AMPP1_ASPFN
ID AMPP1_ASPFN Reviewed; 654 AA.
AC B8NEI6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=AFLA_061840;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963477; EED51921.1; -; Genomic_DNA.
DR RefSeq; XP_002378928.1; XM_002378887.1.
DR AlphaFoldDB; B8NEI6; -.
DR SMR; B8NEI6; -.
DR STRING; 5059.CADAFLAP00006793; -.
DR MEROPS; M24.009; -.
DR EnsemblFungi; EED51921; EED51921; AFLA_061840.
DR VEuPathDB; FungiDB:AFLA_061840; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_2_1; -.
DR OMA; YRPGKWG; -.
DR Proteomes; UP000001875; 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.
FT CHAIN 1..654
FT /note="Probable Xaa-Pro aminopeptidase P"
FT /id="PRO_0000411780"
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; 72826 MW; BBF674FFF5A43198 CRC64;
MLFSRPPIRS PWISAFRSAS QLPLSRPRFF SISLSRYSVD METVNTSERL SRLRELMQEH
KVDVYIVPSE DSHQSEYIAP CDGRREFISG FSGSAGTAIV SLSKAALSTD GRYFNQASKQ
LDNNWQLLKR GVEGFPTWQE WTTEQAEGGK VVGVDPALIT ASGARSLSET LKKNGSTLVG
VQQNLVDLVW GKDRPAPPRE KVRVHPEKYA GKSFQEKISE LRKELESRKS AGFIVSMLDE
IAWLFNLRGS DIPYNPVFFS FATITPTTTE LYVDADKLTP EVTAHLGQDV VIKPYDAIYA
DAKALSETRK QEAGETASKF LLSNKASWAL SLSLGGEGQV EEVRSPIGDA KAVKNDVELA
GMRACHIRDG AALTEYFAWL ENELVNKKST LDEVDAADKL EQIRSKHDLF VGLSFDTISS
TGPNGAVIHY KPEKGSCSII DPNAIYLCDS GAQYLDGTTD VTRTFHFGQP TELEKKAFTL
VLKGVIGLDT AVFPKGTSGF ALDVLARQYL WKEGLDYLHG TGHGIGSYLN VHEGPIGVGT
RVQYTEVPIA PGNVISDEPG FYEDGKFGIR IENVIMAREV QTTHKFGDKP WLGFEHVTMA
PIGRNLIEPS LLSDAELKWV NDYHREIWEK THHFFENDEY TRSWLQRETQ PISK
