AMPP3_PARBA
ID AMPP3_PARBA Reviewed; 468 AA.
AC C1H9Q9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Probable Xaa-Pro aminopeptidase PEPP;
DE EC=3.4.11.9;
DE AltName: Full=Aminoacylproline aminopeptidase;
DE AltName: Full=Prolidase;
GN Name=PEPP; ORFNames=PAAG_07500;
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; KN294015; EEH37082.1; -; Genomic_DNA.
DR RefSeq; XP_002790641.1; XM_002790595.2.
DR AlphaFoldDB; C1H9Q9; -.
DR SMR; C1H9Q9; -.
DR STRING; 502779.C1H9Q9; -.
DR EnsemblFungi; EEH37082; EEH37082; PAAG_07500.
DR GeneID; 9093819; -.
DR KEGG; pbl:PAAG_07500; -.
DR VEuPathDB; FungiDB:PAAG_07500; -.
DR eggNOG; KOG2737; Eukaryota.
DR HOGENOM; CLU_017266_1_2_1; -.
DR OMA; DQKFIYN; -.
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 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.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW Protease; Reference proteome.
FT CHAIN 1..468
FT /note="Probable Xaa-Pro aminopeptidase PEPP"
FT /id="PRO_0000411879"
FT BINDING 264
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 468 AA; 51814 MW; 1EA557012799E21B CRC64;
MAVSVDQTLA GKYPAKLHAK RVAARIQELG HGDSGIIYLE GQKTHMIEDS DGEMPFRQRR
NFFYLSGCPL PDSYLTYDIK ADKLTIFIPP IDPASVIWSG LPLSVEEALE IYDVDAVLST
AEVNASLAHY CSAQGGKKVF AIADQVSPHI TFLPFQEIDF DVLKRAAEES RVVKDSYEIA
LLRRANEISS KAHVAVFKAA MSARNERELE AIFVGACMSS GCREQSYHPI FASGTNAATL
HYQKNDEDLV DSVTGQRRLN MLIDAGAEYR NYCADITRVV PLSGKFSPES RQIYDIVLEM
QNSSLAMIKA GVMWEDVHST SHRVAIRGLL KLGILRGTEE ELFEKGISVA FFPHGLGHYL
GMDTHDTGGN PNYADKDPKF KYLRLRGPLA SGGVVTVEPG IYFCRFIIDP YLSSPDLGKY
INADVLGRYW SVGGVRIEDN VVVTDNGYDN LTTAPKLPEE IEKLATEK