ID   AMPP1_PARBP             Reviewed;         616 AA.
AC   C0SCV1;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 2.
DT   02-SEP-2026, entry version 66.
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=PABG_05506;
OS   Paracoccidioides brasiliensis (strain Pb03).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Paracoccidioides.
OX   NCBI_TaxID=482561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb03;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN305539; EEH23295.2; -; Genomic_DNA.
DR   AlphaFoldDB; C0SCV1; -.
DR   SMR; C0SCV1; -.
DR   VEuPathDB; FungiDB:PABG_05506; -.
DR   HOGENOM; CLU_011781_2_3_1; -.
DR   OrthoDB; 2480at33183; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   CDD; cd01085; APP; 1.
DR   FunFam; 3.40.350.10:FF:000010; Probable Xaa-Pro aminopeptidase P; 1.
DR   FunFam; 3.90.230.10:FF:000007; Xaa-Pro aminopeptidase P; 1.
DR   FunFam; 3.40.350.10:FF:000003; Xaa-pro aminopeptidase P; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_N.
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   InterPro; IPR050422; X-Pro_aminopeptidase_P.
DR   PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF16189; Creatinase_N_2; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease.
FT   CHAIN           1..616
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411802"
FT   BINDING         413
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         424
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         424
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         522
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         536
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         536
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   616 AA;  68630 MW;  6DCF53A5BD637D6B CRC64;
     METVDTSQRL ARLRELMKER NVDVYLVPSE DSHQSEYIAP CDGRREFISG FSGSAGCAIV
     SMTKAALSTD GRYFNQASKQ LDNNWLLLKR GIESMPTWQE WTAEQLEGGK VVGVDPSLIT
     ASDARSLSET IKKSGGSLLG VQENLVDLVW GKDRPCRPSE KVTVHPVEFA GKSFEEKITD
     LRKELEKKKS AGFVVSMLDE VAWLFNLRGN DIPYNPVFFS YAIITPSTAD LYIDEEKLSA
     DVKKHLGDKV SLKPYTSIFE DAKALGQSAQ AEVNGGASDP PRKFFISTKA SWSLSLALGG
     ANKVEEVRSP ISDAKAIKND TELEGMRACH IRDGAALTKY FAWLENELVN KKTVLNEVEA
     SDKLEEIRSK QKNFVGLSFD TISSSGPNAA VVHYKAERKN CSIIDPEAVY LCDSGAQYLD
     GTTDTTRTLH FGEPTEKERK AYTLVLKGMI AIDTAIFPKG TTGFSLDTLA RQFLWKEGLD
     YLHGTGHGVG SYLNVHEGPI GIGTRVQYSE TPLSVGNVIS DEPGYYEDGK FGIRIENIIM
     AREVKTTFSF GERPWLGFEH VTMTPLCRKL IDPSLLNDAE KKWINEYHSE VWEKTSGYFA
     EDELTRNWLK RETQPI
//