BGLE_NEOFI
ID BGLE_NEOFI Reviewed; 1045 AA.
AC A1DLJ5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=NFIA_050080;
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 / NRRL 181
RC / 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: 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; DS027698; EAW15666.1; -; Genomic_DNA.
DR RefSeq; XP_001257563.1; XM_001257562.1.
DR AlphaFoldDB; A1DLJ5; -.
DR SMR; A1DLJ5; -.
DR STRING; 36630.CADNFIAP00005089; -.
DR EnsemblFungi; EAW15666; EAW15666; NFIA_050080.
DR GeneID; 4584078; -.
DR KEGG; nfi:NFIA_050080; -.
DR VEuPathDB; FungiDB:NFIA_050080; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OMA; VMCSYQM; -.
DR OrthoDB; 559385at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 2.60.40.10; -; 1.
DR Gene3D; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 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 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; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 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..1045
FT /note="Probable beta-glucosidase E"
FT /id="PRO_0000394875"
FT TOPO_DOM 1..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..1045
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 430
FT /evidence="ECO:0000250"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 902
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 988
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1045 AA; 114875 MW; 9587BF4A3DA770F8 CRC64;
MAPPDSTHGG SFRDHLKTND RSSTSKGKQR YAPLHEAIPE EISSFRSPSE YADADTDSDS
DHENSGSYQL RPVDRYGSHH SSAFIPVIRD DGGVETYLDS ITEAEQELLS ASKQYDLFDD
DDSDDLDSDE EATLRYKLKD RLKRRRARLQ AWPPVKYARI WWRTLLAVIV TLAVVVWGFL
SFAVSHREEP KVWPMVPSDS WFPSPKGGTL KHWEESYKKA QSLVRNMTLV EKVNITTGIG
WQMGLCVGNT GLRFADHVSA FPAGITTGST WNRELMRERG VAMGREARLK GVNVLLGPSM
GPLGMMPAGG RNWEGFGSDP VLQAVAAAET IRGIQSNGVM ATAKHFVMNE QEHFRQPFEW
GIPTALSSNV GDRALHEVFA WPFAESIRAD VASVMCSYQM VNNSHACENS KLLNGILKDE
LGFQGFVQSD WLAQRSGINS VLGGLDMSMP GDGLHWVDGK SLWGSELTRA VLNTSVPVER
LNDMVTRIVA AWYHLGQDTW ERPPPEGNGG PNFSSWTNDK VGWLHTGSND GSYAVVNHYV
DAQGTGPEAH SIIARKVAAE GTVLLKNVDR TLPLSRNASS PSGGILRVGI YGDDAGPASG
PNACPDRGCN QGTLATGWGS GTVEFPYLVS PIEALESAWS TEIESTAYLR NAVMPADAVD
KDLCLVFVNA DSGEGYISAG GIHGDRNDLF LQKGGDTLVR TVASNCGGGQ GKTVIVIHAV
GPVVMESWID LPGVHAVLLS NLPGQESGNA LMDVLFGEVD ASGRLPYTIG KSLEDYGPGA
QVLYEPNAPV PQADFLDALY IDYRHFDRYN ITPRFEFGFG LSYTTFELSD LSISPLQRKS
RSPPPRPADA VAPPVYDTSL PDPASALFPT GFQPIFKYIY PYLSNLDGTA PRNYSFYPKG
YNETQSPSPA GGGAGGHPAL YEEMVSVKLQ VSNTGDRKGQ EVVQLYVSFP PDVTEEGDWV
EVDSDADKTG EKQRERMKIE FPERVLRNFT KIELEPSERR EVQMTLSRKD LSYWSTREQN
WVMPEGKFQI WVGRSSRDLP LMGEY
