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        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982206741   5 GIHHVSALTADAQKNLDFYKKVLGLKLVKKSVNQDEPTMYHLFYGDEVANPGTELTFFEIPRIAPFHAGTNSISSIGLRV 84
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 982206741  85 PStEALHYWKERFEEHQVAYSGIAKRAGRDILAFQDHEGQRLVLT 129
Cdd:cd08346   81 PK-GSLSFWAERLEKFGVPHSEVVTRFGEKYLRFEDPDGTRLFLV 124

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        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982206741   5 GIHHVSALTADAQKNLDFYKKVLGLKLVKKSVNQDEPTMYHLFYGDEVANPGTELTFFEIPRIAPFHAGTNSISSIGLRV 84
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 982206741  85 PStEALHYWKERFEEHQVAYSGIAKRAGRDILAFQDHEGQRLVLT 129
Cdd:cd08346   81 PK-GSLSFWAERLEKFGVPHSEVVTRFGEKYLRFEDPDGTRLFLV 124

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 982206741   5 GIHHVSALTADAQKNLDFYKKVLGLKLVKKsVNQDEPTMYHLFYGdevANPGTELTFFEIPRIAPFHaGTNSISSIGLRV 84
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKR-TDFGDGGFGHAFLR---LGDGTELELFEAPGAAPAP-GGGGLHHLAFRV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 982206741  85 PsteALHYWKERFEEHQVAYSGIAKRA--GRDILAFQDHEGQRLVLTADEKG 134
Cdd:COG0346   77 D---DLDAAYARLRAAGVEIEGEPRDRayGYRSAYFRDPDGNLIELVEPPPG 125

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982206741    5 GIHHVSALTADAQKNLDFYKKVLGLKLVKKSVNQDEPTMYHLFygdeVANPGTELTFFEIPRIAPFHAGTNSiSSIGLRV 84
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAF----FLAGGRVLELLLNETPPPAAAGFGG-HHIAFIA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 982206741   85 PSTEALHYWKERFEEHQVAYSGIAKRAGRD--ILAFQDHEGQRLVL 128
Cdd:pfam00903  76 FSVDDVDAAYDRLKAAGVEIVREPGRHGWGgrYSYFRDPDGNLIEL 121

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        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982206741   5 GIHHVSALTADAQKNLDFYKKVLGLKLVKKSVNQDEPTMYHLFYGDEVANPGTELTFFEIPRIAPFHAGTNSISSIGLRV 84
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 982206741  85 PStEALHYWKERFEEHQVAYSGIAKRAGRDILAFQDHEGQRLVLT 129
Cdd:cd08346   81 PK-GSLSFWAERLEKFGVPHSEVVTRFGEKYLRFEDPDGTRLFLV 124

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 982206741   5 GIHHVSALTADAQKNLDFYKKVLGLKLVKKsVNQDEPTMYHLFYGdevANPGTELTFFEIPRIAPFHaGTNSISSIGLRV 84
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKR-TDFGDGGFGHAFLR---LGDGTELELFEAPGAAPAP-GGGGLHHLAFRV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 982206741  85 PsteALHYWKERFEEHQVAYSGIAKRA--GRDILAFQDHEGQRLVLTADEKG 134
Cdd:COG0346   77 D---DLDAAYARLRAAGVEIEGEPRDRayGYRSAYFRDPDGNLIELVEPPPG 125

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982206741   3 VNGIHHVSALTADAQKNLDFYKKVLGLKLVkksvnQDEPTMYHLfygdEVANPGTELTFFEIPRiAPFHAGTNSISSIGL 82
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVV-----EREGGRVYL----RADGGEHLLVLEEAPG-APPRPGAAGLDHVAF 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 982206741  83 RVPSTEALHYWKERFEEHQVAYSGIAKRAGRDILAFQDHEGQRLVLTADEKG 134
Cdd:COG2514   71 RVPSRADLDAALARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIELYTDRPR 122

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982206741    5 GIHHVSALTADAQKNLDFYKKVLGLKLVKKSVNQDEPTMYHLFygdeVANPGTELTFFEIPRIAPFHAGTNSiSSIGLRV 84
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAF----FLAGGRVLELLLNETPPPAAAGFGG-HHIAFIA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 982206741   85 PSTEALHYWKERFEEHQVAYSGIAKRAGRD--ILAFQDHEGQRLVL 128
Cdd:pfam00903  76 FSVDDVDAAYDRLKAAGVEIVREPGRHGWGgrYSYFRDPDGNLIEL 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 982206741 154 GLGPVELTVPYAEPTLHVLTNILGFTEISREAvegqGTAVIlesGEGGAATEIHLIERNDLPRERQGKGSVHHVAFRVRD 233
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGLSVLKQNA----SRAYL---GVDGKQVLLVLEAIPDAVLAPRSTTGLYHFAILLPD 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 982206741 234 EEELAGWHQIISREGYSNSGiVERYYFKALYFREP--NGIlfELSTDGP 280
Cdd:cd07255   75 RKALGRALAHLAEHGPLIGA-ADHGVSEAIYLSDPegNGI--EIYADRP 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 982206741   8 HVSALTADAQKNLDFYKKVLGLKLVKKSVNqdeptMYHLFYGDEvanPGTELTFFEIPRiaPFHAGTNSISSIGLRVPST 87
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEG-----GGFAFLRLG---PGLRLALLEGPE--PERPGGGGLFHLAFEVDDV 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 982206741  88 EALHYW-KERFEEHQVAYSGIAKRAGRDILAFQDHEGQRLVL 128
Cdd:cd06587   71 DEVDERlREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 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 982206741   6 IHHVSALTADAQKNLDFYKKVLGLKLVKKSVNQD---------EPTMYHLFygdeVANPGTELTFFEIPRIAPfHagtns 76
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLEEVPRPPFLKfggawlylgGGQQIHLV----VEQNPSELPRPEHPGRDR-H----- 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 982206741  77 issIGLRVPSTEALhywKERFEEHQVAYS-GIAKRAGRDILAFQDHEGQRL 126
Cdd:cd07245   71 ---PSFSVPDLDAL---KQRLKEAGIPYTeSTSPGGGVTQLFFRDPDGNRL 115

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        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982206741  15 DAQKNLDFYKKVLGLKLVKKSVNQDEP-TMYHLFYGDEVANPGTELTFFEIPRIA----------------PFHAGtNS- 76
Cdd:cd07233   10 DPKKSLKFYTEVLGMKLLRKKDFPEMKfSLYFLGYEDPKDIPKDPRTAWVFSREGtlelthnwgtendedpVYHNG-NSd 88

                         90       100       110
                 ....*....|....*....|....*....|.
gi 982206741  77 ---ISSIGLRVPSTEALHywkERFEEHQVAY 104
Cdd:cd07233   89 prgFGHIGIAVDDVYAAC---ERFEELGVKF 116

Zn-dependent glyoxalase, PhnB family [Energy production and conversion];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 982206741  13 TADAQKNLDFYKKVLGLKLVKKSVNQDEPTMYHlfygdEVANPGTELTFFEIPRIAPFHAGTNsiSSIGLRVPSTEALH 91
Cdd:COG2764    8 VDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHA-----ELRIGGSVLMLSDAPPDSPAAEGNG--VSLSLYVDDVDALF 79

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 982206741 209 IERNDLPRErQGKGSVHhVAFRVrDEEELAGWHQIISREGYSnsgiVERYYF-----KALYFREPNGILFELST 277
Cdd:cd08354   55 VRTGEVPGH-GASGHGH-FAFAV-PTEELAAWEARLEAKGVP----IESYTQwpeggKSLYFRDPAGNLVELAS 121

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 982206741  15 DAQKNLDFYKKVLGLKLVkksvnqdeptmYHLFYGD--EVANPGTELTFFEIPRIAPFHAGTNsissIGLRVPSTEALHy 92
Cdd:cd08349    8 DIDKTLAFYVDVLGFEVD-----------YERPPPGyaILSRGGVELHLFEHPGLDPAGSGVA----AYIRVEDIDALH- 71

                         90
                 ....*....|....*..
gi 982206741  93 wkERFEEHQVAYSGIAK 109
Cdd:cd08349   72 --AELKAAGLPLFGIPR 86