BGL14_ARATH
ID BGL14_ARATH Reviewed; 489 AA.
AC Q9SLA0;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Beta-glucosidase 14;
DE Short=AtBGLU14;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU14; OrderedLocusNames=At2g25630; ORFNames=F3N11.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15604686; DOI=10.1007/s11103-004-0790-1;
RA Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R.,
RA Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.;
RT "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT family 1.";
RL Plant Mol. Biol. 55:343-367(2004).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD31364.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006053; AAD31364.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07728.1; -; Genomic_DNA.
DR PIR; G84650; G84650.
DR RefSeq; NP_850065.1; NM_179734.1.
DR AlphaFoldDB; Q9SLA0; -.
DR SMR; Q9SLA0; -.
DR STRING; 3702.AT2G25630.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q9SLA0; -.
DR PRIDE; Q9SLA0; -.
DR ProteomicsDB; 240470; -.
DR EnsemblPlants; AT2G25630.1; AT2G25630.1; AT2G25630.
DR GeneID; 817104; -.
DR Gramene; AT2G25630.1; AT2G25630.1; AT2G25630.
DR KEGG; ath:AT2G25630; -.
DR Araport; AT2G25630; -.
DR TAIR; locus:2050306; AT2G25630.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9SLA0; -.
DR OMA; DICFKHY; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9SLA0; -.
DR BioCyc; ARA:AT2G25630-MON; -.
DR BRENDA; 3.2.1.21; 399.
DR PRO; PR:Q9SLA0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SLA0; baseline and differential.
DR Genevisible; Q9SLA0; AT.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0019762; P:glucosinolate catabolic process; IBA:GO_Central.
DR GO; GO:0009860; P:pollen tube growth; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IBA:GO_Central.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..489
FT /note="Beta-glucosidase 14"
FT /id="PRO_0000389577"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 396
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 441
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 448..449
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 218..226
FT /evidence="ECO:0000250"
SQ SEQUENCE 489 AA; 55009 MW; 0AF3D3AD5235218C CRC64;
MTSKYFSVLV FIILASNEVV AKRHSSTPKL RKTDFPEDFI FGAATSAYQV EGAAQEDGRG
PSIWDTFSEK YPEKIKDGSN GSIADDSYHL YKEDVGLLHQ IGFNAYRFSI SWSRILPRGN
LKGGINQAGI DYYNNLINEL LSKGIKPFAT IFHWDTPQDL EDAYGGFRGA EIVNDFRDYA
DICFKSFGDR VKHWITLNEP LTVVQQGYVA GVMAPGRCSK FTNPNCTAGN GATEPYIVGH
NLILAHGEAI KVYRKKYKAS QKGQVGIALN AGWNLPYTES AEDRLAAARA MAFTFDYFME
PLVTGKYPVD MVNNVKGGRL PTFTSKQSNM LKGSYDFIGI NYYSSSYAKD VPCSSENVTM
FSDPCASVTG ERDGGIRDLI LYAKYKFKDP VMYITENGRD EASTGKILLK DGDRIDYYAR
HLKMVQDAIL IGANVKGFFA WSLLDNFEWA SGYTVRFGLV YVDFNDRRKR YLKKSAHWFR
HLLNGKKEN
