BGL26_ARATH
ID BGL26_ARATH Reviewed; 560 AA.
AC O64883;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Beta-glucosidase 26, peroxisomal;
DE Short=AtBGLU26;
DE EC=3.2.1.21 {ECO:0000269|PubMed:19095900};
DE AltName: Full=Protein PENETRATION 2;
GN Name=BGLU26; Synonyms=PEN2; OrderedLocusNames=At2g44490; ORFNames=F4I1.30;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-183.
RX PubMed=16293760; DOI=10.1126/science.1119409;
RA Lipka V., Dittgen J., Bednarek P., Bhat R., Wiermer M., Stein M.,
RA Landtag J., Brandt W., Rosahl S., Scheel D., Llorente F., Molina A.,
RA Parker J., Somerville S., Schulze-Lefert P.;
RT "Pre- and postinvasion defenses both contribute to nonhost resistance in
RT Arabidopsis.";
RL Science 310:1180-1183(2005).
RN [6]
RP FUNCTION.
RX PubMed=19095898; DOI=10.1126/science.1164627;
RA Clay N.K., Adio A.M., Denoux C., Jander G., Ausubel F.M.;
RT "Glucosinolate metabolites required for an Arabidopsis innate immune
RT response.";
RL Science 323:95-101(2009).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF GLU-183.
RX PubMed=19095900; DOI=10.1126/science.1163732;
RA Bednarek P., Pislewska-Bednarek M., Svatos A., Schneider B., Doubsky J.,
RA Mansurova M., Humphry M., Consonni C., Panstruga R., Sanchez-Vallet A.,
RA Molina A., Schulze-Lefert P.;
RT "A glucosinolate metabolism pathway in living plant cells mediates broad-
RT spectrum antifungal defense.";
RL Science 323:101-106(2009).
CC -!- FUNCTION: Possesses beta-glucosidase activity toward 4-methyl-
CC umbelliferyl-beta-D-glucoside in vitro. Possesses myrosinase activity
CC toward indol-3-yl-methylglucosinolate (I3M) and 4-methoxy-indol-3-yl-
CC methylglucosinolate (4MO-I3M) in vivo (PubMed:19095900). Component of
CC an inducible preinvasion resistance mechanism that prevents penetration
CC of the nonhost fungal species B.graminis and E.pisi (PubMed:16293760).
CC Involved in indole glucosinolate (IGS) activation during pattern-
CC triggered immunity (PTI). Functions as myrosinase for the breakdown of
CC flg22-triggered IGS. Required for both callose deposition and
CC glucosinolate activation during pathogen-triggered resistance
CC (PubMed:19095898). During fungal attack, required for IGS activation
CC that mediates broad-spectrum antifungal defense (PubMed:19095900).
CC {ECO:0000269|PubMed:16293760, ECO:0000269|PubMed:19095898,
CC ECO:0000269|PubMed:19095900}.
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:19095900};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=722 uM for indol-3-yl-methylglucosinolate
CC {ECO:0000269|PubMed:19095900};
CC KM=150 uM for 4-methyl-umbelliferyl-beta-D-glucoside
CC {ECO:0000269|PubMed:19095900};
CC Vmax=7.5 umol/min/mg enzyme with indol-3-yl-methylglucosinolate as
CC substrate {ECO:0000269|PubMed:19095900};
CC Vmax=0.76 umol/min/mg enzyme with 4-methyl-umbelliferyl-beta-D-
CC glucoside as substrate {ECO:0000269|PubMed:19095900};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:19095900};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16293760}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AC004521; AAC16095.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10428.1; -; Genomic_DNA.
DR EMBL; AY091016; AAM14038.1; -; mRNA.
DR EMBL; BT000990; AAN41390.1; -; mRNA.
DR PIR; T02404; T02404.
DR RefSeq; NP_181977.1; NM_130012.4.
DR AlphaFoldDB; O64883; -.
DR SMR; O64883; -.
DR BioGRID; 4392; 4.
DR IntAct; O64883; 3.
DR STRING; 3702.AT2G44490.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; O64883; -.
DR PRIDE; O64883; -.
DR ProteomicsDB; 241213; -.
DR EnsemblPlants; AT2G44490.1; AT2G44490.1; AT2G44490.
DR GeneID; 819056; -.
DR Gramene; AT2G44490.1; AT2G44490.1; AT2G44490.
DR KEGG; ath:AT2G44490; -.
DR Araport; AT2G44490; -.
DR TAIR; locus:2050544; AT2G44490.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; O64883; -.
DR OMA; NEPWIYS; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; O64883; -.
DR BioCyc; MetaCyc:AT2G44490-MON; -.
DR BRENDA; 3.2.1.147; 399.
DR PRO; PR:O64883; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64883; baseline and differential.
DR Genevisible; O64883; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA: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:0019137; F:thioglucosidase activity; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0019762; P:glucosinolate catabolic process; IBA:GO_Central.
DR GO; GO:0019760; P:glucosinolate metabolic process; IMP:TAIR.
DR GO; GO:0042344; P:indole glucosinolate catabolic process; IMP:TAIR.
DR GO; GO:0009682; P:induced systemic resistance; IMP:TAIR.
DR GO; GO:0009617; P:response to bacterium; IMP: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 1: Evidence at protein level;
KW Glycosidase; Hydrolase; Peroxisome; Plant defense; Reference proteome.
FT CHAIN 1..560
FT /note="Beta-glucosidase 26, peroxisomal"
FT /id="PRO_0000389588"
FT ACT_SITE 183
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 398
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 457..458
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 183
FT /note="E->D: Susceptibility to the nonhost powdery mildew
FT species B.graminis and E.pisi. Loss of myrosinase activity
FT but intact glucosidase activity."
FT /evidence="ECO:0000269|PubMed:16293760,
FT ECO:0000269|PubMed:19095900"
SQ SEQUENCE 560 AA; 63916 MW; BDDE6F7ED328CCBC CRC64;
MAHLQRTFPT EMSKGRASFP KGFLFGTASS SYQYEGAVNE GARGQSVWDH FSNRFPHRIS
DSSDGNVAVD FYHRYKEDIK RMKDINMDSF RLSIAWPRVL PYGKRDRGVS EEGIKFYNDV
IDELLANEIT PLVTIFHWDI PQDLEDEYGG FLSEQIIDDF RDYASLCFER FGDRVSLWCT
MNEPWVYSVA GYDTGRKAPG RCSKYVNGAS VAGMSGYEAY IVSHNMLLAH AEAVEVFRKC
DHIKNGQIGI AHNPLWYEPY DPSDPDDVEG CNRAMDFMLG WHQHPTACGD YPETMKKSVG
DRLPSFTPEQ SKKLIGSCDY VGINYYSSLF VKSIKHVDPT QPTWRTDQGV DWMKTNIDGK
QIAKQGGSEW SFTYPTGLRN ILKYVKKTYG NPPILITENG YGEVAEQSQS LYMYNPSIDT
ERLEYIEGHI HAIHQAIHED GVRVEGYYVW SLLDNFEWNS GYGVRYGLYY IDYKDGLRRY
PKMSALWLKE FLRFDQEDDS STSKKEEKKE SYGKQLLHSV QDSQFVHSIK DSGALPAVLG
SLFVVSATVG TSLFFKGANN
