AMPP1_PHANO
ID AMPP1_PHANO Reviewed; 650 AA.
AC Q0UFY4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=SNOG_09330;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445338; EAT83522.1; -; Genomic_DNA.
DR RefSeq; XP_001799625.1; XM_001799573.1.
DR AlphaFoldDB; Q0UFY4; -.
DR SMR; Q0UFY4; -.
DR STRING; 13684.SNOT_09330; -.
DR MEROPS; M24.A10; -.
DR PRIDE; Q0UFY4; -.
DR EnsemblFungi; SNOT_09330; SNOT_09330; SNOG_09330.
DR GeneID; 5976526; -.
DR KEGG; pno:SNOG_09330; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_3_1; -.
DR InParanoid; Q0UFY4; -.
DR OMA; YRPGKWG; -.
DR OrthoDB; 417805at2759; -.
DR Proteomes; UP000001055; 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..650
FT /note="Probable Xaa-Pro aminopeptidase P"
FT /id="PRO_0000411805"
FT BINDING 447
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 556
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 570
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 570
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 650 AA; 72750 MW; E1C17EFDC9A294D1 CRC64;
MPRDALSFEL QLSAGLEATE HKLDMLTRLL RRTHVAVKHP LLASRAFHTS PALRAIDMAK
VDTTERLAEL RKLMKERKVD VYTYISGFTG SAGYAVVTHD KAALATDGRY FNQAEKQLDS
NWELLKQGIQ DVPTIQEWTA DQVEGGKVVG VDPSVVTGAD ARKLAEKIKK KGGEYKAVDD
NLVDLVWAAE RPARPSEKVI VQPMEYSGKS FDEKVEDLRK ELEKKKSLGF VVSMLDEVAW
LFNLRGNDIP YNPVFFSYAV ITPTVVTLYV DESKLPKEVK DHLGDKVAIR PYEAIFGDIT
ALSKDAFEAA DADATKKFLT SNRASWALNK ALGGDDKVEE IRSPIGDAKA VKNEVELEGM
RQCHIRDGAA ISEYFAWLED QLLNKKATLD EVDGADKLEA IRKKHDKFMG LSFDTISSTG
PNGAVIHYKP EKGACSIIDP NAIYLCDSGA QYHDGTTDTT RTLHFTKPTD MEKKAYTLVL
KGNIALERVK FPKGTTGFAL DSIARQFLWA EGLDYRHGTG HGVGSFLNVH EGPIGIGTRV
QYSEVSLAVG NVISDEPGYY EDGKFGIRIE NMIMVKEVET NHKFGDKPYL GFEHVTLTPH
CRNLVDMTLL TEDEKKFIND YHKEVFEKTS KFFENDKLTM DWLKRETAPY
