePKAERPTPGSADLCFIVAT 77
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVeetdaGEEGGLRSAFFlaGGRVLELLLNET---PPPAAAGFGGHHIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 15596077    78 P--LEAVAEQLRQQAVEILEGPvQRTGAGGpiLSLYLRDPDLNLIEL 122
Cdd:pfam00903  78 VddVDAAYDRLKAAGVEIVREP-GRHGWGG--RYSYFRDPDGNLIEL 121

lactoylglutathione lyase

                         10        20
                 ....*....|....*....|....*.
gi 15596077    5 RLDHLVLTVRDIDASIDFYTRVLGMR 30
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMK 49

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 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 15596077   3 IDRLDHLVLTVRDIDASIDFYTRVLGMRAVTFGAGRKALAFGAQKINLHQAGGEFEPKAERPTPGSADLCFIVATPLEAV 82
Cdd:cd07253   1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15596077  83 AEQLRQQAVEILEGPVQRTGAGGPILSLYLRDPDLNLIELSNP 125
Cdd:cd07253  81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596077   3 IDRLDHLVLTVRDIDASIDFYTRVLGMRAVTFGAGRKALAF--GAQKINLHQAGGefePKAERPTPGSADLCFIVATP-- 78
Cdd:COG2514   1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdgGEHLLVLEEAPG---APPRPGAAGLDHVAFRVPSRad 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15596077  79 LEAVAEQLRQQAVEIlEGPVQRTGAggpiLSLYLRDPDLNLIEL 122
Cdd:COG2514  78 LDAALARLAAAGVPV-EGAVDHGVG----ESLYFRDPDGNLIEL 116

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596077     5 RLDHLVLTVRDIDASIDFYTRVLGMRAV-----TFGAGRKALAF--GAQKINLHQAGGefePKAERPTPGSADLCFIVAT 77
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVeetdaGEEGGLRSAFFlaGGRVLELLLNET---PPPAAAGFGGHHIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 15596077    78 P--LEAVAEQLRQQAVEILEGPvQRTGAGGpiLSLYLRDPDLNLIEL 122
Cdd:pfam00903  78 VddVDAAYDRLKAAGVEIVREP-GRHGWGG--RYSYFRDPDGNLIEL 121

N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC 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 15596077   5 RLDHLVLTVRDIDASIDFYTRVLGMRAVTFGAGRKALAFGAQK--INLHQAGGefEPKAERPTPGSADLCFIVATPLE-- 80
Cdd:cd07255   2 RIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQvlLVLEAIPD--AVLAPRSTTGLYHFAILLPDRKAlg 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15596077  81 -AVAEQLRQQAVEilegpvqrtGAGGPILS--LYLRDPDLNLIEL 122
Cdd:cd07255  80 rALAHLAEHGPLI---------GAADHGVSeaIYLSDPEGNGIEI 115

C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family contains the C-terminal, catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596077   7 DHLVLTVRDIDASIDFYTRVLGMRA--VTFGAGRKALAFgaqkinLHQAGGEFEPK---AERPTPGSADLCFIVATpLEA 81
Cdd:cd08343   1 GHVVLCSPDVEASRDFYTDVLGFRVsdRIVDPGVDGGAF------LHCDRGTDHHTvalAGGPHPGLHHVAFEVHD-LDD 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15596077  82 V---AEQLRQQAVEILEGPVqRTGAGGPIlSLYLRDPDLNLIELS 123
Cdd:cd08343  74 VgrgHDRLREKGYKIEWGPG-RHGLGSQV-FDYWFDPSGNRVEYY 116

The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus globerulus P6 BphC2-RGP6 and BphC3-RGP6, and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, yielding 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid. This is the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Most type I extradiol dioxygenases are activated by Fe(II). Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, which form hexamers. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, its two domains do not belong to this subfamily.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596077   5 RLDHLVLTVRD--IDASIDFYTRVLGMRAVTFGAGRKALAFGAQ--KINLHQAGGEFEPKAERPT-PGSADLCFIVATpL 79
Cdd:cd08348   1 KLAHFVLRTNPekFEAMVQWYLDILGARIVARNAKGCFLSFDEEhhRIAIFGAPGGAQPPDKRPTrVGLAHIAFTYAS-L 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15596077  80 EAVA---EQLRQQAVEILEgPVQRtgagGPILSLYLRDPDLNLIEL 122
Cdd:cd08348  80 DDLArnyAQLKERGIKPVW-PVNH----GVTTSIYYRDPDGNMLEM 120

Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. The three types of fosfomycin resistance proteins, employ different mechanisms to render fosfomycin [(1R,2S)-epoxypropylphosphonic acid] inactive. FosB catalyzes the addition of L-cysteine to the epoxide ring of fosfomycin. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of configuration at C1. FosA catalyzes the addition of glutathione to the antibiotic fosfomycin, making it inactive. Catalytic activities of both FosX and FosA are Mn(II)-dependent, but FosB is activated by Mg(II). Fosfomycin resistant proteins are evolutionarily related to glyoxalase I and type I extradiol dioxygenases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596077   8 HLVLTVRDIDASIDFYTRVLGMRAVtfgAGRKALAFGAQKINLHQAGGEFEPKAERPTPGSAD---LCF-IVATPLEAVA 83
Cdd:cd08345   1 HITLIVRDLEKSTAFLQDIFGAREV---YSSGDKTFSLSKEKFFLLGGLWIALMEGESLQERSythIAFqIQSEDFDRYA 77

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15596077  84 EQLRQQAVEILEGPVQRTGAGgpiLSLYLRDPDLNLIEL 122
Cdd:cd08345  78 ERLGALGVEMRPPRPRVEGEG---RSIYFYDPDNHLFEL 113

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 15596077  11 LTVRDIDASIDFYTRVLGMRAVTFGAGRKALAFGAQKINLHQAGGEFEPKAERPTP-----GSADLCFIVATplEAVAE- 84
Cdd:cd08354   6 LYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGPQVLLVFDPGATSKDVRTGEVPghgasGHGHFAFAVPT--EELAAw 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15596077  85 --QLRQQAVEIlEGPVQrTGAGGPilSLYLRDPDLNLIELSNP 125
Cdd:cd08354  84 eaRLEAKGVPI-ESYTQ-WPEGGK--SLYFRDPAGNLVELASA 122

C-terminal, catalytic domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, a key step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). BphC belongs to the type I extradiol dioxygenase family, which requires a metal ion in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. This subfamily of BphC is represented by the enzyme purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8. The members in this family of BphC enzymes may use either Mn(II) or Fe(II) as cofactors. The enzyme purified from Bacillus sp. JF8 is Mn(II)-dependent, however, the enzyme from Rhodococcus jostii RHAI has Fe(II) bound to it. BphC_JF8 is thermostable and its optimum activity is at 85 degrees C. The enzymes in this family have an internal duplication. This family represents the C-terminal repeat.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596077   5 RLDHLVLTVRDIDASIDFYTRVLGMR---AVTFGAGRKALAFGAQKINLHQAGGEFEPKAErptPGS-ADLCFIVATPLE 80
Cdd:cd09014   6 RIDHLNLLASDVTANRQFMSDTLGFRlreQIRDNNGGEAGAWMSVSSLVHDVAVMRDGKGE---PGRlHHLAYWYGTPED 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15596077  81 AV--AEQLRQQAVEILEGP----VQRTgaggpiLSLYLRDPDLNLIELSN 124
Cdd:cd09014  83 LLraADIFREHGIQIEAGPgkhgISQA------FFLYVYEPGGNRVELFG 126

Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that prefers the divalent cation zinc 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
                ....*....|....*....|....*....|....*....|.
gi 15596077   6 LDHLVLTVRDIDASIDFYTRVLGMRAVT---FGAGRKALAF 43
Cdd:cd07233   1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRkkdFPEMKFSLYF 41

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
                ....*....|....*....|...
gi 15596077   8 HLVLTVRDIDASIDFYTRVLGMR 30
Cdd:cd16358   3 HTMLRVGDLDRSIKFYTEVLGMK 25

phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596077  10 VLTVRDIDASIDFYTRVLGMRAV----TFGAgrKALAFGAqKINLhQAGGEFEPKAErPTPGSADLCFIVAT--PLEAVA 83
Cdd:cd07261   3 ILYVDNPERSTEFYRFLLGKEPVesspTFAS--FVLSGGA-KLGL-WSSEEVEPKVA-VTGGGAELSFMVPSgeQVDEVY 77

                        90
                ....*....|....*.
gi 15596077  84 EQLRQQAVEILEGPVQ 99
Cdd:cd07261  78 AEWKAMGIPIIQEPTT 93

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 15596077  11 LTVRDIDASIDFYTRVLGMRAVTFGAGRKALAFGAQKINLHqaGGEFEPKAERPTPGSADLCFIVATPLEAVAEQLRQQA 90
Cdd:cd07247   6 LPTTDLERAKAFYGAVFGWTFEDEGDGGGDYALFTAGGGAV--GGLMRAPEEVAGAPPGWLIYFAVDDLDAALARVEAAG 83

                        90       100       110
                ....*....|....*....|....*....|
gi 15596077  91 VEILEGPvQRTGAGGPIlsLYLRDPDLNLI 120
Cdd:cd07247  84 GKVVVPP-TDIPGGGRF--AVFADPEGNRF 110

C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; Uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC 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 15596077   8 HLVLTVRDIDASIDFYTRVLGMRAVtfGAGRKALAFGAQKINLHQA----GGEFEPKAERPTPGSADLCFIVAT--PLEA 81
Cdd:cd16359   2 HIHLRVSDLKAASHFYHQVLGFDIK--SRRPGALFLSAGGYHHHIGlntwAGRGLPLPPEDATGLAYFTIVLPDqeALAA 79

                        90
                ....*....|..
gi 15596077  82 VAEQLRQQAVEI 93
Cdd:cd16359  80 ILERLDLAGYDV 91

N-terminal domain of type I, class II extradiol dioxygenases; This family contains the N-terminal non-catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596077   8 HLVLTVRDIDASIDFYTRVLGMRAVTFGAGR---KALAFGAQKINLHQAggefepkaerPTPGSADLCFIVATP--LEAV 82
Cdd:cd16360   1 YAELGVPDLEKALEFYTDVLGLQVAKRDGNSvylRGYEDEHHSLVLYEA----------PEAGLKHFAFEVASEedLERA 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15596077  83 AEQLRQQAVEILEGPVQRTGAGGpiLSLYLRDPDLNLIELS 123
Cdd:cd16360  71 AASLTALGCDVTWGPDGEVPGGG--KGFRFQDPSGHLLELF 109

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];

                        10        20        30
                ....*....|....*....|....*....|....
gi 15596077   1 MQIDRLDHLVLTVR--DIDASIDFYTRVLGMRAV 32
Cdd:COG3185 142 AGLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEI 175

C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC 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 15596077   8 HLVLTVRDIDASIDFYTRVLGMRAVTFGAGRKALAFGAQ--KINLHQAGGEFE 58
Cdd:cd16357   1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSEKSALLGYGEDqaKLELVDIPEPVD 53

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 15596077   4 DRLDHLVLTVRDIDASIDFYTRVLGMRAV--TFGAGRKA----LAFGAQKINLHqaggEFEPKAERPTPGSA----DLCF 73
Cdd:cd08352   1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIreHYRPERNDikldLALGGYQLELF----IKPDAPARPSYPEAlglrHLAF 76

                        90
                ....*....|....*....
gi 15596077  74 IVATpLEAVAEQLRQQAVE 92
Cdd:cd08352  77 KVED-VEATVAELKSLGIE 94

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; 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 15596077   5 RLDHLVLTVRDIDASIDFYTRVLGMRA---------------VTFGAGrkalafgaQKINLHQAGGEFEPKAERPTPGSA 69
Cdd:cd07241   1 KIEHVALWTNDLERMKDFYVKYFGAESndiyhnkkkgfrsyfLTFDSG--------ARLELMSRPDVTDPDKEVERTGLA 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596077  70 DLCFIVATPlEAV---AEQLRQQAVEILEGPvqRTGAGGPILSLyLRDPDLNLIELS 123
Cdd:cd07241  73 HIAFSVGSK-EAVdelTERLRADGYAVVGGP--RTTGDGYYESV-ILDPEGNRIEIT 125

N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily contains the N-terminal, non-catalytic, domain of HPCD. HPCD catalyses the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. The aromatic ring of 4-hydroxyphenylacetate is opened by this dioxygenase to yield the 3,4-diol product, 2-hydroxy-5-carboxymethylmuconate semialdehyde. HPCD is a homotetramer and each monomer contains two structurally homologous barrel-shaped domains at the N- and C-terminus. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism. Most extradiol dioxygenases contain Fe(II) in their active site, but HPCD can be activated by either Mn(II) or Fe(II). These enzymes belong to the type I class II family of extradiol dioxygenases. The class III 3,4-dihydroxyphenylacetate 2,3-dioxygenases belong to a different superfamily.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596077   3 IDRLDHLVLTVRDIDASIDFYTRVLGMRAVTFGAG----RKALAFGAQKINLHQAggefepkaerPTPGSADLCFIVATP 78
Cdd:cd07266   2 IIRLAHAELVVTDLAASREFYVDTLGLHVTDEDDNaiylRGVEEFIHHTLVLRKA----------PEAAVGHLGFRVRDE 71

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15596077  79 --LEAVAEQLRQQAVeilegPVQRTGAGGPILSLYLRDP 115
Cdd:cd07266  72 adLDKAAAFYKELGL-----PTEWREEPGQGRTLRVEDP 105

lactoylglutathione lyase

                         10        20
                 ....*....|....*....|....*.
gi 15596077    5 RLDHLVLTVRDIDASIDFYTRVLGMR 30
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMK 49

Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.

                          10        20
                  ....*....|....*....|....*..
gi 15596077     6 LDHLVLTVRDIDASIDFYTRVLGMRAV 32
Cdd:pfam13468   1 LDHVVLAVPDLDEAAARFARALGFTVT 27

N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The N-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain 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.

                        10        20
                ....*....|....*....|....*..
gi 15596077   6 LDHLVLTVRDIDASIDFYTRVLGMRAV 32
Cdd:cd08346   2 IHHITAITGDAQENVDFYVKVLGLRLV 28