ID   BGLA_ASPKW              Reviewed;         860 AA.
AC   P87076; G7X8K7;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Beta-glucosidase A;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase A;
DE   AltName: Full=Cellobiase A;
DE   AltName: Full=Gentiobiase A;
DE   Flags: Precursor;
GN   Name=bglA; Synonyms=bgl1; ORFNames=AKAW_01481;
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 178-189; 405-414 AND
RP   603-618, SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=NBRC 4308;
RX   PubMed=10584016; DOI=10.1128/aem.65.12.5546-5553.1999;
RA   Iwashita K., Nagahara T., Kimura H., Takano M., Shimoi H., Ito K.;
RT   "The bglA gene of Aspergillus kawachii encodes both extracellular and cell
RT   wall-bound beta-glucosidases.";
RL   Appl. Environ. Microbiol. 65:5546-5553(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RX   PubMed=22045919; DOI=10.1128/ec.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
CC   -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC       involved in the degradation of cellulosic biomass. Catalyzes the last
CC       step releasing glucose from the inhibitory cellobiose.
CC       {ECO:0000269|PubMed:10584016}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000269|PubMed:10584016};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000269|PubMed:10584016}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:10584016}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; AB003470; BAA19913.1; -; Genomic_DNA.
DR   EMBL; DF126449; GAA83366.1; -; Genomic_DNA.
DR   AlphaFoldDB; P87076; -.
DR   SMR; P87076; -.
DR   STRING; 40384.P87076; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   VEuPathDB; FungiDB:AKAW_01481; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   InParanoid; P87076; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..860
FT                   /note="Beta-glucosidase A"
FT                   /id="PRO_0000394096"
FT   REGION          719..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000250|UniProtKB:P29090"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        442
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        523
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        542
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        564
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        658
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        690
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        712
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        522
FT                   /note="R -> K (in Ref. 1; BAA19913)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        850
FT                   /note="L -> P (in Ref. 1; BAA19913)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   860 AA;  93349 MW;  DA0FEF8C42CDBA37 CRC64;
     MRFTLIEAVA LTAVSLASAD ELAYSPPYYP SPWANGQGDW AQAYQRAVDI VSQMTLAEKV
     NLTTGTGWEL ELCVGQTGGV PRLGVPGMCL QDSPLGVRDS DYNSAFPSGM NVAATWDKNL
     AYLRGKAMGQ EFSDKGADIQ LGPAAGPLGR SPDGGRNWEG FSPDPALSGV LFAETIKGIQ
     DAGVVATAKH YIAYEQEHFR QAPEAQGYGF NISESGSANL DDKTMHELYL WPFADAIRAG
     AGAVMCSYNQ INNSYGCQNS YTLNKLLKAE LGFQGFVMSD WAAHHAGVSG ALAGLDMSMP
     GDVDYDSGTS YWGTNLTVSV LNGTVPQWRV DDMAVRIMAA YYKVGRDRLW TPPNFSSWTR
     DEYGYKYYYV SEGPYEKVNH YVNVQRNHSE LIRRIGADST VLLKNDGALP LTGKERLVAL
     IGEDAGSNPY GANGCSDRGC DNGTLAMGWG SGTANFPYLV TPEQAISNEV LKNKNGVFTA
     TDNWAIDQIE ALAKTASVSL VFVNADSGEG YINVDGNLGD RRNLTLWRNG DNVIKAAASN
     CNNTIVIIHS VGPVLVNEWY DNPNVTAILW GGLPGQESGN SLADVLYGRV NPGAKSPFTW
     GKTREAYQDY LVTEPNNGNG APQEDFVEGV FIDYRGFDKR NETPIYEFGY GLSYTTFNYS
     NLEVQVLSAP AYEPASGETE AAPTFGEVGN ASNYLYPDGL QKITKFIYPW LNSTDLEASS
     GDASYGQDSS DYLPEGATDG SAQPILPAGG GPGGNPRLYD ELIRVSVTIK NTGKVAGDEV
     PQLYVSLGGP NEPKIVLRQF ERITLQPSEE TKWSTTLTRR DLANWNVEKQ DWEITSYPKM
     VFVGSSSRKL PLRASLPTVH