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DNPEP_ASPOR
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   03-AUG-2022, entry version 93.
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   PRIDE; 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   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   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
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
 
 
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