MES4_ARATH
ID MES4_ARATH Reviewed; 263 AA.
AC O80474;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Methylesterase 4 {ECO:0000303|PubMed:18467465};
DE Short=AtMES4 {ECO:0000303|PubMed:18467465};
DE EC=3.1.1.- {ECO:0000269|PubMed:18467465};
DE AltName: Full=Alpha/beta fold hydrolase/esterase 4;
GN Name=MES4 {ECO:0000303|PubMed:18467465}; Synonyms=ABE4;
GN OrderedLocusNames=At2g23580 {ECO:0000312|Araport:AT2G23580};
GN ORFNames=F26B6.23 {ECO:0000312|EMBL:AAC23771.1};
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 and
CC methyl salicylate (MeSA) esterase activity in vitro.
CC {ECO:0000269|PubMed:18467465, ECO:0000269|PubMed:18643994}.
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 Vmax=16.07 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O80474-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase
CC family. {ECO:0000305}.
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DR EMBL; AC003040; AAC23771.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07468.1; -; Genomic_DNA.
DR EMBL; BT010429; AAQ62430.1; -; mRNA.
DR EMBL; AK175772; BAD43535.1; -; mRNA.
DR PIR; T01147; T01147.
DR RefSeq; NP_179939.1; NM_127922.3. [O80474-1]
DR AlphaFoldDB; O80474; -.
DR SMR; O80474; -.
DR BioGRID; 2242; 1.
DR IntAct; O80474; 1.
DR STRING; 3702.AT2G23580.1; -.
DR ESTHER; arath-MES4; Hydroxynitrile_lyase.
DR PaxDb; O80474; -.
DR PRIDE; O80474; -.
DR ProteomicsDB; 232250; -. [O80474-1]
DR EnsemblPlants; AT2G23580.1; AT2G23580.1; AT2G23580. [O80474-1]
DR GeneID; 816890; -.
DR Gramene; AT2G23580.1; AT2G23580.1; AT2G23580. [O80474-1]
DR KEGG; ath:AT2G23580; -.
DR Araport; AT2G23580; -.
DR TAIR; locus:2046827; AT2G23580.
DR eggNOG; ENOG502QR2J; Eukaryota.
DR HOGENOM; CLU_046066_0_1_1; -.
DR InParanoid; O80474; -.
DR OMA; CADHMAM; -.
DR OrthoDB; 923240at2759; -.
DR PhylomeDB; O80474; -.
DR BioCyc; ARA:AT2G23580-MON; -.
DR PRO; PR:O80474; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80474; baseline and differential.
DR Genevisible; O80474; AT.
DR GO; GO:0005773; C:vacuole; HDA: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; IBA:GO_Central.
DR GO; GO:0080032; F:methyl jasmonate esterase activity; IBA:GO_Central.
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:0009696; P:salicylic acid metabolic process; IDA: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 Alternative splicing; Hydrolase; Reference proteome.
FT CHAIN 1..263
FT /note="Methylesterase 4"
FT /id="PRO_0000418179"
FT ACT_SITE 84
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"
SQ SEQUENCE 263 AA; 29582 MW; E8EAE4A37C5C3800 CRC64;
MEKNNKKRFV LVHGLCHGAW CWYKVKTHLE AVGHCVTAVD LAASGINMTR LEEIQTLKDY
CKPLLELLNS LGSDDDKVIL VAHSMGGIPA ALASDIFPSK IATIVFLTAF MPDTRNLPAY
VYQKLIRSVP QEGWLDTVFG TYGKHECPLE FALFGPKFMA KNLYQLSPVQ DLELAKMLVR
VNPIITNNLA GTRSFSEEGY GTVTRIYIVC GEDMAVPEDY QWWMIKNFPP KEVMEIKCAD
HMAMFSKPHK LCALLVEIAC KYA
