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Conserved domains on  [gi|1384944075|gb|AWG41960|]
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FosA [Klebsiella variicola]

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 ...
 4-128 3.35e-70

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: 206.75  E-value: 3.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   4 GLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGDLWLCLSLDPQrriiPPEESDYTHYAFSISEADFASFAAR 83
Cdd:cd07244     1 GINHITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYLTAGDLWLCLSLDPA----AEPSPDYTHIAFTVSEEDFEELSER 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1384944075  84 LEVAGVAVWKLNRSEGASHYFLDPDGHKLELHVGSLAQRLAACRE 128
Cdd:cd07244    77 LRAAGVKIWQENSSEGDSLYFLDPDGHKLELHVGSLESRLASLRE 121
 
Name Accession Description Interval E-value
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 4-128 3.35e-70

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: 206.75  E-value: 3.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   4 GLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGDLWLCLSLDPQrriiPPEESDYTHYAFSISEADFASFAAR 83
Cdd:cd07244     1 GINHITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYLTAGDLWLCLSLDPA----AEPSPDYTHIAFTVSEEDFEELSER 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1384944075  84 LEVAGVAVWKLNRSEGASHYFLDPDGHKLELHVGSLAQRLAACRE 128
Cdd:cd07244    77 LRAAGVKIWQENSSEGDSLYFLDPDGHKLELHVGSLESRLASLRE 121
PRK04101 PRK04101
metallothiol transferase FosB;
1-138 1.12e-34

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 117.35  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   1 MLSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGDLWLCLSLDPQrriIPPEE--SDYTHYAFSISEADFA 78
Cdd:PRK04101    1 MLKGINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWIALNEEKD---IPRNEihQSYTHIAFSIEEEDFD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1384944075  79 SFAARLEVAGVAVWK-LNRSE--GASHYFLDPDGHKLELHVGSLAQRLAACREQPyKGMVFFD 138
Cdd:PRK04101   78 HWYQRLKENDVNILPgRERDErdKKSIYFTDPDGHKFEFHTGTLQDRLNYYKEEK-PHMTFYD 139
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
2-114 3.83e-20

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 80.00  E-value: 3.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   2 LSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFC--GDLWLCLSLDPQRRiIPPEESDYTHYAFSI-SEADFA 78
Cdd:COG2514     1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdgGEHLLVLEEAPGAP-PRPGAAGLDHVAFRVpSRADLD 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1384944075  79 SFAARLEVAGVAV-WKLNRSEGASHYFLDPDGHKLEL 114
Cdd:COG2514    80 AALARLAAAGVPVeGAVDHGVGESLYFRDPDGNLIEL 116
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-114 3.13e-17

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 72.10  E-value: 3.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   4 GLNHLTLAVSQLAPSVAFYQQLLGMTLHARWD-------SGAYLFCGDLWLCLSLDPQRRIIPPEESDYTHYAFSISEAD 76
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDageegglRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1384944075  77 FASFAARLEVAGVAVWKLNRSEGASH---YFLDPDGHKLEL 114
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 ...
 4-128 3.35e-70

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: 206.75  E-value: 3.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   4 GLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGDLWLCLSLDPQrriiPPEESDYTHYAFSISEADFASFAAR 83
Cdd:cd07244     1 GINHITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYLTAGDLWLCLSLDPA----AEPSPDYTHIAFTVSEEDFEELSER 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1384944075  84 LEVAGVAVWKLNRSEGASHYFLDPDGHKLELHVGSLAQRLAACRE 128
Cdd:cd07244    77 LRAAGVKIWQENSSEGDSLYFLDPDGHKLELHVGSLESRLASLRE 121
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 7-119 5.03e-35

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: 117.66  E-value: 5.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   7 HLTLAVSQLAPSVAFYQQLLGMTLHARWDS-------GAYLFCGDLWLCLSLDPQrriipPEESDYTHYAFSISEADFAS 79
Cdd:cd08345     1 HITLIVRDLEKSTAFLQDIFGAREVYSSGDktfslskEKFFLLGGLWIALMEGES-----LQERSYTHIAFQIQSEDFDR 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1384944075  80 FAARLEVAGVAVWKLNRS---EGASHYFLDPDGHKLELHVGSL 119
Cdd:cd08345    76 YAERLGALGVEMRPPRPRvegEGRSIYFYDPDNHLFELHTGTL 118
PRK04101 PRK04101
metallothiol transferase FosB;
1-138 1.12e-34

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 117.35  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   1 MLSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGDLWLCLSLDPQrriIPPEE--SDYTHYAFSISEADFA 78
Cdd:PRK04101    1 MLKGINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWIALNEEKD---IPRNEihQSYTHIAFSIEEEDFD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1384944075  79 SFAARLEVAGVAVWK-LNRSE--GASHYFLDPDGHKLELHVGSLAQRLAACREQPyKGMVFFD 138
Cdd:PRK04101   78 HWYQRLKENDVNILPgRERDErdKKSIYFTDPDGHKFEFHTGTLQDRLNYYKEEK-PHMTFYD 139
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 5-129 1.66e-31

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: 108.98  E-value: 1.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   5 LNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGDLWLCLSLDPQrriIPPEESD--YTHYAFSISEADFASFAA 82
Cdd:cd08363     1 INHITFSVSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNGLWLALNVQED---IPRNEIShsYTHIAFSIDEEDLDAFKE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1384944075  83 RLEVAGVAVWKlNRS----EGASHYFLDPDGHKLELHVGSLAQRLAACREQ 129
Cdd:cd08363    78 RLKDNGVNILE-GRKrdilEGQSIYFTDPDGHLFELHTGTLEDRLEYYKEE 127
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 3-125 6.28e-23

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: 86.94  E-value: 6.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   3 SGLNHLTLAVSQLAPSVAFYQQLLGmtlhAR--WDSGAYLFC---------GDLWLCLSLDPqrriiPPEESDYTHYAFS 71
Cdd:cd08364     2 EGISHITFIVKDLDRTAAFLTEIFG----AEevYDSGAETFSlspekffliGGLWIAIMEGE-----PLLERSYNHIAFK 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1384944075  72 ISEADFASFAARLEVAGVAVwKLNRS----EGASHYFLDPDGHKLELHVGSLAQRLAA 125
Cdd:cd08364    73 VSEGDLDEYRARIKKLGLEI-RPPRSrvqgEGRSLYFYDFDNHLFELHTGTLEERLAR 129
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
2-114 3.83e-20

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 80.00  E-value: 3.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   2 LSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFC--GDLWLCLSLDPQRRiIPPEESDYTHYAFSI-SEADFA 78
Cdd:COG2514     1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRAdgGEHLLVLEEAPGAP-PRPGAAGLDHVAFRVpSRADLD 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1384944075  79 SFAARLEVAGVAV-WKLNRSEGASHYFLDPDGHKLEL 114
Cdd:COG2514    80 AALARLAAAGVPVeGAVDHGVGESLYFRDPDGNLIEL 116
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 4-115 1.22e-18

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: 75.80  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   4 GLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSG------AYLFCGD---LWLCLSLDPQRriiPPEESDYTHYAFSISe 74
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGdggfghAFLRLGDgteLELFEAPGAAP---APGGGGLHHLAFRVD- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1384944075  75 aDFASFAARLEVAGVAVWKLNRSEGASH---YFLDPDGHKLELH 115
Cdd:COG0346    78 -DLDAAYARLRAAGVEIEGEPRDRAYGYrsaYFRDPDGNLIELV 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-114 3.13e-17

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 72.10  E-value: 3.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   4 GLNHLTLAVSQLAPSVAFYQQLLGMTLHARWD-------SGAYLFCGDLWLCLSLDPQRRIIPPEESDYTHYAFSISEAD 76
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDageegglRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1384944075  77 FASFAARLEVAGVAVWKLNRSEGASH---YFLDPDGHKLEL 114
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGrysYFRDPDGNLIEL 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-114 1.43e-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: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   7 HLTLAVSQLAPSVAFYQQLLGMTLHARWDSG--AYLFCGDLwLCLSLDPQRRIIPPEESDYTHYAFSI-SEADFASFAAR 83
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGgfAFLRLGPG-LRLALLEGPEPERPGGGGLFHLAFEVdDVDEVDERLRE 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1384944075  84 LEVAGVAVWKLN--RSEGASHYFLDPDGHKLEL 114
Cdd:cd06587    80 AGAEGELVAPPVddPWGGRSFYFRDPDGNLIEF 112
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-114 2.27e-11

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: 56.99  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075  10 LAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGDLWLcLSLDPQ-------RRIIPPEE-SDYTHYAFSISEADFASFA 81
Cdd:cd08354     6 LYADDLDAAEAFYEDVLGLKPMLRSGRHAFFRLGPQVL-LVFDPGatskdvrTGEVPGHGaSGHGHFAFAVPTEELAAWE 84

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1384944075  82 ARLEVAGVAVWKLNRSE--GASHYFLDPDGHKLEL 114
Cdd:cd08354    85 ARLEAKGVPIESYTQWPegGKSLYFRDPAGNLVEL 119
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-114 6.29e-11

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: 55.79  E-value: 6.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   5 LNHLTLAVSQLAPSVAFYQQLLGMTLHARWDS----GAYLFCGDLW-LCLSLDPQRRIIPPEESDY--THYAFSIseADF 77
Cdd:cd07245     1 LDHVALACPDLERARRFYTDVLGLEEVPRPPFlkfgGAWLYLGGGQqIHLVVEQNPSELPRPEHPGrdRHPSFSV--PDL 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1384944075  78 ASFAARLEVAGVAVWKLNRSEGASH--YFLDPDGHKLEL 114
Cdd:cd07245    79 DALKQRLKEAGIPYTESTSPGGGVTqlFFRDPDGNRLEF 117
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-115 1.33e-08

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 49.63  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   1 MLSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYlfcgdlWLCLSLDPQRRII---PPEESDYTHYAFSISEADF 77
Cdd:COG3324     1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGD------YAEFDTDGGQVGGlmpGAEEPGGPGWLLYFAVDDL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1384944075  78 ASFAARLEVAGVAVWKLNRSE---GASHYFLDPDGHKLELH 115
Cdd:COG3324    75 DAAVARVEAAGGTVLRPPTDIppwGRFAVFRDPEGNRFGLW 115
ChaP_like cd08351
ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and ...
 5-114 4.25e-08

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: 48.27  E-value: 4.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   5 LNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGDLwLCLSLDPQRRIIPPeesdyTHYAFSISEADFASFAARL 84
Cdd:cd08351     3 LNHTIVPARDKEASARFLAEILGLPAPPPWGPFAPVRLNNG-LTLDFADPRGEIAP-----QHYAFLVSDDEFDAILARI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1384944075  85 EVAGVAVW---------KLNRSEGASH-YFLDPDGHKLEL 114
Cdd:cd08351    77 RARGLEYWadpqhrepgEINHNDGGRGvYFRDPDGHLLEI 116
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 5-121 6.53e-08

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.


Pssm-ID: 319936  Cd Length: 137  Bit Score: 48.29  E-value: 6.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   5 LNHLTLAVSQLAP--SVAFYQQLLGMTLHARWDSGAYLFCG--DLWLCLSLDPQRRIIPPEES---DYTHYAFSI-SEAD 76
Cdd:cd08348     2 LAHFVLRTNPEKFeaMVQWYLDILGARIVARNAKGCFLSFDeeHHRIAIFGAPGGAQPPDKRPtrvGLAHIAFTYaSLDD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1384944075  77 FASFAARLEVAGV-AVWKLNRSEGASHYFLDPDGHKLELHVGSLAQ 121
Cdd:cd08348    82 LARNYAQLKERGIkPVWPVNHGVTTSIYYRDPDGNMLEMQVDNFDT 127
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 3-115 1.28e-07

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: 47.15  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   3 SGLNHLTLAVSQLAPSVAFYQQLLGMTL---HARWDSGAYLF---CGDLWLCL--SLDPQRRIIPPEESDYTHYAFSIse 74
Cdd:cd08352     1 KKIHHIAIICSDYEKSKDFYVDKLGFEIireHYRPERNDIKLdlaLGGYQLELfiKPDAPARPSYPEALGLRHLAFKV-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1384944075  75 ADFASFAARLEVAGVAVWKLNRSE--GASHYFL-DPDGHKLELH 115
Cdd:cd08352    79 EDVEATVAELKSLGIETEPIRVDDftGKKFTFFfDPDGLPLELY 122
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 4-116 1.78e-07

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: 46.92  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   4 GLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCG---DLwLCLSLDPQRRIIPPEESDYTHYAFSI-SEADFAS 79
Cdd:cd07255     2 RIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDgkqVL-LVLEAIPDAVLAPRSTTGLYHFAILLpDRKALGR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1384944075  80 FAARLevagvavWKLNRSEGAS-H------YFLDPDGHKLELHV 116
Cdd:cd07255    81 ALAHL-------AEHGPLIGAAdHgvseaiYLSDPEGNGIEIYA 117
BphC-JF8_N_like cd09013
N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 2-114 1.47e-06

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: 44.26  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   2 LSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGDLWLCLSLdpqrRIIPPEESDYTHYAFSI-SEADFASF 80
Cdd:cd09013     4 LAQLAHVELLTPKPEESLWFFTDVLGLEETHREGQSVYLRAWGDWEHHTL----KLTESPEAGLGHIAWRAsSPEALERR 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1384944075  81 AARLEVAGVAV-WKLNRS-EGASHYFLDPDGHKLEL 114
Cdd:cd09013    80 VAALEASGVGIgWIDGDLgQGPAYRFQSPDGHPMEI 115
BphC1-RGP6_N_like cd07252
N-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ...
 3-117 2.64e-06

N-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the N-terminal, non-catalytic, domain of BphC1-RGP6 and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, 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. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of 2,3-dihydroxybiphenyl 1,2-dioxygenases. 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. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, and has Fe(II) at the catalytic site. Its N-terminal repeat is represented in this subfamily. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, they belong to a different family, the ED_TypeI_classII_C (C-terminal domain of type I, class II extradiol dioxygenases) family.


Pssm-ID: 319915  Cd Length: 120  Bit Score: 43.74  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   3 SGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGDLWlclsldPQRRIIPPEESD---YTHYAFSiSEADFAS 79
Cdd:cd07252     1 RSLGYLGFEVSDLDAWREFATDVLGLQVADDGPDDALYLRMDDR------AHRIAVHPGEVDdlaYAGWEVA-DEAALDA 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1384944075  80 FAARLEVAGVAVWKLNRSEGASH------YFLDPDGHKLELHVG 117
Cdd:cd07252    74 LAERLEAAGIEVTTGSAELAAERgvlgliKFTDPSGNPHEIFYG 117
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 9-114 3.47e-06

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 43.28  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   9 TLAVSQLAPSVAFYQQLlGMTLHARWDSGAYLFC---GDLWLCL-SLDPQRRIIPPEESDYTHYA---FSI---SEADFA 78
Cdd:COG3607     8 NLPVADLERSRAFYEAL-GFTFNPQFSDEGAACFvlgEGIVLMLlPREKFATFTGKPIADATGFTevlLALnveSREEVD 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1384944075  79 SFAARLEVAGVAVWKLNRSEGA--SHYFLDPDGHKLEL 114
Cdd:COG3607    87 ALVAKALAAGGTVLKPPQDVGGmySGYFADPDGHLWEV 124
2_3_CTD_N cd07265
N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, ...
 5-116 1.98e-05

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: 41.18  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   5 LNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSG-AYLFCGDLWlclslDPQRRII-PPEESDYTHYAFSI-SEADFASFA 81
Cdd:cd07265     5 PGHVQLRVLDLEEAIKHYREVLGLVETGRDDQGrVYLKAWDEY-----DHHSIILrEADTAGLDFMGFKVlDDADLEQLE 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1384944075  82 ARLEVAGVAVWKL----NRSEGASHYFLDPDGHKLELHV 116
Cdd:cd07265    80 ARLQAYGVTVTRIpageLPGVGRRVRFQLPSGHTMELYA 118
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-113 6.16e-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: 39.90  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   5 LNHLTLAVSQLAPSVAFYQQLLG-MTLHARWDSGAYLFCG-----DLWLCLSLDPQrriiPPEESDYTHYAF---SISEA 75
Cdd:cd07262     1 ISHVTIGVNDLERSRAFYDAALApLGYKRGFEDGGRVGYGleggpDFWVTEPFDGE----PATAGNGTHVAFaapSRAAV 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1384944075  76 DfASFAARLEVAGvavwklnRSEGA------------SHYFLDPDGHKLE 113
Cdd:cd07262    77 D-AFHAAALAAGG-------TDNGApglrphyhpgyyAAYVRDPDGNKIE 118
MhqB_like_N cd08344
N-terminal domain of MhqB, a type I extradiol dioxygenase, and similar proteins; This ...
 3-117 6.45e-05

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.


Pssm-ID: 319932  Cd Length: 112  Bit Score: 39.71  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   3 SGLNHLTLAVSQLAPSVAFYQqLLGMTLHARWDsgaylfcgDLWLCLSLDPQR--RIIPPEESDYTHYAFSISEADFASF 80
Cdd:cd08344     1 HSIDHFALEVPDLEVARRFYE-AFGLDVRETGE--------DLELRAPGNDHVwaRLIQGARKRLAYLSFGIFGDDLARF 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1384944075  81 AARLEVAGVAVWKLNRSEGASH-YFLDPDGHKLELHVG 117
Cdd:cd08344    72 AAHLDAAGVALIAAPPGADPDGvWFEDPDGNLLQVRVA 109
PRK11478 PRK11478
VOC family protein;
2-115 6.57e-04

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 37.18  E-value: 6.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   2 LSGLNHLTLAVSQLAPSVAFYQQLLGMTLHAR-WDSGAYLFCGDLWL-------CLSLD-PQRRIIPPEESDYTHYAFSI 72
Cdd:PRK11478    4 LKQVHHIAIIATDYAVSKAFYCDILGFTLQSEvYREARDSWKGDLALngqyvieLFSFPfPPERPSRPEACGLRHLAFSV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1384944075  73 SEADFAsfAARLEVAGV---AVWKLNRSEGASHYFLDPDGHKLELH 115
Cdd:PRK11478   84 DDIDAA--VAHLESHNVkceAIRVDPYTQKRFTFFNDPDGLPLELY 127
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-116 1.32e-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: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 36.29  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   7 HLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGDLWLCLSLDPQRRiiPPEESDYtHYAFSISEAD-FASFAARLE 85
Cdd:cd07254     4 HLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFMLEDPPLNLALLVNDR--KEPYGLN-HLGIQVDSKEeVAALKARAE 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1384944075  86 VAGVAVWKLNRSE-----GASHYFLDPDGHKLELHV 116
Cdd:cd07254    81 AAGLPVRKEPRTTccyavQDKFWLTDPDGNAWEFYA 116
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 2-114 1.71e-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: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   2 LSGLNHLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFC-GDLWLCLSL--DPQRRIippeesdyTHYAFS-ISEADF 77
Cdd:cd08362     1 VTHLRYVALGVPDLAAEREFYTEVWGLEEVAEDDDVVYLRAeGSEHHVLRLrqSDENRL--------DLIAFAaATRADV 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1384944075  78 ASFAARLEVAGVavwKLNRSEGASH-----Y---FLDPDGHKLEL 114
Cdd:cd08362    73 DALAARLAAAGV---RILSEPGPLDdpgggYgfrFFDPDGRTIEV 114
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 7-44 2.12e-03

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: 35.61  E-value: 2.12e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1384944075   7 HLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGD 44
Cdd:cd16357     1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSEKSALLGYGE 38
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 7-117 2.39e-03

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: 35.37  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   7 HLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFC-GDLWLCLsldpqrRIIPPEESDYTHYAFSI-SEADFASFAARL 84
Cdd:cd16360     1 YAELGVPDLEKALEFYTDVLGLQVAKRDGNSVYLRGyEDEHHSL------VLYEAPEAGLKHFAFEVaSEEDLERAAASL 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1384944075  85 EVAGVAVWKLNRSE----GASHYFLDPDGHKLELHVG 117
Cdd:cd16360    75 TALGCDVTWGPDGEvpggGKGFRFQDPSGHLLELFVE 111
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 1-35 2.77e-03

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: 36.41  E-value: 2.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1384944075   1 MLSGLNHLTLAVS--QLAPSVAFYQQLLGMTLHARWD 35
Cdd:COG3185   143 GLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEIREED 179
VOC_BsCatE_like_C cd16359
C-terminal of Bacillus subtilis CatE like protein, a vicinal oxygen chelate subfamily; ...
 7-114 5.26e-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: 34.65  E-value: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   7 HLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAYLFCGD----LWLCLSLDPQRRIIPPEESDYTHYAFSISE-ADFASFA 81
Cdd:cd16359     2 HIHLRVSDLKAASHFYHQVLGFDIKSRRPGALFLSAGGyhhhIGLNTWAGRGLPLPPEDATGLAYFTIVLPDqEALAAIL 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1384944075  82 ARLEVAGVAVWKLNrsegASHYFLDPDGHKLEL 114
Cdd:cd16359    82 ERLDLAGYDVEALD----DGLELTDPWGITVKF 110
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-115 5.34e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 34.61  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1384944075   7 HLTLAVSQLAPSVAFYQQLLGMTLHARWDSGAY--LFCGDLWLCL-SLDPQRRIIPPEESDyTHYAFSISEADFASFAAR 83
Cdd:cd07264     3 YIVLYVDDFAASLRFYRDVLGLPPRFLHEEGEYaeFDTGETKLALfSRKEMARSGGPDRRG-SAFELGFEVDDVEATVEE 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1384944075  84 LEVAGVAVWKLNRSEGASH---YFLDPDGHKLELH 115
Cdd:cd07264    82 LVERGAEFVREPANKPWGQtvaYVRDPDGNLIEIC 116
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 5-35 5.44e-03

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.


Pssm-ID: 319900 [Multi-domain]  Cd Length: 142  Bit Score: 34.99  E-value: 5.44e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1384944075   5 LNHLTLAVSQLAPSVAFYQQLLGMTLHARWD 35
Cdd:cd07233     1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKD 31
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 10-60 7.68e-03

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: 34.12  E-value: 7.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1384944075  10 LAVSQLAPSVAFYQQLLGMTL--HARWDSGAYLFCGDLWLCLSLDPQRRIIPP 60
Cdd:cd08349     4 LPVRDIDKTLAFYVDVLGFEVdyERPPPGYAILSRGGVELHLFEHPGLDPAGS 56
 
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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