| IED ID | IndEnz0008000185 |
| Enzyme Type ID | cellulase000185 |
| Protein Name |
Chorismate mutase CM EC 5.4.99.5 TpARO7 |
| Gene Name | ARO7 A9Z42_0036180 |
| Organism | Trichoderma parareesei (Filamentous fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Hypocreaceae Trichoderma Trichoderma parareesei (Filamentous fungus) |
| Enzyme Sequence | MDSAVDMADSERALNLTHIRFQLIRLEDTITFHLIERVQFPYNKTIYTPGAISIPDSKLSFFDWYFFQQEKLQSLIRRFESPDEYPYFPEAVQKPILKPLNYPKILHNNTVCVNDKIKKFYIEKFLPKVCPDFGREDRGEAQENYGSTSTCDIACLQALSRRIHFGKFVAESKFQSDPEYYTKLIQAEDREAIGESITNAAVEKQVLDRLRLKVETYGKDPSLLEGVEQPIKINVDAVVSMYKDFVIPLTKEVEVEYLMQRLIPEE |
| Enzyme Length | 266 |
| Uniprot Accession Number | A0A0S0FTT9 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Each dimer has two allosteric binding sites that can bind the regulatory effectors tryptophan or tyrosine (By similarity). Can bind either one tryptophan or one tyrosine, two tryptophan or two tyrosine or one tryptophan and one tyrosine, which differentially affect the catalytic activity (By similarity). Activated by tryptophan and subject to feedback inhibition by tyrosine (By similarity). In the presence of both tryptophan and tyrosine, the enzyme is in the activated state (By similarity). {ECO:0000250|UniProtKB:P32178}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000305|PubMed:26579090};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13898; Evidence={ECO:0000305|PubMed:26579090}; |
| DNA Binding | |
| EC Number | 5.4.99.5 |
| Enzyme Function | FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate (PubMed:26579090). Acts at the first branch point in the aromatic amino acid pathway where it steers biosynthesis towards phenylalanine and tyrosine, and away from tryptophan (By similarity). {ECO:0000250|UniProtKB:P32178, ECO:0000269|PubMed:26579090}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. {ECO:0000305|PubMed:26579090}. |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Region (2); Site (1) |
| Keywords | Allosteric enzyme;Amino-acid biosynthesis;Aromatic amino acid biosynthesis;Cytoplasm;Isomerase;Phenylalanine biosynthesis;Tyrosine biosynthesis |
| Interact With | |
| Induction | INDUCTION: Induced by aromatic amino acids and chorismate. {ECO:0000269|PubMed:26579090}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32178}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 30,982 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:13897; RHEA:13898 |
| Cross Reference Brenda | 5.4.99.5; |