ID AMPP1_ASPOR Reviewed; 654 AA.
AC Q2U7S5; Q76LL3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 109.
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; Synonyms=app; ORFNames=AO090701000720;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 42149 / RIB 40;
RA Matsushima K., Koyama Y., Takahashi T., Matsuda T., Ito K., Nakahara T.,
RA Umitsuki G.;
RT "Cloning and expression of aminopeptidase-P from Aspergillus oryzae.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE62390.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB078875; BAD00702.1; -; mRNA.
DR EMBL; AP007164; BAE62390.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001823523.2; XM_001823471.2.
DR AlphaFoldDB; Q2U7S5; -.
DR SMR; Q2U7S5; -.
DR STRING; 510516.Q2U7S5; -.
DR MEROPS; M24.A10; -.
DR EnsemblFungi; BAE62390; BAE62390; AO090701000720.
DR GeneID; 5995580; -.
DR KEGG; aor:AO090701000720; -.
DR VEuPathDB; FungiDB:AO090701000720; -.
DR OMA; EPGMILS; -.
DR OrthoDB; 869at2759; -.
DR BRENDA; 3.4.11.9; 522.
DR Proteomes; UP000006564; Chromosome 5.
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; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
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 PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 2: Evidence at transcript level;
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_0000411783"
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"
FT CONFLICT 640
FT /note="Y -> C (in Ref. 1; BAD00702)"
FT /evidence="ECO:0000305"
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
//
