AMPP1_PARBA
ID AMPP1_PARBA Reviewed; 616 AA.
AC C1H978;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 2.
DT 03-AUG-2022, entry version 66.
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=PAAG_07319;
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; KN294014; EEH36901.2; -; Genomic_DNA.
DR RefSeq; XP_015700634.1; XM_015846199.1.
DR AlphaFoldDB; C1H978; -.
DR SMR; C1H978; -.
DR STRING; 502779.C1H978; -.
DR EnsemblFungi; EEH36901; EEH36901; PAAG_07319.
DR GeneID; 9094019; -.
DR KEGG; pbl:PAAG_07319; -.
DR VEuPathDB; FungiDB:PAAG_07319; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_3_1; -.
DR OMA; YRPGKWG; -.
DR OrthoDB; 417805at2759; -.
DR Proteomes; UP000002059; Partially assembled 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..616
FT /note="Probable Xaa-Pro aminopeptidase P"
FT /id="PRO_0000411800"
FT BINDING 413
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 536
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 616 AA; 68618 MW; C20A276188A80237 CRC64;
METVDTSQRL ACLRELMKER KVDVYLVPSE DSHQSEYIAP CDGRREFISG FSGSAGCAIV
SMTKAALSTD GRYFNQASKQ LDNNWLLLKR GIESMPTWQE WTAEQLEGGK VVGVDPSLIT
ASDARSLSET IKKSGGSLLG LQENLVDLVW GKDRPSRPSK KVTVHPVEFA GKSFEEKITD
LRKELEKKKS AGFVVSMLDE IAWLFNLRGN DIPYNPVFFA YAIITPSTAD LYIDEDKLSA
DVKKHLGDKV SLKPYTSIFE DAKALGQSAQ AEVNGGASDP PRKFFISTKA SWSLSLALGG
ENKVEEVRSP ISDAKAIKND AELEGMRACH IRDGAALTKY FAWLENELLN KKTVLNEVEA
SDKLEEIRSK QKNFVGLSFD TISSSGPNAA VIHYKAERNN CSIIDPEAVY LCDSGAQYLD
GTTDTTRTLH FGEPTEKERK AYTLVLKGMI AIDTAIFPKG TTGFSLDTFA RQFLWKEGLD
YLHGTGHGVG SYLNVHEGPI GIGTRVQYSE VPISAGNVIS DEPGFYEDGN FGIRIENIIM
AREVKTTFSF GERPWLGFEH VTMTPLCRKL TDPSLLSDAE KIWINEYHNE VWEKTSGYFE
EDELTRNWLK RETQPI
