BGL37_ARATH
ID BGL37_ARATH Reviewed; 547 AA.
AC Q9C5C2; Q0WWL9; Q3E943; Q42595; Q56WQ3; Q56ZB8; Q8H7E3; Q9ASV0;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Myrosinase 2;
DE EC=3.2.1.147;
DE AltName: Full=Beta-glucosidase 37;
DE Short=AtBGLU37;
DE AltName: Full=Sinigrinase 2;
DE AltName: Full=Thioglucosidase 2;
DE Flags: Precursor;
GN Name=TGG2; Synonyms=BGLU37; OrderedLocusNames=At5g25980; ORFNames=T1N24.18;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-208.
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 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 [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [9]
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 [10]
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).
RN [11]
RP INTERACTION WITH MVP1.
RX PubMed=19880612; DOI=10.1104/pp.109.145078;
RA Agee A.E., Surpin M., Sohn E.J., Girke T., Rosado A., Kram B.W., Carter C.,
RA Wentzell A.M., Kliebenstein D.J., Jin H.C., Park O.K., Jin H., Hicks G.R.,
RA Raikhel N.V.;
RT "MODIFIED VACUOLE PHENOTYPE1 is an Arabidopsis myrosinase-associated
RT protein involved in endomembrane protein trafficking.";
RL Plant Physiol. 152:120-132(2010).
CC -!- FUNCTION: May degrade 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 TGG1. {ECO:0000269|PubMed:16640593,
CC ECO:0000269|PubMed:19433491}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a thioglucoside + H2O = a sugar + a thiol.; EC=3.2.1.147;
CC -!- SUBUNIT: Interacts with MVP1. {ECO:0000269|PubMed:19880612}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C5C2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C5C2-2; Sequence=VSP_038466;
CC -!- TISSUE SPECIFICITY: Expressed in phloem-associated cells.
CC {ECO:0000269|PubMed:16640593}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAD40134.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK32833.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN60275.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD94532.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA55787.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X79195; CAA55787.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF149413; AAD40134.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED93507.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93508.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93509.1; -; Genomic_DNA.
DR EMBL; AF360348; AAK28645.1; -; mRNA.
DR EMBL; AF361821; AAK32833.1; ALT_INIT; mRNA.
DR EMBL; AY078042; AAL77743.1; -; mRNA.
DR EMBL; AY113880; AAM44928.1; -; mRNA.
DR EMBL; AK221048; BAD94810.1; -; mRNA.
DR EMBL; AK221982; BAD94532.1; ALT_INIT; mRNA.
DR EMBL; AK226328; BAE98479.1; -; mRNA.
DR EMBL; AF083717; AAN60275.1; ALT_SEQ; mRNA.
DR PIR; S56654; S56654.
DR RefSeq; NP_001031940.1; NM_001036863.1. [Q9C5C2-2]
DR RefSeq; NP_568479.1; NM_122499.4. [Q9C5C2-1]
DR RefSeq; NP_851076.2; NM_180745.2. [Q9C5C2-2]
DR AlphaFoldDB; Q9C5C2; -.
DR SMR; Q9C5C2; -.
DR BioGRID; 17942; 8.
DR STRING; 3702.AT5G25980.2; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR MetOSite; Q9C5C2; -.
DR PaxDb; Q9C5C2; -.
DR PRIDE; Q9C5C2; -.
DR ProteomicsDB; 240621; -. [Q9C5C2-1]
DR EnsemblPlants; AT5G25980.1; AT5G25980.1; AT5G25980. [Q9C5C2-2]
DR EnsemblPlants; AT5G25980.2; AT5G25980.2; AT5G25980. [Q9C5C2-1]
DR EnsemblPlants; AT5G25980.3; AT5G25980.3; AT5G25980. [Q9C5C2-2]
DR GeneID; 832667; -.
DR Gramene; AT5G25980.1; AT5G25980.1; AT5G25980. [Q9C5C2-2]
DR Gramene; AT5G25980.2; AT5G25980.2; AT5G25980. [Q9C5C2-1]
DR Gramene; AT5G25980.3; AT5G25980.3; AT5G25980. [Q9C5C2-2]
DR KEGG; ath:AT5G25980; -.
DR Araport; AT5G25980; -.
DR TAIR; locus:2180567; AT5G25980.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9C5C2; -.
DR OMA; FGMASVT; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9C5C2; -.
DR BioCyc; MetaCyc:AT5G25980-MON; -.
DR BRENDA; 3.2.1.147; 399.
DR PRO; PR:Q9C5C2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5C2; baseline and differential.
DR Genevisible; Q9C5C2; 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:0009506; C:plasmodesma; HDA:TAIR.
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; IMP: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 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; Plant defense; Reference proteome;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..547
FT /note="Myrosinase 2"
FT /id="PRO_0000389599"
FT ACT_SITE 430
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 486..487
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..460
FT /evidence="ECO:0000250"
FT DISULFID 44..456
FT /evidence="ECO:0000250"
FT DISULFID 236..244
FT /evidence="ECO:0000250"
FT VAR_SEQ 468..547
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038466"
FT CONFLICT 100
FT /note="D -> N (in Ref. 6; AAN60275)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="E -> K (in Ref. 6; AAN60275)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="I -> N (in Ref. 4; AAL77743/AAK32833)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="L -> P (in Ref. 5; BAE98479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 62732 MW; 3902D25F45B9DFAA CRC64;
MQHNTYIYIL TMKLLGFALA ILLVVATCKP EEEITCEENV PFTCSQTDRF NKQDFESDFI
FGVASSAYQI EGGRGRGLNV WDGFTHRYPE KGGADLGNGD TTCDSYRTWQ KDLDVMEELG
VKGYRFSFAW SRILPKGKRS RGINEDGINY YSGLIDGLIA RNITPFVTLF HWDLPQSLQD
EYEGFLDRTI IDDFKDYADL CFERFGDRVK HWITINQLFT VPTRGYALGT DAPGRCSQWV
DKRCYGGDSS TEPYIVAHNQ LLAHATVVDL YRTRYKYQGG KIGPVMITRW FLPYDDTLES
KQATWRAKEF FLGWFMEPLT KGKYPYIMRK LVGNRLPKFN STEARLLKGS YDFLGLNYYV
TQYAHALDPS PPEKLTAMTD SLANLTSLDA NGQPPGPPFS KGSYYHPRGM LNVMEHFKTK
YGDPLIYVTE NGFSTSGGPI PFTEAFHDYN RIDYLCSHLC FLRKAIKEKR VNVKGYFVWS
LGDNYEFCNG YTVRFGLSYV DFNNVTADRD LKASGLWYQS FLRDTTKNQD ILRSSLPFKN
GDRKSLT
