BGL42_ARATH
ID BGL42_ARATH Reviewed; 490 AA.
AC Q9FIW4; Q2V330;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Beta-glucosidase 42 {ECO:0000303|PubMed:15604686};
DE Short=AtBGLU42 {ECO:0000303|PubMed:15604686};
DE EC=3.2.1.21 {ECO:0000250|UniProtKB:Q8L7J2};
GN Name=BGLU42 {ECO:0000303|PubMed:15604686};
GN OrderedLocusNames=At5g36890 {ECO:0000312|Araport:AT5G36890};
GN ORFNames=MLF18.1 {ECO:0000312|EMBL:BAB11630.1};
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
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, DISRUPTION PHENOTYPE, INDUCTION BY PSEUDOMONAS FLUORESCENS, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25138267; DOI=10.1111/nph.12980;
RA Zamioudis C., Hanson J., Pieterse C.M.J.;
RT "beta-Glucosidase BGLU42 is a MYB72-dependent key regulator of
RT rhizobacteria-induced systemic resistance and modulates iron deficiency
RT responses in Arabidopsis roots.";
RL New Phytol. 204:368-379(2014).
CC -!- FUNCTION: Involved in the secretion of root-derived phenolics upon iron
CC ions (Fe) depletion. Promotes disease resistance toward B.cinerea,
CC H.arabidopsidis and P.syringae pv. tomato DC3000. Required during
CC rhizobacteria-mediated (e.g. P.fluorescens WCS417r) broad-spectrum
CC induced systemic resistance (ISR) against several pathogens.
CC {ECO:0000269|PubMed:25138267}.
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:Q8L7J2};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FIW4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FIW4-2; Sequence=VSP_038498, VSP_038499;
CC -!- TISSUE SPECIFICITY: Expressed at low levels predominantly in root
CC epidermal cells. {ECO:0000269|PubMed:25138267}.
CC -!- INDUCTION: Accumulates upon rhizobacteria-mediated (e.g. P.fluorescens
CC WCS417r) induced systemic resistance (ISR) in root trichoblasts and, to
CC a lesser extent, in cortical cells. {ECO:0000269|PubMed:25138267}.
CC -!- DISRUPTION PHENOTYPE: Reduced secretion of root-derived phenolics upon
CC iron ions (Fe) depletion, thus leading to their accumulation in the
CC root interior. Impaired P.fluorescens WCS417r-mediated broad-spectrum
CC induced systemic resistance (ISR) against several pathogens.
CC {ECO:0000269|PubMed:25138267}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AB016877; BAB11630.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94122.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94123.1; -; Genomic_DNA.
DR EMBL; BT010611; AAQ89633.1; -; mRNA.
DR EMBL; AK175760; BAD43523.1; -; mRNA.
DR RefSeq; NP_001031975.1; NM_001036898.2. [Q9FIW4-2]
DR RefSeq; NP_198505.2; NM_123047.4. [Q9FIW4-1]
DR PDB; 7F3A; X-ray; 1.70 A; A=1-490.
DR PDBsum; 7F3A; -.
DR AlphaFoldDB; Q9FIW4; -.
DR SMR; Q9FIW4; -.
DR BioGRID; 18907; 1.
DR STRING; 3702.AT5G36890.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q9FIW4; -.
DR PRIDE; Q9FIW4; -.
DR ProteomicsDB; 240623; -. [Q9FIW4-1]
DR EnsemblPlants; AT5G36890.1; AT5G36890.1; AT5G36890. [Q9FIW4-1]
DR EnsemblPlants; AT5G36890.2; AT5G36890.2; AT5G36890. [Q9FIW4-2]
DR GeneID; 833656; -.
DR Gramene; AT5G36890.1; AT5G36890.1; AT5G36890. [Q9FIW4-1]
DR Gramene; AT5G36890.2; AT5G36890.2; AT5G36890. [Q9FIW4-2]
DR KEGG; ath:AT5G36890; -.
DR Araport; AT5G36890; -.
DR TAIR; locus:2167479; AT5G36890.
DR eggNOG; KOG0626; Eukaryota.
DR InParanoid; Q9FIW4; -.
DR OMA; VEACDRK; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9FIW4; -.
DR BioCyc; ARA:AT5G36890-MON; -.
DR PRO; PR:Q9FIW4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIW4; baseline and differential.
DR Genevisible; Q9FIW4; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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:0030245; P:cellulose catabolic process; IEA:InterPro.
DR GO; GO:0009866; P:induced systemic resistance, ethylene mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0031349; P:positive regulation of defense response; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:1990641; P:response to iron ion starvation; IMP:UniProtKB.
DR GO; GO:0019748; P:secondary metabolic process; IMP:UniProtKB.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
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 TIGRFAMs; TIGR03356; BGL; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Glycoprotein; Glycosidase; Hydrolase;
KW Plant defense; Reference proteome.
FT CHAIN 1..490
FT /note="Beta-glucosidase 42"
FT /id="PRO_0000390315"
FT ACT_SITE 183
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT ACT_SITE 388
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT BINDING 437
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT BINDING 444..445
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 487
FT /note="G -> E (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038498"
FT VAR_SEQ 488..490
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038499"
SQ SEQUENCE 490 AA; 56077 MW; 50DED68FBF06D538 CRC64;
MAQKLNLLNL AVPPVTHRSN FPSTFTFGVA TSAYQIEGGW NEGKKGPSIW DKFTHIEGKI
LDGSNGDVAV DHYHRYKEDV DLIGQLGFGA YRFSISWSRI FPDGLGTEVN EEGIAFYNDL
INTLLEKGIQ PYVTLYHWDL PSHLQEAIGG WTNRKIVDYF GLYADACFAN FGDRVKHWIT
LNEPLQTSVN GHCIGIFAPG RNEKPLIEPY LVSHHQVLAH ATAVSIYRSK YKESQGGQIG
LSVDCEWAEP NSEKPEDKVA ADRRIDFQLG WFLDPLFFGD YPASMRQKLG DNLPRFTPEE
KEFMLQNSWD FLGLNHYTSR LISHVSNKEA ESNFYQAQEL ERIVELENGD LIGERAASDW
LYAVPWGIRK TLNYMSKKYN HPPIFITENG MDDEDDGSAS IHDMLDDKRR VDYFKSYLAN
VSQAIEDGVD IKGYFAWSLL DNFEWAQGYT KRFGLVYVDY KNGLTRHPKS SAYWFMKFLK
GDEENKGKKE
