MULTISPECIES: VOC family protein [Bacillus]
VOC family protein( domain architecture ID 10790122)
vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms
List of domain hits
Name | Accession | Description | Interval | E-value | |||
VOC | COG3324 | Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ... |
1-114 | 1.47e-14 | |||
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only]; : Pssm-ID: 442553 [Multi-domain] Cd Length: 119 Bit Score: 64.27 E-value: 1.47e-14
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Name | Accession | Description | Interval | E-value | |||
VOC | COG3324 | Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ... |
1-114 | 1.47e-14 | |||
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only]; Pssm-ID: 442553 [Multi-domain] Cd Length: 119 Bit Score: 64.27 E-value: 1.47e-14
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VOC_like | cd07264 | uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ... |
11-115 | 7.19e-07 | |||
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping. Pssm-ID: 319925 [Multi-domain] Cd Length: 118 Bit Score: 44.24 E-value: 7.19e-07
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Name | Accession | Description | Interval | E-value | |||
VOC | COG3324 | Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ... |
1-114 | 1.47e-14 | |||
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only]; Pssm-ID: 442553 [Multi-domain] Cd Length: 119 Bit Score: 64.27 E-value: 1.47e-14
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GloA | COG0346 | Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ... |
3-114 | 8.19e-12 | |||
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: 57.31 E-value: 8.19e-12
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VOC_like | cd07264 | uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ... |
11-115 | 7.19e-07 | |||
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping. Pssm-ID: 319925 [Multi-domain] Cd Length: 118 Bit Score: 44.24 E-value: 7.19e-07
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CatE | COG2514 | Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism]; |
2-112 | 6.33e-06 | |||
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 442004 [Multi-domain] Cd Length: 141 Bit Score: 42.25 E-value: 6.33e-06
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Blast search parameters | ||||
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