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Conserved domains on  [gi|727180921|ref|WP_033643393|]
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MULTISPECIES: fosfomycin resistance glutathione transferase [Serratia]

Protein Classification

fosfomycin resistance glutathione transferase( domain architecture ID 10163491)

fosfomycin resistance glutathione transferase such as glutathione transferase FosA is a metalloglutathione transferase which confers resistance to fosfomycin by catalyzing the addition of glutathione to fosfomycin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 4-126 1.54e-72

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


:

Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 212.14  E-value: 1.54e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   4 GLNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWLCLSLDEArtQPRARDYTHYAFSVAPEHIERVSERLR 83
Cdd:cd07244    1 GINHITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYLTAGDLWLCLSLDPA--AEPSPDYTHIAFTVSEEDFEELSERLR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 727180921  84 QSGAEEWKSNRSEGESLYFLDPDGHQLEIHAGDLASRLAACRE 126
Cdd:cd07244   79 AAGVKIWQENSSEGDSLYFLDPDGHKLELHVGSLESRLASLRE 121
 
Name Accession Description Interval E-value
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 4-126 1.54e-72

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 212.14  E-value: 1.54e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   4 GLNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWLCLSLDEArtQPRARDYTHYAFSVAPEHIERVSERLR 83
Cdd:cd07244    1 GINHITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYLTAGDLWLCLSLDPA--AEPSPDYTHIAFTVSEEDFEELSERLR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 727180921  84 QSGAEEWKSNRSEGESLYFLDPDGHQLEIHAGDLASRLAACRE 126
Cdd:cd07244   79 AAGVKIWQENSSEGDSLYFLDPDGHKLELHVGSLESRLASLRE 121
PRK04101 PRK04101
metallothiol transferase FosB;
1-135 9.51e-35

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 117.35  E-value: 9.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   1 MLTGLNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWlcLSLDEARTQPR---ARDYTHYAFSVAPEHIER 77
Cdd:PRK04101   1 MLKGINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLW--IALNEEKDIPRneiHQSYTHIAFSIEEEDFDH 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727180921  78 VSERLRQSGA---EEWKSNRSEGESLYFLDPDGHQLEIHAGDLASRLAACR-EKPYqgMVFY 135
Cdd:PRK04101  79 WYQRLKENDVnilPGRERDERDKKSIYFTDPDGHKFEFHTGTLQDRLNYYKeEKPH--MTFY 138
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
2-112 5.15e-23

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 87.32  E-value: 5.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   2 LTGLNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSL--GALWLCL-SLDEARTQPRARDYTHYAFSVA-PEHIER 77
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdgGEHLLVLeEAPGAPPRPGAAGLDHVAFRVPsRADLDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 727180921  78 VSERLRQSGAE-EWKSNRSEGESLYFLDPDGHQLEI 112
Cdd:COG2514   81 ALARLAAAGVPvEGAVDHGVGESLYFRDPDGNLIEL 116
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-112 5.56e-15

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 66.32  E-value: 5.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921    4 GLNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWL-----CLSLDEARTQPRAR----DYTHYAFSVAPEH 74
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFlaggrVLELLLNETPPPAAagfgGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 727180921   75 IERVSERLRQSGAEEWKSNRSEGESL---YFLDPDGHQLEI 112
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGrysYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 4-126 1.54e-72

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 212.14  E-value: 1.54e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   4 GLNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWLCLSLDEArtQPRARDYTHYAFSVAPEHIERVSERLR 83
Cdd:cd07244    1 GINHITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYLTAGDLWLCLSLDPA--AEPSPDYTHIAFTVSEEDFEELSERLR 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 727180921  84 QSGAEEWKSNRSEGESLYFLDPDGHQLEIHAGDLASRLAACRE 126
Cdd:cd07244   79 AAGVKIWQENSSEGDSLYFLDPDGHKLELHVGSLESRLASLRE 121
PRK04101 PRK04101
metallothiol transferase FosB;
1-135 9.51e-35

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 117.35  E-value: 9.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   1 MLTGLNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWlcLSLDEARTQPR---ARDYTHYAFSVAPEHIER 77
Cdd:PRK04101   1 MLKGINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLW--IALNEEKDIPRneiHQSYTHIAFSIEEEDFDH 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727180921  78 VSERLRQSGA---EEWKSNRSEGESLYFLDPDGHQLEIHAGDLASRLAACR-EKPYqgMVFY 135
Cdd:PRK04101  79 WYQRLKENDVnilPGRERDERDKKSIYFTDPDGHKFEFHTGTLQDRLNYYKeEKPH--MTFY 138
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 7-117 1.04e-34

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.


Pssm-ID: 319933  Cd Length: 118  Bit Score: 116.50  E-value: 1.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   7 HLTLAVSDLDRSFDFYRHLLGFTPHARWQG-------GAYLSLGALWLCLSLDEartQPRARDYTHYAFSVAPEHIERVS 79
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGAREVYSSGDktfslskEKFFLLGGLWIALMEGE---SLQERSYTHIAFQIQSEDFDRYA 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 727180921  80 ERLRQSGAEEWKSNRS---EGESLYFLDPDGHQLEIHAGDL 117
Cdd:cd08345   78 ERLGALGVEMRPPRPRvegEGRSIYFYDPDNHLFELHTGTL 118
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 5-122 3.55e-29

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.


Pssm-ID: 319951 [Multi-domain]  Cd Length: 131  Bit Score: 102.81  E-value: 3.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   5 LNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWLCLSLDE--ARTQpRARDYTHYAFSVAPEHIERVSERL 82
Cdd:cd08363    1 INHITFSVSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNGLWLALNVQEdiPRNE-ISHSYTHIAFSIDEEDLDAFKERL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 727180921  83 RQSGA---EEWKSNRSEGESLYFLDPDGHQLEIHAGDLASRLA 122
Cdd:cd08363   80 KDNGVnilEGRKRDILEGQSIYFTDPDGHLFELHTGTLEDRLE 122
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
2-112 5.15e-23

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 87.32  E-value: 5.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   2 LTGLNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSL--GALWLCL-SLDEARTQPRARDYTHYAFSVA-PEHIER 77
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdgGEHLLVLeEAPGAPPRPGAAGLDHVAFRVPsRADLDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 727180921  78 VSERLRQSGAE-EWKSNRSEGESLYFLDPDGHQLEI 112
Cdd:COG2514   81 ALARLAAAGVPvEGAVDHGVGESLYFRDPDGNLIEL 116
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 3-113 8.20e-21

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 81.19  E-value: 8.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   3 TGLNHLTLAVSDLDRSFDFYRHLLGFTPHARWQ------GGAYLSLG-ALWLCL-SLDEARTQPRARDYTHYAFSVapEH 74
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDfgdggfGHAFLRLGdGTELELfEAPGAAPAPGGGGLHHLAFRV--DD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 727180921  75 IERVSERLRQSGAE--EWKSNRSEGE-SLYFLDPDGHQLEIH 113
Cdd:COG0346   79 LDAAYARLRAAGVEieGEPRDRAYGYrSAYFRDPDGNLIELV 120
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 3-123 1.45e-20

fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin resistant protein. FosX is a Mn(II)-dependent fosfomycin-specific epoxide hydrolase. Fosfomycin inhibits the enzyme UDP-Nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of the configuration at C1 in the presence of Mn(II). The hydrated fosfomycin loses the inhibition activity. FosX is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319952  Cd Length: 130  Bit Score: 80.78  E-value: 1.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   3 TGLNHLTLAVSDLDRSFDFYRHLLGftphAR--WQGGA---------YLSLGALWLCLSLDEArtqPRARDYTHYAFSVA 71
Cdd:cd08364    2 EGISHITFIVKDLDRTAAFLTEIFG----AEevYDSGAetfslspekFFLIGGLWIAIMEGEP---LLERSYNHIAFKVS 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 727180921  72 PEHIERVSERLRQSGAEEwKSNRS----EGESLYFLDPDGHQLEIHAGDLASRLAA 123
Cdd:cd08364   75 EGDLDEYRARIKKLGLEI-RPPRSrvqgEGRSLYFYDFDNHLFELHTGTLEERLAR 129
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-112 5.56e-15

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 66.32  E-value: 5.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921    4 GLNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWL-----CLSLDEARTQPRAR----DYTHYAFSVAPEH 74
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFlaggrVLELLLNETPPPAAagfgGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 727180921   75 IERVSERLRQSGAEEWKSNRSEGESL---YFLDPDGHQLEI 112
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGrysYFRDPDGNLIEL 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-112 1.49e-12

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.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 59.85  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   7 HLTLAVSDLDRSFDFYRHLLGFTPHARWQGG--AYLSLGA-LWLCLSLDEARTQPRARDYTHYAFSVapEHIERVSERLR 83
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGgfAFLRLGPgLRLALLEGPEPERPGGGGLFHLAFEV--DDVDEVDERLR 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 727180921  84 QSGAEEWKSNRSE-----GESLYFLDPDGHQLEI 112
Cdd:cd06587   79 EAGAEGELVAPPVddpwgGRSFYFRDPDGNLIEF 112
ChaP_like cd08351
ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and ...
 5-112 1.41e-11

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.


Pssm-ID: 319939  Cd Length: 118  Bit Score: 57.13  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   5 LNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALwLCLSLDEARTQPRArdyTHYAFSVAPEHIERVSERLRQ 84
Cdd:cd08351    3 LNHTIVPARDKEASARFLAEILGLPAPPPWGPFAPVRLNNG-LTLDFADPRGEIAP---QHYAFLVSDDEFDAILARIRA 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 727180921  85 SGAEEW---------KSNRSE-GESLYFLDPDGHQLEI 112
Cdd:cd08351   79 RGLEYWadpqhrepgEINHNDgGRGVYFRDPDGHLLEI 116
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-113 2.93e-11

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 56.57  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   1 MLTGLNHLTLAVSDLDRSFDFYRHLLGFTPHARW-QGGAYLSLGALW-LCLSLDEARTQPrARDYTHYAFSVapEHIERV 78
Cdd:COG3324    1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAgPGGDYAEFDTDGgQVGGLMPGAEEP-GGPGWLLYFAV--DDLDAA 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 727180921  79 SERLRQSGAE---EWKSNRSEGESLYFLDPDGHQLEIH 113
Cdd:COG3324   78 VARVEAAGGTvlrPPTDIPPWGRFAVFRDPEGNRFGLW 115
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 3-114 9.34e-11

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.


Pssm-ID: 319918  Cd Length: 124  Bit Score: 55.40  E-value: 9.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   3 TGLNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLG----ALWLCLSLDEARTQPRARDYTHYAFSV-APEHIER 77
Cdd:cd07255    1 TRIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDgkqvLLVLEAIPDAVLAPRSTTGLYHFAILLpDRKALGR 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 727180921  78 VSERLRQSGAEEWKSNRSEGESLYFLDPDGHQLEIHA 114
Cdd:cd07255   81 ALAHLAEHGPLIGAADHGVSEAIYLSDPEGNGIEIYA 117
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 3-113 1.16e-10

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.


Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 54.86  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   3 TGLNHLTLAVSDLDRSFDFYRHLLGFT---PHARWQGGAY---LSLGALWLCL-SLDEAR---TQPRARDYTHYAFSVap 72
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEiirEHYRPERNDIkldLALGGYQLELfIKPDAParpSYPEALGLRHLAFKV-- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 727180921  73 EHIERVSERLRQSG--AEEWKSNRSEGESLYFL-DPDGHQLEIH 113
Cdd:cd08352   79 EDVEATVAELKSLGieTEPIRVDDFTGKKFTFFfDPDGLPLELY 122
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 9-112 2.88e-10

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 54.07  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   9 TLAVSDLDRSFDFYRHlLGFTPHARWQGGAYLSL---GALWLCLsLDEAR----TQPRARDYTHY-----AFSVA-PEHI 75
Cdd:COG3607    8 NLPVADLERSRAFYEA-LGFTFNPQFSDEGAACFvlgEGIVLML-LPREKfatfTGKPIADATGFtevllALNVEsREEV 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 727180921  76 ERVSERLRQSGAEEWKSNRSE--GESLYFLDPDGHQLEI 112
Cdd:COG3607   86 DALVAKALAAGGTVLKPPQDVggMYSGYFADPDGHLWEV 124
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 2-112 1.58e-08

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.


Pssm-ID: 319916 [Multi-domain]  Cd Length: 123  Bit Score: 49.53  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   2 LTGLNHLTLAVSDLDRSFDFYRHLLGFTP-------HARWQGGAYLSLGALwlclsldEARTQPRARDYT----HYAFSV 70
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVvtfkegrKALRFGNQKINLHQK-------GKEFEPKASAPTpgsaDLCFIT 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 727180921  71 APEhIERVSERLRQ------SGAEEWKSNRSEGESLYFLDPDGHQLEI 112
Cdd:cd07253   74 ETP-IDEVLEHLEAcgvtieEGPVKRTGALGPILSIYFRDPDGNLIEL 120
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-112 2.59e-08

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.


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 48.85  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   5 LNHLTLAVSDLDRSFDFYRHLLGFT----PHARWQGGAYLSLGALWLcLSLDEARTQPRARDYT------HYAFSVapEH 74
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLEevprPPFLKFGGAWLYLGGGQQ-IHLVVEQNPSELPRPEhpgrdrHPSFSV--PD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 727180921  75 IERVSERLRQSGAE-EWKSNRSEGE-SLYFLDPDGHQLEI 112
Cdd:cd07245   78 LDALKQRLKEAGIPyTESTSPGGGVtQLFFRDPDGNRLEF 117
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-112 5.13e-08

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.


Pssm-ID: 319942  Cd Length: 122  Bit Score: 48.13  E-value: 5.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921  10 LAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWLCL-----SLDEARTQPRARD----YTHYAFSVAPEHIERVSE 80
Cdd:cd08354    6 LYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGPQVLLVfdpgaTSKDVRTGEVPGHgasgHGHFAFAVPTEELAAWEA 85

                         90       100       110
                 ....*....|....*....|....*....|....
gi 727180921  81 RLRQSGAEEWKSNRSE--GESLYFLDPDGHQLEI 112
Cdd:cd08354   86 RLEAKGVPIESYTQWPegGKSLYFRDPAGNLVEL 119
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-112 9.24e-08

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.


Pssm-ID: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 47.29  E-value: 9.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   9 TLAVSDLDRSFDFYRHlLGFTPHARWQGG-AYLSLGALWLCL----------SLDEARTQPRARDYTHYAFSvaPEHIER 77
Cdd:cd07251    3 TLGVRDLERSARFYEA-LGWKPNLDPNDGvVFFQLGGTVLALyprdalaedaGVSVTGAGFSGVTLAHNVRS--REEVDQ 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 727180921  78 VSERLRQSGAEEWKSNRS---EGESLYFLDPDGHQLEI 112
Cdd:cd07251   80 LLAKAVAAGGKILKPPQEvfwGGYSGYFADPDGHIWEV 117
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 7-115 1.06e-07

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.


Pssm-ID: 319967  Cd Length: 111  Bit Score: 46.93  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   7 HLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYL-SLGALWLCLSLDEArtqPRARdYTHYAFSVA-PEHIERVSERLRQ 84
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKRDGNSVYLrGYEDEHHSLVLYEA---PEAG-LKHFAFEVAsEEDLERAAASLTA 76

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 727180921  85 SGAE-EWKSN---RSEGESLYFLDPDGHQLEIHAG 115
Cdd:cd16360   77 LGCDvTWGPDgevPGGGKGFRFQDPSGHLLELFVE 111
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-113 3.96e-07

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.


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 45.79  E-value: 3.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   7 HLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAY--LSLGALWLCLSL--DEARTQPRARDYTHYAFSVAPEHIERVSERL 82
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLGLPPRFLHEEGEYaeFDTGETKLALFSrkEMARSGGPDRRGSAFELGFEVDDVEATVEEL 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 727180921  83 RQSGAE--------EWKsnrseGESLYFLDPDGHQLEIH 113
Cdd:cd07264   83 VERGAEfvrepankPWG-----QTVAYVRDPDGNLIEIC 116
BphC-JF8_N_like cd09013
N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 5-112 4.09e-07

N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Bacillus sp. JF8, and similar proteins; 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 N-terminal repeat.


Pssm-ID: 319955  Cd Length: 121  Bit Score: 45.80  E-value: 4.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   5 LNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWL--CLSLDEArtqPRARdYTHYAFSV-APEHIERVSER 81
Cdd:cd09013    7 LAHVELLTPKPEESLWFFTDVLGLEETHREGQSVYLRAWGDWEhhTLKLTES---PEAG-LGHIAWRAsSPEALERRVAA 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 727180921  82 LRQSGAE-EWKSNRS-EGESLYFLDPDGHQLEI 112
Cdd:cd09013   83 LEASGVGiGWIDGDLgQGPAYRFQSPDGHPMEI 115
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 7-115 5.53e-07

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.


Pssm-ID: 319931  Cd Length: 132  Bit Score: 45.39  E-value: 5.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   7 HLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAylSLGALWLCLSLDE-----ARTQPRARDYTHYAFSVAP-EHIERVSE 80
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRVSDRIVDPG--VDGGAFLHCDRGTdhhtvALAGGPHPGLHHVAFEVHDlDDVGRGHD 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 727180921  81 RLRQSGAE-EWKSNR---SEGESLYFLDPDGHQLEIHAG 115
Cdd:cd08343   80 RLREKGYKiEWGPGRhglGSQVFDYWFDPSGNRVEYYTD 118
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 10-112 3.16e-06

uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319962  Cd Length: 121  Bit Score: 43.25  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921  10 LAVSDLDRSFDFYRHLLGFTphARWQGGAYLSLGAL-------WLCLSLDEART----QPRARDYTHYAFSVAPEHIERV 78
Cdd:cd16355    5 LNVSDIPASFAWFEKVLGFQ--KDWDWGDPPTFGSVgsgeceiFLCQGGQGGSLrlgpCGDALPSYGAWMSVWVDDVDAL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 727180921  79 SERLRQSGAE--------EWKSnrsegESLYFLDPDGHQLEI 112
Cdd:cd16355   83 HRECRARGADirqpptdmPWGM-----REMHVRHPDGHRFRV 119
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
10-114 5.38e-06

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 42.54  E-value: 5.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921  10 LAVSDLDRSFDFYRHLLGFTPHARWQGG------AYLSLGALWLCLSlDEARTQPRARDyTHYAFSVAPEHIERVSERLR 83
Cdd:COG2764    6 LVVDDAEEALEFYEDVFGFEVVFRMTDPdgkimhAELRIGGSVLMLS-DAPPDSPAAEG-NGVSLSLYVDDVDALFARLV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 727180921  84 QSGAE--------EWksnrseGESLY-FLDPDGHQLEIHA 114
Cdd:COG2764   84 AAGATvvmplqdtFW------GDRFGmVRDPFGVLWMINT 117
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 5-114 1.59e-05

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.


Pssm-ID: 319927  Cd Length: 118  Bit Score: 41.24  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   5 LNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSlgalwlclSLDEAR------TQPRARDYTHYAFSVA-PEHIER 77
Cdd:cd07266    5 LAHAELVVTDLAASREFYVDTLGLHVTDEDDNAIYLR--------GVEEFIhhtlvlRKAPEAAVGHLGFRVRdEADLDK 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 727180921  78 VSERLRQSG-AEEWKSNRSEGESLYFLDPDGHQLEIHA 114
Cdd:cd07266   77 AAAFYKELGlPTEWREEPGQGRTLRVEDPFGFPIEFYL 114
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 5-112 2.09e-05

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.


Pssm-ID: 319905  Cd Length: 125  Bit Score: 41.24  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   5 LNHLTLAVSDLDRSFDFYRHLLGFTP----HARWQG--GAYLSL--GALWLCLSLDEARTQP---RARDYTHYAFSV-AP 72
Cdd:cd07241    2 IEHVALWTNDLERMKDFYVKYFGAESndiyHNKKKGfrSYFLTFdsGARLELMSRPDVTDPDkevERTGLAHIAFSVgSK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 727180921  73 EHIERVSERLRQSGAEEWKSNRSEGESLY---FLDPDGHQLEI 112
Cdd:cd07241   82 EAVDELTERLRADGYAVVGGPRTTGDGYYesvILDPEGNRIEI 124
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-114 2.85e-05

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.


Pssm-ID: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 40.91  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   7 HLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWLCLSLDEARTQPRARDYtHYAFSV-APEHIERVSERLRQS 85
Cdd:cd07254    4 HLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFMLEDPPLNLALLVNDRKEPYGLN-HLGIQVdSKEEVAALKARAEAA 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 727180921  86 GAEEWKSNRSE-----GESLYFLDPDGHQLEIHA 114
Cdd:cd07254   83 GLPVRKEPRTTccyavQDKFWLTDPDGNAWEFYA 116
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 4-115 6.89e-05

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; 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.


Pssm-ID: 319906  Cd Length: 126  Bit Score: 39.78  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   4 GLNHLTLAVSDLDRSFDFYRHLL--GFTPHARWQGG-AYLSLGALWLCLSLDEARTQP---RAR-DYTHYAFSVAP-EHI 75
Cdd:cd07242    1 GVSHVELAVSDLHRSFKWFEWILglGWKEYDTWSFGpSWKLSGGSLLVVQQTDEFATPefdRARvGLNHLAFHAESrEAV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 727180921  76 ERVSERLRQSGAEEWKSNRS------EGESLYFLDPDGHQLEIHAG 115
Cdd:cd07242   81 DELTEKLAKIGGVRTYGDRHpfaggpPHYAAFCEDPDGIKLELVAP 126
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-113 9.32e-05

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.


Pssm-ID: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 39.13  E-value: 9.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   5 LNHLTLAVSDLDRSFDFYRHL---LGFTPhaRWQGGAYLSLG-----ALWLCLSLDEARTQPRARdyTHYAFSVA-PEHI 75
Cdd:cd07262    1 ISHVTIGVNDLERSRAFYDAAlapLGYKR--GFEDGGRVGYGleggpDFWVTEPFDGEPATAGNG--THVAFAAPsRAAV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 727180921  76 ERVSERLRQSGAeewKSN-----RSEGESLYF----LDPDGHQLEIH 113
Cdd:cd07262   77 DAFHAAALAAGG---TDNgapglRPHYHPGYYaayvRDPDGNKIEAV 120
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 10-110 9.48e-05

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.


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 39.13  E-value: 9.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921  10 LAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWLCLSLDEARTQPRARDYThyAFSVAPEHIERVSERLRQSG--A 87
Cdd:cd08349    4 LPVRDIDKTLAFYVDVLGFEVDYERPPPGYAILSRGGVELHLFEHPGLDPAGSGV--AAYIRVEDIDALHAELKAAGlpL 81

                         90       100
                 ....*....|....*....|....*....
gi 727180921  88 EEWKSNRSEGESLY----FL--DPDGHQL 110
Cdd:cd08349   82 FGIPRITPIEDKPWgmreFAvvDPDGNLL 110
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 5-123 1.71e-04

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


Pssm-ID: 433233  Cd Length: 175  Bit Score: 39.24  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921    5 LNHLTLAVSDLDRSFDFYRHLLGFTP-----HARWQ--------GGAYLSLgalwlcLSLDEARTQPR-----ARDYTHY 66
Cdd:pfam13468   1 LDHVVLAVPDLDEAAARFARALGFTVtpggrHPGMGtanalimfGDGYLEL------LAVDPEAPAPPrgrwfGLDRLAD 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727180921   67 -----AFSVAPEHIERVSERLRQSGAEEWKSNRSEGESLYFldpdgHQLEIHAGDLASRLAA 123
Cdd:pfam13468  75 gegllGWALRTDDIDAVAARLRAAGVEPGRRVRPDGGDLRW-----RLLFLADGALPAGGLL 131
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 1-34 2.39e-04

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


Pssm-ID: 442418 [Multi-domain]  Cd Length: 333  Bit Score: 39.49  E-value: 2.39e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 727180921   1 MLTGLNHLTLAVS--DLDRSFDFYRHLLGFTPHARW 34
Cdd:COG3185  143 GLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEIREE 178
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 7-86 3.18e-04

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.


Pssm-ID: 319964  Cd Length: 114  Bit Score: 37.92  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   7 HLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLGALWLCLSLDEARTQ-PRARDYTHYAFSVAPEHIERVSERLRQS 85
Cdd:cd16357    1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSEKSALLGYGEDQAKLELVDIPEPvDHGTAFGRIAFSCPADELPPIEEKVKAA 80


                 .
gi 727180921  86 G 86
Cdd:cd16357   81 G 81
2_3_CTD_N cd07265
N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, ...
 5-114 9.11e-04

N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, non-catalytic, domain of catechol 2,3-dioxygenase. Catechol 2,3-dioxygenase (2,3-CTD, catechol:oxygen 2,3-oxidoreductase) catalyzes an extradiol cleavage of catechol to form 2-hydroxymuconate semialdehyde with the insertion of two atoms of oxygen. The enzyme is a homotetramer and contains catalytically essential Fe(II) . The reaction proceeds by an ordered bi-unit mechanism. First, catechol binds to the enzyme, this is then followed by the binding of dioxygen to form a tertiary complex, and then the aromatic ring is cleaved to produce 2-hydroxymuconate semialdehyde. Catechol 2,3-dioxygenase belongs to the type I extradiol dioxygenase family. The subunit comprises 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. This subfamily represents the N-terminal domain.


Pssm-ID: 319926  Cd Length: 122  Bit Score: 36.56  E-value: 9.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   5 LNHLTLAVSDLDRSFDFYRHLLGFTPHAR-WQGGAYLSLGALW--LCLSLDEARTQprarDYTHYAFSVAP-EHIERVSE 80
Cdd:cd07265    5 PGHVQLRVLDLEEAIKHYREVLGLVETGRdDQGRVYLKAWDEYdhHSIILREADTA----GLDFMGFKVLDdADLEQLEA 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 727180921  81 RLRQSGAEEWK----SNRSEGESLYFLDPDGHQLEIHA 114
Cdd:cd07265   81 RLQAYGVTVTRipagELPGVGRRVRFQLPSGHTMELYA 118
VOC_BsCatE_like_C cd16359
C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; ...
 7-107 1.18e-03

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.


Pssm-ID: 319966  Cd Length: 110  Bit Score: 36.19  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   7 HLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYLSLG------ALWLCLSLDEARTQPRARDYTHYAFSVA-PEHIERVS 79
Cdd:cd16359    2 HIHLRVSDLKAASHFYHQVLGFDIKSRRPGALFLSAGgyhhhiGLNTWAGRGLPLPPEDATGLAYFTIVLPdQEALAAIL 81

                         90       100
                 ....*....|....*....|....*...
gi 727180921  80 ERLRQSGAEEWKSNrsegESLYFLDPDG 107
Cdd:cd16359   82 ERLDLAGYDVEALD----DGLELTDPWG 105
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 2-118 1.25e-03

N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Rhodococcus rhodochrous K37, and similar proteins; 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). The enzyme contains a N-terminal and a C-terminal domain of similar structure fold, resulting from an ancient gene duplication. BphC belongs to the type I extradiol dioxygenase family, which requires a metal in the active site for its catalytic activity. Polychlorinated biphenyl degrading bacteria demonstrate multiplicity of BphCs. Bacterium Rhodococcus rhodochrous K37 has eight genes encoding BphC enzymes. This family includes the N-terminal domain of BphC5-RrK37. The crystal structure of the protein from Novosphingobium aromaticivorans has a Mn(II)in the active site, although most proteins of type I extradiol dioxygenases are activated by Fe(II).


Pssm-ID: 319950 [Multi-domain]  Cd Length: 120  Bit Score: 36.07  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   2 LTGLNHLTLAVSDLDRSFDFYRHLLGFTPHARWQGGAYL-SLGALWLCLSLDEArTQPRARdytHYAFSVA-PEHIERVS 79
Cdd:cd08362    1 VTHLRYVALGVPDLAAEREFYTEVWGLEEVAEDDDVVYLrAEGSEHHVLRLRQS-DENRLD---LIAFAAAtRADVDALA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 727180921  80 ERLRQSG----AEEWKSNR-SEGESLYFLDPDGHQLEIHAGDLA 118
Cdd:cd08362   77 ARLAAAGvrilSEPGPLDDpGGGYGFRFFDPDGRTIEVSADVAA 120
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 7-108 1.80e-03

Glyoxalase-like domain; This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.


Pssm-ID: 436220  Cd Length: 110  Bit Score: 35.82  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921    7 HLTLAVSDLDRSFDFYRHLLGFTPHAR------WQGGAYLSLGALWLCLSLDEARTQPRARdyTHyaFSVAPEHIERVSE 80
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDdtalpdPDGGGPIGGGGPRLLFQRVPEPKPGKNR--VH--LDLAVDDLEAAVA 76

                          90       100
                  ....*....|....*....|....*....
gi 727180921   81 RLRQSGAEE-WKSNRSEGESLYFLDPDGH 108
Cdd:pfam18029  77 RLVALGATVlDDGDDPDGGRWVLADPEGN 105
HPCD_C_class_II cd07256
C-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 5-116 3.99e-03

C-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily contains the C-terminal, 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.


Pssm-ID: 319919  Cd Length: 160  Bit Score: 35.55  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   5 LNHLTLAVSDLDRSFDFYRHLlGF-----------TPHARW---QGGAYlslgalwlclslDEARTQPRARDYTHYAFSV 70
Cdd:cd07256    4 IDHFNQRVPDVDAGLRYYEDL-GFrvseytedddgETWAAWmhrKGGVH------------DTALTNGNGPRLHHVAFWV 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 727180921  71 -APEHIERVSERL---RQSGAEEWKSNR---SEGESLYFLDPDGHQLEIHAGD 116
Cdd:cd07256   71 pEPHNIIQTCDLMaaaRYSDRIERGPGRhgvSNAFFLYILDPDGHRIEIYTSD 123
PRK11478 PRK11478
VOC family protein;
2-113 4.53e-03

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 34.87  E-value: 4.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   2 LTGLNHLTLAVSDLDRSFDFYRHLLGFTPHAR--------WQGGayLSLGALWL----CLSLDEAR-TQPRARDYTHYAF 68
Cdd:PRK11478   4 LKQVHHIAIIATDYAVSKAFYCDILGFTLQSEvyreardsWKGD--LALNGQYVielfSFPFPPERpSRPEACGLRHLAF 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 727180921  69 SVapEHIERVSERLRQSGA--EEWKSNRSEGESL-YFLDPDGHQLEIH 113
Cdd:PRK11478  82 SV--DDIDAAVAHLESHNVkcEAIRVDPYTQKRFtFFNDPDGLPLELY 127
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-113 8.01e-03

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


Pssm-ID: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 34.19  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921   7 HLTLAVSDLDRSFDFYRHLLGFTPHARWQGGaylslGALWLCL---------------SLDEARTQPRARDYTHYAFSVA 71
Cdd:cd07263    1 QVMLYVDDQDKALDFYVEKLGFEVVEDVPMG-----GMRWVTVappgspgtslllepkAHPAQMPQSPEAAGGTPGILLA 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 727180921  72 PEHIERVSERLRQSGAEEWKSNRSEGESL--YFLDPDGHQLEIH 113
Cdd:cd07263   76 TDDIDATYERLTAAGVTFVQEPTQMGGGRvaNFRDPDGNLFALM 119
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-112 8.28e-03

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.


Pssm-ID: 319953  Cd Length: 122  Bit Score: 33.98  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727180921  10 LAVSDLDRSFDFYRHLLG------FTPHARWQGGAYLSLGALWL-CLSLDEARTQPRARDYTHYaFSVapEHIERVSERL 82
Cdd:cd09011    8 LVVKDIEKSKKFYEDVLGqkilldFGENVVFEGGFALQEKKSWLeTIIISDLSIKQQSNNFELY-FEV--DDFDAFFEKL 84

                         90       100       110
                 ....*....|....*....|....*....|....
gi 727180921  83 RQSGAEEW----KSNRSEGESLYFLDPDGHQLEI 112
Cdd:cd09011   85 NPHKDIEFihpiLEHPWGQRVFRFYDPDGHIIEI 118
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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