| IED ID | IndEnz0002008237 |
| Enzyme Type ID | protease008237 |
| Protein Name |
Dipeptidase sirJ EC 3.4.13.19 Sirodesmin biosynthesis protein J |
| Gene Name | sirJ |
| Organism | Leptosphaeria maculans (Blackleg fungus) (Phoma lingam) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Leptosphaeriaceae Leptosphaeria Leptosphaeria maculans species complex Leptosphaeria maculans (Blackleg fungus) (Phoma lingam) |
| Enzyme Sequence | MKSEPGNEFLERAANLLSRVPLIDGHNDWANIIRGYYSNKIHVRNFSREESLVGHVDIKKLRKGLVGGTFWSAYVDCPAQDKINVFNDDSYLETIRETLQQIDLILRLIKKYPDDLELATTSSGILSSFQNGKIASLLGIEGLHQIGNSPSVLRMFYNLGVRYATLTHNHNNAYADSATAKTPVHNGLSIKGRAIIQEMNRLGMIIDLSHTSEQTAEDVLRQTRAPIIFSHSSAFGVHPHPRNVKDNILHMLKSNKGLIMISFVPEFSSADPGLSSLMDVVKHIIYVGELIGYDHVGIGSDFDGMARAVLGLSDTSTFPRLVAELIANQIPEGDVEKIVGGNLIRVMGDVEAVAHRQCEDDILELEEEVKPLWDDAFKAKIAAAYPEALALNAL |
| Enzyme Length | 394 |
| Uniprot Accession Number | Q6Q886 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 168; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 242; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 301; /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 sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola (PubMed:15387811, PubMed:18272357, PubMed:19762440). SirD catalyzes the O-prenylation of L-tyrosine (L-Tyr) in the presence of dimethylallyl diphosphate (DMAPP) to yield 4-O-dimethylallyl-L-Tyr, and therefore represents probably the first pathway-specific enzyme in the biosynthesis of sirodesmin PL (PubMed:19762440, PubMed:21038099, PubMed:24083562). 4-O-dimethylallyl-L-Tyr, then undergoes condensation with L-Ser in a reaction catalyzed by the non-ribosomal peptide synthase sirP to form the diketopiperazine (DKP) backbone (PubMed:18272357). Further bishydroxylation of the DKP performed by the cytochrome P450 monooxygenase sirC leads to the production of the intermediate phomamide (PubMed:27390873). This step is essential to form the reactive thiol group required for toxicity of sirodesmin PL (PubMed:27390873). The next steps of sirodesmin biosynthesis are not well understood yet, but some predictions could be made from intermediate compounds identification (PubMed:18272357). Phomamide is converted into phomalizarine via oxidation, probably by sirT (PubMed:18272357). Further oxidation, methylation (by sirM or sirN) and reduction steps convert phomalizarine to deacetyl sirodesmin (PubMed:18272357). Finally, acetyltransferase sirH probably acetylates deacetyl sirodesmin to produce sirodesmin PL (PubMed:18272357). {ECO:0000269|PubMed:19762440, ECO:0000269|PubMed:21038099, ECO:0000269|PubMed:24083562, ECO:0000269|PubMed:27390873, ECO:0000305|PubMed:15387811, ECO:0000305|PubMed:18272357}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:15387811}. |
| nucleotide Binding | |
| Features | Binding site (3); Chain (1); Metal binding (3) |
| Keywords | Dipeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Virulence;Zinc |
| Interact With | |
| Induction | INDUCTION: Expression is co-regulated with the other genes from the sirodesmin cluster and corresponds with sirodesmin production (PubMed:15387811). {ECO:0000269|PubMed:15387811}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,535 |
| Kinetics | |
| Metal Binding | METAL 26; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 28; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 141; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073 |
| Rhea ID | RHEA:48940 |
| Cross Reference Brenda |