BSMT1_ARATH
ID BSMT1_ARATH Reviewed; 379 AA.
AC Q6XMI3; Q9CAX9;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Salicylate/benzoate carboxyl methyltransferase;
DE AltName: Full=Benzoate O-methyltransferase;
DE EC=2.1.1.273;
DE AltName: Full=S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase;
DE AltName: Full=S-adenosyl-L-methionine:salicylate acid carboxyl methyltransferase;
DE AltName: Full=SABATH methyltransferase;
DE AltName: Full=Salicylate carboxymethyltransferase;
DE EC=2.1.1.274;
GN Name=BSMT1; OrderedLocusNames=At3g11480; ORFNames=F24K9.15;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION BY BIOTIC AND
RP ABIOTIC STRESSES, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=14617060; DOI=10.1046/j.1365-313x.2003.01902.x;
RA Chen F., D'Auria J.C., Tholl D., Ross J.R., Gershenzon J., Noel J.P.,
RA Pichersky E.;
RT "An Arabidopsis thaliana gene for methylsalicylate biosynthesis, identified
RT by a biochemical genomics approach, has a role in defense.";
RL Plant J. 36:577-588(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION BY JASMONIC ACID.
RX PubMed=17364223; DOI=10.1007/s11103-006-9123-x;
RA Koo Y.J., Kim M.A., Kim E.H., Song J.T., Jung C., Moon J.K., Kim J.H.,
RA Seo H.S., Song S.I., Kim J.K., Lee J.S., Cheong J.J., Choi Y.D.;
RT "Overexpression of salicylic acid carboxyl methyltransferase reduces
RT salicylic acid-mediated pathogen resistance in Arabidopsis thaliana.";
RL Plant Mol. Biol. 64:1-15(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19669626; DOI=10.1007/s10059-009-0108-x;
RA Song J.T., Koo Y.J., Park J.B., Seo Y.J., Cho Y.J., Seo H.S., Choi Y.D.;
RT "The expression patterns of AtBSMT1 and AtSAGT1 encoding a salicylic acid
RT (SA) methyltransferase and a SA glucosyltransferase, respectively, in
RT Arabidopsis plants with altered defense responses.";
RL Mol. Cells 28:105-109(2009).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20407809; DOI=10.1007/s10886-010-9787-1;
RA Snoeren T.A., Mumm R., Poelman E.H., Yang Y., Pichersky E., Dicke M.;
RT "The herbivore-induced plant volatile methyl salicylate negatively affects
RT attraction of the parasitoid Diadegma semiclausum.";
RL J. Chem. Ecol. 36:479-489(2010).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19958141; DOI=10.1094/mpmi-23-1-0082;
RA Liu P.P., Yang Y., Pichersky E., Klessig D.F.;
RT "Altering expression of benzoic acid/salicylic acid carboxyl
RT methyltransferase 1 compromises systemic acquired resistance and PAMP-
RT triggered immunity in arabidopsis.";
RL Mol. Plant Microbe Interact. 23:82-90(2010).
CC -!- FUNCTION: Methyltransferase involved in the biosynthesis of
CC methylsalicylate in response to stresses. Utilizes salicylic acid (SA)
CC more efficiently than benzoic acid (BA). Can also use anthranilic acid
CC and m-hydroxybenzoic acid as substrate. {ECO:0000269|PubMed:14617060,
CC ECO:0000269|PubMed:19669626, ECO:0000269|PubMed:19958141,
CC ECO:0000269|PubMed:20407809}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoate + S-adenosyl-L-methionine = methyl benzoate + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:36099, ChEBI:CHEBI:16150,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:72775;
CC EC=2.1.1.273; Evidence={ECO:0000269|PubMed:14617060};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + salicylate = methyl salicylate + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:36095, ChEBI:CHEBI:30762,
CC ChEBI:CHEBI:31832, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC EC=2.1.1.274; Evidence={ECO:0000269|PubMed:14617060};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9FLN8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=67 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:14617060};
CC KM=65 uM for benzoic acid {ECO:0000269|PubMed:14617060};
CC KM=16 uM for salicylic acid {ECO:0000269|PubMed:14617060};
CC Note=kcat is 0.19 sec(-1) for benzoic acid. kcat is 0.07 sec(-1) for
CC salicylic acid.;
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:14617060};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14617060}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and at lower levels in leaves
CC and stems. Hardly detected in roots and siliques. Expressed in the
CC sepals and the leaf trichomes and hydathodes.
CC {ECO:0000269|PubMed:14617060}.
CC -!- INDUCTION: Up-regulated by alamethicin, herbivory, uprooting,
CC woundingd, jasmonic acid and methyl jasmonate, but not by salicylic
CC acid. Induced specifically around the lesions.
CC {ECO:0000269|PubMed:14617060, ECO:0000269|PubMed:17364223}.
CC -!- DISRUPTION PHENOTYPE: Loss of accumulation of methyl salicylate upon
CC pathogen infection, no accumulation of salicylic acid or its glucoside
CC in uninoculated leaves and no development of systemic acquired
CC resistance. Increased attractivity to parasitoids.
CC {ECO:0000269|PubMed:19669626, ECO:0000269|PubMed:19958141,
CC ECO:0000269|PubMed:20407809}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. SABATH subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51446.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY224595; AAP57210.1; -; mRNA.
DR EMBL; AC008153; AAG51446.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75053.1; -; Genomic_DNA.
DR EMBL; BT022049; AAY25461.1; -; mRNA.
DR EMBL; AK221911; BAD94303.1; -; mRNA.
DR RefSeq; NP_187755.2; NM_111981.5.
DR AlphaFoldDB; Q6XMI3; -.
DR SMR; Q6XMI3; -.
DR STRING; 3702.AT3G11480.1; -.
DR PaxDb; Q6XMI3; -.
DR PRIDE; Q6XMI3; -.
DR ProteomicsDB; 240291; -.
DR EnsemblPlants; AT3G11480.1; AT3G11480.1; AT3G11480.
DR GeneID; 820321; -.
DR Gramene; AT3G11480.1; AT3G11480.1; AT3G11480.
DR KEGG; ath:AT3G11480; -.
DR Araport; AT3G11480; -.
DR TAIR; locus:2080747; AT3G11480.
DR eggNOG; ENOG502QQVK; Eukaryota.
DR HOGENOM; CLU_019628_2_1_1; -.
DR InParanoid; Q6XMI3; -.
DR OMA; FQKDFTM; -.
DR OrthoDB; 689338at2759; -.
DR PhylomeDB; Q6XMI3; -.
DR BioCyc; MetaCyc:AT3G11480-MON; -.
DR BRENDA; 2.1.1.273; 399.
DR BRENDA; 2.1.1.274; 399.
DR PRO; PR:Q6XMI3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q6XMI3; baseline and differential.
DR Genevisible; Q6XMI3; AT.
DR GO; GO:0052624; F:2-phytyl-1,4-naphthoquinone methyltransferase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0080150; F:S-adenosyl-L-methionine:benzoic acid carboxyl methyl transferase activity; IDA:TAIR.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEP:TAIR.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR GO; GO:0051707; P:response to other organism; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 1.10.1200.270; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR005299; MeTrfase_7.
DR InterPro; IPR042086; MeTrfase_capping.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31009; PTHR31009; 1.
DR Pfam; PF03492; Methyltransf_7; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Methyltransferase; Plant defense;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..379
FT /note="Salicylate/benzoate carboxyl methyltransferase"
FT /id="PRO_0000422309"
FT BINDING 40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 43..47
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 81..82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 117..120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 155..157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 172..174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 173..177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
SQ SEQUENCE 379 AA; 43365 MW; 09C96CCB184D25F9 CRC64;
MDPRFINTIP SLRYDDDKCD DEYAFVKALC MSGGDGANSY SANSRLQKKV LSMAKPVLVR
NTEEMMMNLD FPTYIKVAEL GCSSGQNSFL AIFEIINTIN VLCQHVNKNS PEIDCCLNDL
PENDFNTTFK FVPFFNKELM ITNKSSCFVY GAPGSFYSRL FSRNSLHLIH SSYALHWLSK
VPEKLENNKG NLYITSSSPQ SAYKAYLNQF QKDFTMFLRL RSEEIVSNGR MVLTFIGRNT
LNDPLYRDCC HFWTLLSNSL RDLVFEGLVS ESKLDAFNMP FYDPNVQELK EVIQKEGSFE
INELESHGFD LGHYYEEDDF EAGRNEANGI RAVSEPMLIA HFGEEIIDTL FDKYAYHVTQ
HANCRNKTTV SLVVSLTKK
