ID   AMPP1_TALMQ             Reviewed;         657 AA.
AC   B6QG01;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=PMAA_083920;
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; DS995901; EEA24386.1; -; Genomic_DNA.
DR   RefSeq; XP_002147897.1; XM_002147861.1.
DR   AlphaFoldDB; B6QG01; -.
DR   SMR; B6QG01; -.
DR   STRING; 441960.B6QG01; -.
DR   MEROPS; M24.009; -.
DR   EnsemblFungi; EEA24386; EEA24386; PMAA_083920.
DR   GeneID; 7025520; -.
DR   KEGG; tmf:PMAA_083920; -.
DR   VEuPathDB; FungiDB:PMAA_083920; -.
DR   HOGENOM; CLU_011781_2_2_1; -.
DR   OrthoDB; 417805at2759; -.
DR   PhylomeDB; B6QG01; -.
DR   Proteomes; UP000001294; 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   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.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome.
FT   CHAIN           1..657
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411804"
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   657 AA;  73149 MW;  22A7CB34F1E6AED2 CRC64;
     MLFLCRASPL LQRTALSSPL RFFAPPKSSF NRTFANTAVR LSIEMETVDT SERLVQLREL
     MKRNNLDVYI VPSEDSHQSE YIAHCDARRE FISGFTGSAG TAVISSTAAA LSTDGRYFNQ
     AAKQLDSNWT LLKRGLEGVP TWQEWTTEQA EGGKTVGVDP SVITAASARK LSETLEKSGS
     KLIGIEQNLV DQIWGDKRPA RPNETVKIHP AEYAGKPFQE KIADLRKELK TKKRAGFIVS
     VLDEIAWLFN LRGNDIPYNP VFFSYAVITP ETVDLYINDE KLSPEVKAHL GSDVVVKPYE
     SIFADARALS VNAPLTENGS PMKYLTSNKA SWALSLSFGG EKKLDEARSP ISDAKAIKNE
     VELKGMRNCH IRDGAALSEY FAWLENELIN KKSTLDEVDG ADKLEQIRSK HDKFVGLSFD
     TISSTGPNAA VIHYKPEKGI CSVIDPNAIY LCDSGGQYLD GTTDTTRTFH FGTPTEMEKK
     AFTLVLKGLI ALDTAVFPKG TSGFALDALA RQHLWRYGLD YLHGTGHGVG AYLNVHEGPI
     GVGTRIQYSE VSLSPGNVIS DEPGYYEDGK FGIRIENIIM AREVETPYKF GEKSWLGFEH
     VTMTPIGQNL IETSLLSEEE RQWVNNYHAE VWEKTSGYFK QDELTLNWLK KETKPLK