Detail Information for IndEnz0002003482
IED ID IndEnz0002003482
Enzyme Type ID protease003482
Protein Name Probable dipeptidyl-aminopeptidase B
DPAP B
EC 3.4.14.5
Gene Name DAPB GSTUM_00010539001
Organism Tuber melanosporum (strain Mel28) (Perigord black truffle)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina Pezizomycetes Pezizales Tuberaceae Tuber (truffles) Tuber melanosporum (Perigord truffle) Tuber melanosporum (strain Mel28) (Perigord black truffle)
Enzyme Sequence MYDQVPYRDTDEATPQIKNDASDSNRSSIDTTSTTSLILERLHREDPDDSPGEYESSGPSQRGKPDEDDDLEIGRAARLKPMERKVRRAMYLLAFLMIGGWFLALAVYVSREHFGTPDTAHDPSATATRKAGKKITLNQVMRGAWRSKTHGIQWINGPHGDQDGLLLTQNSFGDGNFLEVQDVKNDSNTIVLIKDGALQGSGQPVSAIKGWPSSDLKKVLVASDHEKRWRHSYNARYWIYDVEKATTEPLVPSEPEARLSLATWSPKGDAIAFVKDNNVFIRQLGLDLTSEYYSVTQVTKDGGPDLFYGIPDWVYEEEVFSGNSALWWSQDGEFLAFLRTNETEVPEYPIQYFVSRPSGNNPPNGLENYPELEFIKYPKAGAPNPVVHLRFYDLKKKEDFAVTVENDFPDDDRLITEVVWSDGKYLLVRETNRESDVLRMVLIDVSARSGKVVREVDISAIDGGWFEVSKNTRYIPADPASGRPYEGYIDTVIHEGYDHLGYFTPLDNKDPILLTKGQWEVVDAPSAVDLKNGIVYFVATEKSPIERHVYSVKLDGSNFRPVTSTSEDGRYDVSFSKLSGYALLTYEGPGIPWQKVVGTPSGDQSFVKDIEKNQGLATLAAKHELPTFHYSTVNIDGFDLHVVERRPPHFNKKRKYPVLFQVYGGPGSQQVSKSFSIDFQAYIAAGLEYIVVTVDGRGTGFIGRKARVAVRGNLGYWEAHDQIETAKIWGKKGYVDKKRIAIWGWSYGGFMTLKTLEQDAGRTFSYGMAVAPVTDWRFYDSIYTERYMHTPQHNQEGYRNATISDTQALSKSVRFLLMHGVADDNVHMQNSLALLDKLDLASVENYDVHVFPDSDHSIYFHNANRMVYDRLEQWLIRAFNGEFLKLDGLKPIREISEPLRKRNRELV
Enzyme Length 907
Uniprot Accession Number D5GM60
Absorption
Active Site ACT_SITE 746; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 823; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 856; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.; EC=3.4.14.5;
DNA Binding
EC Number 3.4.14.5
Enzyme Function FUNCTION: Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Compositional bias (1); Glycosylation (3); Region (1); Topological domain (2); Transmembrane (1)
Keywords Aminopeptidase;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Serine protease;Signal-anchor;Transmembrane;Transmembrane helix;Vacuole
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Lysosome-like vacuoles. {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 102,621
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda