ID   BTGE_ASPOR              Reviewed;         602 AA.
AC   Q2US39;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=AO090005000582;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007151; BAE55626.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2US39; -.
DR   SMR; Q2US39; -.
DR   STRING; 510516.Q2US39; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   EnsemblFungi; BAE55626; BAE55626; AO090005000582.
DR   VEuPathDB; FungiDB:AO090005000582; -.
DR   HOGENOM; CLU_027285_2_1_1; -.
DR   OMA; VVCPYAT; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000006564; Chromosome 1.
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..602
FT                   /note="Probable beta-glucosidase btgE"
FT                   /id="PRO_0000395134"
FT   REGION          61..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        443
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        538
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
SQ   SEQUENCE   602 AA;  61824 MW;  94BCCF3A057E95D7 CRC64;
     MRGAFLAAAA AVAGTAMADV AHMRRHGHDS FHHNRAYQPE VPAEGDENCE CTTKVITITG
     PPTLVPINTP APEPSSSSSS EVPSVPSSES SVVTSEAVTT LHSTSTATVT VVTTPGVDAT
     GAQTPTGGVP GTPEASSPAG TPEASTPAVP ATSESPLPTP GVTSFSSTGI YTIPATTVTV
     RDTTTVCGAT TTELPSGTHT FGGVTTVVST ATTVTCPVAT VEPSGSTVTS KIYTTTYVCP
     SAGTYTIAPT TTYVPTSTVV VYPTPATITP GTYTQDEQTV TVTRTDFTYV CPFTGNDQPT
     SAPVASTSAV PVTTTAAPST TSAVASSSAS ASSTATAVPT GVSGQQMGMT YSPYTNEGGC
     QSKDQVLKDV ALIKQKGFTH VRVYSTDCNG LEYIGEAARE NGLKMIIGVF ISSTGISGAQ
     EQVTAITKWA QWDLVTLVVV GNEAIQNGYT DASSLAGFIS SCKSSFQASG YSGQVTTTEP
     INVWQQSGSA LCGAVDILGA NLHPFFNADV TPDQAGSFVR AQIKDLEAVC NKDVINLETG
     WPSAGNANGK AVPGTAQQAA AIKALVEEVG SQSVFFSYSN DLWKDAGEFD VERYWGCIDQ
     FK