ID   EXGA_ASPTN              Reviewed;         416 AA.
AC   Q0CR35;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=ATEG_03849;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476598; EAU35651.1; -; Genomic_DNA.
DR   RefSeq; XP_001213027.1; XM_001213027.1.
DR   AlphaFoldDB; Q0CR35; -.
DR   SMR; Q0CR35; -.
DR   STRING; 341663.Q0CR35; -.
DR   PRIDE; Q0CR35; -.
DR   EnsemblFungi; EAU35651; EAU35651; ATEG_03849.
DR   GeneID; 4318487; -.
DR   VEuPathDB; FungiDB:ATEG_03849; -.
DR   eggNOG; ENOG502QPYU; Eukaryota.
DR   HOGENOM; CLU_004624_0_1_1; -.
DR   OMA; DTHHYQV; -.
DR   OrthoDB; 896412at2759; -.
DR   Proteomes; UP000007963; 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; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..416
FT                   /note="Probable glucan 1,3-beta-glucosidase A"
FT                   /id="PRO_0000393531"
FT   ACT_SITE        209
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        308
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   DISULFID        290..415
FT                   /evidence="ECO:0000250"
FT   DISULFID        316..341
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  45747 MW;  24F9987F9D3BA259 CRC64;
     MLYNLSKAVL ALSVLAASAD AAGIRLEKRA STFDYETEMV RGVCLGGWLV LEPWLSPGLF
     DAAPDGAVDE WTYTEILGQD EAKARLIGHW DTFITEQDFF DIAAAGMNHV RIPIGYWAVE
     ALPGDPYVDG QLEYLDRAIE WAGAAGLKVI VDLHGAPGSQ NGFDNSGRKG AIQWGQGDTL
     GQTVNAFRKL AERYVPSSDV VTAIEAVNEP FIPGGVNEDQ LKEYYQQAYD IVTQMSPDVD
     LVFSDGFINP TPWNGFISDS GNIVMDNHHY EVFDINLLRM SVDDHVRSVC DFGRTQLAPA
     TKPVVVGEWT GAMTDCARYL NGRGVGARYD GAMGGESVGD CGPFIQGSVS DLSPDDQKNM
     RRFIEAQLDA WEMKSGWLFW NWKTEQGAPG WDMKDLLDNG VFPFPLESRK YPGQCG