ID B8NE00_ASPFN Unreviewed; 815 AA.
AC B8NE00;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=AFLA_057310 {ECO:0000313|EMBL:EED51468.1};
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 {ECO:0000313|EMBL:EED51468.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED51468.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
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 -!- 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 Evidence={ECO:0000256|ARBA:ARBA00000448};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; EQ963477; EED51468.1; -; Genomic_DNA.
DR RefSeq; XP_002378475.1; XM_002378434.1.
DR AlphaFoldDB; B8NE00; -.
DR STRING; 332952.B8NE00; -.
DR EnsemblFungi; EED51468; EED51468; AFLA_057310.
DR VEuPathDB; FungiDB:AFLA_004778; -.
DR eggNOG; ENOG502QQ55; Eukaryota.
DR HOGENOM; CLU_004542_5_1_1; -.
DR OMA; MSAYHSY; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
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; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..815
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002878231"
FT TRANSMEM 142..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 734..803
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 815 AA; 88894 MW; 0ACB4782CCFBF308 CRC64;
MVSGVFTKGV LLLGLLSGLA LGQDEKPRYK DPSVPVEERV TDLLGRMTLE EKMSQLIQGA
IGIVSFLPTG GDITNWMNET TGEFNLTGLE WSTKMRGGMF YAMAFSWISG ALGLHRRQCQ
ESSGLYSPKH DSRDSRHCSD RMYVLVMFDS LNPALIILAL IALHGFLIGN ATIYNSPIGF
ACSFNPELIE KMARLIGQEA SALGVNHVMG PVVDLARELR FGRVEETYGE DPFLAGEIGY
HYTKGIQSHN ISANVKHFVG FSQPEQGLNT APVHGGERYL RTTWLPSFKR AIMDAGAWSI
MSAYHSYDGI PAVADYHTLT EILREEWGYK YWVTSDAGAS DRVCTAFKLC RADPIDKEAV
TLAILPAGND VEMGGGSYNF ETIIDLVNAG KLDIEIVNTA VSRVLRAKFE MGLFENPYNA
APASEWNKLI HTQEAVDLAR ELDRESIVLL ENHDNALPLK KSGSIAVIGP MAHGFMNYGD
YVVYESQYRG VTPLDGIKAA VGDKATINYA QGCERWSNDQ SGFAEAVEAA KKSDVAVVVV
GTWSRDQKEL WAGLNATTGE HVDVNSLSLV GAQAPLIKAI IDTGVPTVVV LSSGKPITEP
WLSNNTAALV QQFYPSEQGG NALADVLFGD YNPSGKLSVS FPHSVGDLPI YYDYLNSARE
IGDAGYIYSN GTLEFGHQYA LGNPKAWYPF GYGKSYSSFE YGAVKLDKTN VTEADTVTVS
VDVKNTDAAR EGTEVVQVYV VDEVASVVVP NRLLKGFKKV VIPAGQTKTV EIPLKVQDLG
LWNVRMKYVV EPGAFGVLVG SSSEDIRGNA TFYVQ
//
