metallothiol transferase FosB;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489172727   1 MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYggPAAD----YTHYAFGIAAADFAR 76
Cdd:PRK04101   1 MLKGINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWIALNEEKDI--PRNEihqsYTHIAFSIEEEDFDH 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489172727  77 FAAQLRAHGV-----REwkqnRSEGD--SFYFLDPDGHRLEAHVGDLRSRLA 121
Cdd:PRK04101  79 WYQRLKENDVnilpgRE----RDERDkkSIYFTDPDGHKFEFHTGTLQDRLN 126

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489172727    4 GLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLEL-------GSLWLCL---SREPQYGGPAADYTHYAFGIAAAD 73
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLrsafflaGGRVLELllnETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 489172727   74 FARFAAQLRAHGVREWKQNRSEGDS---FYFLDPDGHRLE 110
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGgrySYFRDPDGNLIE 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 489172727   7 HLTLAVADLPASIAFYRDLLGFRLEARW-------DQGAYLELGSLWLCLSREPQYggPAADYTHYAFGIAAADFARFAA 79
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGAREVYSSgdktfslSKEKFFLLGGLWIALMEGESL--QERSYTHIAFQIQSEDFDRYAE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489172727  80 QLRAHGVREWKQNRS---EGDSFYFLDPDGHRLEAHVGDL 116
Cdd:cd08345   79 RLGALGVEMRPPRPRvegEGRSIYFYDPDNHLFELHTGTL 118

fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin resistant protein. FosB is a Mg(2+)-dependent L-cysteine thiol transferase. Fosfomycin inhibits the enzyme UDP-nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosB catalyzes the Mg(II) dependent addition of L-cysteine to the epoxide ring of fosfomycin, (1R,2S)-epoxypropylphosphonic acid, rendering it inactive. FosB is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489172727   5 LNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYggPAAD----YTHYAFGIAAADFARFAAQ 80
Cdd:cd08363    1 INHITFSVSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNGLWLALNVQEDI--PRNEishsYTHIAFSIDEEDLDAFKER 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489172727  81 LRAHGV-----RewKQNRSEGDSFYFLDPDGHRLEAHVGDLRSRLA 121
Cdd:cd08363   79 LKDNGVnilegR--KRDILEGQSIYFTDPDGHLFELHTGTLEDRLE 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 489172727   3 TGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQG------AYLELGS---LWLCLSREPQYGGPAADYTHYAFGIaaAD 73
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGdggfghAFLRLGDgteLELFEAPGAAPAPGGGGLHHLAFRV--DD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489172727  74 FARFAAQLRAHGVREWKQNRSEGD---SFYFLDPDGHRLEAH 112
Cdd:COG0346   79 LDAAYARLRAAGVEIEGEPRDRAYgyrSAYFRDPDGNLIELV 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 489172727   7 HLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGS---LWLCLSREPQYGGPAAD-YTHYAF---GIAAADFARFAA 79
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLgpgLRLALLEGPEPERPGGGgLFHLAFevdDVDEVDERLREA 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489172727  80 QLRAHGVREWKQNRSEGDSFYFLDPDGHRLE 110
Cdd:cd06587   81 GAEGELVAPPVDDPWGGRSFYFRDPDGNLIE 111

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 489172727  10 LAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCL-----SREPQYGGP-----AADYTHYAFGIAAADFARFAA 79
Cdd:cd08354    6 LYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGPQVLLVfdpgaTSKDVRTGEvpghgASGHGHFAFAVPTEELAAWEA 85

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489172727  80 QLRAHGVREWKQNRSE--GDSFYFLDPDGHRLE 110
Cdd:cd08354   86 RLEAKGVPIESYTQWPegGKSLYFRDPAGNLVE 118

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489172727   1 MLTGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYlelgslWLCLSREPQYGG--------PAADYTHYAFGIaaA 72
Cdd:COG3324    1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGD------YAEFDTDGGQVGglmpgaeePGGPGWLLYFAV--D 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489172727  73 DFARFAAQLRAHG---VREWKQNRSEGDSFYFLDPDGHRLE 110
Cdd:COG3324   73 DLDAAVARVEAAGgtvLRPPTDIPPWGRFAVFRDPEGNRFG 113

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 489172727  10 LAVADLPASIAFYRDLLGFRLEARWDQG--AYLELGSLWLCLSREPQYgGPAADYThyAFGIAAADFARFAAQLRAHGV- 86
Cdd:cd08349    4 LPVRDIDKTLAFYVDVLGFEVDYERPPPgyAILSRGGVELHLFEHPGL-DPAGSGV--AAYIRVEDIDALHAELKAAGLp 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 489172727  87 -REWKQNRSEGDSFY----FL--DPDGHRL 109
Cdd:cd08349   81 lFGIPRITPIEDKPWgmreFAvvDPDGNLL 110

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 489172727   5 LNHLTLAVAD--LPASIAFYRDLLGFRLEARWDQGAYLELGSLWLCLSREPQYGG--------PAADYTHYAFGIAAAD- 73
Cdd:cd08348    2 LAHFVLRTNPekFEAMVQWYLDILGARIVARNAKGCFLSFDEEHHRIAIFGAPGGaqppdkrpTRVGLAHIAFTYASLDd 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489172727  74 FARFAAQLRAHGVR-EWKQNRSEGDSFYFLDPDGHRLEAHV 113
Cdd:cd08348   82 LARNYAQLKERGIKpVWPVNHGVTTSIYYRDPDGNMLEMQV 122

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 489172727   3 TGLNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYL--ELGSLWLCLSREPQYGG---PAADYTHYAF--------GI 69
Cdd:cd07255    1 TRIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLgvDGKQVLLVLEAIPDAVLaprSTTGLYHFAIllpdrkalGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489172727  70 AAADFARFAAQLRA--HGVREwkqnrsegdSFYFLDPDGHRLE 110
Cdd:cd07255   81 ALAHLAEHGPLIGAadHGVSE---------AIYLSDPEGNGIE 114

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 489172727   3 TGLNHLTLAVADLPASIAFYRDLLGFRLEA---RWDQGAY---LELGSLWLCL------SREPQYgGPAADYTHYAFGIa 70
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIRehyRPERNDIkldLALGGYQLELfikpdaPARPSY-PEALGLRHLAFKV- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489172727  71 aADFARFAAQLRAHGVR--EWKQNRSEGDSFYFL-DPDGHRLEAH 112
Cdd:cd08352   79 -EDVEATVAELKSLGIEtePIRVDDFTGKKFTFFfDPDGLPLELY 122

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 489172727   5 LNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYL----ELGSLWLCLSRepqygGPAADYTHYAFGIAAADFA-RFAA 79
Cdd:cd07266    5 LAHAELVVTDLAASREFYVDTLGLHVTDEDDNAIYLrgveEFIHHTLVLRK-----APEAAVGHLGFRVRDEADLdKAAA 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489172727  80 QLRAHGVR-EWKQNRSEGDSFYFLDPDGHRLE 110
Cdd:cd07266   80 FYKELGLPtEWREEPGQGRTLRVEDPFGFPIE 111

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 489172727   5 LNHLTLAVADLPASIAFYRDLLG-FRLEARWDQGAYLELG-----SLWLClsrEPQYGGPA--ADYTHYAFgiaaadfar 76
Cdd:cd07262    1 ISHVTIGVNDLERSRAFYDAALApLGYKRGFEDGGRVGYGleggpDFWVT---EPFDGEPAtaGNGTHVAF--------- 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489172727  77 fAAQLRAHgVREWKQ------NRSEGD------------SFYFLDPDGHRLEAH 112
Cdd:cd07262   69 -AAPSRAA-VDAFHAaalaagGTDNGApglrphyhpgyyAAYVRDPDGNKIEAV 120

ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and similar proteins; ChaP is an enzyme involved in the biosynthesis of the potent antitumor agent chartreusin (cha). Cha is an aromatic polyketide glycoside produced by Streptomyces chartreusis. ChaP may play a role as a meta-cleavage dioxygenase in the oxidative rearrangement of the anthracyclic polyketide. ChaP 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 489172727   5 LNHLTLAVADLPASIAFYRDLLGFRLEARWDQGAYLELGSLwLCLsrepQYGGPAADYT--HYAFGIAAADFARFAAQLR 82
Cdd:cd08351    3 LNHTIVPARDKEASARFLAEILGLPAPPPWGPFAPVRLNNG-LTL----DFADPRGEIApqHYAFLVSDDEFDAILARIR 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489172727  83 AHGVREW---------KQNRSEGDS-FYFLDPDGHRLE 110
Cdd:cd08351   78 ARGLEYWadpqhrepgEINHNDGGRgVYFRDPDGHLLE 115

N-terminal domain of MhqB, a type I extradiol dioxygenase, and similar proteins; This subfamily contains the N-terminal, non-catalytic, domain of Burkholderia sp. NF100 MhqB and similar proteins. MhqB is a type I extradiol dioxygenase involved in the catabolism of methylhydroquinone, an intermediate in the degradation of fenitrothion. The purified enzyme has shown extradiol ring cleavage activity toward 3-methylcatechol. Fe2+ was suggested as a cofactor, the same as most other enzymes in the family. Burkholderia sp. NF100 MhqB is encoded on the plasmid pNF1. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489172727   5 LNHLTLAVADLPASIAFYRdllGFRLEARwDQGAYLELGS-----LWLCLSRepqygGPAADYTHYAFGIAAADFARFAA 79
Cdd:cd08344    3 IDHFALEVPDLEVARRFYE---AFGLDVR-ETGEDLELRApgndhVWARLIQ-----GARKRLAYLSFGIFGDDLARFAA 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489172727  80 QLRAHGVREWKQNRS-EGDSFYFLDPDGHRLEAHVGD 115
Cdd:cd08344   74 HLDAAGVALIAAPPGaDPDGVWFEDPDGNLLQVRVAD 110

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489172727  10 LAVADLPASIAFYRDLLGFRLEARWDQG------AYLELGSLWLCLSREPQyGGPAADYTHYAFGIAAADFARFAAQLRA 83
Cdd:COG2764    6 LVVDDAEEALEFYEDVFGFEVVFRMTDPdgkimhAELRIGGSVLMLSDAPP-DSPAAEGNGVSLSLYVDDVDALFARLVA 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 489172727  84 HG---VREWkQNRSEGD-SFYFLDPDGHRL 109
Cdd:COG2764   85 AGatvVMPL-QDTFWGDrFGMVRDPFGVLW 113

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
                 ....*....|....*....|....*....|.
gi 489172727   5 LNHLTLAVADLPASIAFYRDLLGFRLEARWD 35
Cdd:cd07233    1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKD 31

methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 489172727    5 LNHLTLAVADLPASIAFYRDLLGFRL---EARWDQG---AYLELG 43
Cdd:TIGR03081   2 IDHVGIAVPDLEEAAKFYEDVLGAQVseiEELPEQGvkvVFIALG 46

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.

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gi 489172727   7 HLTLAVADLPASIAFYRDLLGFRLEARWD 35
Cdd:cd16358    3 HTMLRVGDLDRSIKFYTEVLGMKLLRKRD 31

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.

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gi 489172727   9 TLAVADLPASIAFYRDlLGFRLEARWDQG-AYLELGSLWLCL 49
Cdd:cd07251    3 TLGVRDLERSARFYEA-LGWKPNLDPNDGvVFFQLGGTVLAL 43