JOX1_ARATH
ID JOX1_ARATH Reviewed; 400 AA.
AC Q9SRM3;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Jasmonate-induced oxygenase 1 {ECO:0000303|PubMed:28559313};
DE EC=1.14.11.- {ECO:0000269|PubMed:28559313};
DE AltName: Full=2-oxoglutarate-dependent dioxygenase JOX1 {ECO:0000305};
DE AltName: Full=Jasmonic acid oxidase 1 {ECO:0000303|PubMed:28760569};
GN Name=JOX1 {ECO:0000303|PubMed:28559313};
GN Synonyms=JAO1 {ECO:0000303|PubMed:28760569};
GN OrderedLocusNames=At3g11180 {ECO:0000312|Araport:AT3G11180};
GN ORFNames=F11B9.11 {ECO:0000312|EMBL:AAG50980.1},
GN F9F8.3 {ECO:0000312|EMBL:AAF01507.1};
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 DEVELOPMENTAL STAGE.
RX PubMed=18775970; DOI=10.1104/pp.108.126375;
RA Wang Y., Zhang W.Z., Song L.F., Zou J.J., Su Z., Wu W.H.;
RT "Transcriptome analyses show changes in gene expression to accompany pollen
RT germination and tube growth in Arabidopsis.";
RL Plant Physiol. 148:1201-1211(2008).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=23791732; DOI=10.1016/j.cub.2013.05.021;
RA Leydon A.R., Beale K.M., Woroniecka K., Castner E., Chen J., Horgan C.,
RA Palanivelu R., Johnson M.A.;
RT "Three MYB transcription factors control pollen tube differentiation
RT required for sperm release.";
RL Curr. Biol. 23:1209-1214(2013).
RN [5]
RP INDUCTION BY WOUNDING.
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 [6]
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:28559313). Converts JA to 12-hydroxyjasmonate (12OH-JA), an
CC inactive form of JA (PubMed:28559313). Prevents over-accumulation of JA
CC and indirectly its bioactive form JA-Ile under stress response
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 and the herbivorous caterpillar Mamestra brassicae
CC (PubMed:28559313). {ECO:0000269|PubMed:28559313}.
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67145;
CC Evidence={ECO:0000269|PubMed:28559313};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:28559313};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805,
CC ECO:0000269|PubMed:28559313};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q9SRM3-1; Sequence=Displayed;
CC -!- DEVELOPMENTAL STAGE: Expressed during pollen germination and pollen
CC tube growth. {ECO:0000269|PubMed:18775970,
CC ECO:0000269|PubMed:23791732}.
CC -!- INDUCTION: Induced at low levels by wounding (PubMed:28760569). Induced
CC by methyl jasmonate (MeJA), infection by the fungal pathogen Botrytis
CC cinerea and infestation with the caterpillar Mamestra brassicae
CC (PubMed:28559313). {ECO:0000269|PubMed:28559313,
CC 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; AC009991; AAF01507.1; -; Genomic_DNA.
DR EMBL; AC073395; AAG50980.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75010.1; -; Genomic_DNA.
DR RefSeq; NP_187728.1; NM_111954.3. [Q9SRM3-1]
DR AlphaFoldDB; Q9SRM3; -.
DR SMR; Q9SRM3; -.
DR STRING; 3702.AT3G11180.2; -.
DR iPTMnet; Q9SRM3; -.
DR PRIDE; Q9SRM3; -.
DR ProteomicsDB; 222155; -. [Q9SRM3-1]
DR EnsemblPlants; AT3G11180.1; AT3G11180.1; AT3G11180. [Q9SRM3-1]
DR GeneID; 820289; -.
DR Gramene; AT3G11180.1; AT3G11180.1; AT3G11180. [Q9SRM3-1]
DR KEGG; ath:AT3G11180; -.
DR Araport; AT3G11180; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_0_1; -.
DR OMA; NSHPHAF; -.
DR PhylomeDB; Q9SRM3; -.
DR PRO; PR:Q9SRM3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRM3; 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; IMP:UniProtKB.
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 Alternative splicing; Dioxygenase; Iron; Jasmonic acid signaling pathway;
KW Metal-binding; Oxidoreductase; Plant defense; Reference proteome.
FT CHAIN 1..400
FT /note="Jasmonate-induced oxygenase 1"
FT /id="PRO_0000438436"
FT DOMAIN 248..349
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 254
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 256
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 258
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 273
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 275
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 330
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 340
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 342
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 379
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
FT BINDING 383
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9FFF6"
SQ SEQUENCE 400 AA; 45620 MW; 045070525F390AA1 CRC64;
MNNLDEIKIE SKTCLNDQEQ EVKIDNMHMS DQDKNKIEIK NKSGLGEKWP EPIVRVQSLA
ESNLTSLPDR YIKPPSQRPQ TTIIDHQPEV ADINIPIIDL DSLFSGNEDD KKRISEACRE
WGFFQVINHG VKPELMDAAR ETWKSFFNLP VEAKEVYSNS PRTYEGYGSR LGVEKGAILD
WNDYYYLHFL PLALKDFNKW PSLPSNIREM NDEYGKELVK LGGRLMTILS SNLGLRAEQL
QEAFGGEDVG ACLRVNYYPK CPQPELALGL SPHSDPGGMT ILLPDDQVVG LQVRHGDTWI
TVNPLRHAFI VNIGDQIQIL SNSKYKSVEH RVIVNSEKER VSLAFFYNPK SDIPIQPMQQ
LVTSTMPPLY PPMTFDQYRL FIRTQGPRGK SHVESHISPR
