ID   BTGE_ASPTN              Reviewed;         558 AA.
AC   Q0CEX9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Probable beta-glucosidase btgE;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase btgE;
DE   AltName: Full=Cellobiase btgE;
DE   AltName: Full=Gentiobiase btgE;
DE   Flags: Precursor;
GN   Name=btgE; ORFNames=ATEG_07755;
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-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, cell wall {ECO:0000250}.
CC       Note=Covalently-linked to the cell wall. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; CH476604; EAU32017.1; -; Genomic_DNA.
DR   RefSeq; XP_001216376.1; XM_001216376.1.
DR   AlphaFoldDB; Q0CEX9; -.
DR   SMR; Q0CEX9; -.
DR   STRING; 341663.Q0CEX9; -.
DR   EnsemblFungi; EAU32017; EAU32017; ATEG_07755.
DR   GeneID; 4322886; -.
DR   VEuPathDB; FungiDB:ATEG_07755; -.
DR   eggNOG; ENOG502QS0R; Eukaryota.
DR   HOGENOM; CLU_027285_2_1_1; -.
DR   OMA; VVCPYAT; -.
DR   OrthoDB; 1142019at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall; Cellulose degradation; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..558
FT                   /note="Probable beta-glucosidase btgE"
FT                   /id="PRO_0000395135"
FT   REGION          64..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        399
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        495
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
SQ   SEQUENCE   558 AA;  58036 MW;  6192971E1E0EFE0F CRC64;
     MKAAILATAA ALTGSALADV AHMRRGHDSF HHRRAMHAQE PEETCGCTTE VITFYGSPTL
     VPISTPSATP TPAPAPETTS TEEVTTTLHS TSTSTVTVTA TPETPEVTLP TPGVTSFSST
     GVYTIPATTL TVTDTTTVCG ATSTELPSGT ATYGGVTTVV ETSTTVVCPY ATVKPSGSTV
     TSVIETTTYV CPSAGTYTVV PPTTTYVPTS TVMVYPTPAT FTPGTYTQDA QTVTVTRTDY
     TYVCPTFHPE LPSSSAPAPT TSAVPTTTAV PTSTVVPSST TSVPASSSSS SAEVPQTTGS
     GQMGMTYSPY TNAGGCKSKA DVLQDIATIK QKGFTHVRVY STDCSSLEWI GEGAKQQGLI
     MILGVYIDSS GVSGAQSQVT DIANWAEWDL VSLIVVGNEA IQNGYCTASE LASFITSAKQ
     AFKAAGYSGQ VTTTEPINVW ESSGSALCSS IDILGANIHP FFNSEVTASQ AGKFVQSQVD
     ILEKICPGKD VINLETGWPS KGSANGLAIP GTSQQSEAIK SLRNDVGALS VFFSFSNDLW
     KSPGAFDVEQ YWGCIDQF