ID BGLD_ASPFN Reviewed; 752 AA.
AC B8NJF4;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=Probable beta-glucosidase D;
DE EC=3.2.1.21;
DE AltName: Full=Beta-D-glucoside glucohydrolase D;
DE AltName: Full=Cellobiase D;
DE AltName: Full=Gentiobiase D;
DE Flags: Precursor;
GN Name=bglD; ORFNames=AFLA_066750;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EED49853.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EQ963479; EED49853.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002380234.1; XM_002380193.1.
DR AlphaFoldDB; B8NJF4; -.
DR SMR; B8NJF4; -.
DR STRING; 332952.B8NJF4; -.
DR GlyCosmos; B8NJF4; 12 sites, No reported glycans.
DR EnsemblFungi; EED49853; EED49853; AFLA_066750.
DR VEuPathDB; FungiDB:AFLA_008611; -.
DR eggNOG; ENOG502R4T1; Eukaryota.
DR OrthoDB; 5486783at2759; -.
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; 3.40.50.1700; 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; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF14; BETA-GLUCOSIDASE D-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; Cellulose degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..752
FT /note="Probable beta-glucosidase D"
FT /id="PRO_0000394106"
FT ACT_SITE 265
FT /evidence="ECO:0000250"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 752 AA; 80200 MW; EF4A1C9545347B7A CRC64;
MRFVSLAVGA ALLGAAGASS ISSNVGLLKA NGVALGNWEA AYEKASAFVS GLTTDQKLAL
ITGSNVESTN GNFTPLYFLD GDMGLQDFYY VSAFSLSSAL AMTWDRDAIY EQAKAVGSEF
YNKGVQVVAG PTSQPLGRTP WGGRGVEGFG PDPYLNGLAT GLTTKGYVDA GVIPGGKHFL
LYEQETNRTS SFGSSGEGSP YSSNADDKTI HETYLWPFYD AVKNGAGAVM CAMTKVNGTM
ACENSDLLMK MLKTELGFPG MVWPDMNGQN SAKGSALGGE DYGSSSIWST STMESFLSNG
TLSEARLNDM AIRNLIGYYY VNLDNGRQPT RQTTDVYVDV RANHSKLIRE NGAKSMALLK
NEGVLPLSKP RVMSIFGAHA GPIMGGPNSN VDVMGSGPTY QGHLATGSGS GMASMPYLIT
PYGALTNKAA QDGTVLRWVL NDTYSSGGGS SLVPSSTSST AVEPSFENFA TGSDICLVFI
NALAGEGADR TELYNADQDA MVNTVADNCN NTVAVVNTVG PRLLDQWIEH DNVTAVLYGS
LLGQESGNSI VDLLYGDVNP SGRLVHTIAK NESDYNVGLC YTAQCNFTEG VYLDYRYFDA
HNITPRYPFG HGLSYTTFHY SSLAIKAPSS ITKAPKGNLT VGGPSDLWDV VGTVSARIAN
NGTLSGAEVP QLYLGFPDSA DQPVRQLRGF DRVELSAGQE AVVTFNLRRR DISYWNVKTQ
QWMVAGGKYT VFVGGSSRDL RLNGTFFLWV GS
//
