ID   BGLE_EMENI              Reviewed;        1023 AA.
AC   Q5AYH8; C8V1D9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=Probable beta-glucosidase E;
DE            EC=3.2.1.21;
DE   AltName: Full=Beta-D-glucoside glucohydrolase E;
DE   AltName: Full=Cellobiase E;
DE   AltName: Full=Gentiobiase E;
GN   Name=bglE; ORFNames=AN6652;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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: Cell membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; AACD01000110; EAA58181.1; -; Genomic_DNA.
DR   EMBL; BN001301; CBF71178.1; -; Genomic_DNA.
DR   RefSeq; XP_664256.1; XM_659164.1.
DR   AlphaFoldDB; Q5AYH8; -.
DR   SMR; Q5AYH8; -.
DR   STRING; 227321.Q5AYH8; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; Q5AYH8; 7 sites, No reported glycans.
DR   EnsemblFungi; CBF71178; CBF71178; ANIA_06652.
DR   GeneID; 2870419; -.
DR   KEGG; ani:AN6652.2; -.
DR   VEuPathDB; FungiDB:AN6652; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_2_0_1; -.
DR   InParanoid; Q5AYH8; -.
DR   OMA; VVMESWI; -.
DR   OrthoDB; 5486783at2759; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000000560; Chromosome I.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF20; BETA-GLUCOSIDASE E-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell membrane; Cellulose degradation;
KW   Glycoprotein; Glycosidase; Hydrolase; Membrane; Polysaccharide degradation;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1023
FT                   /note="Probable beta-glucosidase E"
FT                   /id="PRO_0000394874"
FT   TOPO_DOM        1..128
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..1023
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          822..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        415
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        497
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        848
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        964
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        979
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1023 AA;  112164 MW;  F69D09D353F85C37 CRC64;
     MPKSYTPVHD SIPEEDHFSS DDESNFRLHR IDRSASRSQS PKENEGEPSI LAPLVRKSTD
     FETYLDSLTE DEQQLLSASK DHDIEDLDRF GDGTAAARRR FSESKKRRKL LAKRGGWRAV
     YYSKTWWRTL VVVIIALGLL VWGFLKYAST RGDIWEEYDM PGPDSYFPTP KGGTLKHWAE
     SYEKASKLVE RMTLIEKVNI TTGTGWQMGI NSKLTISGPA ALVGFPSLCL QDGPLGIRFA
     DHITAFPAGI TTGATWNRDL MRQRGAAIGL EARLKGVNVI LGPSMGPLGM MPAGGRNWEG
     FGSDPVLQAV AAVETIHGIQ SNGVMATAKH YIMNEQEHFR QPNEWGIPYA LSSNIDDRAL
     HEVFLWPFAE SIRADVASVM CSYNQVNNSH ACENSKLLNG ILKDELGFQG FVQSDWLAQR
     SGVNSALGGL DMSMPGDGLH WADGRSLWGS ELTRAALNTS VPMERLNDMV TRIVAAWYQL
     GQDSWESPAP DGDGGPNFSS WTDDEFGFRY PGSPGDTSAA RVNRFIDAQG RGEEGHWNIA
     RKVAAEGIVL VKNVGGVLPL SRSPRANAER PYRVGVYGDD GGPAAGPNIC TDRGCNSGTL
     AMGWGSGTVE FPYLISPIDA LQGAWQSDVQ MTPYLRNAVM PADTSDKDLC LVFVNADSGE
     GYISAGGIHG DRNNLFLQKG GDTLVHTVAT NCGGPTVVVV HAVGPVIVEP WIDLPGVQAV
     LFAHLPGEES GNALLDVLFG DVDASGRLPY TVGKSLEDYG PGAQVLYEPN APVPQVDFSD
     ALYIDHRYFD RNNINPRYEF GFGLSYTKWE LTNMKITRLQ RNPSRLPAAR PPDAVAPPSY
     DANPPLANES VLFPPGFRIL SKYIYPYLPT LEATTPPPPN PEASGSATDQ KPHRTKPSDA
     GGGAGGNPSL YEEVARIDLT VQNTGTRSGQ QVIQLYVSFP HTVTESSGQK SHENIDFPDR
     VLRNFTKISL APGQKMDVNM TLTRKDLSYW SVREQNWVLP KDEFYFWVGY SSRNLPLGKP
     FDP
//