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Conserved domains on  [gi|2074233095|ref|WP_219377067|]
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MULTISPECIES: VOC family protein [Citrobacter]

Protein Classification

VOC family protein( domain architecture ID 10163535)

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
PubMed:  21820381

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 6-128 1.14e-55

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


:

Pssm-ID: 319916 [Multi-domain]  Cd Length: 123  Bit Score: 169.71  E-value: 1.14e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   6 IDHLDHLVLTTNHEEACVRFYVELLGMRLETFAQGRKAFVFGNQKINLHIRGKEFEPKAYAPTPGALDLCFITTRTLEEV 85
Cdd:cd07253     1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2074233095  86 METFQTHGVDIIEGPVARTGATGPIRSVYVRDPDLNLIEIAVY 128
Cdd:cd07253    81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123
 
Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 6-128 1.14e-55

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319916 [Multi-domain]  Cd Length: 123  Bit Score: 169.71  E-value: 1.14e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   6 IDHLDHLVLTTNHEEACVRFYVELLGMRLETFAQGRKAFVFGNQKINLHIRGKEFEPKAYAPTPGALDLCFITTRTLEEV 85
Cdd:cd07253     1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2074233095  86 METFQTHGVDIIEGPVARTGATGPIRSVYVRDPDLNLIEIAVY 128
Cdd:cd07253    81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 8-131 1.22e-19

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: 78.11  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   8 HLDHLVLTTNHEEACVRFYVELLGMRL---ETFAQGRKAFVF----GNQKINLHirgkEFEPKAYAPTPGALD-LCFITT 79
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDVLGLELvkrTDFGDGGFGHAFlrlgDGTELELF----EAPGAAPAPGGGGLHhLAFRVD 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2074233095  80 rTLEEVMETFQTHGVDIIEGPvaRTGATGPiRSVYVRDPDLNLIEIAVYPAD 131
Cdd:COG0346    78 -DLDAAYARLRAAGVEIEGEP--RDRAYGY-RSAYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
8-125 4.55e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 45.52  E-value: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   8 HLDHLVLTTNHEEACVRFYVELLGMRL-----ETFAQGRKAFVFGNQKINLHIRGKEFEPKAYAPTPGA-LDLCFITTRT 81
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLveetdAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHhIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2074233095  82 LEEVMETFQTHGVDIIEGPVaRTGATGpiRSVYVRDPDLNLIEI 125
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPG-RHGWGG--RYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 6-128 1.14e-55

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319916 [Multi-domain]  Cd Length: 123  Bit Score: 169.71  E-value: 1.14e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   6 IDHLDHLVLTTNHEEACVRFYVELLGMRLETFAQGRKAFVFGNQKINLHIRGKEFEPKAYAPTPGALDLCFITTRTLEEV 85
Cdd:cd07253     1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEGRKALRFGNQKINLHQKGKEFEPKASAPTPGSADLCFITETPIDEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2074233095  86 METFQTHGVDIIEGPVARTGATGPIRSVYVRDPDLNLIEIAVY 128
Cdd:cd07253    81 LEHLEACGVTIEEGPVKRTGALGPILSIYFRDPDGNLIELSNY 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 8-131 1.22e-19

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: 78.11  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   8 HLDHLVLTTNHEEACVRFYVELLGMRL---ETFAQGRKAFVF----GNQKINLHirgkEFEPKAYAPTPGALD-LCFITT 79
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDVLGLELvkrTDFGDGGFGHAFlrlgDGTELELF----EAPGAAPAPGGGGLHhLAFRVD 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2074233095  80 rTLEEVMETFQTHGVDIIEGPvaRTGATGPiRSVYVRDPDLNLIEIAVYPAD 131
Cdd:COG0346    78 -DLDAAYARLRAAGVEIEGEP--RDRAYGY-RSAYFRDPDGNLIELVEPPPG 125
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
6-129 1.79e-12

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 59.97  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   6 IDHLDHLVLTTNHEEACVRFYVELLGMRLETFAQGRKAFVFGNQKINLHIRGKEfEPKAYAPTPGALDLCFI--TTRTLE 83
Cdd:COG2514     1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLEEAP-GAPPRPGAAGLDHVAFRvpSRADLD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2074233095  84 EVMETFQTHGVDiIEGPVARTGAtgpiRSVYVRDPDLNLIEIAVYP 129
Cdd:COG2514    80 AALARLAAAGVP-VEGAVDHGVG----ESLYFRDPDGNLIELYTDR 120
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 11-125 1.50e-09

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: 51.76  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095  11 HLVLTTNHEEACVRFYVELLGMR-LETFAQGRKAFVFGNQKINLHIRgkEFEPKAYAPTPGALDLCFiTTRTLEEVMETF 89
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEvVSRNEGGGFAFLRLGPGLRLALL--EGPEPERPGGGGLFHLAF-EVDDVDEVDERL 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2074233095  90 QTHGVDiIEGPVARTGATGPIRSVYVRDPDLNLIEI 125
Cdd:cd06587    78 REAGAE-GELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
8-125 4.55e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 45.52  E-value: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   8 HLDHLVLTTNHEEACVRFYVELLGMRL-----ETFAQGRKAFVFGNQKINLHIRGKEFEPKAYAPTPGA-LDLCFITTRT 81
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLveetdAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHhIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2074233095  82 LEEVMETFQTHGVDIIEGPVaRTGATGpiRSVYVRDPDLNLIEI 125
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPG-RHGWGG--RYSYFRDPDGNLIEL 121
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 5-125 2.99e-06

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 43.47  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   5 MIDHLDHLVLTTNHEEACVRFYVELLGMRLETFA--QGRKAFVFGNQKINLHIRGKEFEPkayaPTPGAldLCFITTRTL 82
Cdd:COG3324     1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAgpGGDYAEFDTDGGQVGGLMPGAEEP----GGPGW--LLYFAVDDL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2074233095  83 EEVMETFQTHGVDIIEGPVArTGATGpiRSVYVRDPDLNLIEI 125
Cdd:COG3324    75 DAAVARVEAAGGTVLRPPTD-IPPWG--RFAVFRDPEGNRFGL 114
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 11-126 3.29e-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: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095  11 HLVLTTNHEEACVRFYVELLGM--RLETFAQGRKAFVFGNQKINLHIRGKEFEPKAYAPTPGALDLCFiTTRTLEEVMET 88
Cdd:cd07264     3 YIVLYVDDFAASLRFYRDVLGLppRFLHEEGEYAEFDTGETKLALFSRKEMARSGGPDRRGSAFELGF-EVDDVEATVEE 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2074233095  89 FQTHGVDIIEGPVART-GATgpirSVYVRDPDLNLIEIA 126
Cdd:cd07264    82 LVERGAEFVREPANKPwGQT----VAYVRDPDGNLIEIC 116
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 25-126 4.94e-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: 319942  Cd Length: 122  Bit Score: 42.74  E-value: 4.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095  25 FYVELLGmrLETFAQGRKAFVF--GNQKINLHIRGKEFEPKAYAPTPGALD-----LCF-ITTRTLEEVMETFQTHGVDI 96
Cdd:cd08354    17 FYEDVLG--LKPMLRSGRHAFFrlGPQVLLVFDPGATSKDVRTGEVPGHGAsghghFAFaVPTEELAAWEARLEAKGVPI 94

                          90       100       110
                  ....*....|....*....|....*....|
gi 2074233095  97 IEgpVARTGATGpiRSVYVRDPDLNLIEIA 126
Cdd:cd08354    95 ES--YTQWPEGG--KSLYFRDPAGNLVELA 120
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-125 7.83e-05

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


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 39.61  E-value: 7.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   9 LDHLVLTTNHEEACVRFYVELLGM----RLETFAQGRKAFVFGNQKInLHI-RGKEFEPKAYAPTPGALD-LCFiTTRTL 82
Cdd:cd07245     1 LDHVALACPDLERARRFYTDVLGLeevpRPPFLKFGGAWLYLGGGQQ-IHLvVEQNPSELPRPEHPGRDRhPSF-SVPDL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2074233095  83 EEVMETFQTHGVDIIEGPVARTGatgpIRSVYVRDPDLNLIEI 125
Cdd:cd07245    79 DALKQRLKEAGIPYTESTSPGGG----VTQLFFRDPDGNRLEF 117
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 7-125 3.14e-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: 37.91  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   7 DHLDHLVLTTNHEEACVRFYVELLGMRL--ETFAQGRKAFVF----GNQKINLHIrgKEFEPK--AYAPTPGALDLCFiT 78
Cdd:cd08352     1 KKIHHIAIICSDYEKSKDFYVDKLGFEIirEHYRPERNDIKLdlalGGYQLELFI--KPDAPArpSYPEALGLRHLAF-K 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2074233095  79 TRTLEEVMETFQTHGVDIieGPVARTGATGPiRSVYVRDPDLNLIEI 125
Cdd:cd08352    78 VEDVEATVAELKSLGIET--EPIRVDDFTGK-KFTFFFDPDGLPLEL 121
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 9-127 6.82e-04

The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus globerulus P6 BphC2-RGP6 and BphC3-RGP6, and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, yielding 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid. This is the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Most type I extradiol dioxygenases are activated by Fe(II). Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, which form hexamers. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, its two domains do not belong to this subfamily.


Pssm-ID: 319936  Cd Length: 137  Bit Score: 37.11  E-value: 6.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   9 LDHLVLTTNHE--EACVRFYVELLGMRLETFAQGRKAFVFGNQKINLHIRGKE--FEPKAYAPTPGALDLCFITTRTLEE 84
Cdd:cd08348     2 LAHFVLRTNPEkfEAMVQWYLDILGARIVARNAKGCFLSFDEEHHRIAIFGAPggAQPPDKRPTRVGLAHIAFTYASLDD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2074233095  85 VM---ETFQTHGVDIIEgPVARtgatGPIRSVYVRDPDLNLIEIAV 127
Cdd:cd08348    82 LArnyAQLKERGIKPVW-PVNH----GVTTSIYYRDPDGNMLEMQV 122
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 10-129 9.63e-04

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: 36.93  E-value: 9.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095  10 DHLVLTTNHEEACVRFYVELLG----MRLETFAQG-------------------RKAFV-FGNqKINLHIrgkeFE---P 62
Cdd:cd16361     3 NHVGITVPDLDAAVEFYTDVLGaevvYRSTPLAEGdrgggemraagfvpgfaraRIAMLrLGP-GPGIEL----FEykgP 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2074233095  63 KAYAPTP-----GALDLCfITTRTLEEVMETFQTHGVDIIEGPVART--GATGPIRSVYVRDPDLNLIEIAVYP 129
Cdd:cd16361    78 EQRAPVPrnsdvGIFHFA-LQVDDVEAAAERLAAAGGKVLMGPREIPdgGPGKGNRMVYLRDPWGTLIELVSHP 150
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 9-120 2.48e-03

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


Pssm-ID: 433233  Cd Length: 175  Bit Score: 36.16  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074233095   9 LDHLVLTTNHEEACVRFYVELLGMRLEtfAQGRKAF--------VFGNQKINL---------HIRGKEFEPKAYAPTPGA 71
Cdd:pfam13468   1 LDHVVLAVPDLDEAAARFARALGFTVT--PGGRHPGmgtanaliMFGDGYLELlavdpeapaPPRGRWFGLDRLADGEGL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2074233095  72 LDLCFiTTRTLEEVMETFQTHGVDIIeGPVARTGATGPIRSVYVRDPDL 120
Cdd:pfam13468  79 LGWAL-RTDDIDAVAARLRAAGVEPG-RRVRPDGGDLRWRLLFLADGAL 125
MhqB_like_C cd08360
C-terminal domain of Burkholderia sp. NF100 MhqB and similar proteins; This subfamily contains ...
 9-47 6.55e-03

C-terminal domain of Burkholderia sp. NF100 MhqB and similar proteins; This subfamily contains the C-terminal, 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: 319948  Cd Length: 134  Bit Score: 34.41  E-value: 6.55e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2074233095   9 LDHLVLTTNHEEACVRFYVELLGMRLETFAQGRKAFVFG 47
Cdd:cd08360     4 LGHVLLFSPDVDRSVDFYRDLLGLKVSDRSFDIIAFMRG 42
 
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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