ID   AMPP3_TALMQ             Reviewed;         465 AA.
AC   B6Q8T5;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=PMAA_069810;
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; DS995900; EEA25889.1; -; Genomic_DNA.
DR   RefSeq; XP_002146436.1; XM_002146400.1.
DR   AlphaFoldDB; B6Q8T5; -.
DR   SMR; B6Q8T5; -.
DR   STRING; 441960.B6Q8T5; -.
DR   PRIDE; B6Q8T5; -.
DR   EnsemblFungi; EEA25889; EEA25889; PMAA_069810.
DR   GeneID; 7024116; -.
DR   KEGG; tmf:PMAA_069810; -.
DR   VEuPathDB; FungiDB:PMAA_069810; -.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   OrthoDB; 352329at2759; -.
DR   PhylomeDB; B6Q8T5; -.
DR   Proteomes; UP000001294; Unassembled WGS sequence.
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:UniProtKB-KW.
DR   Gene3D; 3.40.350.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR007865; Aminopep_P_N.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   Pfam; PF05195; AMP_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SMART; SM01011; AMP_N; 1.
DR   SUPFAM; SSF53092; SSF53092; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome.
FT   CHAIN           1..465
FT                   /note="Probable Xaa-Pro aminopeptidase pepP"
FT                   /id="PRO_0000411883"
FT   BINDING         261
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         395
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         435
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         435
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  51734 MW;  146C726B9A8AF0C3 CRC64;
     MTSTDGILAG KYPAKAHARR VVEYLRQNGF QGDGVLYLEA QKTRMIEDND SEQPFRQRRF
     FFYLSGCLLP DAHLTYHIST DKLTLFIPPL DPESVIWSGL PLSPAQAKEL YDVDEVLYTT
     DVNPTLAHLA SKVGFVFAID GQISDDVSLK SFPDTDKVAL KTAIEECRAV KDAYEVAMIR
     KANDVTSQAH VAVLKAAKSA TNERELEAAF IGTCIAQGCR EMAYHPIVAS GTSSATLHYV
     NNDEPLIDSS TNKKKLNLLL DAAGEYKAYC ADVTRTFPLS GKFSPESREI YDIVLEMQTE
     SLAMLKEGVL WEDVHITAHR VAIKGLLKLG ILRGSEEELL EKRVSVAFFP HGLGHYLGMD
     THDTGGHANY ADKDKMFQYL RVRGKLPAGS VITVEPGVYF CRFIIEPYLK DSELSKYIDA
     DVLEKYWEVG GVRIEDNIHI TKEGHENLTT APKTADQVEL MINGS