ID   AMPP2_ASPNC             Reviewed;         491 AA.
AC   A2QAW7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase An01g13040;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   ORFNames=An01g13040;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM269986; CAK37351.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2QAW7; -.
DR   SMR; A2QAW7; -.
DR   PaxDb; A2QAW7; -.
DR   PRIDE; A2QAW7; -.
DR   EnsemblFungi; CAK37351; CAK37351; An01g13040.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.350.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR007865; Aminopep_P_N.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   Pfam; PF05195; AMP_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SMART; SM01011; AMP_N; 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..491
FT                   /note="Probable Xaa-Pro aminopeptidase An01g13040"
FT                   /id="PRO_0000411827"
FT   BINDING         276
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         420
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         459
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         459
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   491 AA;  54950 MW;  E44B2BDF7387C28D CRC64;
     MRVSIPPELV SSLGACDLRV TVRGEGIDKY PGGPGAAKQH ARKVAMKLGV SSGLIYLVGK
     PTINWGDSDQ PQPFRQRRYF YYLSGADEPD CYLTYDINND LLVLYVPDFD LHRAIWMGPT
     LTTDEAERRF DVDKVRYYAS LQSDIQSWVG KYNDAAPVYI LHSSQQPQFS VQQLHIDDQR
     LLPAMDAARV VKDDYELRMI RHANKISGLA HRKVLEQIHK MSNEAQIEGL FLDTCVSHGA
     KNQAYEIIAG SGPNAATLHY VKNNEPLKGR QLVCLDAGAE WECYASDVTR TFPLAADWPS
     SHARDVYQIV EEMQEQCIKR IKPGVRFRDL QVLAHDIAIR GLQKLGVLKP GTVEEIRVSG
     ASAIFFPHGL GHHVGLEVHD VSEKPITGMG LPNRPCRPDF IPAMSQSVPL LEEGMVVTIE
     PGVYFSKLAL ANSRKLPQAR YINFDEAEKY IPIGGVRIED DILVTRTGYE NLTTAPKGDE
     MLEIIRRGID N