BGLA_ASPTN
ID BGLA_ASPTN Reviewed; 861 AA.
AC Q0CTD7;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Probable beta-glucosidase A;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase A;
DE AltName: Full=Cellobiase A;
DE AltName: Full=Gentiobiase A;
DE Flags: Precursor;
GN Name=bglA; Synonyms=bgl1; ORFNames=ATEG_03047;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476597; EAU36321.1; -; Genomic_DNA.
DR RefSeq; XP_001212225.1; XM_001212225.1.
DR AlphaFoldDB; Q0CTD7; -.
DR SMR; Q0CTD7; -.
DR STRING; 341663.Q0CTD7; -.
DR EnsemblFungi; EAU36321; EAU36321; ATEG_03047.
DR GeneID; 4318025; -.
DR VEuPathDB; FungiDB:ATEG_03047; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OMA; EAQGYGF; -.
DR OrthoDB; 559385at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000007963; 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 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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..861
FT /note="Probable beta-glucosidase A"
FT /id="PRO_0000394099"
FT REGION 735..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /evidence="ECO:0000250"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 861 AA; 93356 MW; 053DBE0B894FFBC2 CRC64;
MKLSILEAAA LTAASVVSAQ DDLAYSPPYY PSPWADGHGE WSNAYKRAVD IVSQMTLTEK
VNLTTGTGWE LERCVGQTGS VPRLGIPSLC LQDSPLGIRM SDYNSAFPAG INVAATWDKK
LAYQRGKAMG EEFSDKGIDV QLGPAAGPLG RSPDGGRNWE GFSPDPALTG VLFAETIKGI
QDAGVIATAK HYILNEQEHF RQVGEAQGYG FNITETVSSN VDDKTMHELY LWPFADAVRA
GVGAVMCSYN QINNSYGCQN SLTLNKLLKA ELGFQGFVMS DWSAHHSGVG AALAGLDMSM
PGDISFDSGT SFYGTNLTVG VLNGTIPQWR VDDMAVRIMA AYYKVGRDRL WTPPNFSSWT
RDEYGFAHFF PSEGAYERVN EFVNVQRDHA QVIRRIGADS VVLLKNDGAL PLTGQEKTVG
ILGEDAGSNP KGANGCSDRG CDKGTLAMAW GSGTANFPYL VTPEQAIQNE VLKGRGNVFA
VTDNYDTQQI AAVASQSTVS LVFVNADAGE GFLNVDGNMG DRKNLTLWQN GEEVIKTVTE
HCNNTVVVIH SVGPVLIDEW YAHPNVTGIL WAGLPGQESG NAIADVLYGR VNPGGKTPFT
WGKTRASYGD YLLTEPNNGN GAPQDNFNEG VFIDYRRFDK YNETPIYEFG HGLSYTTFEL
SGLQVQLING SSYVPTTGQT SAAQAFGKVE DASSYLYPEG LKRISKFIYP WLNSTDLKAS
TGDPEYGEPN FEYIPEGATD GSPQPRLPAS GGPGGNPGLY EDLFQVSVTI TNTGKVAGDE
VPQLYVSLGG PNEPKRVLRK FERLHIAPGQ QKVWTTTLNR RDLANWDVVA QDWKITPYAK
TIFVGTSSRK LPLAGRLPRV Q
