Detail Information for IndEnz0002019338
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