ID   EXGA_ASPFN              Reviewed;         405 AA.
AC   B8N151;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Probable 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=AFLA_028260;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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   -!- 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; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; EQ963473; EED55554.1; -; Genomic_DNA.
DR   RefSeq; XP_002374336.1; XM_002374295.1.
DR   AlphaFoldDB; B8N151; -.
DR   SMR; B8N151; -.
DR   STRING; 5059.CADAFLAP00002201; -.
DR   EnsemblFungi; EED55554; EED55554; AFLA_028260.
DR   VEuPathDB; FungiDB:AFLA_028260; -.
DR   eggNOG; ENOG502QPYU; Eukaryota.
DR   HOGENOM; CLU_004624_0_1_1; -.
DR   OMA; WTFVGEW; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycosidase; Hydrolase; Manganese; Metal-binding;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..405
FT                   /note="Probable glucan 1,3-beta-glucosidase A"
FT                   /id="PRO_0000393529"
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