ID   AMPP1_BLAGS             Reviewed;         617 AA.
AC   C5K105; A0A179UZJ0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=BDBG_08499;
OS   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081;
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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=OAT13260.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; GG657471; OAT13260.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_002621127.1; XM_002621081.1.
DR   AlphaFoldDB; C5K105; -.
DR   SMR; C5K105; -.
DR   STRING; 559298.C5K105; -.
DR   MEROPS; M24.009; -.
DR   EnsemblFungi; OAT13260; OAT13260; BDBG_08499.
DR   GeneID; 8508590; -.
DR   KEGG; bgh:BDBG_08499; -.
DR   HOGENOM; CLU_011781_2_2_1; -.
DR   Proteomes; UP000002038; Unassembled WGS sequence.
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..617
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411774"
FT   BINDING         414
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         425
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         425
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         523
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         537
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         537
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   617 AA;  68558 MW;  72FC451A8CEEC371 CRC64;
     MGPVDTSQRL ARLRELMQER KVDVYIVPSE DSHQSEYIAP CDGRREFISG FTGSAGCAIV
     SMSKAALSTD GRYFNQAAKQ LDNNWMLLKR GFENMPTWQE WTAEQAEGGK VVGVDPSLIT
     ASEARSLSET IEKSGGSLQG VQENLIDLVW GKKRPARPSE KVALHPIEFA GKSFEEKISD
     LRKELQKKKS AGFVISMLDE IAWLFNLRGN DIPYNPVFFA YAIITPTTAD LYIDDEKLPA
     EVKKYLGDQV SVKPYGSIFE DAKALSQSAQ KKSDGDASTS PSEKFLISTK ASWSLSLALG
     GEKNVEEVRS PITDAKAIKN EAELEGMRAC HIRDGAALTE YFAWLENELV NKKTVLNEVD
     GSDKLEQIRS KHKHFVGLSF DTISSTGPNA AVIHYKAERD TCSIIDPKAV YLCDSGAQYL
     DGTTDTTRTL HFGEPTEMER KAYTLVLKGL ISIDTAVFPK GTTGFALDAF ARQHLWKEGL
     DYLHGTGHGV GSYLNVHEGP IGLGTRVQYA EVAITPGNVI SDEPGFYEDG VFGIRIENII
     IAKEVKTTHG FGEKPWLGFE HVTMTPLCQK LINPSLLTDG EKKWVNDYHS KVWEKTSSYF
     ENDELTRNWL KRETQPI