ID   EXGA_ASPFC              Reviewed;         416 AA.
AC   B0XN12;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=AFUB_004010;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499594; EDP55704.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0XN12; -.
DR   SMR; B0XN12; -.
DR   PRIDE; B0XN12; -.
DR   EnsemblFungi; EDP55704; EDP55704; AFUB_004010.
DR   VEuPathDB; FungiDB:AFUB_004010; -.
DR   HOGENOM; CLU_004624_0_1_1; -.
DR   PhylomeDB; B0XN12; -.
DR   Proteomes; UP000001699; 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   Glycoprotein; Glycosidase; Hydrolase; Manganese; Metal-binding;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..416
FT                   /note="Probable glucan 1,3-beta-glucosidase A"
FT                   /id="PRO_0000393528"
FT   ACT_SITE        211
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        308
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        291..415
FT                   /evidence="ECO:0000250"
FT   DISULFID        316..342
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  45745 MW;  B55EB08627F6F28D CRC64;
     MIFKFSQKAL VALYLVVGLA EAVPSKSRVV SRASTFDYNG IVRGVNIGGW LVLEPWITPS
     IFDNAGDAAV DEWTLTATLG QDQAKAVLSQ HWSTFITQDD FQQIAQAGMN HVRIPIGYWA
     VSSLPDEPYV DGQLEYLDNA ISWAREAGLK VVIDLHGAPG SQNGFDNSGR KGPIAWQQGD
     TVSQTVDAFR ALAERYLPQS DVVTAIEALN EPNIPGGVSE AGLRDYYNQI ADVVRQIDPD
     TSVFLSDGFL STESWNGFKT GEDVVMDTHH YEMFDNYLIS LDIDGHVKSA CDFGKQIEGS
     DKPVVVGEWS GAVTDCTKHL NGKGVSTRYQ GEYANNVKYG DCANTTQGSV ADLSDQERTD
     TRRFIEAQLD AYEGKNGWLF WTWKTEGAPG WDMQDLLANG VFPSPLTDRQ FPNQCA