AMPP1_NEOFI
ID AMPP1_NEOFI Reviewed; 654 AA.
AC A1DF27;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=NFIA_079250;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027696; EAW17984.1; -; Genomic_DNA.
DR RefSeq; XP_001259881.1; XM_001259880.1.
DR AlphaFoldDB; A1DF27; -.
DR SMR; A1DF27; -.
DR STRING; 36630.CADNFIAP00006844; -.
DR MEROPS; M24.009; -.
DR EnsemblFungi; EAW17984; EAW17984; NFIA_079250.
DR GeneID; 4586437; -.
DR KEGG; nfi:NFIA_079250; -.
DR VEuPathDB; FungiDB:NFIA_079250; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_2_1; -.
DR OMA; YRPGKWG; -.
DR OrthoDB; 417805at2759; -.
DR Proteomes; UP000006702; 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..654
FT /note="Probable Xaa-Pro aminopeptidase P"
FT /id="PRO_0000411798"
FT BINDING 449
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 558
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 572
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 572
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 654 AA; 72591 MW; B4DEDC5D791C4A61 CRC64;
MLGFRSPIRL CKLSALGSAP LLPISRPKLF STAVARYAAD METVNTTERL ARLRQLMQEH
KVDVYIVPSE DSHQSEYIAP CDGRREFISG FSGSAGTAIV SMTKAALSTD GRYFNQASKQ
LDSNWELLKR GVENVPTWQE WTTEQAEGGK VVGVDPSLIT ASGARSLEET LKRNGSSLVG
ISQNLVDLVW GKDRPAPPRE KVRVHPDKFA GKTFQEKIAD LRKELEKKKT AGFVISMLDE
IAWLFNLRGS DIPYNPVFFA YAIITPTKAE LYIDDDKITP EVVAHLGQDV VIKPYNSIFA
DAKALSEARK QEAGETASKF LLSNKASWAL SLSLGGEEHV EETRSPIADA KAIKNEVELA
GMRACHIRDG AALIEYFAWL ENELVNKKTV LDEVDAADKL ERIRTKHDLF AGLSFDTISS
TGPNGAVIHY KPEKGTCSII DPDAIYLCDS GAQYLDGTTD VTRTFHFGKP TELEKKAFTL
VLKGLIAIDT AVFPKGTSGF ALDALARQYL WKEGLDYLHG TGHGIGSYLN VHEGPIGIGT
RVQYTEVPIA PGNVISDEPG FYEDGKFGIR IENVIMAREV QTTHKFGDKP WLGFEHVTMA
PIGRNLIQPS LLSDLELKWV NDYHAEVWDK THHFFENDEF TRSWLQRETA PITK
