BGL38_ARATH
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 03-AUG-2022, entry version 165.
DE RecName: Full=Myrosinase 1;
DE EC=3.2.1.147;
DE AltName: Full=Beta-glucosidase 38;
DE Short=AtBGLU38;
DE EC=3.2.1.21;
DE AltName: Full=Sinigrinase 1;
DE AltName: Full=Thioglucosidase 1;
DE Flags: Precursor;
GN Name=TGG1; Synonyms=BGLU38; OrderedLocusNames=At5g26000; ORFNames=T1N24.7;
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. Cvi-0,
RC cv. Db-1, cv. Ei-2, cv. HOG, cv. Ka-0, cv. Ler-1, cv. Lip-0, cv. Ll-0,
RC cv. Mh-0, cv. Mr-0, cv. Mrk-0, cv. Mt-0, cv. No-0, cv. Per-1, cv. Petergof,
RC cv. Pi-0, cv. Rsch-0, cv. Sei-0, cv. Su-0, cv. Ta-0, cv. Tac-0, cv. Tsu-1,
RC 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, 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 -!- 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 -!- 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 AlphaFoldDB; P37702; -.
DR SMR; P37702; -.
DR BioGRID; 17944; 7.
DR IntAct; P37702; 1.
DR STRING; 3702.AT5G26000.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR iPTMnet; P37702; -.
DR MetOSite; P37702; -.
DR SWISS-2DPAGE; P37702; -.
DR PaxDb; P37702; -.
DR PRIDE; P37702; -.
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; locus:2180597; AT5G26000.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; P37702; -.
DR OMA; DETKNSY; -.
DR PhylomeDB; P37702; -.
DR BioCyc; MetaCyc:AT5G26000-MON; -.
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 Genevisible; P37702; AT.
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 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; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Metal-binding; Plant defense;
KW 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="substrate"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 475..476
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..449
FT /evidence="ECO:0000250"
FT DISULFID 32..445
FT /evidence="ECO:0000250"
FT DISULFID 224..232
FT /evidence="ECO:0000250"
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. Ta-
FT 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
