ID   BTGE_ASPCL              Reviewed;         564 AA.
AC   A1C499;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 74.
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=ACLA_059020;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS026990; EAW15239.1; -; Genomic_DNA.
DR   RefSeq; XP_001276665.1; XM_001276664.1.
DR   AlphaFoldDB; A1C499; -.
DR   SMR; A1C499; -.
DR   STRING; 344612.A1C499; -.
DR   GlyCosmos; A1C499; 1 site, No reported glycans.
DR   EnsemblFungi; EAW15239; EAW15239; ACLA_059020.
DR   GeneID; 4708849; -.
DR   KEGG; act:ACLA_059020; -.
DR   VEuPathDB; FungiDB:ACLA_059020; -.
DR   eggNOG; ENOG502QS0R; Eukaryota.
DR   HOGENOM; CLU_027285_2_1_1; -.
DR   OMA; VVCPYAT; -.
DR   OrthoDB; 71256at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006701; 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; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..564
FT                   /note="Probable beta-glucosidase btgE"
FT                   /id="PRO_0000395130"
FT   REGION          285..304
FT                   /note="Disordered"
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"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   564 AA;  58575 MW;  B95D30B0D0B75AF0 CRC64;
     MRGAFLATAA AIAGTAMADI AHMRRHGHDS FHQRRAVEQP APEADATCGC TTEVVTSWGP
     PTLIPIATSS PSSTVTSEVV TTLHSTSYST VTLVVTPSGA SPNRESAPAT PAVTLPTPGV
     TSFSTTGTYT IPATTLTVTH STTVCGATTT ELPSGTHTYG GVTTVVDRHT TVVCPYATVE
     PSGSTVTSVI RTTTYVCPSA GTYTIAPTTT YVPTSTVIVY PTPATITPGT YTQPAQTITV
     TRDNYIYVCP FTGQQLPTTA PVAPATTAVP ATTTAVPATT TAVPATSSVA PSSSPSKPAA
     PSGAVSGQMG MTYSPYTNEG GCKDKASIIS EVALLKSKGF THVRVYSTDC GSLEFIGEAA
     RTSGLRMIIG VFIKQSGVAG AQDQVTAISK WAQWDLVSLI VVGNESIQNH FCDASTLAGF
     IVSAKQSFKA AGYSGQVTTT EPINVWQANG DALCGAVDII GANIHPFFNA DVSAAEAGKF
     VAQEFKTLKG ICPGKDVINL ETGWPHSGEA NGKAIPSREE QAIAIKAIAD EVGSMSVFFS
     YFDDLWKQPG AFGVERYWGC IENF
//