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Conserved domains on  [gi|2199952110|ref|WP_239875001|]
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MULTISPECIES: VOC family protein [Vibrio]

Protein Classification

VOC family protein( domain architecture ID 10163530)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms; similar to type I extradiol dioxygenase, glyoxalase I and a group of antibiotic resistance proteins such as Staphylococcus aureus bleomycin resistance protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-128 1.29e-56

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


:

Pssm-ID: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 172.48  E-value: 1.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   7 IITLGVSQLKTSFNFYTKLGFESAQTPEEGIVFFKTRGTCLALYPLEALADDVSPDftAKRAGFSGITLAHNTRSKDEVD 86
Cdd:cd07251     1 LITLGVRDLERSARFYEALGWKPNLDPNDGVVFFQLGGTVLALYPRDALAEDAGVS--VTGAGFSGVTLAHNVRSREEVD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2199952110  87 DILRVAVEAGGKLVKPAQDVFWGGYSGYFSDPDGYLWEVAYG 128
Cdd:cd07251    79 QLLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVAYN 120
 
Name Accession Description Interval E-value
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-128 1.29e-56

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


Pssm-ID: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 172.48  E-value: 1.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   7 IITLGVSQLKTSFNFYTKLGFESAQTPEEGIVFFKTRGTCLALYPLEALADDVSPDftAKRAGFSGITLAHNTRSKDEVD 86
Cdd:cd07251     1 LITLGVRDLERSARFYEALGWKPNLDPNDGVVFFQLGGTVLALYPRDALAEDAGVS--VTGAGFSGVTLAHNVRSREEVD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2199952110  87 DILRVAVEAGGKLVKPAQDVFWGGYSGYFSDPDGYLWEVAYG 128
Cdd:cd07251    79 QLLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVAYN 120
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 2-127 2.68e-46

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 146.51  E-value: 2.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   2 EPRISIITLGVSQLKTSFNFYTKLGFE-SAQTPEEGIVFFKT-RGTCLALYPLEALADDVSPDFTAKrAGFSGITLAHNT 79
Cdd:COG3607     1 MPRIIFVNLPVADLERSRAFYEALGFTfNPQFSDEGAACFVLgEGIVLMLLPREKFATFTGKPIADA-TGFTEVLLALNV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2199952110  80 RSKDEVDDILRVAVEAGGKLVKPAQDVFWgGYSGYFSDPDGYLWEVAY 127
Cdd:COG3607    80 ESREEVDALVAKALAAGGTVLKPPQDVGG-MYSGYFADPDGHLWEVAW 126
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-125 7.45e-17

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 71.33  E-value: 7.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   4 RISIITLGVSQLKTSFNFYTK-LGFE-SAQTPEEG-----IVFFKTRGTCLALYPLEALADDvspdftakRAGFSGITLA 76
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDvLGFKlVEETDAGEegglrSAFFLAGGRVLELLLNETPPPA--------AAGFGGHHIA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2199952110  77 HNTRSKDEVDDILRVAVEAGGKLVKPAQDVFWGGYSGYFSDPDGYLWEV 125
Cdd:pfam00903  73 FIAFSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-128 1.29e-56

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


Pssm-ID: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 172.48  E-value: 1.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   7 IITLGVSQLKTSFNFYTKLGFESAQTPEEGIVFFKTRGTCLALYPLEALADDVSPDftAKRAGFSGITLAHNTRSKDEVD 86
Cdd:cd07251     1 LITLGVRDLERSARFYEALGWKPNLDPNDGVVFFQLGGTVLALYPRDALAEDAGVS--VTGAGFSGVTLAHNVRSREEVD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2199952110  87 DILRVAVEAGGKLVKPAQDVFWGGYSGYFSDPDGYLWEVAYG 128
Cdd:cd07251    79 QLLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVAYN 120
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 2-127 2.68e-46

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 146.51  E-value: 2.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   2 EPRISIITLGVSQLKTSFNFYTKLGFE-SAQTPEEGIVFFKT-RGTCLALYPLEALADDVSPDFTAKrAGFSGITLAHNT 79
Cdd:COG3607     1 MPRIIFVNLPVADLERSRAFYEALGFTfNPQFSDEGAACFVLgEGIVLMLLPREKFATFTGKPIADA-TGFTEVLLALNV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2199952110  80 RSKDEVDDILRVAVEAGGKLVKPAQDVFWgGYSGYFSDPDGYLWEVAY 127
Cdd:COG3607    80 ESREEVDALVAKALAAGGTVLKPPQDVGG-MYSGYFADPDGHLWEVAW 126
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-125 7.45e-17

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 71.33  E-value: 7.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   4 RISIITLGVSQLKTSFNFYTK-LGFE-SAQTPEEG-----IVFFKTRGTCLALYPLEALADDvspdftakRAGFSGITLA 76
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDvLGFKlVEETDAGEegglrSAFFLAGGRVLELLLNETPPPA--------AAGFGGHHIA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2199952110  77 HNTRSKDEVDDILRVAVEAGGKLVKPAQDVFWGGYSGYFSDPDGYLWEV 125
Cdd:pfam00903  73 FIAFSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 4-127 1.02e-14

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: 65.78  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   4 RISIITLGVSQLKTSFNFYTK-LGFESAQTPEEG-----IVFFKT-RGTCLALYPlealaddvSPDFTAKRAGFSGITLA 76
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDvLGLELVKRTDFGdggfgHAFLRLgDGTELELFE--------APGAAPAPGGGGLHHLA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2199952110  77 HNTrskDEVDDILRVAVEAGGKLVKPAQDVFWGGYSGYFSDPDGYLWEVAY 127
Cdd:COG0346    74 FRV---DDLDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121
VOC_like cd09012
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-127 9.75e-14

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: 319954  Cd Length: 127  Bit Score: 63.17  E-value: 9.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   8 ITLGVSQLKTSFNFYTKLGFESAQ--TPEEGIVFFKTRGTCLALYPLEALADDVSPDFTAKRAGFSGITLAHNTRSKDEV 85
Cdd:cd09012     4 INLPVTDLEASTAFYEALGFKKNPqfSDEHASCMVVSDNIFVMLLAHDRFKTFIPEPIAVDAKKSTEVLLTLSAKSRQEV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2199952110  86 DDILRVAVEAGGKLVKPAQDVFWGG-YSGYFSDPDGYLWEVAY 127
Cdd:cd09012    84 DAFVDKAVEAGGKADPYVNGGDEGFmYGRSFEDLDGHLWEVVW 126
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
7-127 1.08e-13

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 62.95  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   7 IITLGVSQLKTSFNFYTK-LGFESAQT---PEEGIVF--FKTRGTCLALYplealadDVSPDFTAKRAgfSGITLAHNTr 80
Cdd:COG2764     3 TPYLVVDDAEEALEFYEDvFGFEVVFRmtdPDGKIMHaeLRIGGSVLMLS-------DAPPDSPAAEG--NGVSLSLYV- 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2199952110  81 skDEVDDILRVAVEAGGKLVKPAQDVFWGGYSGYFSDPDGYLWEVAY 127
Cdd:COG2764    73 --DDVDALFARLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLWMINT 117
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 8-125 5.97e-11

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: 55.61  E-value: 5.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   8 ITLGVSQLKTSFNFYTK-LGFESAQTPEEG-IVFFKT-RGTCLALyplealaDDVSPDFTAKRAGFSGITLAhnTRSKDE 84
Cdd:cd06587     2 VALRVPDLDASVAFYEEvLGFEVVSRNEGGgFAFLRLgPGLRLAL-------LEGPEPERPGGGGLFHLAFE--VDDVDE 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2199952110  85 VDDILRVAVEAGGKLVKPAQDVfWGGYSGYFSDPDGYLWEV 125
Cdd:cd06587    73 VDERLREAGAEGELVAPPVDDP-WGGRSFYFRDPDGNLIEF 112
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 21-120 3.21e-10

Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme and similar proteins; Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme 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: 319963  Cd Length: 119  Bit Score: 53.97  E-value: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110  21 FYTKL-GFEsaQTPEEGIVFFK---TRGTCLALYPLEALADDVSPDFTAKRAGFSGITLahNTRSKDEVDDILRVAVEAG 96
Cdd:cd16356    15 FYSELfGLE--EIFEIRSPIFRglrTGDSCLGFNAPEAYELLGLPEFSDTPGIRILLTF--DVDDVEAVDRLVPRAAALG 90

                          90       100
                  ....*....|....*....|....
gi 2199952110  97 GKLVKPAQDVFWGGYSGYFSDPDG 120
Cdd:cd16356    91 ATLIKPPYDTYYGWYQAVLLDPEG 114
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-125 1.73e-09

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 51.95  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   1 MEPRISIITLGVSQLKTSFNFYTK-LGFESAQTPEEG---IVFFKTRGTCLALYPLEAladdvspdftakRAGFSGITLA 76
Cdd:COG3324     1 MPGTIVWVELPVDDLERAKAFYEEvFGWTFEDDAGPGgdyAEFDTDGGQVGGLMPGAE------------EPGGPGWLLY 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2199952110  77 HNTrskDEVDDILRVAVEAGGKLVKPAQDVFWGGYSGYFSDPDGYLWEV 125
Cdd:COG3324    69 FAV---DDLDAAVARVEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGL 114
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-126 2.18e-09

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: 51.56  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   5 ISIITLGVSQLKTSFNFYTK-LGFESAQTPEEGIVF-FKTRGTCLALYPLEALADDVSPDftAKRAGFSgitLAHNTrsk 82
Cdd:cd07264     1 IAYIVLYVDDFAASLRFYRDvLGLPPRFLHEEGEYAeFDTGETKLALFSRKEMARSGGPD--RRGSAFE---LGFEV--- 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2199952110  83 DEVDDILRVAVEAGGKLVKPAQDVFWGGYSGYFSDPDGYLWEVA 126
Cdd:cd07264    73 DDVEATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEIC 116
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 83-126 3.59e-07

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


Pssm-ID: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 46.14  E-value: 3.59e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2199952110  83 DEVDDILRVAVEAGGKLVKPAQDVFWGGYSGYFSDPDGYLWEVA 126
Cdd:cd07246    79 EDVDATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGHVWWLA 122
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 10-124 3.78e-07

N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.


Pssm-ID: 319911 [Multi-domain]  Cd Length: 114  Bit Score: 45.72  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110  10 LGVSQLKTSFNFYTKL---GFESAQTPEEGIVFFKTRGTCLAlypleALADdvSPDFTAKRAGFSGITLAhntrsKDEVD 86
Cdd:cd07247     6 LPTTDLERAKAFYGAVfgwTFEDEGDGGGDYALFTAGGGAVG-----GLMR--APEEVAGAPPGWLIYFA-----VDDLD 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2199952110  87 DILRVAVEAGGKLVKPAQDVFWGGYSGYFSDPDGY---LWE 124
Cdd:cd07247    74 AALARVEAAGGKVVVPPTDIPGGGRFAVFADPEGNrfgLWS 114
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
4-127 4.75e-07

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 46.10  E-value: 4.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   4 RISIITLGVSQLKTSFNFYTK-LGFESAQTpEEGIVFFKTRG--TCLALYPlealADDVSPdftakRAGFSGIT-LAHNT 79
Cdd:COG2514     3 RLGHVTLRVRDLERSAAFYTDvLGLEVVER-EGGRVYLRADGgeHLLVLEE----APGAPP-----RPGAAGLDhVAFRV 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2199952110  80 RSKDEVDDILRVAVEAGGKLVKPAQdvFWGGYSGYFSDPDGYLWEVAY 127
Cdd:COG2514    73 PSRADLDAALARLAAAGVPVEGAVD--HGVGESLYFRDPDGNLIELYT 118
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-120 4.14e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 42.99  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   5 ISIITLGVSQLKTSFNFYTK----LGFESAQTPEEGIVFFKTRGTCLALYplealaddvSPDFTAKRAGFSGITLAHNTR 80
Cdd:cd07262     1 ISHVTIGVNDLERSRAFYDAalapLGYKRGFEDGGRVGYGLEGGPDFWVT---------EPFDGEPATAGNGTHVAFAAP 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2199952110  81 SKDEVDDILRVAVEAGGKLV-KPAQDVFWGG--YSGYFSDPDG 120
Cdd:cd07262    72 SRAAVDAFHAAALAAGGTDNgAPGLRPHYHPgyYAAYVRDPDG 114
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 8-126 5.36e-06

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: 42.62  E-value: 5.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   8 ITLGVSQLKTSFNFYTKLGFESAQTPEEGIVFFktRGTCLALYPLEALADDvspdftakRAGFSGITLAHNTRSkdEVDD 87
Cdd:cd08362     7 VALGVPDLAAEREFYTEVWGLEEVAEDDDVVYL--RAEGSEHHVLRLRQSD--------ENRLDLIAFAAATRA--DVDA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2199952110  88 ILRVAVEAGGKLVKP--AQDVFWGGYSGYFSDPDGYLWEVA 126
Cdd:cd08362    75 LAARLAAAGVRILSEpgPLDDPGGGYGFRFFDPDGRTIEVS 115
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 9-128 7.99e-05

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: 39.61  E-value: 7.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   9 TLGVSQLKTSFNFYTK-LGFESAQTpEEGIVFFKTRGT---CLALYplealaddvspdfTAKRAGFSGITLAhnTRSKDE 84
Cdd:cd16360     3 ELGVPDLEKALEFYTDvLGLQVAKR-DGNSVYLRGYEDehhSLVLY-------------EAPEAGLKHFAFE--VASEED 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2199952110  85 VDDiLRVAVEAGG--KLVKPAQDVFWGGYSGYFSDPDGYLWEVAYG 128
Cdd:cd16360    67 LER-AAASLTALGcdVTWGPDGEVPGGGKGFRFQDPSGHLLELFVE 111
TioX_like cd08355
Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of ...
 57-125 1.21e-03

Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of the thiocoraline biosynthetic gene cluster. Thiocoraline is a thiodepsipeptide with potent antitumor activity. TioX may be involved in thiocoraline resistance or secretion. TioX belongs to vicinal oxygen chelate (VOC) superfamily that 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: 319943  Cd Length: 123  Bit Score: 36.63  E-value: 1.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2199952110  57 DDVSPDFTAKRAGF--SGITLAHntrskDEVDDILRVAVEAGGKLVKPAQDVFWGGYSGYFSDPDGYLWEV 125
Cdd:cd08355    55 DEARPDRPADAGGHgtQSVYVAV-----ADPDAHYERARAAGAEIVMEPTDTDYGSRDYSARDPEGHLWSF 120
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-125 2.68e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 35.37  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2199952110   8 ITLGVSQLKTSFNFYTK-LGFESAQTPEegivFFKTRGTCLALYPLEALADDVSPDFTAKRAGFSGITLAHNTRSKDEVD 86
Cdd:cd07245     4 VALACPDLERARRFYTDvLGLEEVPRPP----FLKFGGAWLYLGGGQQIHLVVEQNPSELPRPEHPGRDRHPSFSVPDLD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2199952110  87 DILRVAVEAGgklVKPAQDVFWGGYSG--YFSDPDGYLWEV 125
Cdd:cd07245    80 ALKQRLKEAG---IPYTESTSPGGGVTqlFFRDPDGNRLEF 117
 
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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