BGLI_ASPCL
ID BGLI_ASPCL Reviewed; 838 AA.
AC A1CA51;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Probable beta-glucosidase I;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase I;
DE AltName: Full=Cellobiase I;
DE AltName: Full=Gentiobiase I;
GN Name=bglI; ORFNames=ACLA_010450;
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: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR EMBL; DS027049; EAW12619.1; -; Genomic_DNA.
DR RefSeq; XP_001274045.1; XM_001274044.1.
DR AlphaFoldDB; A1CA51; -.
DR SMR; A1CA51; -.
DR STRING; 5057.CADACLAP00001066; -.
DR PRIDE; A1CA51; -.
DR EnsemblFungi; EAW12619; EAW12619; ACLA_010450.
DR GeneID; 4706951; -.
DR KEGG; act:ACLA_010450; -.
DR VEuPathDB; FungiDB:ACLA_010450; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_4_0_1; -.
DR OMA; GPTINTQ; -.
DR OrthoDB; 175854at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; 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; IPR019800; Glyco_hydro_3_AS.
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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted.
FT CHAIN 1..838
FT /note="Probable beta-glucosidase I"
FT /id="PRO_0000394883"
FT DOMAIN 395..555
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT ACT_SITE 225
FT /evidence="ECO:0000250"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 838 AA; 92243 MW; C7AE89A3507382F3 CRC64;
MVQFDVEKTL EELTLGEKVA LTAGTDFWHT AAVPRLNIPS LRMSDGPNGV RGTRFFNGTR
AACFPCSTAL GATWDTELLY EVGRLMAEES IAKGSHIILG PTINTQRSPL GGRGFESFAE
DGVLSGLLAG NYCKGLQDKG VAATLKHFVC NDQEHERLAV DSIVTMRAMR EIYLMPFHLA
MRLCKTACVM TAYNKINGTH VSENKQIITD ILRKEWGWDG LVMSDWFGTY STSDAINAGL
DLEMPGPTRW RGTALAHAVS SNKAFEYVLD ERVRNVLNLH NFVEPLGIPE NAPEEALNRP
EDQALLRRAA AESVVLMKNE DNILPLKKEK SILVIGPNAK TAAYCGGGSA SLDAYYTVAP
FDGVKAKSEG EVSFSQGVYS YNELPVLGPL LKTEEGEKGF KFRVYNEPSS NPNRELLDEL
RLENSLGFLM DYKHPKVTSF LFYADMEGYF TPEEDGIYDF GVTVQGTGKL YIDGELVVDN
SKNQRQGTAF FGNATVEEKG SKELKAGQTY KVVVEFGSAP TSDLDMRGVV VFGPGGFRFG
AARRVGQEEL ISKAAELASQ ADQVVIFAGL TSEWETEGHD RDHMDLPAGS DEMISRVLDA
NPNAVVVIQS GTPVTMPWAH KTKALLQAWF GGNECGNGIA DVLYGDVNPS AKLPLSFPVR
LQDNPSYLNF RSERGRVLYG EDVYVGYRYY EKVDLAPLFP FGHGLSYTTF SRSDLSLATV
PEKRQLEDGE PITATVTVTN TGDVAGAEVV QLWIVPPPTG VNRPVRELKG FAKVFLNPGE
SKTVEIVVEK KLATSWWDEQ REKWASEKGT YKVLVTGTGD EVLKSSFEVE KTRFWLGL
