ID   AMPP1_PODAN             Reviewed;         680 AA.
AC   B2AWV6; A0A090CXB1;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   02-SEP-2026, entry version 84.
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; OrderedLocusNames=Pa_7_8470; ORFNames=PODANS_7_8470;
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
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; CU633900; CAP68880.1; -; Genomic_DNA.
DR   EMBL; FO904942; CDP32352.1; -; Genomic_DNA.
DR   RefSeq; XP_001908207.1; XM_001908172.1.
DR   AlphaFoldDB; B2AWV6; -.
DR   SMR; B2AWV6; -.
DR   FunCoup; B2AWV6; 378.
DR   STRING; 515849.B2AWV6; -.
DR   MEROPS; M24.A10; -.
DR   GeneID; 6192025; -.
DR   KEGG; pan:PODANSg5242; -.
DR   VEuPathDB; FungiDB:PODANS_7_8470; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_3_1; -.
DR   InParanoid; B2AWV6; -.
DR   OrthoDB; 9995434at2759; -.
DR   Proteomes; UP000001197; Chromosome 7.
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..680
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411806"
FT   BINDING         477
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         488
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         488
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         586
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         600
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         600
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   680 AA;  75096 MW;  37534DD2228663E8 CRC64;
     MRHIWALPSL TALSLFQASA ASAVPRARQA INTSSPLAPF RTKRRFRTQA QLLSNSATKT
     TLVEEMVTVD TTSRLAALRS LMKERNLHVY VVPSEDSHAS EYIADCDARR TFISGFSGSA
     GTAIVTLDKA ALATDGRYFN QASKQLDSNW YLLKTGMQDV PTWQEWATQE AEGGKLIGVD
     PQLISSAIAE KLDEDIKNAG GGGLVGIKEN LVDLVWGSEQ PPRPSNSVFL LGQQYAGKDT
     AAKLADLRKE LDKKKAAGFV LSMLDEIAWL FNLRGSDIAY NPVFFSYAIV TQASATLYID
     EAKLTDECKT YLERNKVTIK PYGALFEDSE ELARRAEADS KDAKPRKYLI SSKGSWALKL
     ALGGNKFVDE VRSPVGDAKA VKNDVELNGM RNCHIRDGAA LTEFFAWLED QLVNQKAQLD
     EVDAADKLEQ IRSKHKDFVG LSFDTISSTG ANAAVIHYKP EKGACKIIDP NAIYLCDSGA
     QYLDGTTDTT RTLHFGTPTA KEKKAYTLVL KGNIALDSVV FPKGTSGFAI DVMARQFLWK
     YGLDYRHGTG HGVGSFLNVH EGPIGIGTRK QYIDVALAAG NVLSIEPGYY EDEAFGIRIE
     NLAIVKEVKT EHSFGDKPYL GFEHVTMVPY ARNLIDETLL TPDEKDWLNR ANKKILEKTL
     GYFENDPLTK AWLLRETQPF
//