ID   BTGE_ASPFC              Reviewed;         565 AA.
AC   B0Y9Q9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   25-MAY-2022, entry version 51.
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=AFUB_081940;
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-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDP48752.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DS499600; EDP48752.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; B0Y9Q9; -.
DR   SMR; B0Y9Q9; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000001699; 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; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..565
FT                   /note="Probable beta-glucosidase btgE"
FT                   /id="PRO_0000395131"
FT   REGION          246..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        405
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        501
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
SQ   SEQUENCE   565 AA;  58148 MW;  4D06B871D8835ACC CRC64;
     MRGAILATAA ALAGTAMADV AHMRRHGHDS FHQRRSPLAE ADATCGCTTE VVTVWGPPTL
     IPVASPTPST VTSEAVTTLH STSTTTVTVI ASASTPAASP SPATDKVPLP TPAITNFPST
     GVYTIPATTV TVFDTTTVCG ATTTELPAGT HTYGGVTTVV ETATTVVCPY ATVEPSGTTV
     TSVIKTTTYV CPSAGTYTIA PTTTTVPTST VIVYPTPAVI TPGTYTQPEQ TVTVTRTDYT
     YVCPFTGQDE PTSAPAAPST TAVPATTTAA PETTTAAPDT TTAVPSTSSA APSSSSTAPA
     STGAVSGQMG MTYTPYTKGG DCKDKSSVLS EVAALKSKGF THVRVYSTDC NSLEYIGEAA
     RTSGLQMIIG VFISSTGVSG AQDQVTAISK WAQWDLVSLI VVGNEAIQNG YCDASTLAGF
     ISSAKSAFQA AGYTGKVTTT EPINVWQAHG STLCGVCDIV GANIHPFFNA DVSADQAGKF
     VAQEIKVLES ICPGKDVLNL ETGWPHAGNA NGKAVPGTSE QAIAIKSIAD EVGSKSVFFS
     YFDDLWKEPG QFGVERYWGC FDTFN