IED ID | IndEnz0002019011 |
Enzyme Type ID | protease019011 |
Protein Name |
Putative dipeptidase TRV_05564 EC 3.4.13.19 |
Gene Name | TRV_05564 |
Organism | Trichophyton verrucosum (strain HKI 0517) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton verrucosum (Cattle ringworm fungus) Trichophyton verrucosum (strain HKI 0517) |
Enzyme Sequence | MAALFVSLLALTSLVPVQGAATVPQTDYAKRAERVLKSAPLIDGHNDLLYAIRRSTNDQIYDGKLPFETSLKGHTDLPRMRKGRMGGQFWSVFIACPSDPNAPINTPKFATRDTLEQIDVARRLVDKYSKDLMYCDNPGCAKRAFREGKIGSFIGIEGGHQVGSSIAALRQAFYAGARYMTLTHNCDNAWATAASTVRAGKPDLGMTDFGPALIKEMNRLGMLVDLSHVSHQTMRDVLKITKAPVIFSHSSAYEVSKHLRNVPDDVLKTVAKNNGVVMVTFVSSFVKVDDPDSADVNTVVKHIFHIAEVAGWDHVGLGGDYDGTTELPKGLEDVSKYPYLIEKVLEAGATEEQARKLVGENVLRVWTEVEQIAKKIQRSGVLPVEEVWKGRNGTALSERSTFIEGPAPLEYGCD |
Enzyme Length | 414 |
Uniprot Accession Number | D4DEJ7 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 184; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 260; /note=Substrate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; BINDING 320; /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: Hydrolyzes a wide range of dipeptides. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Binding site (3); Chain (1); Disulfide bond (1); Glycosylation (1); Metal binding (6); Signal peptide (1) |
Keywords | Dipeptidase;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Signal;Zinc |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 45,407 |
Kinetics | |
Metal Binding | METAL 45; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 47; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 157; /note=Zinc 1; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 157; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 228; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073; METAL 249; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10073 |
Rhea ID | RHEA:48940 |
Cross Reference Brenda |