AMPP1_PARBD
ID AMPP1_PARBD Reviewed; 616 AA.
AC C1GEY4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 2.
DT 03-AUG-2022, entry version 59.
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=PADG_05820;
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18;
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; KN275963; EEH49741.2; -; Genomic_DNA.
DR RefSeq; XP_010761227.1; XM_010762925.1.
DR AlphaFoldDB; C1GEY4; -.
DR SMR; C1GEY4; -.
DR STRING; 121759.XP_010761227.1; -.
DR EnsemblFungi; EEH49741; EEH49741; PADG_05820.
DR GeneID; 22584675; -.
DR KEGG; pbn:PADG_05820; -.
DR VEuPathDB; FungiDB:PADG_05820; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_3_1; -.
DR OMA; YRPGKWG; -.
DR Proteomes; UP000001628; 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..616
FT /note="Probable Xaa-Pro aminopeptidase P"
FT /id="PRO_0000411801"
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; 68631 MW; F94FCDFFB839F606 CRC64;
METVDTSQRL ARLRELMKER NVDVYLVPSE DSHQSEYIAP CDGRREFISG FSGSAGCAIV
SMTKAALSTD GRYFNQASKQ LDNNWLLLKR GIESMPTWQE WTAEQLEGGK VVGVDPSLIT
ASDARSLSET IKRSGGSLLG VQENLVDLVW GKDRPCRPSE KVTVHPVEFA GKSFEEKITD
LRKELEKKKS AGFVVSMLDE VAWLFNLRGN DIPYNPVFFS YAIITPSTAD LYIDEEKLSA
DVKKHLGDKV SLKPYTSIFE DAKALGQSAQ AEVNGGASDP PRKFFISTKA SWSLSLALGG
ANKVEEVRSP ISDAKAIKND TELEGMRACH IRDGAALTKY FAWLENELVN KKTVLNEVEA
SDKLEEIRSK QKNFVGLSFD TISSSGPNAA VVHYKAERNN CSIIDPEAVY LCDSGAQYLD
GTTDTTRTLH FGEPTEKERK AYTLVLKGMI AIDTAIFPKG TTGFSLDTLA RQFLWKEGLD
YLHGTGHGVG SYLNVHEGPI GIGTRVQYSE TPLSVGNVIS DEPGYYEDGK FGIRIENIIM
AREVKTTFSF GERPWLGFEH VTMTPLCRKL TDPSLLNDAE KKWINEYHSE VWEKTSGYFA
EDELTRNWLK RETQPI
