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Salicylate/benzoate carboxyl methyltransferase (Benzoate O-methyltransferase) (EC 2.1.1.273) (S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase) (S-adenosyl-L-methionine:salicylate acid carboxyl methyltransferase) (SABATH methyltransferase) (Salicylate carboxymethyltransferase) (EC 2.1.1.274)

 BSMT1_ARATH             Reviewed;         379 AA.
Q6XMI3; Q9CAX9;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
27-SEP-2017, entry version 85.
RecName: Full=Salicylate/benzoate carboxyl methyltransferase;
AltName: Full=Benzoate O-methyltransferase;
EC=2.1.1.273;
AltName: Full=S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase;
AltName: Full=S-adenosyl-L-methionine:salicylate acid carboxyl methyltransferase;
AltName: Full=SABATH methyltransferase;
AltName: Full=Salicylate carboxymethyltransferase;
EC=2.1.1.274;
Name=BSMT1; OrderedLocusNames=At3g11480; ORFNames=F24K9.15;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION BY BIOTIC
AND ABIOTIC STRESSES, AND SUBUNIT.
STRAIN=cv. Columbia;
PubMed=14617060; DOI=10.1046/j.1365-313X.2003.01902.x;
Chen F., D'Auria J.C., Tholl D., Ross J.R., Gershenzon J., Noel J.P.,
Pichersky E.;
"An Arabidopsis thaliana gene for methylsalicylate biosynthesis,
identified by a biochemical genomics approach, has a role in
defense.";
Plant J. 36:577-588(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
INDUCTION BY JASMONIC ACID.
PubMed=17364223; DOI=10.1007/s11103-006-9123-x;
Koo Y.J., Kim M.A., Kim E.H., Song J.T., Jung C., Moon J.K., Kim J.H.,
Seo H.S., Song S.I., Kim J.K., Lee J.S., Cheong J.J., Choi Y.D.;
"Overexpression of salicylic acid carboxyl methyltransferase reduces
salicylic acid-mediated pathogen resistance in Arabidopsis thaliana.";
Plant Mol. Biol. 64:1-15(2007).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19669626; DOI=10.1007/s10059-009-0108-x;
Song J.T., Koo Y.J., Park J.B., Seo Y.J., Cho Y.J., Seo H.S.,
Choi Y.D.;
"The expression patterns of AtBSMT1 and AtSAGT1 encoding a salicylic
acid (SA) methyltransferase and a SA glucosyltransferase,
respectively, in Arabidopsis plants with altered defense responses.";
Mol. Cells 28:105-109(2009).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20407809; DOI=10.1007/s10886-010-9787-1;
Snoeren T.A., Mumm R., Poelman E.H., Yang Y., Pichersky E., Dicke M.;
"The herbivore-induced plant volatile methyl salicylate negatively
affects attraction of the parasitoid Diadegma semiclausum.";
J. Chem. Ecol. 36:479-489(2010).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19958141; DOI=10.1094/MPMI-23-1-0082;
Liu P.P., Yang Y., Pichersky E., Klessig D.F.;
"Altering expression of benzoic acid/salicylic acid carboxyl
methyltransferase 1 compromises systemic acquired resistance and PAMP-
triggered immunity in arabidopsis.";
Mol. Plant Microbe Interact. 23:82-90(2010).
-!- FUNCTION: Methyltransferase involved in the biosynthesis of
methylsalicylate in response to stresses. Utilizes salicylic acid
(SA) more efficiently than benzoic acid (BA). Can also use
anthranilic acid and m-hydroxybenzoic acid as substrate.
{ECO:0000269|PubMed:14617060, ECO:0000269|PubMed:19669626,
ECO:0000269|PubMed:19958141, ECO:0000269|PubMed:20407809}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + benzoate = S-
adenosyl-L-homocysteine + methyl benzoate.
{ECO:0000269|PubMed:14617060}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + salicylate = S-
adenosyl-L-homocysteine + methyl salicylate.
{ECO:0000269|PubMed:14617060}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9FLN8};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:Q9FLN8};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=67 uM for S-adenosyl-L-methionine
{ECO:0000269|PubMed:14617060};
KM=65 uM for benzoic acid {ECO:0000269|PubMed:14617060};
KM=16 uM for salicylic acid {ECO:0000269|PubMed:14617060};
Note=kcat is 0.19 sec(-1) for benzoic acid. kcat is 0.07 sec(-1)
for salicylic acid.;
pH dependence:
Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:14617060};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14617060}.
-!- TISSUE SPECIFICITY: Expressed in flowers and at lower levels in
leaves and stems. Hardly detected in roots and siliques. Expressed
in the sepals and the leaf trichomes and hydathodes.
{ECO:0000269|PubMed:14617060}.
-!- INDUCTION: Up-regulated by alamethicin, herbivory, uprooting,
woundingd, jasmonic acid and methyl jasmonate, but not by
salicylic acid. Induced specifically around the lesions.
{ECO:0000269|PubMed:14617060, ECO:0000269|PubMed:17364223}.
-!- DISRUPTION PHENOTYPE: Loss of accumulation of methyl salicylate
upon pathogen infection, no accumulation of salicylic acid or its
glucoside in uninoculated leaves and no development of systemic
acquired resistance. Increased attractivity to parasitoids.
{ECO:0000269|PubMed:19669626, ECO:0000269|PubMed:19958141,
ECO:0000269|PubMed:20407809}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
methyltransferase family. SABATH subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG51446.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AY224595; AAP57210.1; -; mRNA.
EMBL; AC008153; AAG51446.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002686; AEE75053.1; -; Genomic_DNA.
EMBL; BT022049; AAY25461.1; -; mRNA.
EMBL; AK221911; BAD94303.1; -; mRNA.
RefSeq; NP_187755.2; NM_111981.5.
UniGene; At.39742; -.
ProteinModelPortal; Q6XMI3; -.
STRING; 3702.AT3G11480.1; -.
PaxDb; Q6XMI3; -.
EnsemblPlants; AT3G11480.1; AT3G11480.1; AT3G11480.
GeneID; 820321; -.
Gramene; AT3G11480.1; AT3G11480.1; AT3G11480.
KEGG; ath:AT3G11480; -.
Araport; AT3G11480; -.
TAIR; locus:2080747; AT3G11480.
eggNOG; ENOG410IKGQ; Eukaryota.
eggNOG; ENOG4112BHH; LUCA.
HOGENOM; HOG000238197; -.
InParanoid; Q6XMI3; -.
KO; K21484; -.
OMA; ESITITH; -.
OrthoDB; EOG09360CFU; -.
PhylomeDB; Q6XMI3; -.
BioCyc; MetaCyc:AT3G11480-MONOMER; -.
BRENDA; 2.1.1.273; 399.
BRENDA; 2.1.1.274; 399.
PRO; PR:Q6XMI3; -.
Proteomes; UP000006548; Chromosome 3.
Genevisible; Q6XMI3; AT.
GO; GO:0052624; F:2-phytyl-1,4-naphthoquinone methyltransferase activity; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0080150; F:S-adenosyl-L-methionine:benzoic acid carboxyl methyl transferase activity; IDA:TAIR.
GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:TAIR.
GO; GO:0006952; P:defense response; IEP:TAIR.
GO; GO:0051707; P:response to other organism; IEP:TAIR.
GO; GO:0009611; P:response to wounding; IEP:TAIR.
InterPro; IPR005299; MeTrfase_7.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF03492; Methyltransf_7; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
Complete proteome; Magnesium; Metal-binding; Methyltransferase;
Plant defense; Reference proteome; S-adenosyl-L-methionine;
Transferase.
CHAIN 1 379 Salicylate/benzoate carboxyl
methyltransferase.
/FTId=PRO_0000422309.
REGION 43 47 Substrate binding.
{ECO:0000250|UniProtKB:A4GE69}.
REGION 81 82 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9FLN8}.
REGION 117 120 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:A4GE70}.
REGION 155 157 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9FLN8}.
REGION 172 174 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9FLN8}.
REGION 173 177 Substrate binding.
{ECO:0000250|UniProtKB:A4GE70}.
METAL 188 188 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q9FLN8}.
METAL 275 275 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q9FLN8}.
METAL 277 277 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q9FLN8}.
METAL 278 278 Magnesium.
{ECO:0000250|UniProtKB:Q9FLN8}.
BINDING 40 40 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:A4GE70}.
BINDING 40 40 Substrate.
{ECO:0000250|UniProtKB:A4GE70}.
BINDING 81 81 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:A4GE69}.
BINDING 87 87 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:A4GE70}.
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


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