ID   AMPP1_ASPN4             Reviewed;         654 AA.
AC   Q5AVF0; C8VDJ5;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   04-NOV-2026, entry version 126.
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=AN11005;
OS   Aspergillus nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Emericella nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA61245.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000131; EAA61245.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001304; CBF79990.1; -; Genomic_DNA.
DR   RefSeq; XP_680999.2; XM_675907.2.
DR   AlphaFoldDB; Q5AVF0; -.
DR   SMR; Q5AVF0; -.
DR   FunCoup; Q5AVF0; 370.
DR   STRING; 227321.Q5AVF0; -.
DR   MEROPS; M24.009; -.
DR   EnsemblFungi; CBF79990; CBF79990; ANIA_11005.
DR   GeneID; 2869597; -.
DR   KEGG; ani:ANIA_11005; -.
DR   VEuPathDB; FungiDB:AN11005; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_002492_0_0_1; -.
DR   InParanoid; Q5AVF0; -.
DR   OMA; AAAWSCH; -.
DR   OrthoDB; 9995434at2759; -.
DR   Proteomes; UP000000560; Chromosome IV.
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_0000411791"
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;  72691 MW;  7AD6FCE3658C5174 CRC64;
     MLFSRPPARL SWILAFQPSQ KLPRYSPRFF SISVSRFAID MEAVDTTKRL SSLRQLMREH
     KVDVYIVPSE DSHQSEYIAP CDGRREFISG FSGSAGTAII SLNEAALSTD GRYFNQAAKQ
     LDNNWTLLKR GVEGVPTSQE WITQQAEGGK VVGVDPALIT GAAARSLSDA LQKSGASLIG
     VSQNLVDLVW GNDRPAPPRE KVRVHPEKYA GKSFQEKVSD LRKELENKKA AGFVISMLDE
     IAWLLNLRGS DIPYNPVFIS YCIVTPTKVE LYIDDEKLTP EVKAHLGDDV IIKPYDSIFA
     DAKALFEAKK KDPDAPSSKF LLSNRASWAL NLSLGGEDHV EEIRSPIGDA KAVKNEVELA
     GMRACHIRDG AALIEYFAWL ENELVNKKST LDEVDAADKL EQLRSKQELF AGLSFDTISS
     TGPNGAVIHY KPEKGSCSVI DPNAIYLCDS GGQYLDGTTD VTRTFHFGQP TELEKKAFTL
     VLKGCIGLDS AVFPKGTSGF ALDVLARQHL WKEGLDFLHG TGHGIGSYLN VHEGPVGIGT
     RVQYTEVPLA PGNVISDEPG FYEDGKFGIR IENVIMVREV QTTHKFGERP WLGFEHVTMC
     PIGQNLIEPS LLSDSEIKWL NDYHAEVWEK THKYFENDEV TRKWLERETR PISK
//