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   27-MAR-2024, entry version 123.
DE   RecName: Full=Beta-glucosidase 14 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU14 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000250|UniProtKB:O64879};
DE   Flags: Precursor;
GN   Name=BGLU14 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At2g25630 {ECO:0000312|Araport:AT2G25630};
GN   ORFNames=F3N11.8 {ECO:0000312|EMBL:AAD31364.1};
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         Evidence={ECO:0000250|UniProtKB:O64879};
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.Q9SLA0; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q9SLA0; 3 sites, No reported glycans.
DR   PaxDb; 3702-AT2G25630-1; -.
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; AT2G25630; BGLU14.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; Q9SLA0; -.
DR   OMA; NYYQTIT; -.
DR   OrthoDB; 3373839at2759; -.
DR   PhylomeDB; Q9SLA0; -.
DR   BioCyc; ARA:AT2G25630-MONOMER; -.
DR   BRENDA; 3.2.1.21; 399.
DR   PRO; PR:Q9SLA0; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SLA0; baseline and differential.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009860; P:pollen tube growth; IEP:TAIR.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF224; BETA-GLUCOSIDASE 12-RELATED; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
DR   Genevisible; Q9SLA0; AT.
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|UniProtKB:Q7XSK0"
FT   ACT_SITE        396
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         49
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         153
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         198..199
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         343
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         396
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         441
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         448..449
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         457
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        218..226
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
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
//