Detail Information for IndEnz0002016666
IED ID IndEnz0002016666
Enzyme Type ID protease016666
Protein Name Probable Xaa-Pro aminopeptidase SNOG_02267
EC 3.4.11.9
Aminoacylproline aminopeptidase
Prolidase
Gene Name SNOG_02267
Organism Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Phaeosphaeriaceae Parastagonospora Phaeosphaeria nodorum (Glume blotch fungus) (Parastagonospora nodorum) Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum)
Enzyme Sequence MEVLDATSLAERLKWEAKGYWLHFEAETPLEKYPAKQHARRVQEKLGIEEGLIYLSGQQARNNEDSDMPAPFRQLRYFYYLSGGPTLAEALVKYDVDEVYYSDEVSDYIIDWYHHSCNRGKLYTLHDPAKSPIGNHHAPIDSVSLQPAMNVARMIKDEHEIKLIRKANDISSKAHREVLSNILKFTNEAQVEGLFLDVCVSHQAKQQAYDPIAASGPNAGTLHYDANDEDFGKRQLMCLDAGCEYELYASDITRTFPLSSKWPSKEAANIYRLVERMQELCIKRLAPGVRYLDLHILAHQIAIDGLLALGILHNGTKEEIYKAGTSRAFFPHGLGHHIGLEVHDVGQAELMSVRRGKQVLEQSSHLEEGMIVTVEPGIYFSVYALQHFYLPSPVHSKYINLEVLNRYLPVGGVRIEDDILITAKSYENLTTAPKGDEMLEIIQRGRSNVNSIPARRQSGRTQITEDEPPLLRAPGISASTPQSILRPIARSSTMPAELKQDKSVDFEPFEGPSLFSNFRRSMTTDEKIQRWQQDHIPTTATRINLTPSSQYKSVCGSNTREVKHVYMISGSFPPGTARGALREQILPACKQCTILCETLDRLRQSLSMSKESPEAELDVSPVISQKQIRNRRSVSSTARHDLRGDRERPQHSPMTGLANGLSAMCLEPLNHVSESPTPSQRRAGGCTPHWRGQNRADQSGDDALRAAQETQILQSKPSVRSNPATDQLSAKAVSDVLLELQRQGPAAGSDRCTLGKQEGVEGIPAISRAKNFHVSTGGSMVGEARRAEE
Enzyme Length 789
Uniprot Accession Number Q0V147
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9;
DNA Binding
EC Number 3.4.11.9
Enzyme Function FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (1); Metal binding (6); Region (2)
Keywords Aminopeptidase;Hydrolase;Manganese;Metal-binding;Metalloprotease;Protease;Reference proteome
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 88,042
Kinetics
Metal Binding METAL 240; /note=Manganese 2; /evidence=ECO:0000250; METAL 251; /note=Manganese 1; /evidence=ECO:0000250; METAL 251; /note=Manganese 2; /evidence=ECO:0000250; METAL 375; /note=Manganese 1; /evidence=ECO:0000250; METAL 416; /note=Manganese 1; /evidence=ECO:0000250; METAL 416; /note=Manganese 2; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda