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Beta-glucosidase 26, peroxisomal (AtBGLU26) (EC 3.2.1.21) (Protein PENETRATION 2)

 BGL26_ARATH             Reviewed;         560 AA.
O64883;
24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
20-DEC-2017, entry version 110.
RecName: Full=Beta-glucosidase 26, peroxisomal;
Short=AtBGLU26;
EC=3.2.1.21 {ECO:0000269|PubMed:19095900};
AltName: Full=Protein PENETRATION 2;
Name=BGLU26; Synonyms=PEN2; OrderedLocusNames=At2g44490;
ORFNames=F4I1.30;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15604686; DOI=10.1007/s11103-004-0790-1;
Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R.,
Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E.,
Esen A.;
"Functional genomic analysis of Arabidopsis thaliana glycoside
hydrolase family 1.";
Plant Mol. Biol. 55:343-367(2004).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-183.
PubMed=16293760; DOI=10.1126/science.1119409;
Lipka V., Dittgen J., Bednarek P., Bhat R., Wiermer M., Stein M.,
Landtag J., Brandt W., Rosahl S., Scheel D., Llorente F., Molina A.,
Parker J., Somerville S., Schulze-Lefert P.;
"Pre- and postinvasion defenses both contribute to nonhost resistance
in Arabidopsis.";
Science 310:1180-1183(2005).
[6]
FUNCTION.
PubMed=19095898; DOI=10.1126/science.1164627;
Clay N.K., Adio A.M., Denoux C., Jander G., Ausubel F.M.;
"Glucosinolate metabolites required for an Arabidopsis innate immune
response.";
Science 323:95-101(2009).
[7]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF GLU-183.
PubMed=19095900; DOI=10.1126/science.1163732;
Bednarek P., Pislewska-Bednarek M., Svatos A., Schneider B.,
Doubsky J., Mansurova M., Humphry M., Consonni C., Panstruga R.,
Sanchez-Vallet A., Molina A., Schulze-Lefert P.;
"A glucosinolate metabolism pathway in living plant cells mediates
broad-spectrum antifungal defense.";
Science 323:101-106(2009).
-!- FUNCTION: Possesses beta-glucosidase activity toward 4-methyl-
umbelliferyl-beta-D-glucoside in vitro. Possesses myrosinase
activity toward indol-3-yl-methylglucosinolate (I3M) and 4-
methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) in vivo
(PubMed:19095900). Component of an inducible preinvasion
resistance mechanism that prevents penetration of the nonhost
fungal species B.graminis and E.pisi (PubMed:16293760). Involved
in indole glucosinolate (IGS) activation during pattern-triggered
immunity (PTI). Functions as myrosinase for the breakdown of
flg22-triggered IGS. Required for both callose deposition and
glucosinolate activation during pathogen-triggered resistance
(PubMed:19095898). During fungal attack, required for IGS
activation that mediates broad-spectrum antifungal defense
(PubMed:19095900). {ECO:0000269|PubMed:16293760,
ECO:0000269|PubMed:19095898, ECO:0000269|PubMed:19095900}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D-
glucosyl residues with release of beta-D-glucose.
{ECO:0000269|PubMed:19095900}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=722 uM for indol-3-yl-methylglucosinolate
{ECO:0000269|PubMed:19095900};
KM=150 uM for 4-methyl-umbelliferyl-beta-D-glucoside
{ECO:0000269|PubMed:19095900};
Vmax=7.5 umol/min/mg enzyme with indol-3-yl-methylglucosinolate
as substrate {ECO:0000269|PubMed:19095900};
Vmax=0.76 umol/min/mg enzyme with 4-methyl-umbelliferyl-beta-D-
glucoside as substrate {ECO:0000269|PubMed:19095900};
pH dependence:
Optimum pH is 6.0. {ECO:0000269|PubMed:19095900};
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16293760}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AC004521; AAC16095.1; -; Genomic_DNA.
EMBL; CP002685; AEC10428.1; -; Genomic_DNA.
EMBL; AY091016; AAM14038.1; -; mRNA.
EMBL; BT000990; AAN41390.1; -; mRNA.
PIR; T02404; T02404.
RefSeq; NP_181977.1; NM_130012.4.
UniGene; At.36752; -.
ProteinModelPortal; O64883; -.
SMR; O64883; -.
BioGrid; 4392; 4.
STRING; 3702.AT2G44490.1; -.
CAZy; GH1; Glycoside Hydrolase Family 1.
PaxDb; O64883; -.
PRIDE; O64883; -.
EnsemblPlants; AT2G44490.1; AT2G44490.1; AT2G44490.
GeneID; 819056; -.
Gramene; AT2G44490.1; AT2G44490.1; AT2G44490.
KEGG; ath:AT2G44490; -.
Araport; AT2G44490; -.
TAIR; locus:2050544; AT2G44490.
eggNOG; KOG0626; Eukaryota.
eggNOG; COG2723; LUCA.
HOGENOM; HOG000088630; -.
InParanoid; O64883; -.
KO; K01188; -.
OMA; FDIISAG; -.
OrthoDB; EOG0936059B; -.
PhylomeDB; O64883; -.
BioCyc; MetaCyc:AT2G44490-MONOMER; -.
Reactome; R-ATH-189085; Digestion of dietary carbohydrate.
PRO; PR:O64883; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O64883; baseline and differential.
Genevisible; O64883; AT.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0019137; F:thioglucosidase activity; IDA:TAIR.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0009817; P:defense response to fungus, incompatible interaction; IMP:TAIR.
GO; GO:0019760; P:glucosinolate metabolic process; IMP:TAIR.
GO; GO:0042344; P:indole glucosinolate catabolic process; IMP:TAIR.
GO; GO:0009682; P:induced systemic resistance; IMP:TAIR.
GO; GO:0009617; P:response to bacterium; IMP:TAIR.
InterPro; IPR001360; Glyco_hydro_1.
InterPro; IPR033132; Glyco_hydro_1_N_CS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR10353; PTHR10353; 1.
Pfam; PF00232; Glyco_hydro_1; 1.
PRINTS; PR00131; GLHYDRLASE1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
1: Evidence at protein level;
Complete proteome; Glycosidase; Hydrolase; Peroxisome; Plant defense;
Reference proteome.
CHAIN 1 560 Beta-glucosidase 26, peroxisomal.
/FTId=PRO_0000389588.
REGION 457 458 Substrate binding. {ECO:0000250}.
ACT_SITE 183 183 Proton donor. {ECO:0000250}.
ACT_SITE 398 398 Nucleophile. {ECO:0000250}.
BINDING 33 33 Substrate. {ECO:0000250}.
BINDING 137 137 Substrate. {ECO:0000250}.
BINDING 182 182 Substrate. {ECO:0000250}.
BINDING 326 326 Substrate. {ECO:0000250}.
BINDING 450 450 Substrate. {ECO:0000250}.
MUTAGEN 183 183 E->D: Susceptibility to the nonhost
powdery mildew species B.graminis and
E.pisi. Loss of myrosinase activity but
intact glucosidase activity.
{ECO:0000269|PubMed:16293760,
ECO:0000269|PubMed:19095900}.
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


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