ID   BTGE_NEOFI              Reviewed;         552 AA.
AC   A1DBG6;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 77.
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=NFIA_098360;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
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}.
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DR   EMBL; DS027694; EAW20206.1; -; Genomic_DNA.
DR   RefSeq; XP_001262103.1; XM_001262102.1.
DR   AlphaFoldDB; A1DBG6; -.
DR   SMR; A1DBG6; -.
DR   STRING; 331117.A1DBG6; -.
DR   EnsemblFungi; EAW20206; EAW20206; NFIA_098360.
DR   GeneID; 4588449; -.
DR   KEGG; nfi:NFIA_098360; -.
DR   VEuPathDB; FungiDB:NFIA_098360; -.
DR   eggNOG; ENOG502QS0R; Eukaryota.
DR   HOGENOM; CLU_027285_2_1_1; -.
DR   OMA; VVCPYAT; -.
DR   OrthoDB; 71256at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006702; 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   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR16631:SF24; FAMILY 17 GLUCOSIDASE SCW11-RELATED; 1.
DR   PANTHER; PTHR16631; GLUCAN 1,3-BETA-GLUCOSIDASE; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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..552
FT                   /note="Probable beta-glucosidase btgE"
FT                   /id="PRO_0000395137"
FT   REGION          250..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        392
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        488
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
SQ   SEQUENCE   552 AA;  56907 MW;  C8E05DAC3193C2A3 CRC64;
     MRGAILATAA ALAGTAMADV AHMRRHGHDS FHQRRAAVAE ADATCGCTTE VVTVWGPPTL
     IPVATPTPST VTSEAVTTLH STSTSTVTIV ASASTPATSS SPATPKVPLP TPAITNFPST
     GVYTIPATTV TVFDTTTVCG ATTTELPAGT HTYGGVTTVV ETATTVVCPY ATVEPSGTTV
     TSVIKTTTYV CPTPGTYTIA PTTTTVPTST VVVYPTPAVI TPGTYTQPEQ TVTVTRTDYT
     YVCPFTGQNE PTSAPAAPST TAVPATTTAA VPSTSSAAPS SSSTAPASTG AVGGQMGMTY
     TPYTKGGDCK DKSSVLSEVA NLKSKGFTHV RVYSTDCNSL EYIGEAARTS GLQMIIGVFI
     SSTGVSGAQD QVTAISKWAQ WDLVSLIVVG NEAIQNGYCD ASTLAGFISS AKSAFQSAGY
     TGKVTTTEPI NVWQAYGSTL CGVCDIIGAN IHPFFNADVS ADQAGKFVAQ EIKVLEGICP
     GKDVLNLETG WPHAGNANGK AVPGASEQAI AIKSIAQEVG SKSVFFSYFD DLWKEPGQFD
     VERYWGCIDT FN
//