ID   BGL46_ARATH             Reviewed;         516 AA.
AC   O80690; Q66GS1;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Beta-glucosidase 46 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU46 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000269|PubMed:16814332};
DE   Flags: Precursor;
GN   Name=BGLU46 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At1g61820 {ECO:0000312|Araport:AT1G61820};
GN   ORFNames=F8K4.3 {ECO:0000312|EMBL:AAC28502.1};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-516.
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=16814332; DOI=10.1016/j.phytochem.2006.05.022;
RA   Escamilla-Trevino L.L., Chen W., Card M.L., Shih M.-C., Cheng C.-L.,
RA   Poulton J.E.;
RT   "Arabidopsis thaliana beta-glucosidases BGLU45 and BGLU46 hydrolyse
RT   monolignol glucosides.";
RL   Phytochemistry 67:1651-1660(2006).
CC   -!- FUNCTION: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl
CC       beta-D-galactoside and natural glucosides such as salicin, p-coumaryl
CC       alcohol glucoside, phenyl-beta-D-glucoside, coniferin, syringin and
CC       arbutin. May be involved in lignification by hydrolyzing monolignol
CC       glucosides. {ECO:0000269|PubMed:16814332}.
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:0000269|PubMed:16814332};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.2 mM for p-coumaryl alcohol glucoside (at pH 5.5)
CC         {ECO:0000269|PubMed:16814332};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=O80690-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in roots and stems.
CC       {ECO:0000269|PubMed:16814332}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC28502.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAU05454.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC004392; AAC28502.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE33892.1; -; Genomic_DNA.
DR   EMBL; BX816529; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BT015331; AAU05454.1; ALT_INIT; mRNA.
DR   EMBL; BT015708; AAU45206.1; -; mRNA.
DR   PIR; T02128; T02128.
DR   RefSeq; NP_850968.1; NM_180637.2. [O80690-1]
DR   AlphaFoldDB; O80690; -.
DR   SMR; O80690; -.
DR   STRING; 3702.O80690; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; O80690; 2 sites, No reported glycans.
DR   PaxDb; 3702-AT1G61820-1; -.
DR   ProteomicsDB; 240625; -. [O80690-1]
DR   EnsemblPlants; AT1G61820.1; AT1G61820.1; AT1G61820. [O80690-1]
DR   GeneID; 842479; -.
DR   Gramene; AT1G61820.1; AT1G61820.1; AT1G61820. [O80690-1]
DR   KEGG; ath:AT1G61820; -.
DR   Araport; AT1G61820; -.
DR   TAIR; AT1G61820; BGLU46.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; O80690; -.
DR   OMA; YKELMYN; -.
DR   OrthoDB; 3373839at2759; -.
DR   PhylomeDB; O80690; -.
DR   BioCyc; ARA:AT1G61820-MONOMER; -.
DR   SABIO-RK; O80690; -.
DR   PRO; PR:O80690; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O80690; baseline and differential.
DR   GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0047782; F:coniferin beta-glucosidase activity; IDA:UniProtKB.
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:0009809; P:lignin biosynthetic process; IMP:TAIR.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF343; BETA-GLUCOSIDASE 46; 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; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
DR   Genevisible; O80690; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..516
FT                   /note="Beta-glucosidase 46"
FT                   /id="PRO_0000390318"
FT   ACT_SITE        198
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT   BINDING         49
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         152
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         197..198
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         341
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         414
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         463
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         470..471
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         479
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        217..224
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   DISULFID        349..354
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
SQ   SEQUENCE   516 AA;  59113 MW;  7F59D86203B6F416 CRC64;
     MKTFANFAIL FLLQSLLFPL YSSCLHQTSD DSSPFPSDFL FGTASSAFQY EGAFLTDGKG
     LNNWDVFAHE NPGKIVDGSN GDIATDQYHR YMEDIQSMNF LGVNSYRLSI SWSRVLPNGR
     FGVINYKGIK YYNNLIDALI KKGITPFVTL NHFDYPQELE NRFKSWLSSE MQKDFGYLAD
     ICFKHFGDRV KHWITINEPN QHISLAYRSG LFPPARCSMP YGNCTHGNSE TEPFIAAHNM
     ILAHAKAIQI YRTKYQREQK GIIGIVVQTS WFEPISDSIA DKNAAERAQS FYSNWILDPV
     VYGKYPEEMV NLLGSALPKF SSNEMNSLMS YKSDFLGINH YTSYFIQDCL ITACNSGDGA
     SKSEGLALKL DRKGNVSIGE LTDVNWQHID PNGFRKMLNY LKNRYHNIPM YITENGFGQL
     QKPETTVEEL LHDTKRIQYL SGYLDALKAA MRDGANVKGY FAWSLLDNFE WLYGYKVRFG
     LFHVDFTTLK RTPKQSATWY KNFIEQNVNI EDQIDK
//