Detail Information for IndEnz0002011765
IED ID IndEnz0002011765
Enzyme Type ID protease011765
Protein Name Dipeptidase verJ
EC 3.4.13.19
Verticillin biosynthesis cluster protein J
Fragment
Gene Name verJ
Organism Clonostachys rogersoniana
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Bionectriaceae Clonostachys Clonostachys rogersoniana
Enzyme Sequence PIVSKMALLDDNLSKALKLLADVPLIDGHNDFPYFIRGWFPEQIDSLDCRNVRIAHTDLERLNQGRVGGVFWSAYVPCPDRHAKNDFVVDAQYESLRATMQQIDIIHTLIERYSDRLGLARTSSEVWEVFRSGRIASLIGVEGLHQIANSPGVMRNLYRLGVRYITLTHDSNNLYADSTNSSGPFHGGLSRDGISIVKEMNRIGMMVDLSHTSVATQKHVLAISKAPVIFSHSSCASVTEHPRNSPDDVLDMLKANGGVFMITFIRKPTDAESPTLEKVADHVQHVGDRIGYEHVGIGSDFDGVMLTASGLDDVSKFPLLIAELLKRGVSDHSIKNMIGLNVLRVMDSVEEVSMKMKETGEEMLHEVFEEIWDEKMRDEVRKTRDIFD
Enzyme Length 388
Uniprot Accession Number A0A1U9YI27
Absorption
Active Site
Activity Regulation
Binding Site BINDING 169; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 243; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 300; /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:0000250|UniProtKB:Q4WMJ8};
DNA Binding
EC Number 3.4.13.19
Enzyme Function FUNCTION: Dipeptidase; part of the gene cluster that mediates the biosynthesis of 11'-deoxyverticillin A, one of the dimeric epipolythiodioxopiperazines (ETPs) from the verticillin family that act as mycotoxins (PubMed:28376389). 11'-deoxyverticillin A is required for normal conidiation (PubMed:28376389). The nonribosomal peptide synthetase verP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of verticillin, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of 11'-deoxyverticillin A (Probable). {ECO:0000269|PubMed:28376389, ECO:0000305|PubMed:28376389}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:28376389}.
nucleotide Binding
Features Binding site (3); Chain (1); Erroneous gene model prediction (1); Metal binding (3); Non-terminal residue (1)
Keywords Dipeptidase;Hydrolase;Metal-binding;Metalloprotease;Protease;Zinc
Interact With
Induction INDUCTION: Expression is regulated by the cluster-specific regulator verZ. {ECO:0000269|PubMed:29058652}.
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 43,458
Kinetics
Metal Binding METAL 29; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 31; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 142; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073
Rhea ID RHEA:48940
Cross Reference Brenda