MES17_ARATH
ID MES17_ARATH Reviewed; 276 AA.
AC Q9SG92;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Methylesterase 17 {ECO:0000303|PubMed:18467465};
DE Short=AtMES17 {ECO:0000303|PubMed:18467465};
DE EC=3.1.1.- {ECO:0000269|PubMed:18467465};
DE AltName: Full=Methyl indole-3-acetic acid esterase {ECO:0000303|PubMed:18467465};
GN Name=MES17 {ECO:0000303|PubMed:18467465};
GN OrderedLocusNames=At3g10870 {ECO:0000312|Araport:AT3G10870};
GN ORFNames=T7M13.5 {ECO:0000312|EMBL:AAF19562.1};
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, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES,
RP 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 that efficiently and specifically hydrolyzes
CC methyl indole-3-acetic acid (MeIAA) to IAA (auxin). MeIAA is believed
CC to be an inactive form of auxin that needs to be demethylated to exert
CC a biological effect. {ECO:0000269|PubMed:18467465}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for methyl indole-3-acetic acid (MeIAA) (at pH 7.5)
CC {ECO:0000269|PubMed:18467465};
CC Note=kcat is 0.18 sec(-1) with methyl indole-3-acetic acid as
CC substrate. {ECO:0000269|PubMed:18467465};
CC -!- PATHWAY: Plant hormone biosynthesis. {ECO:0000269|PubMed:18467465}.
CC -!- INTERACTION:
CC Q9SG92; Q9MAA7: GID1A; NbExp=3; IntAct=EBI-25529686, EBI-963597;
CC Q9SG92; Q9LYC1: GID1B; NbExp=3; IntAct=EBI-25529686, EBI-963686;
CC -!- TISSUE SPECIFICITY: Expressed in several tissues of seedlings and adult
CC plants, with a higher relative level of expression in the seedling
CC shoot apex and the adult stem.
CC -!- DISRUPTION PHENOTYPE: Longer hypocotyls when grown in presence of
CC exogenous MeIAA. {ECO:0000269|PubMed:18467465}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase
CC family. {ECO:0000305}.
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DR EMBL; AC011708; AAF19562.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74965.1; -; Genomic_DNA.
DR EMBL; AY063992; AAL36348.1; -; mRNA.
DR EMBL; AY096692; AAM20326.1; -; mRNA.
DR RefSeq; NP_187698.1; NM_111924.3.
DR AlphaFoldDB; Q9SG92; -.
DR SMR; Q9SG92; -.
DR BioGRID; 5591; 2.
DR IntAct; Q9SG92; 2.
DR STRING; 3702.AT3G10870.1; -.
DR ESTHER; arath-MES17; Hydroxynitrile_lyase.
DR PaxDb; Q9SG92; -.
DR PRIDE; Q9SG92; -.
DR ProteomicsDB; 232246; -.
DR EnsemblPlants; AT3G10870.1; AT3G10870.1; AT3G10870.
DR GeneID; 820257; -.
DR Gramene; AT3G10870.1; AT3G10870.1; AT3G10870.
DR KEGG; ath:AT3G10870; -.
DR Araport; AT3G10870; -.
DR TAIR; locus:2103202; AT3G10870.
DR eggNOG; ENOG502RZ4X; Eukaryota.
DR HOGENOM; CLU_046066_0_2_1; -.
DR InParanoid; Q9SG92; -.
DR OMA; SGGAWCW; -.
DR OrthoDB; 923240at2759; -.
DR PhylomeDB; Q9SG92; -.
DR BioCyc; ARA:AT3G10870-MON; -.
DR BRENDA; 3.1.1.1; 399.
DR SABIO-RK; Q9SG92; -.
DR PRO; PR:Q9SG92; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SG92; baseline and differential.
DR Genevisible; Q9SG92; 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; IBA:GO_Central.
DR GO; GO:0080031; F:methyl salicylate esterase activity; IBA:GO_Central.
DR GO; GO:0033473; P:indoleacetic acid conjugate metabolic process; IDA:TAIR.
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 GO; GO:0048367; P:shoot system development; 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..276
FT /note="Methylesterase 17"
FT /id="PRO_0000418189"
FT DOMAIN 19..138
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 95
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 252
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
SQ SEQUENCE 276 AA; 30868 MW; 953BAF2DABECBC2D CRC64;
MAEENQEETL ELKPSRKPPH FVLIHGMSLG SWCWYKIKCL MEVSGFTVTC IDLKSSGIDS
SSVDSLTTFD QYNQPLIDFL SSFPEQEQVI LVGHSAGGLS LTSAIQRFPK KICLAVFIGA
SMLKNGLQTD EDMKDGVPDL SEHGDVYELG FGLGPENPPT SAIIKPEYRR KLLYHMSPQQ
ECSLAALMMR PAPILALTTA KLEEEEKEKG QEEQVPRVYI KTLLDRVMKP EQQDAMIRRW
PPSQVYELES DHSPFFSNPF VLFGLLIKAA VSVGSI
