ID DNPEP_ASPOR Reviewed; 498 AA.
AC Q2UPZ7;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 22-FEB-2023, entry version 96.
DE RecName: Full=Aspartyl aminopeptidase;
DE Short=DAP;
DE EC=3.4.11.21;
GN Name=dapA; ORFNames=AO090005001447;
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 [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).
RN [2]
RP PROTEIN SEQUENCE OF 11-22, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=18828788; DOI=10.1111/j.1365-2672.2008.03889.x;
RA Kusumoto K.-I., Matsushita-Morita M., Furukawa I., Suzuki S., Yamagata Y.,
RA Koide Y., Ishida H., Takeuchi M., Kashiwagi Y.;
RT "Efficient production and partial characterization of aspartyl
RT aminopeptidase from Aspergillus oryzae.";
RL J. Appl. Microbiol. 105:1711-1719(2008).
RN [3]
RP CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17928682; DOI=10.1271/bbb.70107;
RA Watanabe J., Tanaka H., Akagawa T., Mogi Y., Yamazaki T.;
RT "Characterization of Aspergillus oryzae aspartyl aminopeptidase expressed
RT in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 71:2557-2560(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000269|PubMed:18828788};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by zinc. Stimulated by calcium and
CC bacitracin. {ECO:0000269|PubMed:18828788}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.78 mM for Asp-pNA {ECO:0000269|PubMed:17928682,
CC ECO:0000269|PubMed:18828788};
CC KM=0.068 mM for angiotensin II {ECO:0000269|PubMed:17928682,
CC ECO:0000269|PubMed:18828788};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17928682,
CC ECO:0000269|PubMed:18828788};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:17928682, ECO:0000269|PubMed:18828788};
CC -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six homodimers.
CC {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
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DR EMBL; AP007151; BAE56368.1; -; Genomic_DNA.
DR RefSeq; XP_001818370.1; XM_001818318.2.
DR AlphaFoldDB; Q2UPZ7; -.
DR SMR; Q2UPZ7; -.
DR STRING; 510516.Q2UPZ7; -.
DR EnsemblFungi; BAE56368; BAE56368; AO090005001447.
DR GeneID; 5990315; -.
DR KEGG; aor:AO090005001447; -.
DR VEuPathDB; FungiDB:AO090005001447; -.
DR HOGENOM; CLU_019532_2_0_1; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 1156at2759; -.
DR BRENDA; 3.4.11.21; 522.
DR SABIO-RK; Q2UPZ7; -.
DR Proteomes; UP000006564; Chromosome 1.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..498
FT /note="Aspartyl aminopeptidase"
FT /id="PRO_0000389137"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 498 AA; 53992 MW; FB6FC817631E3CCF CRC64;
MTSKIAQNLK QPALDFLSFV NASPTPFHAV QSAKELLSKA GFQEIKEKDS WSSTCRPGGK
YYLTRNSSTI VAFAIGKKWK PGNPISMIGA HTDSPVLRIK PVSNKRGEGF VQVGVETYGG
GIWHTWFDRD LGVAGRAMVR TGDGSIVQKL VKIDRPILRI PTLAIHLDRQ ETFAFNKETQ
LFPIAGLVAA ELNRTADSTA TGEKTAANNE TEKGDFAPLK SVTERHHPYL VELIAAEAGV
KPDDILDFEM ILFDTQKSCL GGLLEEFVFS PRLDNLNSSF CATVGLIDSV ADASALDDEP
SIRLIALFDH EEIGSRTAQG ADSNVLPAII RRLSVLPSST SGNEDLATAF EETLSTSFLL
SADMAHAVHP NYAAKYENDH RPEINKGPVI KINANARYAT NSPGIVLLQE VARKAAEDGG
EGVPLQLFVV RNDSSCGSTI GPMLSAALGA RTLDLGNPQL SMHSIRETGG TYDVGHSIRL
FTSFFKHYSN TSKTIFVD
//
