ID   AMPP1_PENRW             Reviewed;         613 AA.
AC   B6HQC9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Pc22g15910;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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; AM920437; CAP98879.1; -; Genomic_DNA.
DR   RefSeq; XP_002565507.1; XM_002565461.1.
DR   AlphaFoldDB; B6HQC9; -.
DR   SMR; B6HQC9; -.
DR   STRING; 1108849.XP_002565507.1; -.
DR   MEROPS; M24.009; -.
DR   EnsemblFungi; CAP98879; CAP98879; PCH_Pc22g15910.
DR   GeneID; 8305145; -.
DR   KEGG; pcs:Pc22g15910; -.
DR   VEuPathDB; FungiDB:PCH_Pc22g15910; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_2_1; -.
DR   OMA; YRPGKWG; -.
DR   OrthoDB; 417805at2759; -.
DR   BioCyc; PCHR:PC22G15910-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c22.
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..613
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411803"
FT   BINDING         408
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         419
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         419
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         517
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         531
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         531
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   613 AA;  67743 MW;  0A49994661C5DCDC CRC64;
     MGAVDTSERL SKLRQLMQQH KVDVYIVPSE DSHQSEYIAP CDARREFISG FSGSAGTAII
     SLSKAALSTD GRYFNQAAKQ LDNNWQLLKG GVEGVPTWQE WTTEEAQGGK AVGVDPSLIT
     ASGARKLAET LKKNGSSLVG VRENLVDLVW GKERPARPSE KVRVHPEKYA GKTFQEKVAE
     LRKELESKKK AGFVISMLDE IAWLFNLRGT DIPYNPVFFS YAVITPTTAE IYVEDDKLTP
     EVKAHLGQDV VVKPYESIFA DAQALSTKSQ SAGENAAKFL LSNKASWALS LSLGGEGQVE
     EARSPVADAK AIKNETELEG MRACHIRDGA ALTEYFAWLE NELINKKTVL DEVDGADKLE
     QIRSKHDLFA GLSFDTISST GPNGAVIHYK PEKGSCAIID PSAIYLCDSG CQYFDGTTDT
     TRTFHFGVPT EFEKRAFTLV LKGTIGIDMA VFPKGTSGFA IDVLARQHLW REGLDFLHGT
     GHGVGSYLNV HEGPIGIGTR VQYTEVPIAA GNVISDEPGY YEDGKFGIRI ENIVMAREVK
     TAHNFGDKQW LGFEHVTMTP IGRNLIEPSL LSDAELKWVN DYHAEIWAKT EHFFREDNLT
     RSWLERETQP ISK