ID   AMPP1_PYRTT             Reviewed;         656 AA.
AC   E3S7K9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase P;
DE            Short=AMPP;
DE            Short=Aminopeptidase P;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   Name=ampp; ORFNames=PTT_18815;
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1;
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
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; GL537558; EFQ86051.1; -; Genomic_DNA.
DR   RefSeq; XP_003305864.1; XM_003305816.1.
DR   AlphaFoldDB; E3S7K9; -.
DR   SMR; E3S7K9; -.
DR   STRING; 861557.E3S7K9; -.
DR   EnsemblFungi; EFQ86051; EFQ86051; PTT_18815.
DR   KEGG; pte:PTT_18815; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_3_1; -.
DR   OrthoDB; 417805at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01085; APP; 1.
DR   Gene3D; 3.40.350.10; -; 2.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR033740; Pept_M24B.
DR   InterPro; IPR032416; Peptidase_M24_C.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 1.
DR   SUPFAM; SSF53092; SSF53092; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome.
FT   CHAIN           1..656
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411808"
FT   BINDING         453
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         464
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         464
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         562
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         576
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         576
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   656 AA;  73488 MW;  BAD2F9E88C9B38F6 CRC64;
     MLLPRIPQLS HATRAAYVAA KSPFSPVPVR PFHASAALRA IDMAKVDTTH RLAELRKLMK
     ERNVDIYMVP SEDSHQSEYI APCDARRAYI SGFTGSAGYA VITHEKAALS TDGRYFNQAE
     KQLDSNWELL KQGIQDVPTI QQWTADQAGG GKVVGVDPSV VTAGDARKLA EKIKKKGGEY
     KAIDENLVDL VWGSERPARP SEKVIVQPKK YAGKGFEDKI DDLRKELEKK KSLGFVVSML
     DEVAWLFNLR GSDIPYNPVF FSYAVVTPTT ATLYVDENKL PEDVKEHLGD KITIRPYEAI
     FGDVTALSKE LFEANDKNET QKKFLTSNTA SWALNKALGG DDKVEETRSP VGDSKAVKNE
     VELEGMRQCH IRDGAALSEY FAWLEDQLIN KKATLDEVDG ADKLEEIRKK HDMFMGLSFD
     TISSTGANAA VIHYKPEKGE CATIDSKAIY LCDSGAQYRD GTTDTTRTLH FTEPTEMERK
     AYTLVLKGNM ALERVKFPKG TTGFALDALA RQFLWAEGLD YRHGTGHGVG SFLNVHEGPI
     GIGTRVQYSE VSLAVGNVVS DEPGYYEDGK FGIRIENMVM VKEVETKHKF GDKPYLGFEH
     VTMTPYCRNL VDMKLLTEDE KKFINDYHKE VYEKTSKYFD KDALTLEWLK RETAPY