Detail Information for IndEnz0002019325
IED ID IndEnz0002019325
Enzyme Type ID protease019325
Protein Name Probable dipeptidyl peptidase 4
EC 3.4.14.5
Dipeptidyl peptidase IV
DPP IV
DppIV
Gene Name dpp4 ACLA_048680
Organism Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus clavatus Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
Enzyme Sequence MKLGKWSVLLLVGCTAAIDIPRKPFPPTGSGHKRLTFNETVVKPVIAPSSTAVEWISTAEDGDYVFQDSDGSLKIQSIVTNHTQTLVPADKVPDDAYSYWIHPNLSSVLWATNYTKQYRYSYFASYYIQDLQSFKLAPLASNQAGDIQYANWSPTGDAIAFVRANNVYVWTAKSTTQITTDGSADLFNGVPDWIYEEEILGDRHALWFSPDAEYLAFLRFNETGVPTFRVPYYMDNEEVAPPYPRELELRYPKVSQTNPTVEVRLLSRATGEVSSVSIKAFNATDLVIGEVAWLTETHSQVAVKAFNRVQDQQKVVTVDVLSLKTKTISERDGTDGWLDNALSITYIGQIGDSKAEYYIDISDESGWAHLWLFPVAGGRPMALTKGEWEVTAILSIDKQRQLVYYLSTQHHSTERHVYSVSWKTFTATPLVDDTVAAVWSASFSSQGGYYILSYRGPDVPYQELYAINSTKPLCTITSNAAVYDVLKQYTLPKISYFELRLPSGETLNVMQRLPVSFSPRKKYPILFTPYGGPGAQEVSKAWQSQTFKSYIASDPELEFVTWTVDNRGTGYKGRRFRGQVAKQLGRLEAQDQVWAAQQAAKLPFIDAEHIAIWGWSYGGYLTGKVIETDSGVFSLGVLTAPVSDWRFYDSMYTERYMKTLQENANGYNASAIWDVAGYKNVRGGVLIQHGTGDDNVHFQNAAALVDRLVGEGVSPDKLQVQWFTDSDHGIRYHGGSVFLYRQLAKRLYEEKHRKKSEGHQWSKRSLEF
Enzyme Length 768
Uniprot Accession Number A1CHP1
Absorption
Active Site ACT_SITE 616; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 693; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 728; /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: Extracellular 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); Glycosylation (8); Signal peptide (1)
Keywords Aminopeptidase;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 86,453
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda