MES9_ARATH
ID MES9_ARATH Reviewed; 256 AA.
AC O23171;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Methylesterase 9 {ECO:0000303|PubMed:18467465};
DE Short=AtMES9 {ECO:0000303|PubMed:18467465};
DE EC=3.1.1.- {ECO:0000269|PubMed:18467465};
GN Name=MES9 {ECO:0000303|PubMed:18467465};
GN OrderedLocusNames=At4g37150 {ECO:0000312|Araport:AT4G37150};
GN ORFNames=AP22.78 {ECO:0000312|EMBL:CAB80381.1},
GN C7A10.210 {ECO:0000312|EMBL:CAB16760.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION
RP BY PATHOGEN.
RX PubMed=18643994; DOI=10.1111/j.1365-313x.2008.03618.x;
RA Vlot A.C., Liu P.P., Cameron R.K., Park S.W., Yang Y., Kumar D., Zhou F.,
RA Padukkavidana T., Gustafsson C., Pichersky E., Klessig D.F.;
RT "Identification of likely orthologs of tobacco salicylic acid-binding
RT protein 2 and their role in systemic acquired resistance in Arabidopsis
RT thaliana.";
RL Plant J. 56:445-456(2008).
RN [8]
RP GENE FAMILY, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=18467465; DOI=10.1104/pp.108.118224;
RA Yang Y., Xu R., Ma C.J., Vlot A.C., Klessig D.F., Pichersky E.;
RT "Inactive methyl indole-3-acetic acid ester can be hydrolyzed and activated
RT by several esterases belonging to the AtMES esterase family of
RT Arabidopsis.";
RL Plant Physiol. 147:1034-1045(2008).
CC -!- FUNCTION: Methylesterase shown to have carboxylesterase activity,
CC methyl indole-3-acetic acid (MeIAA) esterase activity, methyl
CC salicylate (MeSA) esterase activity and methyl jasmonate (MeJA)
CC esterase activity in vitro. Required to convert methyl salicylate
CC (MeSA) to salicylic acid (SA) as part of the signal transduction
CC pathways that activate systemic acquired resistance in systemic tissue.
CC MeSA is believed to be an inactive form that needs to be demethylated
CC to exert a biological effect. {ECO:0000269|PubMed:18467465,
CC ECO:0000269|PubMed:18643994}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methyl (indol-3-yl)acetate = (indol-3-yl)acetate + H(+)
CC + methanol; Xref=Rhea:RHEA:32919, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:30854,
CC ChEBI:CHEBI:72782; Evidence={ECO:0000269|PubMed:18467465};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32920;
CC Evidence={ECO:0000269|PubMed:18467465};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methyl (-)-jasmonate = H(+) + jasmonate + methanol;
CC Xref=Rhea:RHEA:55372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15929, ChEBI:CHEBI:17790, ChEBI:CHEBI:58431;
CC Evidence={ECO:0000269|PubMed:18467465};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55373;
CC Evidence={ECO:0000269|PubMed:18467465};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methyl salicylate = H(+) + methanol + salicylate;
CC Xref=Rhea:RHEA:33611, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17790, ChEBI:CHEBI:30762, ChEBI:CHEBI:31832;
CC Evidence={ECO:0000269|PubMed:18467465};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33612;
CC Evidence={ECO:0000269|PubMed:18467465};
CC -!- ACTIVITY REGULATION: Esterase activity is down-regulated by salicylic
CC acid (SA). {ECO:0000269|PubMed:18643994}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=147.1 uM for methyl salicylate (MeSA)
CC {ECO:0000269|PubMed:18643994};
CC Vmax=25.88 nmol/min/ug enzyme with methyl salicylate (MeSA) as
CC substrate {ECO:0000269|PubMed:18643994};
CC -!- PATHWAY: Plant hormone biosynthesis. {ECO:0000269|PubMed:18467465}.
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC {ECO:0000269|PubMed:18467465}.
CC -!- INTERACTION:
CC O23171; Q9LFT6: HNL; NbExp=3; IntAct=EBI-4446268, EBI-4453194;
CC -!- INDUCTION: By pathogen infection. {ECO:0000269|PubMed:18643994}.
CC -!- MISCELLANEOUS: Expression of MES9 can restore systemic acquired
CC resistance in SAR-deficient tobacco plants.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase
CC family. {ECO:0000305}.
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DR EMBL; Z99707; CAB16760.1; -; Genomic_DNA.
DR EMBL; AL161590; CAB80381.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86759.1; -; Genomic_DNA.
DR EMBL; AK117107; BAC41786.1; -; mRNA.
DR EMBL; BT006227; AAP12876.1; -; mRNA.
DR EMBL; AB493724; BAH30562.1; -; mRNA.
DR PIR; H85438; H85438.
DR RefSeq; NP_195432.1; NM_119878.5.
DR AlphaFoldDB; O23171; -.
DR SMR; O23171; -.
DR BioGRID; 15150; 4.
DR IntAct; O23171; 3.
DR STRING; 3702.AT4G37150.1; -.
DR ESTHER; arath-AT4G37150; Hydroxynitrile_lyase.
DR PaxDb; O23171; -.
DR PRIDE; O23171; -.
DR ProteomicsDB; 232251; -.
DR EnsemblPlants; AT4G37150.1; AT4G37150.1; AT4G37150.
DR GeneID; 829869; -.
DR Gramene; AT4G37150.1; AT4G37150.1; AT4G37150.
DR KEGG; ath:AT4G37150; -.
DR Araport; AT4G37150; -.
DR TAIR; locus:2114985; AT4G37150.
DR HOGENOM; CLU_046066_0_1_1; -.
DR InParanoid; O23171; -.
DR OMA; AKMLMRV; -.
DR OrthoDB; 923240at2759; -.
DR PhylomeDB; O23171; -.
DR BioCyc; ARA:AT4G37150-MON; -.
DR UniPathway; UPA00382; -.
DR PRO; PR:O23171; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23171; baseline and differential.
DR Genevisible; O23171; AT.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:TAIR.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IDA:TAIR.
DR GO; GO:0080032; F:methyl jasmonate esterase activity; IDA:TAIR.
DR GO; GO:0080031; F:methyl salicylate esterase activity; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; TAS:TAIR.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0009694; P:jasmonic acid metabolic process; IDA:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009696; P:salicylic acid metabolic process; IDA:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IGI:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR045889; MES/HNL.
DR PANTHER; PTHR10992; PTHR10992; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Immunity; Innate immunity; Plant defense; Reference proteome.
FT CHAIN 1..256
FT /note="Methylesterase 9"
FT /id="PRO_0000418183"
FT ACT_SITE 78
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
SQ SEQUENCE 256 AA; 28744 MW; 3DDF10EAAAC5C193 CRC64;
MKHYVLVHGG CHGAWCWYKV KPMLEHSGHR VTVFDLTAHG VNMSRVEDIQ TLEDFAKPLL
EVLESFGSDD KVVLVAHSLG GIPAALAADM FPSKISVAVF VTSFMPDTTN PPSYVFEKFL
GSITEEERMD FELGSYGTDD HPLKTAFLGP NYLKNMYLLS PIEDYELAKM LMRVTPAITS
NLTGTKSLTA QGYGSISRVY IVCGEDKGIR VDFQRWMIEN SPVKEVMEIK DADHMPMFSK
PHELCDRLLK IADKYP
