EC Number | Cloned (Comment) | Organism |
---|---|---|
4.2.1.118 | gene asbF, sequence comparisons and phylogenetic analysis | Bacillus anthracis |
4.2.1.118 | gene quiC1, sequence comparisons and phylogenetic analysis | Pseudomonas aeruginosa |
4.2.1.118 | gene quiC1, sequence comparisons and phylogenetic analysis, plasmid-based expression of Pseudomonas putida QuiC1 in the Pseudomonas aeruginosa quiC1 knockout strain, recombinant expression of wild-type and mutant enzymes | Pseudomonas putida |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.2.1.118 | E356A | site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme | Pseudomonas putida |
4.2.1.118 | H168A | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Pseudomonas putida |
4.2.1.118 | additional information | quiC1 transposon quiC1 gene knockout in strain PAO1, recombinant plasmid-based expression of gene quiC1 from Pseudomonas putida QuiC1 in the Pseudomonas aeruginosa quiC1 knockout strain | Pseudomonas aeruginosa |
4.2.1.118 | additional information | the isolated N-terminal domain shows about 1/3 of the wild-type enzyme activity | Pseudomonas putida |
4.2.1.118 | R207A | site-directed mutagenesis, the mutant shows moderately reduced activity compared to the wild-type enzyme | Pseudomonas putida |
4.2.1.118 | R210A | site-directed mutagenesis, inactive mutant | Pseudomonas putida |
4.2.1.118 | S206A | site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme | Pseudomonas putida |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.118 | 0.134 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant mutant H168A | Pseudomonas putida | |
4.2.1.118 | 0.205 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant isolated N-terminal domain of the enzyme | Pseudomonas putida | |
4.2.1.118 | 0.331 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant wild-type enzyme | Pseudomonas putida | |
4.2.1.118 | 0.429 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant mutant E356A | Pseudomonas putida | |
4.2.1.118 | 2.745 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant mutant S206A | Pseudomonas putida | |
4.2.1.118 | 5.311 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant mutant R207A | Pseudomonas putida |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.118 | Co2+ | required | Pseudomonas putida | |
4.2.1.118 | Mg2+ | enzyme bound | Pseudomonas aeruginosa |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.118 | 3-dehydro-shikimate | Pseudomonas aeruginosa | - |
protocatechuate + H2O | - |
? | |
4.2.1.118 | 3-dehydro-shikimate | Pseudomonas putida | - |
protocatechuate + H2O | - |
? | |
4.2.1.118 | 3-dehydro-shikimate | Bacillus anthracis | - |
protocatechuate + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.118 | Bacillus anthracis | Q81RQ4 | - |
- |
4.2.1.118 | Pseudomonas aeruginosa | - |
- |
- |
4.2.1.118 | Pseudomonas putida | A0A379KX44 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.118 | 3-dehydro-shikimate | - |
Pseudomonas aeruginosa | protocatechuate + H2O | - |
? | |
4.2.1.118 | 3-dehydro-shikimate | - |
Pseudomonas putida | protocatechuate + H2O | - |
? | |
4.2.1.118 | 3-dehydro-shikimate | - |
Bacillus anthracis | protocatechuate + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.2.1.118 | More | three-dimensional structure comparisons, superimposition of the QuiC1 N-terminal (DSD) domain with Bacillus anthracis AsbF and structure comparisons with Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase (HPPD), overview | Pseudomonas putida |
4.2.1.118 | More | three-dimensional structure comparisons, superimposition of the QuiC1 N-terminal (DSD) domain with Bacillus anthracis AsbF, and structure comparisons with Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase (HPPD), overview | Pseudomonas aeruginosa |
4.2.1.118 | More | three-dimensional structure comparisons, superimposition of the QuiC1 N-terminal (DSD) domain with Bacillus anthracis AsbF, and structure comparisons with Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase (HPPD), overview | Bacillus anthracis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.2.1.118 | AsbF | - |
Bacillus anthracis |
4.2.1.118 | dehydroshikimate dehydratase | - |
Pseudomonas aeruginosa |
4.2.1.118 | dehydroshikimate dehydratase | - |
Pseudomonas putida |
4.2.1.118 | dehydroshikimate dehydratase | - |
Bacillus anthracis |
4.2.1.118 | DSD | - |
Pseudomonas aeruginosa |
4.2.1.118 | DSD | - |
Pseudomonas putida |
4.2.1.118 | DSD | - |
Bacillus anthracis |
4.2.1.118 | Qui1 | - |
Pseudomonas aeruginosa |
4.2.1.118 | Qui1 | - |
Pseudomonas putida |
4.2.1.118 | quiC1 | - |
Pseudomonas aeruginosa |
4.2.1.118 | quiC1 | - |
Pseudomonas putida |
4.2.1.118 | quiC_1 | - |
Pseudomonas putida |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.118 | 7.7 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant mutant H168A | Pseudomonas putida | |
4.2.1.118 | 61.2 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant isolated N-terminal domain of the enzyme | Pseudomonas putida | |
4.2.1.118 | 99.1 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant mutant R207A | Pseudomonas putida | |
4.2.1.118 | 138.2 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant mutant E356A | Pseudomonas putida | |
4.2.1.118 | 148.1 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant mutant S206A | Pseudomonas putida | |
4.2.1.118 | 163.6 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant wild-type enzyme | Pseudomonas putida |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.2.1.118 | 7.5 | - |
assay at | Pseudomonas putida |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.2.1.118 | evolution | the QuiC1 protein is not related by sequence with previously identified DSDs from the Gram-negative genus, Acinetobacter, but instead shows limited sequence identity in its N-terminal half with fungal DSDs | Pseudomonas aeruginosa |
4.2.1.118 | evolution | the QuiC1 protein is not related by sequence with previously identified DSDs from the Gram-negative genus, Acinetobacter, but instead shows limited sequence identity in its N-terminal half with fungal DSDs | Pseudomonas putida |
4.2.1.118 | additional information | enzyme structure-function analysis, overview | Pseudomonas aeruginosa |
4.2.1.118 | additional information | superimposition of the active sites of the Pseudomonas putida QuiC1 N-terminal domain and Bacillus anthracis AsbF in complex with protocatechuate. AsbF residues occupying the same position as QuiC1 Arg207 and Arg210 are not observed. Enzyme structure-function analysis, overview | Pseudomonas putida |
4.2.1.118 | additional information | superimposition of the active sites of the Pseudomonas putida QuiC1 N-terminal domain and Bacillus anthracis AsbF in complex with protocatechuate. AsbF residues occupying the same position as QuiC1 Arg207 and Arg210 are not observed. Enzyme structure-function analysis, overview | Bacillus anthracis |
4.2.1.118 | physiological function | enzyme Qui1 is important for growth on either quinate or shikimate | Pseudomonas aeruginosa |
4.2.1.118 | physiological function | enzyme Qui1 is important for growth on either quinate or shikimate | Pseudomonas putida |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.118 | 18.7 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant mutant R207A | Pseudomonas putida | |
4.2.1.118 | 53.9 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant mutant S206A | Pseudomonas putida | |
4.2.1.118 | 57.5 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant mutant H168A | Pseudomonas putida | |
4.2.1.118 | 298.5 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant isolated N-terminal domain of the enzyme | Pseudomonas putida | |
4.2.1.118 | 322.2 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant mutant E356A | Pseudomonas putida | |
4.2.1.118 | 494.3 | - |
3-dehydro-shikimate | pH 7.5, temperature not specified in the publication, recombinant wild-type enzyme | Pseudomonas putida |