Detail Information for IndEnz0009000137
IED ID IndEnz0009000137
Enzyme Type ID chitinase000137
Protein Name Probable dipeptidyl-peptidase 5
EC 3.4.14.-
Dipeptidyl-peptidase V
DPP V
DppV
Gene Name dpp5 AN2572
Organism Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Enzyme Sequence MGALRWLSLAAAASSALALTPEQLISAPRRSEAIPNPSGNIAVFSSSQYSFDTHESSSAWNLLDLRSGKITPLTNDSNVSEIVWLNDSTLLYINGTNAQIPGGSELWVSGLSNFPSGYKAASLPASFSGLKAVTTKSGDIKFVAYAQSYRNGTAYNEELAETYLSSARIYDSIYVRHWDTYLTTTFNAVFSGTLKKTQHARYASAGSLKNLVAPIPNAESPYPPFGGSSDYDISADGKWVAYKSKAPDVPQANHTTAYIYLVPHDGSETPVPINGPGSAPEGIEGDSNNPVFSPDSKSLAYLQMKDPTYESDRRVIYIYDLASKKITPLATEWDRSPDSLKWTDKSTIVAGSEDEGSGNLFLIPVKKATGDFIPEKLTNGKYASAFYLASGNTLVVTGSTLYSSWYVDLVSLNPKRGTIKNLVSAHEIDPELSGLGPEDISDIWFAGNWTDIHAWVIYPEGFDKSKTYPLAFLIHGGPQGAWYNSWSSRWNPKVFADQGYVVVAPNPTGSTGYGDELTDAIQNNWGGAPYEDLVKAWEYVRDNLDYVDTDRGVAAGASYGGFMVNWIQGSDLGREFKALVTHDGTFVADAKISTEELWFMEREFNGTFWDVRDNYRRFDPSAPERILRFATPHLIIHNDLDYRLPVAEGLSLFNVLQERGVPSRFLNFPDENHWVTSPENSLVWHQQVLGWLNKYSGIAEDNEDAVTLEDTVVPVVNINPPA
Enzyme Length 722
Uniprot Accession Number Q5BA58
Absorption
Active Site ACT_SITE 558; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 641; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 673; /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 (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..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 79,446
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda