| IED ID | IndEnz0002009326 |
| Enzyme Type ID | protease009326 |
| Protein Name |
Dipeptidase tcpJ EC 3.4.13.19 Thiocalpurine biosynthesis protein J |
| Gene Name | tcpJ CPUR_02673 |
| Organism | Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Clavicipitaceae Claviceps Claviceps purpurea (Ergot fungus) (Sphacelia segetum) Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum) |
| Enzyme Sequence | MATAAQPSLELALELMSKVPLIGNISQSTHKIPIQCTGLTREQDGHNDWMHMIRAYYDFQVDDRFQPTKDLAGHVDLKRLVQGRAGAVFWSVYVECPKGENDFSDAVHHASMRDTFQQIDLLQRIMELYSDRMEMAHKADDVMRIFRSGKCASLMGAEGLHQLGNSSSVLRIFHRLGVRYVTLAHAKNNLYVDSATSEAPIHHGLSPQGRDMVREMNRIGMIVDLSHVSEKAMVDALDVSLAPVIFSHSSAYALVPHVRNVPDHVLDRLKQNRGIIMISFIPWLTNKDPEKATVENVVDHVLHVGNRIGFDHLGLGSDFDGMPSHVQGLEDVSKYPNVVAAMLQRGISTENVEKIMGMNVIRVLREVEDVAASQKGLLPVLEDAVPQLWDDGIRAYVKKLYPHAEHDRTGASETTTVDKAIEKDV |
| Enzyme Length | 425 |
| Uniprot Accession Number | M1VV65 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 185; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 259; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 318; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid; Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, ChEBI:CHEBI:77460; EC=3.4.13.19; Evidence={ECO:0000255|PROSITE-ProRule:PRU10073}; |
| DNA Binding | |
| EC Number | 3.4.13.19 |
| Enzyme Function | FUNCTION: Dipeptidase; part of the gene cluster that mediates the biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) lacking the reactive thiol group important for toxicity (PubMed:27390873). Firstly, L-tyrosine is prenylated by tcpD, before undergoing condensation with L-glycine in a reaction catalyzed by the NRPS tcpP leading to the diketopiperazine (DKP) backbone (PubMed:27390873). Afterwards the alpha-carbon of tyrosine is oxidized by the cytochrome P450 tcpC to form a hydroxyl group (PubMed:27390873). However, in contrast other ETP biosynthesis pathways studied so far, tcpC is not able to bishydroxylate the DKP at both alpha-carbon positions, but hydroxylates the alpha-carbon of the tyrosine part and the nitrogen of the glycine part (PubMed:27390873). The next steps involve an alpha,beta-elimination reaction catalyzed by tcpI, a methylation by the methyltransferase tcpN the action of the four enzyme cascade tcpG/K/J/I (PubMed:27390873). Due to a dysfunctional cytochrome P450 monooxygenase tcpC, the pathway leads to the biosynthesis of probable non-toxic metabolites lacking the reactive thiol group (PubMed:27390873). {ECO:0000269|PubMed:27390873}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (3); Chain (1); Metal binding (3) |
| Keywords | Dipeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | INDUCTION: Expression is positively regulated by the thioclapurine cluster-specific transcription factor tcpZ (PubMed:27390873). {ECO:0000269|PubMed:27390873}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,461 |
| Kinetics | |
| Metal Binding | METAL 46; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 48; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 158; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073 |
| Rhea ID | RHEA:48940 |
| Cross Reference Brenda |