IED ID | IndEnz0002005219 |
Enzyme Type ID | protease005219 |
Protein Name |
Dipeptidyl-peptidase 5 EC 3.4.14.- Dipeptidyl-peptidase V DPP V DppV |
Gene Name | AFUB_024920 |
Organism | Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) |
Enzyme Sequence | MGAFRWLSIAAAASTALALTPEQLITAPRRSEAIPDPSGKVAVFSTSQYSFETHKRTSWWSLLDLKTGQTKVLTNDSSVSEIVWLSDDSILYVNSTNADIPGGVELWVTQASSFAKGYKAASLPASFSGLKAAKTKSGDIRFVAYGQSYPNGTAYNEELATAPLSSARIYDSIYVRHWDYWLSTTFNAVFSGTLKKGHGKNGYSLDGELKNLVSPVKNAESPYPPFGGASDYDLSPDGKWVAFKSKAPELPKANFTTSYIYLVPHDASETARPINGPDSPGTPKGIKGDSSSPVFSPNGDKLAYFQMRDETYESDRRVLYVYSLGSKKTIPSVAGDWDRSPDSVKWTPDGKTLIVGSEDLGRTRLFSLPANAKDDYKPKNFTDGGSVSAYYFLPDSSLLVTGSALWTNWNVYTAKPEKGVIKKIASANEIDPELKGLGPSDISEFYFQGNFTDIHAWVIYPENFDKSKKYPLIFFIHGGPQGNWADGWSTRWNPKAWADQGYVVVAPNPTGSTGFGQALTDAIQNNWGGAPYDDLVKCWEYVHENLDYVDTDHGVAAGASYGGFMINWIQGSPLGRKFKALVSHDGTFVADAKVSTEELWFMQREFNGTFWDARDNYRRWDPSAPERILQFATPMLVIHSDKDYRLPVAEGLSLFNVLQERGVPSRFLNFPDENHWVVNPENSLVWHQQALGWINKYSGVEKSNPNAVSLEDTVVPVVNYN |
Enzyme Length | 721 |
Uniprot Accession Number | B0XRV0 |
Absorption | |
Active Site | ACT_SITE 560; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 643; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 675; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.14.- |
Enzyme Function | FUNCTION: May be involved in metabolism of dipeptides or may affect host defense mechanisms. Has a substrate specificity limited to the hydrolysis of X-Ala, His-Ser, and Ser-Tyr dipeptides at a neutral pH optimum. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5.; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Glycosylation (7); Region (1); Sequence conflict (2); Signal peptide (1) |
Keywords | Direct protein sequencing;Glycoprotein;Hydrolase;Protease;Secreted;Serine protease;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | PTM: N-glycosylated. |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:9045640 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 79,743 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |