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Conserved domains on  [gi|1226657862|ref|WP_093941801|]
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VOC family protein [Actinoalloteichus hoggarensis]

Protein Classification

VOC family protein( domain architecture ID 50733)

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

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List of domain hits

 Name Accession Description Interval E-value
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 145-263 6.55e-26

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.


The actual alignment was detected with superfamily member cd07251:

Pssm-ID: 472697 [Multi-domain]  Cd Length: 120  Bit Score: 98.14  E-value: 6.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862 145 VILGVASPKASTVFYEALGMSADHDYGDKFIDFTIAEGVcrLGLLPRKPLAKDAGVSEAGDGFAALVLTHLAASPTEVDR 224
Cdd:cd07251     2 ITLGVRDLERSARFYEALGWKPNLDPNDGVVFFQLGGTV--LALYPRDALAEDAGVSVTGAGFSGVTLAHNVRSREEVDQ 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1226657862 225 LLAAAAAAGGRVTAPARRTDDGAYVGLFADPDGHHWKVV 263
Cdd:cd07251    80 LLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVA 118
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-124 2.74e-16

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.


The actual alignment was detected with superfamily member cd07251:

Pssm-ID: 472697 [Multi-domain]  Cd Length: 120  Bit Score: 73.10  E-value: 2.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862   7 IIALGVPRLAAARDFYATAFAAPVADDDQSVRLRLHGAGRLTLHPIDELAAEVAVDPATSGFRGYVLSVAVESPAEVEAL 86
Cdd:cd07251     1 LITLGVRDLERSARFYEALGWKPNLDPNDGVVFFQLGGTVLALYPRDALAEDAGVSVTGAGFSGVTLAHNVRSREEVDQL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1226657862  87 LGTAAAQGATVVKQAKKEFFGEFTAVHRAPDGAVWKLA 124
Cdd:cd07251    81 LAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVA 118
 
Name Accession Description Interval E-value
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 145-263 6.55e-26

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: 98.14  E-value: 6.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862 145 VILGVASPKASTVFYEALGMSADHDYGDKFIDFTIAEGVcrLGLLPRKPLAKDAGVSEAGDGFAALVLTHLAASPTEVDR 224
Cdd:cd07251     2 ITLGVRDLERSARFYEALGWKPNLDPNDGVVFFQLGGTV--LALYPRDALAEDAGVSVTGAGFSGVTLAHNVRSREEVDQ 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1226657862 225 LLAAAAAAGGRVTAPARRTDDGAYVGLFADPDGHHWKVV 263
Cdd:cd07251    80 LLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVA 118
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 141-263 5.19e-25

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 96.05  E-value: 5.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862 141 TETAVILGVASPKASTVFYEALGMSADHDYGD-KFIDFTIAEGVcRLGLLPRKPLAKDAGVSEA-GDGFAALVLTHLAAS 218
Cdd:COG3607     3 RIIFVNLPVADLERSRAFYEALGFTFNPQFSDeGAACFVLGEGI-VLMLLPREKFATFTGKPIAdATGFTEVLLALNVES 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1226657862 219 PTEVDRLLAAAAAAGGRVTAPARRTDDGaYVGLFADPDGHHWKVV 263
Cdd:COG3607    82 REEVDALVAKALAAGGTVLKPPQDVGGM-YSGYFADPDGHLWEVA 125
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-124 2.74e-16

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: 73.10  E-value: 2.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862   7 IIALGVPRLAAARDFYATAFAAPVADDDQSVRLRLHGAGRLTLHPIDELAAEVAVDPATSGFRGYVLSVAVESPAEVEAL 86
Cdd:cd07251     1 LITLGVRDLERSARFYEALGWKPNLDPNDGVVFFQLGGTVLALYPRDALAEDAGVSVTGAGFSGVTLAHNVRSREEVDQL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1226657862  87 LGTAAAQGATVVKQAKKEFFGEFTAVHRAPDGAVWKLA 124
Cdd:cd07251    81 LAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVA 118
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 7-124 5.04e-14

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 66.78  E-value: 5.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862   7 IIALGVPRLAAARDFYaTAF---AAPVADDDQSVRLRLHGAGRLTLHPIDELAAEVAVDPA-TSGFRGYVLSVAVESPAE 82
Cdd:COG3607     6 FVNLPVADLERSRAFY-EALgftFNPQFSDEGAACFVLGEGIVLMLLPREKFATFTGKPIAdATGFTEVLLALNVESREE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1226657862  83 VEALLGTAAAQGATVVKQAKKEFFGeFTAVHRAPDGAVWKLA 124
Cdd:COG3607    85 VDALVAKALAAGGTVLKPPQDVGGM-YSGYFADPDGHLWEVA 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
145-260 1.90e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 40.12  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862 145 VILGVASPKASTVFY-EALGM------SADHDYGDKFIDFTIAEGvcRLGLLPRkPLAKDAGVSEAGDGFAALVLThlaa 217
Cdd:pfam00903   5 VALRVGDLEKSLDFYtDVLGFklveetDAGEEGGLRSAFFLAGGR--VLELLLN-ETPPPAAAGFGGHHIAFIAFS---- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1226657862 218 sPTEVDRLLAAAAAAGGRVTAPARRTDDGAYVGLFADPDGHHW 260
Cdd:pfam00903  78 -VDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLI 119
 
Name Accession Description Interval E-value
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 145-263 6.55e-26

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: 98.14  E-value: 6.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862 145 VILGVASPKASTVFYEALGMSADHDYGDKFIDFTIAEGVcrLGLLPRKPLAKDAGVSEAGDGFAALVLTHLAASPTEVDR 224
Cdd:cd07251     2 ITLGVRDLERSARFYEALGWKPNLDPNDGVVFFQLGGTV--LALYPRDALAEDAGVSVTGAGFSGVTLAHNVRSREEVDQ 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1226657862 225 LLAAAAAAGGRVTAPARRTDDGAYVGLFADPDGHHWKVV 263
Cdd:cd07251    80 LLAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVA 118
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 141-263 5.19e-25

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 96.05  E-value: 5.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862 141 TETAVILGVASPKASTVFYEALGMSADHDYGD-KFIDFTIAEGVcRLGLLPRKPLAKDAGVSEA-GDGFAALVLTHLAAS 218
Cdd:COG3607     3 RIIFVNLPVADLERSRAFYEALGFTFNPQFSDeGAACFVLGEGI-VLMLLPREKFATFTGKPIAdATGFTEVLLALNVES 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1226657862 219 PTEVDRLLAAAAAAGGRVTAPARRTDDGaYVGLFADPDGHHWKVV 263
Cdd:COG3607    82 REEVDALVAKALAAGGTVLKPPQDVGGM-YSGYFADPDGHLWEVA 125
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-124 2.74e-16

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: 73.10  E-value: 2.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862   7 IIALGVPRLAAARDFYATAFAAPVADDDQSVRLRLHGAGRLTLHPIDELAAEVAVDPATSGFRGYVLSVAVESPAEVEAL 86
Cdd:cd07251     1 LITLGVRDLERSARFYEALGWKPNLDPNDGVVFFQLGGTVLALYPRDALAEDAGVSVTGAGFSGVTLAHNVRSREEVDQL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1226657862  87 LGTAAAQGATVVKQAKKEFFGEFTAVHRAPDGAVWKLA 124
Cdd:cd07251    81 LAKAVAAGGKILKPPQEVFWGGYSGYFADPDGHIWEVA 118
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 7-124 5.04e-14

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 66.78  E-value: 5.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862   7 IIALGVPRLAAARDFYaTAF---AAPVADDDQSVRLRLHGAGRLTLHPIDELAAEVAVDPA-TSGFRGYVLSVAVESPAE 82
Cdd:COG3607     6 FVNLPVADLERSRAFY-EALgftFNPQFSDEGAACFVLGEGIVLMLLPREKFATFTGKPIAdATGFTEVLLALNVESREE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1226657862  83 VEALLGTAAAQGATVVKQAKKEFFGeFTAVHRAPDGAVWKLA 124
Cdd:COG3607    85 VDALVAKALAAGGTVLKPPQDVGGM-YSGYFADPDGHLWEVA 125
VOC_like cd09012
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 147-263 8.78e-08

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


Pssm-ID: 319954  Cd Length: 127  Bit Score: 49.69  E-value: 8.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862 147 LGVASPKASTVFYEALGMSADHDYGDKFID-FTIAEGVCrLGLLPRKPLAKDAGVSEAGDGFAA--LVLTHLAASPTEVD 223
Cdd:cd09012     6 LPVTDLEASTAFYEALGFKKNPQFSDEHAScMVVSDNIF-VMLLAHDRFKTFIPEPIAVDAKKSteVLLTLSAKSRQEVD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1226657862 224 RLLAAAAAAGGRVTAPARRTDD-GAYVGLFADPDGHHWKVV 263
Cdd:cd09012    85 AFVDKAVEAGGKADPYVNGGDEgFMYGRSFEDLDGHLWEVV 125
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 5-118 2.18e-05

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: 43.06  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862   5 LDIIALGVPRLAAARDFYATAFAAPVADD----DQSVR---LRLHGAGRLTLHPidelAAEVAVDPATSGFRGYVLSVav 77
Cdd:COG0346     3 LHHVTLRVSDLEASLAFYTDVLGLELVKRtdfgDGGFGhafLRLGDGTELELFE----APGAAPAPGGGGLHHLAFRV-- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1226657862  78 espAEVEALLGTAAAQGATVVKQAKKEFFGEFTAVHRAPDG 118
Cdd:COG0346    77 ---DDLDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDG 114
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 6-123 4.89e-05

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: 41.64  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862   6 DIIALgvprlaaaRDFYATAFAAPVADDDQSVRLRLHGAGRLTLHPIDELAAEVAVDPATSGFRG--YVLSVAVESPAEV 83
Cdd:cd16356     8 DIVAL--------SDFYSELFGLEEIFEIRSPIFRGLRTGDSCLGFNAPEAYELLGLPEFSDTPGirILLTFDVDDVEAV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1226657862  84 EALLGTAAAQGATVVKQAKKEFFGEFTAVHRAPDGAVWKL 123
Cdd:cd16356    80 DRLVPRAAALGATLIKPPYDTYYGWYQAVLLDPEGNVFRI 119
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 145-258 1.03e-04

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: 40.78  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862 145 VILGVASPKASTVFYEALGM------SADHDYGDkfidFTIAEgvCRLGLLPRKPLAKDAGVSEAGDGFAalvlthLAAS 218
Cdd:cd07264     4 IVLYVDDFAASLRFYRDVLGlpprflHEEGEYAE----FDTGE--TKLALFSRKEMARSGGPDRRGSAFE------LGFE 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1226657862 219 PTEVDRLLAAAAAAGGRVTAPARRTDDGAYVGLFADPDGH 258
Cdd:cd07264    72 VDDVEATVEELVERGAEFVREPANKPWGQTVAYVRDPDGN 111
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
7-121 1.20e-04

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 40.61  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862   7 IIALGVPRLAAARDFYATAFAAPVA----DDDQSVR---LRLHGAgrlTLHpidelAAEVAVDPATSGFRGYVLSVAVEs 79
Cdd:COG2764     3 TPYLVVDDAEEALEFYEDVFGFEVVfrmtDPDGKIMhaeLRIGGS---VLM-----LSDAPPDSPAAEGNGVSLSLYVD- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1226657862  80 paEVEALLGTAAAQGATVVKQAKKEFFGEFTAVHRAPDGAVW 121
Cdd:COG2764    74 --DVDALFARLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLW 113
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-121 1.57e-04

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 40.39  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862   1 MALSLDIIALGVPRLAAARDFYATAFAAPVADDDQSvrlrlhGAGRLTLHPIDELAAEVAVDPATSGFRGYVLSVAVESp 80
Cdd:COG3324     1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGP------GGDYAEFDTDGGQVGGLMPGAEEPGGPGWLLYFAVDD- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1226657862  81 aeVEALLGTAAAQGATVVKQAKKEFFGEFTAVHRAPDGAVW 121
Cdd:COG3324    74 --LDAAVARVEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
145-260 1.90e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 40.12  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862 145 VILGVASPKASTVFY-EALGM------SADHDYGDKFIDFTIAEGvcRLGLLPRkPLAKDAGVSEAGDGFAALVLThlaa 217
Cdd:pfam00903   5 VALRVGDLEKSLDFYtDVLGFklveetDAGEEGGLRSAFFLAGGR--VLELLLN-ETPPPAAAGFGGHHIAFIAFS---- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1226657862 218 sPTEVDRLLAAAAAAGGRVTAPARRTDDGAYVGLFADPDGHHW 260
Cdd:pfam00903  78 -VDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLI 119
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 145-263 2.28e-04

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: 39.98  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862 145 VILGVASPKASTVFY-EALGM--SADHDYGD---KFIDFTIAEGvCRLGLLPrkplAKDAGVSEAGDGFaalvlTHLAAS 218
Cdd:COG0346     6 VTLRVSDLEASLAFYtDVLGLelVKRTDFGDggfGHAFLRLGDG-TELELFE----APGAAPAPGGGGL-----HHLAFR 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1226657862 219 PTEVDRLLAAAAAAGGRVTAPARRTDDGAYVGLFADPDGHHWKVV 263
Cdd:COG0346    76 VDDLDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
221-260 1.45e-03

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 37.53  E-value: 1.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1226657862 221 EVDRLLAAAAAAGGRVTAPARRTDDGAYVGLFADPDGHHW 260
Cdd:COG2764    74 DVDALFARLVAAGATVVMPLQDTFWGDRFGMVRDPFGVLW 113
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 8-100 1.65e-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: 37.61  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862   8 IALGVPRLAAARDFYATAFA-APVADDDQSVRLRlhGAGR----LTLHPidelAAEVAVDpatsgfrgyVLSVAVESPAE 82
Cdd:cd08362     7 VALGVPDLAAEREFYTEVWGlEEVAEDDDVVYLR--AEGSehhvLRLRQ----SDENRLD---------LIAFAAATRAD 71

                          90
                  ....*....|....*...
gi 1226657862  83 VEALLGTAAAQGATVVKQ 100
Cdd:cd08362    72 VDALAARLAAAGVRILSE 89
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 212-257 3.34e-03

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: 36.63  E-value: 3.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1226657862 212 LTHLAASPTEVDRLLAAAAAAGGRVTAPARRTDDGAYVGLFADPDG 257
Cdd:cd16356    69 LTFDVDDVEAVDRLVPRAAALGATLIKPPYDTYYGWYQAVLLDPEG 114
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 8-118 3.37e-03

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: 36.35  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862   8 IALGVPRLAAARDFYATAFAAPVADDDQSVR---LRLHGAGRLTLHPIDELAAEVavdpatsGFRGYVLSVAVESPAEVE 84
Cdd:cd06587     2 VALRVPDLDASVAFYEEVLGFEVVSRNEGGGfafLRLGPGLRLALLEGPEPERPG-------GGGLFHLAFEVDDVDEVD 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1226657862  85 ALLGTAAAQGATVVKQAKKEFFGEFTAVhRAPDG 118
Cdd:cd06587    75 ERLREAGAEGELVAPPVDDPWGGRSFYF-RDPDG 107
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 145-258 9.31e-03

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: 35.19  E-value: 9.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226657862 145 VILGVASPKASTVFY-EALGMSADHDY-GDKFIDFTIAEGVCrLGLLPRKPLAKDAGVSeagdgfaalvLTHLA---ASP 219
Cdd:cd06587     2 VALRVPDLDASVAFYeEVLGFEVVSRNeGGGFAFLRLGPGLR-LALLEGPEPERPGGGG----------LFHLAfevDDV 70

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1226657862 220 TEVDRLLAAAAAAGGRVTAPaRRTDDGAYVGLFADPDGH 258
Cdd:cd06587    71 DEVDERLREAGAEGELVAPP-VDDPWGGRSFYFRDPDGN 108
 
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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