vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms; similar to Escherichia coli uncharacterized protein YdcJ
uncharacterized metal-dependent enzyme similar to Shigella flexneri YdcJ; The vicinal oxygen ...
8-313
0e+00
uncharacterized metal-dependent enzyme similar to Shigella flexneri YdcJ; 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: 319958 Cd Length: 310 Bit Score: 564.51 E-value: 0e+00
uncharacterized metal-dependent enzyme similar to Shigella flexneri YdcJ; The vicinal oxygen ...
8-313
0e+00
uncharacterized metal-dependent enzyme similar to Shigella flexneri YdcJ; 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: 319958 Cd Length: 310 Bit Score: 564.51 E-value: 0e+00
Domain of unknown function (DUF1338); This domain is found in a variety of bacterial and ...
9-401
3.46e-147
Domain of unknown function (DUF1338); This domain is found in a variety of bacterial and fungal proteins. This entry represents proteins involved in D-lysine metabolism, which catalyze a successive decarboxylation and intramolecular hydroxylation of 2-oxoadipate forming 2-hydroxyglutarate in a Fe(II) and oxygen-dependent manner. The structure of this domain has been solved by structural genomics. The structure implies a zinc-binding function (information derived from TOPSAN for PDB:3iuz).
Pssm-ID: 429271 Cd Length: 320 Bit Score: 422.01 E-value: 3.46e-147
uncharacterized metal-dependent enzyme similar to Shigella flexneri YdcJ; The vicinal oxygen ...
8-313
0e+00
uncharacterized metal-dependent enzyme similar to Shigella flexneri YdcJ; 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: 319958 Cd Length: 310 Bit Score: 564.51 E-value: 0e+00
Domain of unknown function (DUF1338); This domain is found in a variety of bacterial and ...
9-401
3.46e-147
Domain of unknown function (DUF1338); This domain is found in a variety of bacterial and fungal proteins. This entry represents proteins involved in D-lysine metabolism, which catalyze a successive decarboxylation and intramolecular hydroxylation of 2-oxoadipate forming 2-hydroxyglutarate in a Fe(II) and oxygen-dependent manner. The structure of this domain has been solved by structural genomics. The structure implies a zinc-binding function (information derived from TOPSAN for PDB:3iuz).
Pssm-ID: 429271 Cd Length: 320 Bit Score: 422.01 E-value: 3.46e-147
uncharacterized subfamily of the vicinal oxygen chelate (VOC) family; The vicinal oxygen ...
11-295
2.75e-49
uncharacterized subfamily of the 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: 319957 Cd Length: 221 Bit Score: 167.49 E-value: 2.75e-49
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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