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EXGA_ASPOR
ID   EXGA_ASPOR              Reviewed;         405 AA.
AC   Q7Z9L3; Q2UK16;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Glucan 1,3-beta-glucosidase A;
DE            EC=3.2.1.58;
DE   AltName: Full=Exo-1,3-beta-glucanase 1;
DE   AltName: Full=Exo-1,3-beta-glucanase A;
DE   Flags: Precursor;
GN   Name=exgA; Synonyms=exg1; ORFNames=AO090003000990;
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 [GENOMIC DNA].
RA   Riou C., Gunata Z.;
RT   "High glucose-tolerant beta-glucosidase gene from Aspergillus oryzae.";
RL   Submitted (JUN-2003) 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).
RN   [3]
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 11489 / CBS 125.59 / IMI 52143 / NRRL 695;
RX   PubMed=9758774; DOI=10.1128/aem.64.10.3607-3614.1998;
RA   Riou C., Salmon J.-M., Vallier M.-J., Guenata Z., Barre P.;
RT   "Purification, characterization, and substrate specificity of a novel
RT   highly glucose-tolerant beta-glucosidase from Aspergillus oryzae.";
RL   Appl. Environ. Microbiol. 64:3607-3614(1998).
RN   [4]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=17420593; DOI=10.1271/bbb.60591;
RA   Tamano K., Satoh Y., Ishii T., Terabayashi Y., Ohtaki S., Sano M.,
RA   Takahashi T., Koyama Y., Mizutani O., Abe K., Machida M.;
RT   "The beta-1,3-exoglucanase gene exgA (exg1) of Aspergillus oryzae is
RT   required to catabolize extracellular glucan, and is induced in growth on a
RT   solid surface.";
RL   Biosci. Biotechnol. Biochem. 71:926-934(2007).
CC   -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC       the main structural component of the cell wall. It could also function
CC       biosynthetically as a transglycosylase (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:17420593}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC         reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC         EC=3.2.1.58;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:9758774};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9758774}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9758774}.
CC   -!- INDUCTION: The combination of poor nutrition conditions and attachment
CC       of mycelia to a hydrophobic solid surface appears to be a major
CC       inducing factor. {ECO:0000269|PubMed:17420593}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; AJ566365; CAD97460.1; -; Genomic_DNA.
DR   EMBL; AP007155; BAE58099.1; -; Genomic_DNA.
DR   RefSeq; XP_001820101.2; XM_001820049.2.
DR   AlphaFoldDB; Q7Z9L3; -.
DR   SMR; Q7Z9L3; -.
DR   STRING; 510516.Q7Z9L3; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   CLAE; EXG5A_ASPOR; -.
DR   EnsemblFungi; BAE58099; BAE58099; AO090003000990.
DR   GeneID; 5992084; -.
DR   KEGG; aor:AO090003000990; -.
DR   HOGENOM; CLU_004624_0_1_1; -.
DR   BioCyc; MetaCyc:MON-16494; -.
DR   BRENDA; 3.2.1.58; 522.
DR   Proteomes; UP000006564; Chromosome 2.
DR   GO; GO:1990819; C:actin fusion focus; IEA:EnsemblFungi.
DR   GO; GO:0000935; C:division septum; IEA:EnsemblFungi.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IEA:EnsemblFungi.
DR   GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070879; P:fungal-type cell wall beta-glucan metabolic process; IEA:EnsemblFungi.
DR   GO; GO:1904541; P:fungal-type cell wall disassembly involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycosidase; Hydrolase; Manganese; Metal-binding;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..405
FT                   /note="Glucan 1,3-beta-glucosidase A"
FT                   /id="PRO_0000007876"
FT   ACT_SITE        199
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        298
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..405
FT                   /evidence="ECO:0000250"
FT   DISULFID        306..332
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   405 AA;  44373 MW;  FC8D181C0A37A7C9 CRC64;
     MLPLLLCIVP YCWSSRLDPR ASSFDYNGEK VRGVNLGGWL VLEPWITPSI FDAAGAEAVD
     EWSLTKILGK EEAEARLSAH WKSFVSAGDF QRMADAGLNH VRIPIGYWAL GPLEGDPYVD
     GQLEYLDKAV EWAGAAGLKV LIDLHGAPGS QNGFDNSGRR GAIQWQQGDT VEQTLDAFDL
     LAERYLGSDT VAAIEAINEP NIPGGVDQGK LQEYYGSVYG IVNKYNAGTS VVYGDGFLPV
     ESWNGFKTEG SKVVMDTHHY HMFDNGLIAM DIDSHIDAVC QFAHQHLEAS DKPVIVGEWT
     GAVTDCAKYL NGKGNGARYD GSYAADKAIG DCSSLATGFV SKLSDEERSD MRRFIEAQLD
     AFELKSGWVF WTWKTEGAPG WDMSDLLEAG VFPTSPDDRE FPKQC
 
 
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