ID   BGLI_ASPFN              Reviewed;         839 AA.
AC   B8NDE2;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Probable beta-glucosidase I;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase I;
DE   AltName: Full=Cellobiase I;
DE   AltName: Full=Gentiobiase I;
GN   Name=bglI; ORFNames=AFLA_057030;
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-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 (By similarity).
CC       {ECO:0000250}.
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   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EED51440.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; EQ963477; EED51440.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002378447.1; XM_002378406.1.
DR   AlphaFoldDB; B8NDE2; -.
DR   SMR; B8NDE2; -.
DR   STRING; 5059.CADAFLAP00006312; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000001875; 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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   Pfam; PF07691; PA14; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted.
FT   CHAIN           1..839
FT                   /note="Probable beta-glucosidase I"
FT                   /id="PRO_0000394885"
FT   DOMAIN          395..555
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        620
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   839 AA;  92082 MW;  E52897D374F30765 CRC64;
     MPRLDVEKTI EELSLGEKVA LTAGIDFWHT ASVPRLNIPT LRMSDGPNGV RGTRFFNGVP
     AACFPCATAL GATWDTELLH EIGQLMGEES IAKGSHIILG PTINTQRSPL GGRGFESFAE
     DGVLSGLLAG YISKGIQEKG VAATLKHFVC NDQEHQRMAV DSIVTQRALR EIYLLPFQLA
     MRICRTACVM TAYNKVNGTH VSQNKEIITD ILRKEWGWDG LVMSDWFGTY STSDAINAGL
     DLEMPGKTRW RGTALAHAVS SNEVAEFVMD ERVRNVLNLV NFVDGLNIPE NAPEKALNRP
     QDQALLRRAA AESVVLMKNE EDILPLKKEK SILVIGPNSK VAAYCGGGSA SLDAYYTVNP
     FEGVSAQSKG EVKFSQGVYS HKDLPLLGPL LKTADGKTGF SFKVYNEHPS ESNRELIEQL
     HLVSSSGFLM DYVNPKIKSL TYYVDMEGLF TPEEDGVYDF GVTVVGTGQL FIDGELVVDN
     TKNQRQGSAF FGSATVEEKG SKELKAGQTY KVLFQFGTAP TSDLDTRGVV VFGPGGFRFG
     ASRRVGQEEL ISNAVKLASE AEQVVVFAGL TSEWETEGYD RDHMDLPPGS DEMISRVLDV
     NPNAVVVIQS GTPVTMPWAN KTKALLHAWF GGNECGNGIA DVLYGDVNPS GKLPITFPVR
     LQDNPSYVNF RSERGRVLYG EDVYVGYRYY EKVDLAPLFP FGHGLSYTTF TRSDLTLTTT
     PEKPQYEESG EPITATVTVT NTGKVAGAEI VQLWVAPPAT EVNRPVRELK GFTKVFLQPG
     EQKKVEIVVE KKLATSWFDE MREKWASEKG EYGVLVTGTG EGVLKSSFKV EKTRYWLGL