ID BGL38_ARATH Reviewed; 541 AA. AC P37702; B9DHN6; Q3E942; Q3V5A7; Q3V5A8; Q3V5A9; Q3V5B1; Q3V5B2; Q3V5B3; AC Q3V5B4; Q3V5B5; Q3V5B6; Q3V5B7; Q3V5B8; Q3V5B9; Q3V5C0; Q3V5C2; Q3V5C3; AC Q3V5C4; Q3V5C5; Q3V5C8; Q3V5D1; Q3V5D2; Q8H7H2; Q93Z31; Q940N8; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 27-MAR-2024, entry version 174. DE RecName: Full=Myrosinase 1 {ECO:0000303|PubMed:19703694}; DE EC=3.2.1.147 {ECO:0000269|PubMed:19703694}; DE AltName: Full=Beta-glucosidase 38 {ECO:0000303|PubMed:15604686}; DE Short=AtBGLU38 {ECO:0000303|PubMed:15604686}; DE EC=3.2.1.21 {ECO:0000269|PubMed:19703694}; DE AltName: Full=Sinigrinase 1 {ECO:0000303|PubMed:19703694}; DE AltName: Full=Thioglucosidase 1 {ECO:0000303|PubMed:19703694}; DE Flags: Precursor; GN Name=TGG1 {ECO:0000303|PubMed:19703694}; GN Synonyms=BGLU38 {ECO:0000303|PubMed:15604686}; GN OrderedLocusNames=At5g26000 {ECO:0000312|Araport:AT5G26000}; GN ORFNames=T1N24.7 {ECO:0000312|EMBL:AAD40143.1}; 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 [MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX PubMed=8029343; DOI=10.1104/pp.103.2.671; RA Chadchawan S., Bishop J., Thangstad O.P., Bones A.M., Mitchell-Olds T., RA Bradley D.; RT "Arabidopsis cDNA sequence encoding myrosinase."; RL Plant Physiol. 103:671-671(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Columbia; TISSUE=Leaf; RX PubMed=7766881; DOI=10.1007/bf00037019; RA Xue J., Joergensen M., Pihlgren U., Rask L.; RT "The myrosinase gene family in Arabidopsis thaliana: gene organization, RT expression and evolution."; RL Plant Mol. Biol. 27:911-922(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130714; DOI=10.1038/35048507; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., RA Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."; RL Nature 408:823-826(2000). RN [4] 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-226. RA Stracke R., Palme K.; RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves RT and guard cells."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-497; 43-510; 43-511; 43-512; RP 43-513; 43-514; 44-511; 44-512; 44-514; 44-522; 45-511 AND 47-512, RP FUNCTION, AND VARIANTS ASN-128; LYS-261; GLN-264; ALA-427; GLY-459 AND RP ILE-489. RC STRAIN=cv. Abd-0, cv. Ag-0, cv. Ba-1, cv. Cal-0, cv. Columbia, cv. RC Cvi-0, cv. Db-1, cv. Ei-2, cv. HOG, cv. Ka-0, cv. Ler-1, cv. Lip-0, RC cv. Ll-0, cv. Mh-0, cv. Mr-0, cv. Mrk-0, cv. Mt-0, cv. No-0, cv. RC Per-1, cv. Petergof, cv. Pi-0, cv. Rsch-0, cv. Sei-0, cv. Su-0, cv. RC Ta-0, cv. Tac-0, cv. Tsu-1, and cv. Wl-0; RX PubMed=15643972; DOI=10.1111/j.1365-294x.2004.02403.x; RA Stranger B.E., Mitchell-Olds T.; RT "Nucleotide variation at the myrosinase-encoding locus, TGG1, and RT quantitative myrosinase enzyme activity variation in Arabidopsis RT thaliana."; RL Mol. Ecol. 14:295-309(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-541. RC STRAIN=cv. Columbia; RX PubMed=19423640; DOI=10.1093/dnares/dsp009; RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., RA Shinozaki K.; RT "Analysis of multiple occurrences of alternative splicing events in RT Arabidopsis thaliana using novel sequenced full-length cDNAs."; RL DNA Res. 16:155-164(2009). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-250. RC STRAIN=cv. C24; TISSUE=Flower bud; RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x; RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D., RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M., RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C., RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.; RT "An inventory of 1152 expressed sequence tags obtained by partial RT sequencing of cDNAs from Arabidopsis thaliana."; RL Plant J. 4:1051-1061(1993). RN [10] RP TISSUE SPECIFICITY. RX PubMed=15316292; DOI=10.1023/b:plan.0000038272.99590.10; RA Thangstad O.P., Gilde B., Chadchawan S., Seem M., Husebye H., Bradley D., RA Bones A.M.; RT "Cell specific, cross-species expression of myrosinases in Brassica napus, RT Arabidopsis thaliana and Nicotiana tabacum."; RL Plant Mol. Biol. 54:597-611(2004). RN [11] 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 [12] RP FUNCTION. RX PubMed=16640593; DOI=10.1111/j.1365-313x.2006.02716.x; RA Barth C., Jander G.; RT "Arabidopsis myrosinases TGG1 and TGG2 have redundant function in RT glucosinolate breakdown and insect defense."; RL Plant J. 46:549-562(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17951448; DOI=10.1105/tpc.107.050989; RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E., RA Rasche N., Lueder F., Weckwerth W., Jahn O.; RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting RT peptides, metabolic pathways, and defense mechanisms."; RL Plant Cell 19:3170-3193(2007). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=19703694; DOI=10.1016/j.phytochem.2009.07.036; RA Andersson D., Chakrabarty R., Bejai S., Zhang J., Rask L., Meijer J.; RT "Myrosinases from root and leaves of Arabidopsis thaliana have different RT catalytic properties."; RL Phytochemistry 70:1345-1354(2009). RN [15] RP FUNCTION. RX PubMed=19433491; DOI=10.1093/pcp/pcp066; RA Islam M.M., Tani C., Watanabe-Sugimoto M., Uraji M., Jahan M.S., Masuda C., RA Nakamura Y., Mori I.C., Murata Y.; RT "Myrosinases, TGG1 and TGG2, redundantly function in ABA and MeJA signaling RT in Arabidopsis guard cells."; RL Plant Cell Physiol. 50:1171-1175(2009). CC -!- FUNCTION: Degradation of glucosinolates (glucose residue linked by a CC thioglucoside bound to an amino acid derivative) to glucose, sulfate CC and any of the products: thiocyanates, isothiocyanates, nitriles, CC epithionitriles or oxazolidine-2-thiones. These toxic degradation CC products can deter insect herbivores. Seems to function in abscisic CC acid (ABA) and methyl jasmonate (MeJA) signaling in guard cells. CC Functionally redundant with TGG2. Hydrolyzes sinigrin and, with lower CC efficiency, p-nitrophenyl beta-D-glucoside. CC {ECO:0000269|PubMed:15643972, ECO:0000269|PubMed:16640593, CC ECO:0000269|PubMed:19433491, ECO:0000269|PubMed:19703694}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a thioglucoside + H2O = a sugar + a thiol.; EC=3.2.1.147; CC Evidence={ECO:0000269|PubMed:19703694}; 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:19703694}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=45 uM for sinigrin (at pH 4.5) {ECO:0000269|PubMed:19703694}; CC KM=34 mM for p-nitrophenyl beta-D-glucoside (at pH 4.5) CC {ECO:0000269|PubMed:19703694}; CC Vmax=2.3 umol/min/mg enzyme with sinigrin as substrate (at pH 4.5) CC {ECO:0000269|PubMed:19703694}; CC Vmax=1.2 umol/min/mg enzyme with p-nitrophenyl beta-D-glucoside as CC substrate (at pH 4.5) {ECO:0000269|PubMed:19703694}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P37702-1; Sequence=Displayed; CC Name=2; CC IsoId=P37702-2; Sequence=VSP_038446; CC -!- TISSUE SPECIFICITY: Expressed in guard cells, phloem-associated cells CC and myrosin cells. {ECO:0000269|PubMed:15316292}. CC -!- MISCELLANEOUS: It seems that the absence of a catalytic proton donor in CC plant myrosinases is not impairing the hydrolysis of glucosinolates. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L11454; AAC18869.1; -; mRNA. DR EMBL; X79194; CAA55786.1; -; Genomic_DNA. DR EMBL; AF149413; AAD40143.1; -; Genomic_DNA. DR EMBL; CP002688; AED93511.1; -; Genomic_DNA. DR EMBL; CP002688; AED93512.1; -; Genomic_DNA. DR EMBL; AY045681; AAK74039.1; -; mRNA. DR EMBL; AY054237; AAL06896.1; -; mRNA. DR EMBL; AY058182; AAL25596.1; -; mRNA. DR EMBL; AY090382; AAL91284.1; -; mRNA. DR EMBL; AF083677; AAN60236.1; -; mRNA. DR EMBL; AJ831440; CAH40799.1; -; Genomic_DNA. DR EMBL; AJ831441; CAH40800.1; -; Genomic_DNA. DR EMBL; AJ831442; CAH40801.1; -; Genomic_DNA. DR EMBL; AJ831443; CAH40802.1; -; Genomic_DNA. DR EMBL; AJ831444; CAH40803.1; -; Genomic_DNA. DR EMBL; AJ831445; CAH40804.1; -; Genomic_DNA. DR EMBL; AJ831446; CAH40805.1; -; Genomic_DNA. DR EMBL; AJ831447; CAH40806.1; -; Genomic_DNA. DR EMBL; AJ831448; CAH40807.1; -; Genomic_DNA. DR EMBL; AJ831449; CAH40808.1; -; Genomic_DNA. DR EMBL; AJ831450; CAH40809.1; -; Genomic_DNA. DR EMBL; AJ831451; CAH40810.1; -; Genomic_DNA. DR EMBL; AJ831452; CAH40811.1; -; Genomic_DNA. DR EMBL; AJ831453; CAH40812.1; -; Genomic_DNA. DR EMBL; AJ831454; CAH40813.1; -; Genomic_DNA. DR EMBL; AJ831455; CAH40814.1; -; Genomic_DNA. DR EMBL; AJ831456; CAH40815.1; -; Genomic_DNA. DR EMBL; AJ831457; CAH40816.1; -; Genomic_DNA. DR EMBL; AJ831458; CAH40817.1; -; Genomic_DNA. DR EMBL; AJ831459; CAH40818.1; -; Genomic_DNA. DR EMBL; AJ831460; CAH40819.1; -; Genomic_DNA. DR EMBL; AJ831461; CAH40820.1; -; Genomic_DNA. DR EMBL; AJ831462; CAH40821.1; -; Genomic_DNA. DR EMBL; AJ831463; CAH40822.1; -; Genomic_DNA. DR EMBL; AJ831464; CAH40823.1; -; Genomic_DNA. DR EMBL; AJ831465; CAH40824.1; -; Genomic_DNA. DR EMBL; AJ831466; CAH40825.1; -; Genomic_DNA. DR EMBL; AJ831467; CAH40826.1; -; Genomic_DNA. DR EMBL; AK317589; BAH20253.1; -; mRNA. DR EMBL; Z18232; CAA79143.1; -; mRNA. DR PIR; S56653; S56653. DR RefSeq; NP_197972.2; NM_122501.3. [P37702-2] DR RefSeq; NP_851077.1; NM_180746.3. [P37702-1] DR PDB; 7Z1I; X-ray; 3.09 A; A/B/C/D=19-541. DR PDBsum; 7Z1I; -. DR AlphaFoldDB; P37702; -. DR SMR; P37702; -. DR BioGRID; 17944; 7. DR IntAct; P37702; 1. DR STRING; 3702.P37702; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR GlyCosmos; P37702; 8 sites, No reported glycans. DR iPTMnet; P37702; -. DR MetOSite; P37702; -. DR PaxDb; 3702-AT5G26000-1; -. DR ProteomicsDB; 240394; -. [P37702-1] DR EnsemblPlants; AT5G26000.1; AT5G26000.1; AT5G26000. [P37702-1] DR EnsemblPlants; AT5G26000.2; AT5G26000.2; AT5G26000. [P37702-2] DR GeneID; 832669; -. DR Gramene; AT5G26000.1; AT5G26000.1; AT5G26000. [P37702-1] DR Gramene; AT5G26000.2; AT5G26000.2; AT5G26000. [P37702-2] DR KEGG; ath:AT5G26000; -. DR Araport; AT5G26000; -. DR TAIR; AT5G26000; TGG1. DR eggNOG; KOG0626; Eukaryota. DR HOGENOM; CLU_001859_1_0_1; -. DR InParanoid; P37702; -. DR OMA; MRFLVED; -. DR OrthoDB; 648908at2759; -. DR PhylomeDB; P37702; -. DR BioCyc; MetaCyc:AT5G26000-MONOMER; -. DR BRENDA; 3.2.1.147; 399. DR SABIO-RK; P37702; -. DR PRO; PR:P37702; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; P37702; baseline and differential. DR GO; GO:0048046; C:apoplast; HDA:TAIR. DR GO; GO:0009507; C:chloroplast; HDA:TAIR. DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR. DR GO; GO:0005777; C:peroxisome; HDA:TAIR. DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR. DR GO; GO:0009536; C:plastid; HDA:TAIR. DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR. DR GO; GO:0009579; C:thylakoid; HDA:TAIR. DR GO; GO:0008422; F:beta-glucosidase activity; IDA:TAIR. DR GO; GO:0102799; F:glucosinolate glucohydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0019137; F:thioglucosidase activity; IDA:TAIR. DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0002213; P:defense response to insect; IMP:UniProtKB. DR GO; GO:0019762; P:glucosinolate catabolic process; IMP:TAIR. DR GO; GO:0010119; P:regulation of stomatal movement; IMP:UniProtKB. DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB. DR GO; GO:0009625; P:response to insect; IEP:TAIR. DR Gene3D; 3.20.20.80; Glycosidases; 1. 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; GLYCOSYL HYDROLASE; 1. DR PANTHER; PTHR10353:SF218; MYROSINASE 1-RELATED; 1. DR Pfam; PF00232; Glyco_hydro_1; 1. DR PRINTS; PR00131; GLHYDRLASE1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1. DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1. DR SWISS-2DPAGE; P37702; -. DR Genevisible; P37702; AT. PE 1: Evidence at protein level; KW 3D-structure; Abscisic acid signaling pathway; Alternative splicing; KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Metal-binding; KW Plant defense; Reference proteome; Signal; Vacuole; Zinc. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..541 FT /note="Myrosinase 1" FT /id="PRO_0000011773" FT ACT_SITE 420 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055" FT BINDING 57 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 159 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 204..205 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q8GU20" FT BINDING 348 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 420 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q9SPP9" FT BINDING 468 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT BINDING 475..476 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q8L7J2" FT BINDING 484 FT /ligand="a beta-D-glucoside" FT /ligand_id="ChEBI:CHEBI:22798" FT /evidence="ECO:0000250|UniProtKB:Q1XH05" FT CARBOHYD 33 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 108 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 175 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 236 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 356 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 379 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 493 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 512 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT DISULFID 24..449 FT /evidence="ECO:0000250" FT DISULFID 32..445 FT /evidence="ECO:0000250" FT DISULFID 224..232 FT /evidence="ECO:0000250|UniProtKB:Q7XSK0" FT VAR_SEQ 457..541 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_038446" FT VARIANT 128 FT /note="S -> N (in strain: cv. Ta-0)" FT /evidence="ECO:0000269|PubMed:15643972" FT VARIANT 261 FT /note="T -> K (in strain: cv. Ba-1)" FT /evidence="ECO:0000269|PubMed:15643972" FT VARIANT 264 FT /note="K -> Q (in strain: cv. Ba-1)" FT /evidence="ECO:0000269|PubMed:15643972" FT VARIANT 427 FT /note="G -> A (in strain: cv. Ag-0, cv. Ba-1, cv. Mh-0, cv. FT Mr-0 and Tac-0)" FT /evidence="ECO:0000269|PubMed:15643972" FT VARIANT 459 FT /note="N -> G (in strain: cv. Su-0)" FT /evidence="ECO:0000269|PubMed:15643972" FT VARIANT 489 FT /note="V -> I (in strain: cv. No-0, cv. Rsch-0 and cv. FT Ta-0)" FT /evidence="ECO:0000269|PubMed:15643972" FT CONFLICT 385 FT /note="P -> H (in Ref. 5; AAL06896)" FT /evidence="ECO:0000305" FT CONFLICT 426 FT /note="P -> A (in Ref. 5; AAL25596)" FT /evidence="ECO:0000305" FT CONFLICT 434 FT /note="A -> T (in Ref. 8; BAH20253)" FT /evidence="ECO:0000305" FT CONFLICT 441 FT /note="I -> N (in Ref. 8; BAH20253)" FT /evidence="ECO:0000305" SQ SEQUENCE 541 AA; 61133 MW; 3736B735DE7A5BD1 CRC64; MKLLMLAFVF LLALATCKGD EFVCEENEPF TCNQTKLFNS GNFEKGFIFG VASSAYQVEG GRGRGLNVWD SFTHRFPEKG GADLGNGDTT CDSYTLWQKD IDVMDELNST GYRFSIAWSR LLPKGKRSRG VNPGAIKYYN GLIDGLVAKN MTPFVTLFHW DLPQTLQDEY NGFLNKTIVD DFKDYADLCF ELFGDRVKNW ITINQLYTVP TRGYALGTDA PGRCSPKIDV RCPGGNSSTE PYIVAHNQLL AHAAAVDVYR TKYKDDQKGM IGPVMITRWF LPFDHSQESK DATERAKIFF HGWFMGPLTE GKYPDIMREY VGDRLPEFSE TEAALVKGSY DFLGLNYYVT QYAQNNQTIV PSDVHTALMD SRTTLTSKNA TGHAPGPPFN AASYYYPKGI YYVMDYFKTT YGDPLIYVTE NGFSTPGDED FEKATADYKR IDYLCSHLCF LSKVIKEKNV NVKGYFAWSL GDNYEFCNGF TVRFGLSYVD FANITGDRDL KASGKWFQKF INVTDEDSTN QDLLRSSVSS KNRDRKSLAD A //