| IED ID | IndEnz0002019025 | 
| Enzyme Type ID | protease019025 | 
| Protein Name | 
                        
                            
                                Probable dipeptidyl-peptidase 5  EC 3.4.14.- Dipeptidyl-peptidase V DPP V DppV  | 
                    
| Gene Name | dpp5 An12g04700 | 
| Organism | Aspergillus niger (strain CBS 513.88 / FGSC A1513) | 
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus niger Aspergillus niger (strain CBS 513.88 / FGSC A1513) | 
| Enzyme Sequence | MGALQWLSITAAAASAVSALTPEQMIGAPRRTEVIPNPSGDTGLFSTSQWSFDTHSESTWWSLIDLQSGKTTTLTDDSDIEEIIWLGSDNSTLLYINSTNAQVPGGVELWIADSSDFANAYKAASLSAGFLGIKSTVTDSGDVHFILRGKSYPNGTAYNDQLAETYPSTARIYDSIFVRHWDTYLTTASHAVFSGTLQSSTSDDGNVQYTSSGGLTNLVNPVKGAESPFPPFGGNDDYDLSPDGKWVTFKSKAPELPLANNTAAYVYLVPHDGSATAFAVNGPDSPATPEGVEGESNNPVFSPDSDKIAYFQMATNTYESDRNVLYVYSIADDTITPLAKDWDRSPSSVTWVDGDNLVVASQDLGRTRLFAIPGDAGDDFKPTNFTDGGSVSAQYVLSNSTLLVTSSAFWTSWSVYTASPDEGVINTLASANEIDPELSGLSSSDFEEFYFDGNWTTLQGWITYPQDFDSSKKYPLAFLIHGGPEDAWADEWNLKWHSKVFADQGYVVVQPNPTGSTGFGQQLTDAIQLNWTGAAYDDLTKAWQYVHDTYDFIDTDNGVAAGPSFGAFMITWIQGDDFGRKFKALVSHDGPFIGDAWVETDELWFVEHEFNGTFWQARDAFHNTDPSGPSRVLAYSTPQLVIHSDKDYRIPVANGIGLFNTLQERGVPSRFLNFPDEDHWVTGQENSLVWYQQVLGWINRYSGVGGSNPDAIALEDTVNPVVDLNP | 
| Enzyme Length | 726 | 
| Uniprot Accession Number | A2QZF1 | 
| Absorption | |
| Active Site | ACT_SITE 564; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 647; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 679; /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: Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini. {ECO:0000250}. | 
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Glycosylation (9); 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..19; /evidence=ECO:0000255 | 
| Structure 3D | |
| Cross Reference PDB | - | 
| Mapped Pubmed ID | - | 
| Motif | |
| Gene Encoded By | |
| Mass | 79,278 | 
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |