BGLE_ASPCL
ID BGLE_ASPCL Reviewed; 1050 AA.
AC A1CMH6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=ACLA_096980;
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: 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; DS027058; EAW08763.1; -; Genomic_DNA.
DR RefSeq; XP_001270189.1; XM_001270188.1.
DR AlphaFoldDB; A1CMH6; -.
DR SMR; A1CMH6; -.
DR STRING; 5057.CADACLAP00009117; -.
DR PRIDE; A1CMH6; -.
DR EnsemblFungi; EAW08763; EAW08763; ACLA_096980.
DR GeneID; 4702262; -.
DR KEGG; act:ACLA_096980; -.
DR VEuPathDB; FungiDB:ACLA_096980; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OMA; VMCSYQM; -.
DR OrthoDB; 559385at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000006701; 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..1050
FT /note="Probable beta-glucosidase E"
FT /id="PRO_0000394870"
FT TOPO_DOM 1..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..1050
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 458
FT /evidence="ECO:0000250"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 884
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1050 AA; 115389 MW; 0EE88C1BD581414E CRC64;
MPPPDSNPGS FRDHLKHDNK NNNSSTTSKG KQRYTPLHDS IPEEIASPRS ASASSSFDLD
PDLENQSRND YKLRPLARSS STNGGHNYST AYIPVIRDEG DDVETYLDSI TEAEQELLSL
SKQYDFADDS DDFDSDDDAA LRRKVQKQEQ RRRRERLKAK VWTPVKYARI WRRTLVVVIV
ALALLVWGFL RFTAAQRQGP KVWPMLPSDS WFPSPKGGTL KHWEESYRKA QSLVRNMTLI
EKVNITTGTG WQMGMCVGNT GPAELVKFPS LCLQDGPQGL RYADHVTAFP AGITTGSTWN
RTLMRERGIA MGREARLKGV NVLLGPSIGP IGMMPAGGRN WEGFGSDPVL QGVAAAETIR
GIQSNGVMAT AKHFLMNEQE HFRQPFEWGI STALSSNVGD RALHEVFAWP FAESIRADVA
SVMCSYQMVN NSHACENSKL LNGILKDELG FQGFVQSDWL AQRSGINSAL GGLDMSMPGD
GLHWTDGKSL WGRELTRAVL NTSIPMERLN DMVTRIVAAW YQFEQDEWER PPPEGNGGPN
FSSWTGGDVG WLHAGSNDGL YAVVNQYIDA QGTGPEAHSI IARKVAAEGT VLLKNVDHTL
PLSRNASGPS GVMRVGIYGD DAGPAQGPNA CPDRGCNQGT LATGWGSGTV DFPYLVSPLE
ALETAWKTEV EMTAFLRNAV MPADVADKDL CLVFANADSG EGFISAGGIH GDRNDLFLQK
GGDTLIRTVA SHCGEGQGKT VVVIHAVGPV VMESWIDLPG VHAVLLANLP GQESGNALMD
VLFGDVDASG RLPYTIGKSL EEYGTEAQVL YEPNAPVPQV DLLDALFIDY RHFDQYNITP
RFEFGFGLSY TTFKLKDLHV RSLQSKSRSP AARPAAAVSP PEYNTTLPDP ALALFPPGFQ
PVYKYIYPYL PSLDGTAPAN YSYYPKDYNQ TQGPSPAGGG AGGNPALFQE MASVSVQVQN
TGDRKGQEVV QVYVSFPSDE KVKIDFPERV LRNFTKVELE PGERREVQMT LSRKDLSYWS
VREQNWVMPD GDFQIWVGRS SRDLPLQAKY
