MES2_ARATH
ID MES2_ARATH Reviewed; 263 AA.
AC O80476; Q8LCI0;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Methylesterase 2 {ECO:0000303|PubMed:18467465};
DE Short=AtMES2 {ECO:0000303|PubMed:18467465};
DE EC=3.1.1.- {ECO:0000269|PubMed:18467465};
DE AltName: Full=Protein METHYLESTERASE 8;
DE Short=AtME8;
GN Name=MES2 {ECO:0000303|PubMed:18467465}; Synonyms=ACL, ME8;
GN OrderedLocusNames=At2g23600 {ECO:0000312|Araport:AT2G23600};
GN ORFNames=F26B6.25 {ECO:0000312|EMBL:AAC23773.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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 [4]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 [7]
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).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=21764588; DOI=10.1016/j.bmc.2011.06.040;
RA Kaschani F., Nickel S., Pandey B., Cravatt B.F., Kaiser M.,
RA van der Hoorn R.A.;
RT "Selective inhibition of plant serine hydrolases by agrochemicals revealed
RT by competitive ABPP.";
RL Bioorg. Med. Chem. 20:597-600(2012).
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. {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). Down-regulated by agrochemicals Paraoxon, 3,4-DCl and
CC Profenofos. {ECO:0000269|PubMed:18643994, ECO:0000269|PubMed:21764588}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=1.77 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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase
CC family. {ECO:0000305}.
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DR EMBL; AC003040; AAC23773.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07471.1; -; Genomic_DNA.
DR EMBL; AF361627; AAK32795.1; -; mRNA.
DR EMBL; AY056068; AAL06968.1; -; mRNA.
DR EMBL; AK226527; BAE98666.1; -; mRNA.
DR EMBL; AY086590; AAM63650.1; -; mRNA.
DR PIR; T01149; T01149.
DR RefSeq; NP_179941.1; NM_127924.3.
DR AlphaFoldDB; O80476; -.
DR SMR; O80476; -.
DR BioGRID; 2244; 1.
DR IntAct; O80476; 1.
DR STRING; 3702.AT2G23600.1; -.
DR ESTHER; arath-MES2; Hydroxynitrile_lyase.
DR MetOSite; O80476; -.
DR PaxDb; O80476; -.
DR PRIDE; O80476; -.
DR EnsemblPlants; AT2G23600.1; AT2G23600.1; AT2G23600.
DR GeneID; 816892; -.
DR Gramene; AT2G23600.1; AT2G23600.1; AT2G23600.
DR KEGG; ath:AT2G23600; -.
DR Araport; AT2G23600; -.
DR TAIR; locus:2046852; AT2G23600.
DR eggNOG; ENOG502QR2J; Eukaryota.
DR HOGENOM; CLU_046066_0_1_1; -.
DR InParanoid; O80476; -.
DR PhylomeDB; O80476; -.
DR BioCyc; ARA:AT2G23600-MON; -.
DR UniPathway; UPA00382; -.
DR PRO; PR:O80476; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80476; baseline and differential.
DR Genevisible; O80476; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IMP:TAIR.
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; IDA:TAIR.
DR GO; GO:0009694; P:jasmonic acid metabolic process; IBA:GO_Central.
DR GO; GO:1901847; P:nicotinate metabolic process; IMP:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009696; P:salicylic acid metabolic process; IMP: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; Reference proteome.
FT CHAIN 1..263
FT /note="Methylesterase 2"
FT /id="PRO_0000418177"
FT ACT_SITE 85
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT CONFLICT 250
FT /note="L -> V (in Ref. 5; AAM63650)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="C -> S (in Ref. 5; AAM63650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 29667 MW; CB81F98B7B90A0BB CRC64;
MSEEKRKQHF VLVHGACHGA WCWYKVKPLL EALGHRVTAL DLAASGIDTT RSITDISTCE
QYSEPLMQLM TSLPNDEKVV LVGHSFGGLS LALAMDKFPD KISVSVFVTA FMPDTKHSPS
FVEEKFASSM TPEGWMGSEL ETYGSDNSGL SVFFSTDFMK HRLYQLSPVE DLELGLLLKR
PSSLFINELS KMENFSEKGY GSVPRAYIVC KEDNIISEDH QRWMIHNYPA NLVIEMEETD
HMPMFCKPQL LSDHLLAIAD NFC
