MES10_ARATH
ID MES10_ARATH Reviewed; 275 AA.
AC Q8S9K8; F4J0M5; Q9SCT0;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Methylesterase 10 {ECO:0000303|PubMed:18467465};
DE Short=AtMES10 {ECO:0000303|PubMed:18467465};
DE EC=3.1.1.- {ECO:0000269|PubMed:18467465};
GN Name=MES10 {ECO:0000303|PubMed:18467465};
GN OrderedLocusNames=At3g50440 {ECO:0000312|Araport:AT3G50440};
GN ORFNames=T20E23_40 {ECO:0000312|EMBL:CAB62473.1};
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=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 [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 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 methyl jasmonate (MeJA) esterase
CC activity in vitro. {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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB62473.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL133363; CAB62473.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE78667.2; -; Genomic_DNA.
DR EMBL; AY074858; AAL75909.1; -; mRNA.
DR EMBL; AY142031; AAM98295.1; -; mRNA.
DR PIR; T46075; T46075.
DR RefSeq; NP_566932.4; NM_114904.4.
DR AlphaFoldDB; Q8S9K8; -.
DR SMR; Q8S9K8; -.
DR BioGRID; 9526; 2.
DR IntAct; Q8S9K8; 1.
DR STRING; 3702.AT3G50440.1; -.
DR ESTHER; arath-MES10; Hydroxynitrile_lyase.
DR MEROPS; S33.A80; -.
DR PaxDb; Q8S9K8; -.
DR PRIDE; Q8S9K8; -.
DR ProteomicsDB; 232233; -.
DR EnsemblPlants; AT3G50440.1; AT3G50440.1; AT3G50440.
DR GeneID; 824208; -.
DR Gramene; AT3G50440.1; AT3G50440.1; AT3G50440.
DR KEGG; ath:AT3G50440; -.
DR Araport; AT3G50440; -.
DR TAIR; locus:2098685; AT3G50440.
DR eggNOG; ENOG502QQCC; Eukaryota.
DR HOGENOM; CLU_046066_0_1_1; -.
DR InParanoid; Q8S9K8; -.
DR OMA; SLMDCQF; -.
DR OrthoDB; 923240at2759; -.
DR PhylomeDB; Q8S9K8; -.
DR BioCyc; ARA:AT3G50440-MON; -.
DR UniPathway; UPA00382; -.
DR PRO; PR:Q8S9K8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8S9K8; baseline and differential.
DR Genevisible; Q8S9K8; AT.
DR GO; GO:0005829; C:cytosol; 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; IDA:TAIR.
DR GO; GO:0080031; F:methyl salicylate esterase activity; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009694; P:jasmonic acid metabolic process; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009696; P:salicylic acid metabolic process; IBA:GO_Central.
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..275
FT /note="Methylesterase 10"
FT /id="PRO_0000418184"
FT ACT_SITE 96
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT ACT_SITE 253
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
SQ SEQUENCE 275 AA; 31358 MW; 8F8BF932E82554BF CRC64;
MTYQKQYQMQ THHMQQQQLH HFVFVHGSCH GAWCWFKLAA KLKLDGHRVT AIDLGGSGVD
TRQLHEVRLV SAYLEPLMSF MESLPENEKV VLVGHSYGGI GTSLAMERFP TKVSVGIFLS
AYMPHHDSPP AVLIQEYFTR LPEGFAMDCE FTFEEGLEHP PSSVLFGTSF LKEKAYSNCQ
LEDLELAMAL MKPSWLYTKE MGGEDLITKE RYGSGKRVFI VCEGDNVVPE EIQKWMISNY
EPHEVKRIEE AGHMAMLTKP HELSQLLQEI AAKYN
