BGL46_ARATH
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 03-AUG-2022, entry version 123.
DE RecName: Full=Beta-glucosidase 46;
DE Short=AtBGLU46;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=BGLU46; OrderedLocusNames=At1g61820; ORFNames=F8K4.3;
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, AND TISSUE SPECIFICITY.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 mM for p-coumaryl alcohol glucoside (at pH 5.5);
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; 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.AT1G61820.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; O80690; -.
DR PRIDE; O80690; -.
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; locus:2036873; AT1G61820.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; O80690; -.
DR OMA; RYMEDIS; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; O80690; -.
DR BioCyc; ARA:AT1G61820-MON; -.
DR SABIO-RK; O80690; -.
DR PRO; PR:O80690; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80690; baseline and differential.
DR Genevisible; O80690; AT.
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 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; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
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"
FT ACT_SITE 414
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 470..471
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 217..224
FT /evidence="ECO:0000250"
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
