Detail Information for IndEnz0002014136
IED ID IndEnz0002014136
Enzyme Type ID protease014136
Protein Name Probable Xaa-Pro aminopeptidase P
AMPP
Aminopeptidase P
EC 3.4.11.9
Aminoacylproline aminopeptidase
Prolidase
Gene Name AMPP BDCG_09239
Organism Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces dermatitidis)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Ajellomycetaceae Blastomyces Ajellomyces dermatitidis (Blastomyces dermatitidis) Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces dermatitidis)
Enzyme Sequence MGPVDTSQRLARLRELMQERKVDVYIVPSEDSHQSEYIAPCDGRREFISGFTGSAGCAIVSMSKAALSTDGRYFNQAAKQLDNNWMLLKRGFENMPTWQEWTAEQAEGGKVVGVDPSLITASEARSLSETIEKSGGSLQGVQENLIDLVWGKERPARPSEKVALHPIEFAGKSFEEKISDLRKELQKKKSAGFVISMLDEIAWLFNLRGNDIPYNPVFFAYAIITPTTADLYIDDEKLPAEVKKYLGDQVSVKPYGSIFEDAKALSQSAQKKSDGDASTSPSEKFLISTKASWSLSLALGGEKNVEEVRSPITDAKAIKNEAELEGMRACHIRDGAALTEYFAWLENELVNKKTVLNEVDGSDKLEQIRSKHKHFVGLSFDTISSTGPNAAVIHYKAERDTCSIIDPKAVYLCDSGAQYLDGTTDTTRTLHFGEPTEMERKAYTLVLKGLISIDTAVFPKGTTGFALDAFARQHLWKEGLDYLHGTGHGVGSYLNVHEGPIGLGTRVQYAEVAITPGNVISDEPGFYEDGVFGIRIENIIIAKEVKTTHGFGEKPWLGFEHVTMTPLCQKLINPSLLTDGEKKWVNDYHSKVWEKTSSYFENDELTRNWLKRETQPI
Enzyme Length 617
Uniprot Accession Number C5GXZ9
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); Metal binding (6)
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 68,559
Kinetics
Metal Binding METAL 414; /note=Manganese 2; /evidence=ECO:0000250; METAL 425; /note=Manganese 1; /evidence=ECO:0000250; METAL 425; /note=Manganese 2; /evidence=ECO:0000250; METAL 523; /note=Manganese 1; /evidence=ECO:0000250; METAL 537; /note=Manganese 1; /evidence=ECO:0000250; METAL 537; /note=Manganese 2; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda