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Conserved domains on  [gi|872684704|ref|WP_048544119|]
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MULTISPECIES: VOC family protein [Bacillus cereus group]

Protein Classification

VOC family protein( domain architecture ID 10163492)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-118 1.57e-36

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: 120.50  E-value: 1.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872684704   8 IDHVQVAAPvgCEEEARAFYGGKIGMEEIPKPEELKkRGGCWFKCGN-QEIHIGVEQNFT-------PAKKAHPAFYVLK 79
Cdd:cd07245    1 LDHVALACP--DLERARRFYTDVLGLEEVPRPPFLK-FGGAWLYLGGgQQIHLVVEQNPSelprpehPGRDRHPSFSVPD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 872684704  80 IDEFKQELIKQGIEVIDDHARL-DVIRFYVSDPFGNRIEF 118
Cdd:cd07245   78 LDALKQRLKEAGIPYTESTSPGgGVTQLFFRDPDGNRLEF 117
 
Name Accession Description Interval E-value
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-118 1.57e-36

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: 120.50  E-value: 1.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872684704   8 IDHVQVAAPvgCEEEARAFYGGKIGMEEIPKPEELKkRGGCWFKCGN-QEIHIGVEQNFT-------PAKKAHPAFYVLK 79
Cdd:cd07245    1 LDHVALACP--DLERARRFYTDVLGLEEVPRPPFLK-FGGAWLYLGGgQQIHLVVEQNPSelprpehPGRDRHPSFSVPD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 872684704  80 IDEFKQELIKQGIEVIDDHARL-DVIRFYVSDPFGNRIEF 118
Cdd:cd07245   78 LDALKQRLKEAGIPYTESTSPGgGVTQLFFRDPDGNRLEF 117
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-123 1.09e-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: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872684704   6 QGIDHVQVAapVGCEEEARAFYGGKIGMEEIPKPE-ELKKRGGCWFKCGN-QEIHIGVEQNFTPAKKA----HPAFYVLK 79
Cdd:COG0346    1 MGLHHVTLR--VSDLEASLAFYTDVLGLELVKRTDfGDGGFGHAFLRLGDgTELELFEAPGAAPAPGGgglhHLAFRVDD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 872684704  80 IDEFKQELIKQGIEVIDD--HARLDVIRFYVSDPFGNRIEFMENKN 123
Cdd:COG0346   79 LDAAYARLRAAGVEIEGEprDRAYGYRSAYFRDPDGNLIELVEPPP 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-118 7.99e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 47.06  E-value: 7.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872684704    7 GIDHVqvAAPVGCEEEARAFYGGKIGM---EEIPKPEELKKRGGcWFKCGnqEIHIGVEQNFTPAKKAHP---------A 74
Cdd:pfam00903   1 RIDHV--ALRVGDLEKSLDFYTDVLGFklvEETDAGEEGGLRSA-FFLAG--GRVLELLLNETPPPAAAGfgghhiafiA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 872684704   75 FYVLKIDEFKQELIKQGIEVID--DHARLDVIRFYVSDPFGNRIEF 118
Cdd:pfam00903  76 FSVDDVDAAYDRLKAAGVEIVRepGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-118 1.57e-36

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: 120.50  E-value: 1.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872684704   8 IDHVQVAAPvgCEEEARAFYGGKIGMEEIPKPEELKkRGGCWFKCGN-QEIHIGVEQNFT-------PAKKAHPAFYVLK 79
Cdd:cd07245    1 LDHVALACP--DLERARRFYTDVLGLEEVPRPPFLK-FGGAWLYLGGgQQIHLVVEQNPSelprpehPGRDRHPSFSVPD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 872684704  80 IDEFKQELIKQGIEVIDDHARL-DVIRFYVSDPFGNRIEF 118
Cdd:cd07245   78 LDALKQRLKEAGIPYTESTSPGgGVTQLFFRDPDGNRLEF 117
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-123 1.09e-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: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872684704   6 QGIDHVQVAapVGCEEEARAFYGGKIGMEEIPKPE-ELKKRGGCWFKCGN-QEIHIGVEQNFTPAKKA----HPAFYVLK 79
Cdd:COG0346    1 MGLHHVTLR--VSDLEASLAFYTDVLGLELVKRTDfGDGGFGHAFLRLGDgTELELFEAPGAAPAPGGgglhHLAFRVDD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 872684704  80 IDEFKQELIKQGIEVIDD--HARLDVIRFYVSDPFGNRIEFMENKN 123
Cdd:COG0346   79 LDAAYARLRAAGVEIEGEprDRAYGYRSAYFRDPDGNLIELVEPPP 124
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 21-118 2.02e-10

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: 53.68  E-value: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872684704  21 EEARAFYGGKIGMEEIPKPEelkKRGGCWFKCGNQ-EIHI---GVEQNFTPAKKAHPAFYVLKIDEFKQELIKQGIEVI- 95
Cdd:cd06587   10 DASVAFYEEVLGFEVVSRNE---GGGFAFLRLGPGlRLALlegPEPERPGGGGLFHLAFEVDDVDEVDERLREAGAEGEl 86

                         90       100
                 ....*....|....*....|....*.
gi 872684704  96 ---DDHARLDVIRFYVSDPFGNRIEF 118
Cdd:cd06587   87 vapPVDDPWGGRSFYFRDPDGNLIEF 112
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
5-118 2.04e-08

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 49.19  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872684704   5 IQGIDHVQVAAP-VgceEEARAFYGGKIGMEEIPKPEelkkrGGCWFKCGNQEIHIGVEQN-FTPAKKAHPAFYVL---- 78
Cdd:COG2514    1 ITRLGHVTLRVRdL---ERSAAFYTDVLGLEVVEREG-----GRVYLRADGGEHLLVLEEApGAPPRPGAAGLDHVafrv 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 872684704  79 ----KIDEFKQELIKQGIEVIDDHARLDVIRFYVSDPFGNRIEF 118
Cdd:COG2514   73 psraDLDAALARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIEL 116
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-118 7.99e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 47.06  E-value: 7.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872684704    7 GIDHVqvAAPVGCEEEARAFYGGKIGM---EEIPKPEELKKRGGcWFKCGnqEIHIGVEQNFTPAKKAHP---------A 74
Cdd:pfam00903   1 RIDHV--ALRVGDLEKSLDFYTDVLGFklvEETDAGEEGGLRSA-FFLAG--GRVLELLLNETPPPAAAGfgghhiafiA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 872684704   75 FYVLKIDEFKQELIKQGIEVID--DHARLDVIRFYVSDPFGNRIEF 118
Cdd:pfam00903  76 FSVDDVDAAYDRLKAAGVEIVRepGRHGWGGRYSYFRDPDGNLIEL 121
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 21-117 1.67e-05

C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family contains the C-terminal, 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: 319931  Cd Length: 132  Bit Score: 41.15  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872684704  21 EEARAFYGGKIGM---EEIPKPeelKKRGGCWFKCGNQEIH--IGVEQNFTPaKKAHPAFYVLKIDEfkqelIKQGIEVI 95
Cdd:cd08343   11 EASRDFYTDVLGFrvsDRIVDP---GVDGGAFLHCDRGTDHhtVALAGGPHP-GLHHVAFEVHDLDD-----VGRGHDRL 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 872684704  96 DDHARLDV-----------IRFYVSDPFGNRIE 117
Cdd:cd08343   82 REKGYKIEwgpgrhglgsqVFDYWFDPSGNRVE 114
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 21-122 4.19e-05

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 40.00  E-value: 4.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872684704  21 EEARAFYGGKIGMEEIPKPEELkkRGGCWFKCGNQEIHIGVEQNFTPAKK-AHPAFYVLKIDEFKQELIKQGIEVIDDHA 99
Cdd:COG3324   16 ERAKAFYEEVFGWTFEDDAGPG--GDYAEFDTDGGQVGGLMPGAEEPGGPgWLLYFAVDDLDAAVARVEAAGGTVLRPPT 93

                         90       100
                 ....*....|....*....|....*
gi 872684704 100 RLDVI--RFYVSDPFGNRIEFMENK 122
Cdd:COG3324   94 DIPPWgrFAVFRDPEGNRFGLWQPA 118
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 23-118 4.04e-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: 319942  Cd Length: 122  Bit Score: 37.34  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872684704  23 ARAFYGGKIGMEEIPKPEELkkrggCWFKCGNQEIHIgveqnFTPAK-----------------KAHPAFYVL--KIDEF 83
Cdd:cd08354   14 AEAFYEDVLGLKPMLRSGRH-----AFFRLGPQVLLV-----FDPGAtskdvrtgevpghgasgHGHFAFAVPteELAAW 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 872684704  84 KQELIKQGIEVIDDHARLDVIR-FYVSDPFGNRIEF 118
Cdd:cd08354   84 EARLEAKGVPIESYTQWPEGGKsLYFRDPAGNLVEL 119
 
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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