BGLC_ASPFN
ID BGLC_ASPFN Reviewed; 634 AA.
AC B8NGU6;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Probable beta-glucosidase C;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase C;
DE AltName: Full=Cellobiase C;
DE AltName: Full=Gentiobiase C;
DE Flags: Precursor;
GN Name=bglC; ORFNames=AFLA_138140;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963478; EED51050.1; -; Genomic_DNA.
DR RefSeq; XP_002379826.1; XM_002379785.1.
DR AlphaFoldDB; B8NGU6; -.
DR SMR; B8NGU6; -.
DR STRING; 5059.CADAFLAP00007691; -.
DR PRIDE; B8NGU6; -.
DR EnsemblFungi; EED51050; EED51050; AFLA_138140.
DR VEuPathDB; FungiDB:AFLA_138140; -.
DR eggNOG; ENOG502QTBT; Eukaryota.
DR HOGENOM; CLU_004542_8_2_1; -.
DR OMA; VKHWVGY; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000001875; 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; 3.20.20.300; -; 1.
DR Gene3D; 3.40.50.1700; -; 1.
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 Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF52279; SSF52279; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..634
FT /note="Probable beta-glucosidase C"
FT /id="PRO_0000394103"
FT ACT_SITE 337
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 634 AA; 70145 MW; FCF6E0543CFD1F49 CRC64;
MRIDCTVASL TALASGCQAL STRPYVPRGH SLSRRDDSAP IYRDASYCID ERVDDLLARM
TIEEKAGQLF HTRLMDGPLD DEGSGNNAHN STSNMIGEKH MTHFNLASDI TNATETAEFI
NRIQELALQT RLGIPVTVST DPRHSFTENV GTGFKAGVFS QWPESIGLAA LRDPYVVRKF
AEVAKEEYIA VGIRAALHPQ VDLSTEPRWA RISNTWGENS TLTSELLVEY IKGFQGDKLG
PQSVKTVTKH FPGGGPVENG EDSHFAYGKN QTYPGNNLEE HLKPFKAAIA AGATEIMPYY
SRPIGTEYEP VAFSFNKRIV TELLRNELGF EGIVLTDWGL ITDGYIAGQY MPARAWGVEN
LTELERAARI LDAGCDQFGG EERPELIVQL VQEGTVSEDR IDVSVRRLLR EKFVLGLFDN
PFVDPESAGR VVGNDYFVRL GREAQRRSYT LLSNNEDIVP LKKIEQSTKF YIEGFNASFI
ESWNYTVVDS PEEADYALLR YNAPYEPRPG GFEANMHAGS LAFNDTEKAR QAKIYSTVPT
IVDIVMDRPA VIPEIIEQAK AVFASYGSDS NAFLDVVFGV SAPEGKLPFD LPSSMEAVEA
QMEDVPFDTR NPVFKFGHGL SYANPCASSS SKCS
