Detail Information for IndEnz0002018911
IED ID IndEnz0002018911
Enzyme Type ID protease018911
Protein Name Probable dipeptidyl-aminopeptidase B
DPAP B
EC 3.4.14.5
Gene Name dapB Pc20g06070
Organism Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Penicillium Penicillium chrysogenum species complex Penicillium rubens Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum)
Enzyme Sequence MGKFEDDGNSESVPLTRQRSESLASQTSTDSGLSIASESFMKNHKGGNTMPTDGGDGDRYLDVEDGGETGLDEPLISSGTKTGSSSRLRKIVWLLVLLCVGGWVLSFVLFLTQKRPDTAALSSASTVEIHEPGPATGGTSHGKPVTLEQVLSGTWSPKSHAISWIAGPDGEDGLLVEQGEKQDAFLRVKDIRSSEDGVDNLETRVLMKKGYIWFDGEAMLSAKTWPSPDMNRVLVMTDIQSNWRHSYFGKYWILDVATQKAEPLDPGNLSGRVQLAAWSPTSDAVVFVRENNLYLRKLTSLEVTPITKDGDENLFYGVPDWVYEEEVFSGNTGTWWSDDGKFVAFLRTNETAVPEYPIQYFRSRPSGKQPPPGLENYPEVRQIKYPKPGSPNPIVNLQFYDVEKNEVFSFEMPEDFVDDERIIIEVVWASEGKVLIRETNRESDVVKIFVMDTKARTGKLVRSDDIAALDGGWVEPTQSTRVIPADPKNGRPHDGYVDTVIYEGYDHLAYFTPFDNPEPVMLTKGNWEVVNAPSAVDLKKGLVYFVATKEAPTQRHVYSVKLDGSDLRPLTDTSAPGFFDVSFSHGAGYGLLSYKGPAVPWQAVINTQGDEIDFINLIEENVELAKMVEESAIPTEVYSNVTIDGYTLQVLERRPPNFNPEKKYPVLFFLYGGPGSQTVDRKFTIDFQTYVASNLGYIVVTVDGRGTGFIGREARCLVRGNIGHYEAIDQIETAKIWASKSYVDESRMAVWGWSYGGYMTLKVLEQDAGETFQYGMAVAPVTDWRFYDSIYTERYMHTPEHNPSGYANASIDDVMALGHSVRFLIMHGVADDNVHLQNTLVLIDKLDLKNIDNYDMQVFPDSDHSIQFHMAHALVYERLSSWLINAFNGEWHRTANPKPQEST
Enzyme Length 903
Uniprot Accession Number B6HFS8
Absorption
Active Site ACT_SITE 754; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 831; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 864; /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 (4); Region (2); 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 100,902
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda