ID   AMPP3_PYRTR             Reviewed;         463 AA.
AC   B2WMQ2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   04-NOV-2026, entry version 75.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase pepP;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   Name=pepP; ORFNames=PTRG_11262;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
CC   -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC       the N-termini of peptides. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of any N-terminal amino acid, including proline, that
CC         is linked to proline, even from a dipeptide or tripeptide.;
CC         EC=3.4.11.9;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR   EMBL; DS231630; EDU44312.1; -; Genomic_DNA.
DR   RefSeq; XP_001941593.1; XM_001941558.1.
DR   SMR; B2WMQ2; -.
DR   STRING; 426418.B2WMQ2; -.
DR   MEROPS; M24.A09; -.
DR   EnsemblFungi; EDU44312; EDU44312; PTRG_11262.
DR   GeneID; 6349575; -.
DR   KEGG; ptrr:6349575; -.
DR   eggNOG; KOG2737; Eukaryota.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   InParanoid; B2WMQ2; -.
DR   OMA; AACEWEN; -.
DR   OrthoDB; 8615at28556; -.
DR   CDD; cd01087; Prolidase; 1.
DR   FunFam; 3.90.230.10:FF:000002; Xaa-Pro aminopeptidase 3; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR   InterPro; IPR007865; Aminopep_P_N.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_N.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR052433; X-Pro_dipept-like.
DR   PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR   PANTHER; PTHR43226:SF1; XAA-PRO DIPEPTIDASE; 1.
DR   Pfam; PF05195; AMP_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SMART; SM01011; AMP_N; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:TreeGrafter.
DR   AlphaFoldDB; B2WMQ2; -.
DR   FunCoup; B2WMQ2; 392.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease.
FT   CHAIN           1..463
FT                   /note="Probable Xaa-Pro aminopeptidase pepP"
FT                   /id="PRO_0000411886"
FT   BINDING         259
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         433
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         433
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   463 AA;  52110 MW;  F74145C5533E74B4 CRC64;
     MAIAENYEDV LKGKYPAKAH AKKVAEWIIA KGGDKNGTIY LEAQKQKLNE DNDGEAPFRQ
     RRYFFYLSGC ELPDSYLTYE IATEKLTLFI PPVEPDEVIW SGLPMSPEEA KEKYDIDQCL
     TTKDVNAHLT STSESAQSTI YAIPEQVSDH ITFISYKEKE FKQLKPAIEY CRVIKSDYEI
     ALIRKANIIS TAAHEAVMKA ASTAKNECEL EAVFLKACVE RNAKNQAYHS IVAAGEHAAT
     LHYVHNAAPI SDQNLLLLDA GCEVDCYASD ITRTFPLKGK FTTESLAIYK IVLDMQHQCI
     NALKEGVVWD SVHELAHKVA IKGLLELGIL KGDAEEIFTK RISVAFFPHG LGHYLGMDTH
     DTGGNPNYAD KDVMFRYLRT RGSLPERSVI TVEPGVYFCR FIIEPYLKDE EKKKYIDESV
     LEKYWSVGGV RIEDNVLVTK NGFENLTPTP KEIDDITKLI LST
//