JOX3_ARATH
ID JOX3_ARATH Reviewed; 363 AA.
AC Q9LY48;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Jasmonate-induced oxygenase 3 {ECO:0000303|PubMed:28559313};
DE EC=1.14.11.- {ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569};
DE AltName: Full=2-oxoglutarate-dependent dioxygenase JOX3 {ECO:0000305};
DE AltName: Full=Jasmonic acid oxidase 3 {ECO:0000303|PubMed:28760569};
DE AltName: Full=Protein JASMONATE-REGULATED GENE 21 {ECO:0000303|PubMed:15098125};
GN Name=JOX3 {ECO:0000303|PubMed:28559313};
GN Synonyms=JAO3 {ECO:0000303|PubMed:28760569},
GN JRG21 {ECO:0000303|PubMed:20565618};
GN OrderedLocusNames=At3g55970 {ECO:0000312|Araport:AT3G55970};
GN ORFNames=F27K19_150 {ECO:0000312|EMBL:CAB87851.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Bau S.;
RT "Arabidopsis thaliana mRNA for putative leucoanthocyanidin dioxygenase.";
RL Thesis (2001), University of Halle-Wittenberg, Germany.
RN [2]
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 [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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION.
RX PubMed=20565618; DOI=10.1111/j.1364-3703.2004.00242.x;
RA Nickstadt A., Thomma B.P., Feussner I., Kangasjaervi J., Zeier J.,
RA Loeffler C., Scheel D., Berger S.;
RT "The jasmonate-insensitive mutant jin1 shows increased resistance to
RT biotrophic as well as necrotrophic pathogens.";
RL Mol. Plant Pathol. 5:425-434(2004).
RN [6]
RP INDUCTION BY BACTERIAL INFECTION.
RX PubMed=15098125; DOI=10.1007/s00425-004-1272-z;
RA Zeier J., Pink B., Mueller M.J., Berger S.;
RT "Light conditions influence specific defence responses in incompatible
RT plant-pathogen interactions: uncoupling systemic resistance from salicylic
RT acid and PR-1 accumulation.";
RL Planta 219:673-683(2004).
RN [7]
RP INDUCTION BY WOUNDING.
RX PubMed=17544464; DOI=10.1016/j.phytochem.2007.04.024;
RA Delker C., Zolman B.K., Miersch O., Wasternack C.;
RT "Jasmonate biosynthesis in Arabidopsis thaliana requires peroxisomal beta-
RT oxidation enzymes--additional proof by properties of pex6 and aim1.";
RL Phytochemistry 68:1642-1650(2007).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND INDUCTION.
RX PubMed=28760569; DOI=10.1016/j.molp.2017.07.010;
RA Smirnova E., Marquis V., Poirier L., Aubert Y., Zumsteg J., Menard R.,
RA Miesch L., Heitz T.;
RT "Jasmonic acid oxidase 2 hydroxylates jasmonic acid and represses basal
RT defense and resistance responses against Botrytis cinerea infection.";
RL Mol. Plant 10:1159-1173(2017).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28559313; DOI=10.1073/pnas.1701101114;
RA Caarls L., Elberse J., Awwanah M., Ludwig N.R., de Vries M., Zeilmaker T.,
RA Van Wees S.C.M., Schuurink R.C., Van den Ackerveken G.;
RT "Arabidopsis JASMONATE-INDUCED OXYGENASES down-regulate plant immunity by
RT hydroxylation and inactivation of the hormone jasmonic acid.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6388-6393(2017).
CC -!- FUNCTION: 2-oxoglutarate-dependent dioxygenase involved in the
CC oxidation of jasmonate (JA), a stress-induced phytohormone synthesized
CC in response to attack by pathogens and herbivores, which triggers the
CC activation of defense responses via the JA-mediated signaling pathway
CC (PubMed:28760569, PubMed:28559313). Converts JA to 12-hydroxyjasmonate
CC (12OH-JA), an inactive form of JA (PubMed:28760569, PubMed:28559313).
CC Is specific to free JA, and cannot oxidize the bioactive form
CC jasmonoyl-L-isoleucine (JA-Ile) or other JA-amino acid conjugates
CC (PubMed:28760569). Prevents over-accumulation of JA and indirectly its
CC bioactive form JA-Ile under stress response (PubMed:28760569,
CC PubMed:28559313). Acts as negative regulator of JA-mediated defense
CC signaling, by contributing to 12OH-JA accumulation, which represses JA
CC defense responses upon infection by the fungal pathogen Botrytis
CC cinerea (PubMed:28760569, PubMed:28559313). Acts as negative regulator
CC of JA-mediated defense responses upon infestation by the herbivorous
CC caterpillar Mamestra brassicae (PubMed:28559313).
CC {ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + jasmonate + O2 = (1R,2R)-12-hydroxyjasmonate
CC + CO2 + succinate; Xref=Rhea:RHEA:67144, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:58431, ChEBI:CHEBI:132022;
CC Evidence={ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67145;
CC Evidence={ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805,
CC ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- INDUCTION: Induced by methyl jasmonate (MeJA) (PubMed:20565618,
CC PubMed:28559313). Induced by infection with the bacterial pathogen
CC Pseudomonas syringae pv. maculicola (PubMed:20565618, PubMed:15098125).
CC Induced by wounding (PubMed:17544464, PubMed:28760569). Induced by
CC infection with the fungal pathogen Botrytis cinerea (PubMed:28760569,
CC PubMed:28559313). Induced by infestation with the caterpillar Mamestra
CC brassicae (PubMed:28559313). {ECO:0000269|PubMed:15098125,
CC ECO:0000269|PubMed:17544464, ECO:0000269|PubMed:20565618,
CC ECO:0000269|PubMed:28559313, ECO:0000269|PubMed:28760569}.
CC -!- DISRUPTION PHENOTYPE: The quadruple mutant jox1, jox2, jox3 and jox4
CC exhibit reduced root and shoot growth, delayed flowering, reduced seed
CC production, constitutively elevated jasmonate and jasmonoyl-L-
CC isoleucine levels, and enhanced resistance to the necrotrophic fungal
CC pathogen Botrytis cinerea and the herbivorous caterpillar Mamestra
CC brassicae. {ECO:0000269|PubMed:28559313}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AJ298225; CAC19787.1; -; mRNA.
DR EMBL; AL163832; CAB87851.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79462.1; -; Genomic_DNA.
DR EMBL; AK229205; BAF01075.1; -; mRNA.
DR PIR; T49209; T49209.
DR RefSeq; NP_191156.1; NM_115455.5.
DR AlphaFoldDB; Q9LY48; -.
DR SMR; Q9LY48; -.
DR STRING; 3702.AT3G55970.1; -.
DR iPTMnet; Q9LY48; -.
DR PaxDb; Q9LY48; -.
DR PRIDE; Q9LY48; -.
DR ProteomicsDB; 222152; -.
DR EnsemblPlants; AT3G55970.1; AT3G55970.1; AT3G55970.
DR GeneID; 824763; -.
DR Gramene; AT3G55970.1; AT3G55970.1; AT3G55970.
DR KEGG; ath:AT3G55970; -.
DR Araport; AT3G55970; -.
DR TAIR; locus:2082058; AT3G55970.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_0_1; -.
DR InParanoid; Q9LY48; -.
DR OMA; SKCHIDE; -.
DR OrthoDB; 1005149at2759; -.
DR PhylomeDB; Q9LY48; -.
DR BioCyc; ARA:AT3G55970-MON; -.
DR PRO; PR:Q9LY48; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY48; baseline and differential.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0120091; F:jasmonic acid hydrolase; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1900366; P:negative regulation of defense response to insect; IMP:UniProtKB.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IGI:TAIR.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Jasmonic acid signaling pathway; Metal-binding;
KW Oxidoreductase; Plant defense; Reference proteome.
FT CHAIN 1..363
FT /note="Jasmonate-induced oxygenase 3"
FT /id="PRO_0000438433"
FT DOMAIN 210..312
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 216
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 218
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 220
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 235
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 293
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 303
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 305
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 342
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 346
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
SQ SEQUENCE 363 AA; 41442 MW; FB7125684F1DA528 CRC64;
MNIFQDWPEP IVRVQSLSES NLGAIPNRYV KPLSQRPNIT PHNKHNPQTT TIPIIDLGRL
YTDDLTLQAK TLDEISKACR ELGFFQVVNH GMSPQLMDQA KATWREFFNL PMELKNMHAN
SPKTYEGYGS RLGVEKGAIL DWSDYYYLHY QPSSLKDYTK WPSLPLHCRE ILEDYCKEMV
KLCENLMKIL SKNLGLQEDR LQNAFGGKEE SGGCLRVNYY PKCPQPELTL GISPHSDPGG
LTILLPDEQV ASLQVRGSDD AWITVEPAPH AFIVNMGDQI QMLSNSIYKS VEHRVIVNPE
NERLSLAFFY NPKGNVPIEP LKELVTVDSP ALYSSTTYDR YRQFIRTQGP RSKCHIDELK
SPR
