NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|924872605|ref|WP_053551311|]
View 

VOC family protein [Desulfuromonas soudanensis]

Protein Classification

VOC family protein( domain architecture ID 10001243)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms

CATH:  3.10.180.10
Gene Ontology:  GO:0046872|GO:0003824
PubMed:  21820381|11076500

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 13-116 1.17e-13

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: 63.47  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  13 GINHVALEVDDVDAALEFYGRLFEIKLRGRHD------GMAFIDLGDQF-INLSPRRSQQPDQA----RHFGLVVDDREK 81
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDfgdggfGHAFLRLGDGTeLELFEAPGAAPAPGggglHHLAFRVDDLDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 924872605  82 VRQALKGTKATILPSPGLD--------FLDPWGNHVQVVQYRD 116
Cdd:COG0346   82 AYARLRAAGVEIEGEPRDRaygyrsayFRDPDGNLIELVEPPP 124
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 13-116 1.17e-13

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: 63.47  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  13 GINHVALEVDDVDAALEFYGRLFEIKLRGRHD------GMAFIDLGDQF-INLSPRRSQQPDQA----RHFGLVVDDREK 81
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDfgdggfGHAFLRLGDGTeLELFEAPGAAPAPGggglHHLAFRVDDLDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 924872605  82 VRQALKGTKATILPSPGLD--------FLDPWGNHVQVVQYRD 116
Cdd:COG0346   82 AYARLRAAGVEIEGEPRDRaygyrsayFRDPDGNLIELVEPPP 124
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 13-109 1.49e-10

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: 54.98  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  13 GINHVALEVDDVDAALEFYGRLFEIKLRGRHDGMAFIDLGDQFINLS--PRRSQQPDQArHFGLVVD--DREKVRQALKG 88
Cdd:cd07244    1 GINHITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYLTAGDLWLCLSldPAAEPSPDYT-HIAFTVSeeDFEELSERLRA 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 924872605  89 TKATILP---SPG--LDFLDPWGN----HV 109
Cdd:cd07244   80 AGVKIWQensSEGdsLYFLDPDGHklelHV 109
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
13-111 3.62e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 48.98  E-value: 3.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605   13 GINHVALEVDDVDAALEFYGRLFEIKLRGRHD-------GMAFIDLGDQFINLSPRRSQQPDQAR-------HFGLVVDD 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDageegglRSAFFLAGGRVLELLLNETPPPAAAGfgghhiaFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 924872605   79 REKVRQALKGTKATILPSPGLD--------FLDPWGNHVQV 111
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHgwggrysyFRDPDGNLIEL 121
PRK04101 PRK04101
metallothiol transferase FosB;
13-106 8.00e-04

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 37.23  E-value: 8.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  13 GINHVALEVDDVDAALEFYGRLFEIKLRGRHDGMAFIDLGDQFINLsprrSQQPDQAR--------HFGLVVDDR--EKV 82
Cdd:PRK04101   4 GINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWIAL----NEEKDIPRneihqsytHIAFSIEEEdfDHW 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 924872605  83 RQALKGTKATILPSPGLD--------FLDPWG 106
Cdd:PRK04101  80 YQRLKENDVNILPGRERDerdkksiyFTDPDG 111
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 13-116 1.17e-13

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: 63.47  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  13 GINHVALEVDDVDAALEFYGRLFEIKLRGRHD------GMAFIDLGDQF-INLSPRRSQQPDQA----RHFGLVVDDREK 81
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDfgdggfGHAFLRLGDGTeLELFEAPGAAPAPGggglHHLAFRVDDLDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 924872605  82 VRQALKGTKATILPSPGLD--------FLDPWGNHVQVVQYRD 116
Cdd:COG0346   82 AYARLRAAGVEIEGEPRDRaygyrsayFRDPDGNLIELVEPPP 124
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 11-116 1.03e-12

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 60.80  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  11 AVGINHVALEVDDVDAALEFYGRLFEIKLRGRHD---GMAFIDLGD-QFINLSPRRSQQPDQARHFGLVVDDREKVRQAL 86
Cdd:COG3324    2 PGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGpggDYAEFDTDGgQVGGLMPGAEEPGGPGWLLYFAVDDLDAAVARV 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 924872605  87 KGTKATIL------PSPG--LDFLDPWGNHVQVVQYRD 116
Cdd:COG3324   82 EAAGGTVLrpptdiPPWGrfAVFRDPEGNRFGLWQPAA 119
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 13-109 1.49e-10

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: 54.98  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  13 GINHVALEVDDVDAALEFYGRLFEIKLRGRHDGMAFIDLGDQFINLS--PRRSQQPDQArHFGLVVD--DREKVRQALKG 88
Cdd:cd07244    1 GINHITLAVSDLERSLAFYVDLLGFKPHVRWDKGAYLTAGDLWLCLSldPAAEPSPDYT-HIAFTVSeeDFEELSERLRA 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 924872605  89 TKATILP---SPG--LDFLDPWGN----HV 109
Cdd:cd07244   80 AGVKIWQensSEGdsLYFLDPDGHklelHV 109
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
13-116 4.44e-10

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 54.19  E-value: 4.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  13 GINHVALEVDDVDAALEFYGRLFEIKLRGRHDGMAF--IDLGDQFINLSPRRSQQPDQAR----HFGLVVDDREKVRQAL 86
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYlrADGGEHLLVLEEAPGAPPRPGAagldHVAFRVPSRADLDAAL 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 924872605  87 KGTKATILPSPGLD---------FLDPWGNHVQVVQYRD 116
Cdd:COG2514   83 ARLAAAGVPVEGAVdhgvgeslyFRDPDGNLIELYTDRP 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
13-111 3.62e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 48.98  E-value: 3.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605   13 GINHVALEVDDVDAALEFYGRLFEIKLRGRHD-------GMAFIDLGDQFINLSPRRSQQPDQAR-------HFGLVVDD 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDageegglRSAFFLAGGRVLELLLNETPPPAAAGfgghhiaFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 924872605   79 REKVRQALKGTKATILPSPGLD--------FLDPWGNHVQV 111
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHgwggrysyFRDPDGNLIEL 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 16-107 6.04e-08

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: 47.90  E-value: 6.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  16 HVALEVDDVDAALEFYGRLFEIKLRGRHDGMAFIDLGD------QFINLSPRRSQQPDQARHFGLVVDDREKVRQALKGT 89
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLgpglrlALLEGPEPERPGGGGLFHLAFEVDDVDEVDERLREA 80

                         90       100
                 ....*....|....*....|....*...
gi 924872605  90 KATILPSPGLD----------FLDPWGN 107
Cdd:cd06587   81 GAEGELVAPPVddpwggrsfyFRDPDGN 108
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 14-107 1.26e-06

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: 44.62  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  14 INHVALEVDDVDAALEFYGRLF---EIKLR--GRHDGmAFIDLGDQF-INLSPRRSQQPDQA-------RHFGLVVDDRE 80
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLgleEVPRPpfLKFGG-AWLYLGGGQqIHLVVEQNPSELPRpehpgrdRHPSFSVPDLD 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 924872605  81 KVRQALK--GTKAT--ILPSPGLD---FLDPWGN 107
Cdd:cd07245   80 ALKQRLKeaGIPYTesTSPGGGVTqlfFRDPDGN 113
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 16-82 1.69e-06

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: 44.37  E-value: 1.69e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 924872605  16 HVALEVDDVDAALEFYGRLFEIKLRGRHDGMAFIDLGDQFIN--LSPRRSQQPDQARHFGLVVDDREKV 82
Cdd:cd07254    4 HLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFMLEDPPLNlaLLVNDRKEPYGLNHLGIQVDSKEEV 72
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 14-109 5.38e-06

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: 43.09  E-value: 5.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  14 INHVALEVDDVDAALEFYGRLFEIKLRGRHDGMAF--IDLGDQFINLSPR----RSQQPDQARH---FGLVVDDREK-VR 83
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLPPRFLHEEGEYaeFDTGETKLALFSRkemaRSGGPDRRGSafeLGFEVDDVEAtVE 80

                         90       100
                 ....*....|....*....|....*..
gi 924872605  84 QALK-GTKATILPSPgldflDPWGNHV 109
Cdd:cd07264   81 ELVErGAEFVREPAN-----KPWGQTV 102
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 17-113 6.41e-06

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 42.89  E-value: 6.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  17 VALEVDDVDAALEFYGRL-FEIKLRGRHDGMAFIDLGD-QFINLSPRRSQQPDQAR-----------HFGLVVDDREKVR 83
Cdd:COG3607    7 VNLPVADLERSRAFYEALgFTFNPQFSDEGAACFVLGEgIVLMLLPREKFATFTGKpiadatgftevLLALNVESREEVD 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 924872605  84 QAL-KGTKA--TILPSP-------GLDFLDPWGNHVQVVQ 113
Cdd:COG3607   87 ALVaKALAAggTVLKPPqdvggmySGYFADPDGHLWEVAW 126
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 16-107 1.67e-05

uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and type I ring-cleaving dioxygenases; 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: 319945 [Multi-domain]  Cd Length: 124  Bit Score: 41.60  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  16 HVALEVDDVDAALEFYGRLFEIKLrGRhDGMAFIDL---GDQFI-NLSPRRSQQPDQA--------RHFGLVVDDR---- 79
Cdd:cd08357    2 HLAIPVRDLEAARDFYGDVLGCPE-GR-SSETWIDFnffGHQVVaHLVPNYASTSTNAvdghsvpvPHFGLALTVDdfda 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 924872605  80 --EKVRQAlkGTKATILPS------PG----LDFLDPWGN 107
Cdd:cd08357   80 laERLKAA--GVKFYIEPYvrfegePGeqwtMFLLDPSGN 117
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
19-114 2.03e-05

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 41.38  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  19 LEVDDVDAALEFYGRLFEIKLRGRH---DGM---AFIDLGDQFINLSPRRSQQPDQAR---HFGLVVDDREKVRQALKGT 89
Cdd:COG2764    6 LVVDDAEEALEFYEDVFGFEVVFRMtdpDGKimhAELRIGGSVLMLSDAPPDSPAAEGngvSLSLYVDDVDALFARLVAA 85

                         90       100       110
                 ....*....|....*....|....*....|...
gi 924872605  90 KATILPSPGLDF--------LDPWGNHVQVVQY 114
Cdd:COG2764   86 GATVVMPLQDTFwgdrfgmvRDPFGVLWMINTP 118
MhqB_like_N cd08344
N-terminal domain of MhqB, a type I extradiol dioxygenase, and similar proteins; This ...
 14-111 1.69e-04

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: 38.94  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  14 INHVALEVDDVDAALEFYgRLFEIKLRGRHDGMAFIDLGDQFINLsprRSQQPDQAR----HFGLVVDDREKVRQALKGT 89
Cdd:cd08344    3 IDHFALEVPDLEVARRFY-EAFGLDVRETGEDLELRAPGNDHVWA---RLIQGARKRlaylSFGIFGDDLARFAAHLDAA 78

                         90       100
                 ....*....|....*....|....*...
gi 924872605  90 KATILPSP------GLDFLDPWGNHVQV 111
Cdd:cd08344   79 GVALIAAPpgadpdGVWFEDPDGNLLQV 106
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 14-106 2.72e-04

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: 38.49  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  14 INHVALEVDDVDAALEFYGRLFEIKLRGRHDGMAFIDLGDQFINLsprrSQQPDQAR--------HFGLVVDDRE--KVR 83
Cdd:cd08363    1 INHITFSVSNLNKSIAFYKDVLDAKLLVLGEKTAYFDLNGLWLAL----NVQEDIPRneishsytHIAFSIDEEDldAFK 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 924872605  84 QALKGTKATILPSPGLD--------FLDPWG 106
Cdd:cd08363   77 ERLKDNGVNILEGRKRDilegqsiyFTDPDG 107
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 13-87 2.84e-04

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: 38.29  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  13 GINHVALEVDDVDAALEFYGRL--FEIKLR----GRHDGMAFIDLGDQFINL-----SPRRSQQPDQA--RHFGLVVDDR 79
Cdd:cd08352    2 KIHHIAIICSDYEKSKDFYVDKlgFEIIREhyrpERNDIKLDLALGGYQLELfikpdAPARPSYPEALglRHLAFKVEDV 81


                 ....*...
gi 924872605  80 EKVRQALK 87
Cdd:cd08352   82 EATVAELK 89
PRK04101 PRK04101
metallothiol transferase FosB;
13-106 8.00e-04

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 37.23  E-value: 8.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  13 GINHVALEVDDVDAALEFYGRLFEIKLRGRHDGMAFIDLGDQFINLsprrSQQPDQAR--------HFGLVVDDR--EKV 82
Cdd:PRK04101   4 GINHICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAYFDLNGLWIAL----NEEKDIPRneihqsytHIAFSIEEEdfDHW 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 924872605  83 RQALKGTKATILPSPGLD--------FLDPWG 106
Cdd:PRK04101  80 YQRLKENDVNILPGRERDerdkksiyFTDPDG 111
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 13-114 3.64e-03

vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; This subfamily of vicinal oxygen chelate (VOC) family protein includes Streptomyces hygroscopicus ValD protein and similar proteins. ValD protein functions in validamycin biosynthetic pathway. 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: 319968  Cd Length: 150  Bit Score: 35.77  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  13 GINHVALEVDDVDAALEFYGRLF-----------------EIKLRGRHDG-------MAFIDLGDQfINL------SPRR 62
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLgaevvyrstplaegdrgGGEMRAAGFVpgfararIAMLRLGPG-PGIelfeykGPEQ 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  63 SQQPDQ-----ARHFGLVVDDRE----KVRQA----LKGTKATILPSPGLD-----FLDPWGNHVQVVQY 114
Cdd:cd16361   80 RAPVPRnsdvgIFHFALQVDDVEaaaeRLAAAggkvLMGPREIPDGGPGKGnrmvyLRDPWGTLIELVSH 149
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
15-97 5.73e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 34.56  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605   15 NHVALEVDDVDAALEFYGRLFEIKLRGRHD------GMAFIDLGDQFINL---SPRRSQQPDQAR-----HFGLVVDDRE 80
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPEGDYRsepqnvDLAFALLGDGPVEVeliQPLDGDSPLARHgpglhHLAYWVDDLD 80

                          90
                  ....*....|....*..
gi 924872605   81 KVRQALKGTKATILPSP 97
Cdd:pfam13669  81 AAVARLLDQGYRVAPKG 97
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 14-83 6.39e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 34.51  E-value: 6.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 924872605  14 INHVALEVDDVDAALEFYGRLFE---IKLRGRHDGMAF--IDLGDQFINLSPRRSQQPDQAR--HFGLVVDDREKVR 83
Cdd:cd07262    1 ISHVTIGVNDLERSRAFYDAALAplgYKRGFEDGGRVGygLEGGPDFWVTEPFDGEPATAGNgtHVAFAAPSRAAVD 77
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 16-112 7.68e-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: 34.21  E-value: 7.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924872605  16 HVALEVDDVDAALEFYGRLFEIKLRGRHDGMAFIDlGDQFINLSPRRSQQPDQA-RHFGLVVDDREKVRQALK-----GT 89
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKRDGNSVYLR-GYEDEHHSLVLYEAPEAGlKHFAFEVASEEDLERAAAsltalGC 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 924872605  90 KATILPSP-------GLDFLDPWGNHVQVV 112
Cdd:cd16360   80 DVTWGPDGevpgggkGFRFQDPSGHLLELF 109
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH