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 27-MAR-2024, entry version 115.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ566365; CAD97460.1; -; Genomic_DNA.
DR EMBL; AP007155; BAE58099.1; -; Genomic_DNA.
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 HOGENOM; CLU_004624_0_1_1; -.
DR OrthoDB; 1431012at2759; -.
DR BioCyc; MetaCyc:MONOMER-16494; -.
DR BRENDA; 3.2.1.58; 522.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF1; GLUCAN 1,3-BETA-GLUCOSIDASE I_II-RELATED; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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
//
