| IED ID | IndEnz0002019338 |
| Enzyme Type ID | protease019338 |
| Protein Name |
Dipeptidase aclJ EC 3.4.13.19 Aspirochlorine biosynthesis protein J |
| Gene Name | aclJ AO090001000042 |
| Organism | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus oryzae (Yellow koji mold) Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
| Enzyme Sequence | MAMDKKGDLEWMPPRPEPVHWRNRQRSLAYSVTLTLVALFFTFALRPEAFPSFLVRKGLHKSPLEQVLTRVPLTDGHNDFAIWTRAFYQNHIYRANFTDHDELYGQVDFPRLRKGRLGAQFWSVYVECARNPNEPGVQYEIVRDTFQQIDLVHRMINHFPDFLVPASSVADVHHNFYHSPGRISSLLGIEGLHQIGGSASVLRMYHELGVRYASLTHTCHNEYADSEAPEEPRHGGLSTAGEAIVAEMNRMGMIVDLSHTSLATQRAVFNVTRAPVMYSHSSAYALCPHSRNVPDDLLQMLKENDGIVMISLYPEYTNCQDADAASLADVADHIQYVGNLIGYRHVGLGSDFDGMSHGPKGLEDVSKYPDLIQELLDRGVSVDDLVGVTGGNVLRVLGDVEHVARSLADTLPLEDDVKPFFE |
| Enzyme Length | 422 |
| Uniprot Accession Number | Q2UPB0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 217; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 291; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 351; /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 aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells (PubMed:25302411). The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues (PubMed:25302411). One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine (PubMed:25302411). After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT (PubMed:25302411). In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and aclU) act as tailoring enzymes to produce the intermediate dechloroaspirochlorine (PubMed:25302411). Ultimately, chlorination of dechloroaspirochlorine by the halogenase aclH is the last step in the aspirochlorine pathway (PubMed:25302411). {ECO:0000269|PubMed:25302411}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25302411}. |
| nucleotide Binding | |
| Features | Binding site (3); Chain (1); Disulfide bond (2); Glycosylation (2); Metal binding (3); Transmembrane (1) |
| Keywords | Dipeptidase;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,351 |
| Kinetics | |
| Metal Binding | METAL 77; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 79; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 190; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073 |
| Rhea ID | RHEA:48940 |
| Cross Reference Brenda |