MES16_ARATH
ID MES16_ARATH Reviewed; 262 AA.
AC O23512;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=pFDCC methylesterase MES16 {ECO:0000303|PubMed:23723324};
DE EC=3.1.1.- {ECO:0000269|PubMed:23723324};
DE AltName: Full=Methylesterase 16 {ECO:0000303|PubMed:18467465, ECO:0000303|PubMed:22147518};
DE Short=AtMES16 {ECO:0000303|PubMed:18467465, ECO:0000303|PubMed:22147518};
DE AltName: Full=Pheophorbidase {ECO:0000303|PubMed:16384908};
DE Short=AtPPD {ECO:0000303|PubMed:16384908};
GN Name=MES16 {ECO:0000303|PubMed:18467465, ECO:0000303|PubMed:22147518,
GN ECO:0000303|PubMed:23723324}; Synonyms=PPD {ECO:0000303|PubMed:16384908};
GN OrderedLocusNames=At4g16690 {ECO:0000312|Araport:AT4G16690};
GN ORFNames=dl4370c {ECO:0000312|EMBL:CAB10444.1},
GN FCAALL.12 {ECO:0000312|EMBL:CAB78711.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-262.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
RP IDENTIFICATION.
RX PubMed=16384908; DOI=10.1104/pp.105.071290;
RA Suzuki Y., Amano T., Shioi Y.;
RT "Characterization and cloning of the chlorophyll-degrading enzyme
RT pheophorbidase from cotyledons of radish.";
RL Plant Physiol. 140:716-725(2006).
RN [7]
RP GENE FAMILY, FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND
RP 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 FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=22147518; DOI=10.1104/pp.111.188870;
RA Christ B., Schelbert S., Aubry S., Suessenbacher I., Mueller T.,
RA Kraeutler B., Hoertensteiner S.;
RT "MES16, a member of the methylesterase protein family, specifically
RT demethylates fluorescent chlorophyll catabolites during chlorophyll
RT breakdown in Arabidopsis.";
RL Plant Physiol. 158:628-641(2012).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=23723324; DOI=10.1105/tpc.113.112151;
RA Christ B., Suessenbacher I., Moser S., Bichsel N., Egert A., Mueller T.,
RA Kraeutler B., Hoertensteiner S.;
RT "Cytochrome P450 CYP89A9 is involved in the formation of major chlorophyll
RT catabolites during leaf senescence in Arabidopsis.";
RL Plant Cell 25:1868-1880(2013).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND REVIEW.
RX PubMed=24302623; DOI=10.1002/chem.201303398;
RA Suessenbacher I., Christ B., Hoertensteiner S., Kraeutler B.;
RT "Hydroxymethylated phyllobilins: a puzzling new feature of the dioxobilin
RT branch of chlorophyll breakdown.";
RL Chemistry 20:87-92(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), FUNCTION, MUTAGENESIS OF SER-87,
RP AND ACTIVE SITE.
RX PubMed=27109476; DOI=10.1016/j.bbrc.2016.04.115;
RA Li H., Pu H.;
RT "Crystal structure of methylesterase family member 16 (MES16) from
RT Arabidopsis thaliana.";
RL Biochem. Biophys. Res. Commun. 474:226-231(2016).
CC -!- FUNCTION: Involved in the chlorophyll breakdown by its action in
CC fluorescent chlorophyll catabolites (FCCs) demethylation
CC (PubMed:22147518, PubMed:23723324, PubMed:24302623). Demethylates the
CC C13(2)-carboxymethyl group present at the isocyclic ring of chlorophyll
CC (PubMed:22147518). Uses primary fluorescent dioxobilin-type chlorophyll
CC catabolite (pFDCC) as substrate to produce O13(4)-desmethyl pFDCC
CC (PubMed:23723324, PubMed:24302623). Also able to catalyze pheophorbides
CC in vitro (PubMed:22147518). Methylesterase shown to have
CC carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase
CC activity and methyl jasmonate (MeJA) esterase activity in vitro
CC (PubMed:18467465, PubMed:27109476). {ECO:0000269|PubMed:18467465,
CC ECO:0000269|PubMed:22147518, ECO:0000269|PubMed:23723324,
CC ECO:0000269|PubMed:24302623, ECO:0000269|PubMed:27109476}.
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 + primary fluorescent dioxobilin-type chlorophyll
CC catabolite = H(+) + methanol + O13(4)-desmethyl pFDCC;
CC Xref=Rhea:RHEA:67176, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17790, ChEBI:CHEBI:167885, ChEBI:CHEBI:167889;
CC Evidence={ECO:0000269|PubMed:23723324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67177;
CC Evidence={ECO:0000269|PubMed:23723324};
CC -!- PATHWAY: Plant hormone biosynthesis. {ECO:0000269|PubMed:18467465}.
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC {ECO:0000269|PubMed:18467465}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC degradation. {ECO:0000269|PubMed:22147518,
CC ECO:0000269|PubMed:23723324}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22147518}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of fluorescent chlorophyll
CC catabolites (FCC) during senescence (PubMed:24302623). No effect on
CC root length when grown in presence of exogenous MeIAA.
CC {ECO:0000269|PubMed:18467465, ECO:0000269|PubMed:22147518,
CC ECO:0000269|PubMed:24302623}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase
CC family. {ECO:0000305}.
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DR EMBL; Z97341; CAB10444.1; -; Genomic_DNA.
DR EMBL; AL161544; CAB78711.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83784.1; -; Genomic_DNA.
DR EMBL; AY088316; AAM65855.1; -; mRNA.
DR EMBL; BX828808; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; B71434; B71434.
DR RefSeq; NP_193402.1; NM_117770.5.
DR PDB; 5HK8; X-ray; 2.80 A; A/B/C/D/E/F=1-262.
DR PDBsum; 5HK8; -.
DR AlphaFoldDB; O23512; -.
DR SMR; O23512; -.
DR BioGRID; 12664; 1.
DR STRING; 3702.AT4G16690.1; -.
DR ESTHER; arath-AT4G16690; Hydroxynitrile_lyase.
DR iPTMnet; O23512; -.
DR PaxDb; O23512; -.
DR PRIDE; O23512; -.
DR ProteomicsDB; 249343; -.
DR EnsemblPlants; AT4G16690.1; AT4G16690.1; AT4G16690.
DR GeneID; 827371; -.
DR Gramene; AT4G16690.1; AT4G16690.1; AT4G16690.
DR KEGG; ath:AT4G16690; -.
DR Araport; AT4G16690; -.
DR TAIR; locus:2129041; AT4G16690.
DR eggNOG; ENOG502QPPA; Eukaryota.
DR HOGENOM; CLU_046066_0_2_1; -.
DR InParanoid; O23512; -.
DR OMA; VENWPPS; -.
DR OrthoDB; 923240at2759; -.
DR PhylomeDB; O23512; -.
DR BioCyc; ARA:AT4G16690-MON; -.
DR UniPathway; UPA00382; -.
DR UniPathway; UPA00674; -.
DR PRO; PR:O23512; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23512; baseline and differential.
DR Genevisible; O23512; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0035560; F:pheophorbidase activity; ISS:UniProtKB.
DR GO; GO:0106372; F:primary fluorescent dioxobilin-type chlorophyll catabolite methylesterase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0033310; P:chlorophyll a catabolic process; ISS:UniProtKB.
DR GO; GO:0015996; P:chlorophyll catabolic process; IMP:UniProtKB.
DR GO; GO:0070988; P:demethylation; ISS:UniProtKB.
DR GO; GO:0009694; P:jasmonic acid metabolic process; IBA:GO_Central.
DR GO; GO:0010150; P:leaf senescence; ISS:UniProtKB.
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.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll catabolism; Cytoplasm; Hydrolase;
KW Reference proteome.
FT CHAIN 1..262
FT /note="pFDCC methylesterase MES16"
FT /id="PRO_0000391349"
FT ACT_SITE 87
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000269|PubMed:27109476"
FT ACT_SITE 211
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT ACT_SITE 239
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6RYA0"
FT MUTAGEN 87
FT /note="S->A: No esterase activity on methyl indole-3-acetic
FT acid (MeIAA)."
FT /evidence="ECO:0000269|PubMed:27109476"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:5HK8"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:5HK8"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5HK8"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:5HK8"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:5HK8"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:5HK8"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:5HK8"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:5HK8"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:5HK8"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:5HK8"
SQ SEQUENCE 262 AA; 29014 MW; 5CAA518C1A05212D CRC64;
MGGEGGAEPV IHFVFVHGAS HGAWCWYKLT TLLDAAGFKS TSVDLTGAGI SLIDSNIVFD
SDQYNRPLFS LLSDLPPHHK VILVGHSIGG GSVTEALCKF TDKISMAIYL AASMVQPGSI
PSPHLSNIHV GEEDIWEYTY GEGTDKPPTG VLMKPEFIRH YYYSQSPLED VTLSSKLLRP
APMRAFQDLD KLPPNPEAEK VPRVYIKTAK DNLFDSVRQD LLVENWPPSQ LYVLEDSDHS
AFFSVPTTLF AYLLRAVSFL QR
