ID   AMPP1_ASPTN             Reviewed;         654 AA.
AC   Q0CDB3;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   02-SEP-2026, entry version 93.
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=ATEG_08321;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476605; EAU31494.1; -; Genomic_DNA.
DR   RefSeq; XP_001216942.1; XM_001216942.1.
DR   AlphaFoldDB; Q0CDB3; -.
DR   SMR; Q0CDB3; -.
DR   STRING; 341663.Q0CDB3; -.
DR   EnsemblFungi; EAU31494; EAU31494; ATEG_08321.
DR   GeneID; 4353118; -.
DR   VEuPathDB; FungiDB:ATEG_08321; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_2_1; -.
DR   OMA; EPGMILS; -.
DR   OrthoDB; 9995434at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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; Reference proteome.
FT   CHAIN           1..654
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411784"
FT   BINDING         449
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         460
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         460
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         558
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         572
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         572
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   654 AA;  72744 MW;  B70CCB470E934A7F CRC64;
     MLFSHPPIRL AWSSAFRSAR QLPLSRPRFF SISVPRYAVD METVDTTERL SRLRQLMKDH
     QVDVYIVPSE DSHQSEYIAP CDGRREFISG FSGSAGTAIV SLTKAALSTD GRYFNQASKQ
     LDSNWVLLKR GVEGVQTWQE WTTEQAEGGK VVGVDPALIT ASGARSLSET LQKNGSSLKG
     IRPNLVDLVW GNDRPSPPRE KVTVHPEKFA GKSFQDKISE LRKELEKKKT AGFVISMLDE
     IAWLFNLRGT DIPYNPVFFS YAIITPTTAE LYVDDDKLTP EVKAHLGQDV VVKPYDSIYA
     DAEALSAARK QDAGDAAPKF LLSNKASWAL SLSLGGEEQT EEVRSPIADA KAVKNDVELS
     GMRACHIRDG AALIEYFAWL ENELVNKKTT LDEVDAADKL EQIRSKHELF AGLSFDTISS
     TGPNGAVIHY KPEKGSCSII DPNAIYLCDS GAQFLDGTTD VTRTFHFGKP TELEKKAFTL
     VLKGMIALDS AVFPKGTSGF ALDVLARQYL WQEGLDYLHG TGHGIGSYLN VHEGPMGIGT
     RVQYTEVPIA PGNVISNEPG FYEDGKFGIR IENVIMAREV QTPHKFGDRP WLGFEHVTMA
     PIGLNLIEPS LLSDSEIKWV NDYHAEVWEK THHFFQNDER TRSWLQRETQ PISK
//