ID   AMPP2_PARBA             Reviewed;         506 AA.
AC   C1H3X3;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase PAAG_05466;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   ORFNames=PAAG_05466;
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN294005; EEH34417.2; -; Genomic_DNA.
DR   RefSeq; XP_015699808.1; XM_015845582.1.
DR   AlphaFoldDB; C1H3X3; -.
DR   SMR; C1H3X3; -.
DR   STRING; 1048829.XP_002792737.1; -.
DR   EnsemblFungi; EEH34417; EEH34417; PAAG_05466.
DR   GeneID; 9095864; -.
DR   KEGG; pbl:PAAG_05466; -.
DR   VEuPathDB; FungiDB:PAAG_05466; -.
DR   eggNOG; KOG2737; Eukaryota.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   OMA; LHYGANN; -.
DR   OrthoDB; 352329at2759; -.
DR   Proteomes; UP000002059; Partially assembled WGS sequence.
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..506
FT                   /note="Probable Xaa-Pro aminopeptidase PAAG_05466"
FT                   /id="PRO_0000411842"
FT   BINDING         285
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         433
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         471
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         471
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   506 AA;  56245 MW;  68D76DFEE5C20B12 CRC64;
     MGTYPAFSGS LQLPEQRLHG TSNLHPAGGY RIELQVQDAT FDKYPAKQHA QRVAAKLKKE
     KGLIFLMGQK AALLEDSDQE TRFRQRRYFF YMSGVNEADC DLTYDIQSDK LTLYVPNFDL
     RREIWMGPTL GPEEALKRFD IDEAKYQSFL EGDIKQWASC SGHGSTIYIL HGSQKPTGDF
     PNVLMDSETL KPAMNACRVV KDEHEIELMR HANRVSSAAH IAVLQGIRKM TNEAQIEGSF
     LNTCVSLGAH NQAYGIIAAS GANAATLHYS KNNEPLKGRQ FVCLDAGAEW DCYASDVTRT
     FPTAARWPGT EAEQIYALVQ NMQESCILRI KEGVRYLDLH YLAHDILIHG FLAIGIFKAG
     RAEEIKKSGA SSLFFPHGLG HHIGLEVHDV SPDSLFAQDN DRTTDSWLFS STYLSPCTAS
     SPTLKSGMVV TVEPGIYFSQ IALDNAKSEQ LKHIDMDVVK RYMAVGGVRI EDDILVTKDG
     FENLTLAPKG QAMLDYIQQG NGSCNI