BGL39_ARATH
ID BGL39_ARATH Reviewed; 439 AA.
AC Q3E8E5;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Putative myrosinase 3;
DE EC=3.2.1.147;
DE AltName: Full=Beta-glucosidase 39;
DE Short=AtBGLU39;
DE AltName: Full=Sinigrinase 3;
DE AltName: Full=Thioglucosidase 3;
DE Flags: Precursor;
GN Name=TGG3; Synonyms=BGLU39; OrderedLocusNames=At5g48375; ORFNames=K23F3;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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 TISSUE SPECIFICITY.
RX PubMed=12010464; DOI=10.1034/j.1399-3054.2002.1150103.x;
RA Zhang J., Pontoppidan B., Xue J., Rask L., Meijer J.;
RT "The third myrosinase gene TGG3 in Arabidopsis thaliana is a pseudogene
RT specifically expressed in stamen and petal.";
RL Physiol. Plantarum 115:25-34(2002).
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a thioglucoside + H2O = a sugar + a thiol.; EC=3.2.1.147;
CC -!- TISSUE SPECIFICITY: Expressed specifically in stamens and petals.
CC {ECO:0000269|PubMed:12010464}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AP000372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED95661.1; -; Genomic_DNA.
DR RefSeq; NP_680406.1; NM_148101.1.
DR AlphaFoldDB; Q3E8E5; -.
DR SMR; Q3E8E5; -.
DR BioGRID; 20137; 1.
DR STRING; 3702.AT5G48375.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q3E8E5; -.
DR PRIDE; Q3E8E5; -.
DR ProteomicsDB; 240688; -.
DR EnsemblPlants; AT5G48375.1; AT5G48375.1; AT5G48375.
DR GeneID; 834891; -.
DR Gramene; AT5G48375.1; AT5G48375.1; AT5G48375.
DR KEGG; ath:AT5G48375; -.
DR Araport; AT5G48375; -.
DR TAIR; locus:504954978; AT5G48375.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q3E8E5; -.
DR OMA; VVMITRW; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q3E8E5; -.
DR BioCyc; ARA:AT5G48375-MON; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q3E8E5; baseline and differential.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0102799; F:glucosinolate glucohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0019137; F:thioglucosidase activity; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 2.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 5: Uncertain;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..439
FT /note="Putative myrosinase 3"
FT /id="PRO_0000390312"
FT ACT_SITE 386
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 411..412
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 439 AA; 50758 MW; 89D2ADBD5024184E CRC64;
MKFRALGLVL LLAVETCKAE EITCEETKPF TCNQTDRFNR KHFDDDFIFE GGKGRGLNVW
DGFTHRYPEK GGPDLGNGDS TCGSYEHWQK DIDVMTELGV DGYRFSLAWS RIAPRESNQA
GVKYYNDLID GLLAKNITPF VTLFHWDLPQ VLQDEYEGFL NHEIIDDFKD YANLCFKIFG
DRVKKWITIN QLYTVPTRGY AMGTDAPEPY IVAHNQLLAH AKVVHLYRKK YKPKQRGQIG
VVMITRWFVP YDSTQANIDA TERNKEFFLG WFMEPLTKGK YPDIMRKLVG RRLPKFNKKE
AKLVKGSYDF LGINYYQTQY VYAIPANPPN RLTVLNDSLS AFSYENKDGP IGPWFNADSY
YHPRGILNVL EHFKTKYGNP LVYITENGEL LILSGCNVKG YFAWCLGDNY ELWPSRSFHV
SPFYLLHRKD KGAFPSFEA
