BGLE_ASPFU
ID BGLE_ASPFU Reviewed; 1033 AA.
AC Q4WD56;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=AFUA_6G03570;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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: 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; AAHF01000012; EAL85682.1; -; Genomic_DNA.
DR RefSeq; XP_747720.1; XM_742627.1.
DR AlphaFoldDB; Q4WD56; -.
DR SMR; Q4WD56; -.
DR STRING; 746128.CADAFUBP00009206; -.
DR EnsemblFungi; EAL85682; EAL85682; AFUA_6G03570.
DR GeneID; 3505005; -.
DR KEGG; afm:AFUA_6G03570; -.
DR VEuPathDB; FungiDB:Afu6g03570; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR InParanoid; Q4WD56; -.
DR OMA; VMCSYQM; -.
DR OrthoDB; 559385at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000002530; Chromosome 6.
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; 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; 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..1033
FT /note="Probable beta-glucosidase E"
FT /id="PRO_0000394872"
FT TOPO_DOM 1..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..1033
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..71
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 COMPBIAS 52..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 446
FT /evidence="ECO:0000250"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 909
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 918
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 976
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1033 AA; 113423 MW; 68768F797E72DE92 CRC64;
MAPPDSTHGG SFRDHLKTND RSSTSKGKQR YSPLQEAIPE EISSFRSPSE YADTDSDSDL
ERSGSYKLRP VDRYGSHHSS AFIPVIREEN GVETYLDSIT EAEQELLSAS KQYDLVDDDD
SSDFDSDEEA TLRYRLKDRL KRRRARLQAW QPVKYARIWW RTLLAVVVTL VVVVWGFLSF
AVSHREEPTV WPMVPSDSWF PSPKGGTLKH WEESYKKAQS LVRNMTLVEK VNITTGIGWQ
MGLCVGNTGP ADIVKFPSLC LQDGPQGLRF ADHVSAFPAG ITTGSTWNRE LMRERGVAMG
REARLKGVNV LLGPSMGPLG MMPAGGRNWE GFGSDPVLQA VAAAETIRGI QSNGVMATAK
HFVMNEQEHF RQPFEWGIPT ALSSNVGDRA LHEVFAWPFA ESIRADVASV MCSYQMVNNS
HACENSKLLN GILKDELGFQ GFVQSDWLAQ RSGINSALGG LDMSMPGDGL HWVDGKSLWG
SELTRAVLNT SVPVERLNDM VTRIVAAWYH LGQDTWERPP PEGNGGPNFS SWTNDEVGWL
HTGSNDGSYA RVNHYVDAQG TGPEAHSIIA RKVAAEGTVL LKNVDRTLPL SRNASSPSGG
ILRVGIYGDD AGPALGPNAC PDRGCNQGTL ATGWGSGTVE FPYLVSPIEA LESAWSTEIE
STAYLRNAVM PADAVDKDLC LVFVNADSGE GYISAGGIHG DRNDLFLQKG GDTLVRTVSS
NCGGGQGKTV VVIHAVGPVV MESWIDLPGV HAVLLANLPG QESGNALVDV LFGEVDASGR
LPYTIGKSLE DYGPGAQVLY EPNAPVPQVD FLDALYIDYR HFDRHNITPR FEFGFGLSYT
TFELLDLSIS PLQQKSRSVP PRPADAVAPP VYDISLPDPA SALFPAGFQP VFKYIYPYLS
NLDGTAPHNY SFYPKGYNET QRPSPAGGGA GGHPALYEEM VSVKLQVSNT GDRKGQEVVQ
VYVSFPPDFP ERVLRNFTKI ELEPSERREV QMTLSRKDLS YWSTREQNWV MPEGKFQIWV
GRSSRDLPLM GEY
