MES11_ARATH
ID MES11_ARATH Reviewed; 390 AA.
AC Q9FW03;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Putative methylesterase 11, chloroplastic {ECO:0000303|PubMed:18467465};
DE Short=AtMES11 {ECO:0000303|PubMed:18467465};
DE EC=3.1.1.- {ECO:0000250|UniProtKB:Q9SG92};
DE Flags: Precursor;
GN Name=MES11 {ECO:0000303|PubMed:18467465};
GN OrderedLocusNames=At3g29770 {ECO:0000312|Araport:AT3G29770};
GN ORFNames=T26G12.12 {ECO:0000312|EMBL:AP002064};
GN and
GN OrderedLocusNames=At1gXXXXX;
GN ORFNames=F13E17.2 {ECO:0000312|EMBL:AAG12619.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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=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 [5]
RP GENE FAMILY.
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: Putative methylesterase.
CC -!- INTERACTION:
CC Q9FW03; Q9SZI2: NAP1;1; NbExp=3; IntAct=EBI-4426271, EBI-4424361;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase
CC family. {ECO:0000305}.
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DR EMBL; AP002064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC074284; AAG12619.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77609.1; -; Genomic_DNA.
DR EMBL; BT003149; AAO24581.1; -; mRNA.
DR RefSeq; NP_189622.1; NM_113902.4.
DR AlphaFoldDB; Q9FW03; -.
DR SMR; Q9FW03; -.
DR BioGRID; 8004; 2.
DR IntAct; Q9FW03; 2.
DR STRING; 3702.AT3G29770.1; -.
DR ESTHER; arath-MES11; Hydroxynitrile_lyase.
DR iPTMnet; Q9FW03; -.
DR PaxDb; Q9FW03; -.
DR PRIDE; Q9FW03; -.
DR ProteomicsDB; 238957; -.
DR EnsemblPlants; AT3G29770.1; AT3G29770.1; AT3G29770.
DR GeneID; 822677; -.
DR Gramene; AT3G29770.1; AT3G29770.1; AT3G29770.
DR KEGG; ath:AT3G29770; -.
DR Araport; AT3G29770; -.
DR TAIR; locus:2100587; AT3G29770.
DR eggNOG; ENOG502QRBN; Eukaryota.
DR HOGENOM; CLU_046066_8_1_1; -.
DR OMA; LTQYAEP; -.
DR OrthoDB; 923240at2759; -.
DR PhylomeDB; Q9FW03; -.
DR BioCyc; ARA:AT3G29770-MON; -.
DR PRO; PR:Q9FW03; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FW03; baseline and differential.
DR Genevisible; Q9FW03; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0009694; P:jasmonic acid metabolic process; IBA:GO_Central.
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; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..390
FT /note="Putative methylesterase 11, chloroplastic"
FT /id="PRO_0000418185"
FT DOMAIN 137..241
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT ACT_SITE 339
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT ACT_SITE 367
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
SQ SEQUENCE 390 AA; 42663 MW; 970217E926B0EFB2 CRC64;
MGNLCSLFTP PKPVKKRKPI TKRQSSIGAS SSGSGLNSNR WNNRVRSSSS RRDNKFEDAL
IQEHALAAAA VLFRQQNGGG GSLPFDRSAS QRYQGSCSKK NQLPRSSSSR SRSSTDPLLQ
PHQFLNQGIK LDDLETNHFV LVHGGSFGAW CWYKTIALLE EDGFKVTAID LAGCGINSIN
INGIASLSQY VKPLTDILEK LPIGEKVILV GHDFGGACIS YAMELFPSKI SKAVFLAAAM
LTNGQSTLDM FSLKAGQNDL MRKAQIFIYT NGNENPPTAI DLDKSLLKDL LFNQSPSKDV
ALASVSMRSI PFAPVLEKLS LSDANYGSVR RYYIETLEDN AIPVTLQENM INSSPPEKVY
RLKGADHAPF FSKPQALHKL LLEIARISPA
