GH35_ORYSJ
ID GH35_ORYSJ Reviewed; 581 AA.
AC Q6I581; A0A0P0WRM7; Q0DFJ9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Jasmonoyl--L-amino acid synthetase GH3.5 {ECO:0000305};
DE EC=6.3.2.52 {ECO:0000269|PubMed:24033451};
DE AltName: Full=Auxin-responsive GH3-like protein 5 {ECO:0000303|PubMed:15856348};
DE Short=OsGH3-5 {ECO:0000303|PubMed:15856348};
DE AltName: Full=Indole-3-acetic acid-amido synthetase GH3.5 {ECO:0000305};
DE AltName: Full=Jasmonate-amino acid synthetase JAR1 {ECO:0000305};
DE AltName: Full=Jasmonic acid-amido synthetase JAR1 {ECO:0000305};
DE AltName: Full=Protein JASMONATE RESISTANT 1 {ECO:0000303|PubMed:18266905};
DE Short=OsJAR1 {ECO:0000303|PubMed:18266905};
GN Name=GH3.5 {ECO:0000303|PubMed:15856348};
GN Synonyms=JAR1 {ECO:0000303|PubMed:18266905};
GN OrderedLocusNames=Os05g0586200 {ECO:0000312|EMBL:BAF18374.1},
GN LOC_Os05g50890 {ECO:0000305};
GN ORFNames=OsJ_19714 {ECO:0000312|EMBL:EEE64857.1},
GN OSJNBa0009C07.16 {ECO:0000312|EMBL:AAT47070.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP TISSUE SPECIFICITY, INDUCTION, AND NOMENCLATURE.
RX PubMed=15856348; DOI=10.1007/s10142-005-0142-5;
RA Jain M., Kaur N., Tyagi A.K., Khurana J.P.;
RT "The auxin-responsive GH3 gene family in rice (Oryza sativa).";
RL Funct. Integr. Genomics 6:36-46(2006).
RN [8]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18266905; DOI=10.1111/j.1365-3040.2008.01790.x;
RA Riemann M., Riemann M., Takano M.;
RT "Rice JASMONATE RESISTANT 1 is involved in phytochrome and jasmonate
RT signalling.";
RL Plant Cell Environ. 31:783-792(2008).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=21619871; DOI=10.1016/j.bbrc.2011.05.055;
RA Wakuta S., Suzuki E., Saburi W., Matsuura H., Nabeta K., Imai R.,
RA Matsui H.;
RT "OsJAR1 and OsJAR2 are jasmonyl-L-isoleucine synthases involved in
RT wound- and pathogen-induced jasmonic acid signalling.";
RL Biochem. Biophys. Res. Commun. 409:634-639(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23832371; DOI=10.1271/bbb.130272;
RA Shimizu T., Miyamoto K., Miyamoto K., Minami E., Nishizawa Y., Iino M.,
RA Nojiri H., Yamane H., Okada K.;
RT "OsJAR1 contributes mainly to biosynthesis of the stress-induced jasmonoyl-
RT isoleucine involved in defense responses in rice.";
RL Biosci. Biotechnol. Biochem. 77:1556-1564(2013).
RN [11]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23621526; DOI=10.1111/jipb.12057;
RA Fukumoto K., Alamgir K., Yamashita Y., Mori I.C., Matsuura H., Galis I.;
RT "Response of rice to insect elicitors and the role of OsJAR1 in wound and
RT herbivory-induced JA-Ile accumulation.";
RL J. Integr. Plant Biol. 55:775-784(2013).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24033451; DOI=10.1111/pce.12201;
RA Svyatyna K., Jikumaru Y., Brendel R., Reichelt M., Mithoefer A., Takano M.,
RA Kamiya Y., Nick P., Riemann M.;
RT "Light induces jasmonate-isoleucine conjugation via OsJAR1-dependent and
RT -independent pathways in rice.";
RL Plant Cell Environ. 37:827-839(2014).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24947835; DOI=10.1007/s11103-014-0212-y;
RA Xiao Y., Chen Y., Charnikhova T., Mulder P.P., Heijmans J., Hoogenboom A.,
RA Agalou A., Michel C., Morel J.B., Dreni L., Kater M.M., Bouwmeester H.,
RA Wang M., Zhu Z., Ouwerkerk P.B.;
RT "OsJAR1 is required for JA-regulated floret opening and anther dehiscence
RT in rice.";
RL Plant Mol. Biol. 86:19-33(2014).
CC -!- FUNCTION: Catalyzes the synthesis of jasmonate-amino acid conjugates by
CC adenylation. Catalyzes the conjugation of jasmonate (JA) to Ile when
CC expressed in a heterologous system (E.Coli) (PubMed:21619871).
CC Catalyzes in vitro the conjugation of jasmonate (JA) to Ile, Phe, Cys,
CC Leu, Met, Ala, Val and Trp (PubMed:24033451). Involved in the
CC production of JA-Ile in response to infection by the rice blast fungus
CC Magnaporthe oryzae (PubMed:21619871, PubMed:23832371). Required for the
CC accumulation of the flavonoid phytoalexin sakuranetin in response to
CC infection by the rice blast fungus (PubMed:23832371). Involved in
CC herbivory-induced JA-Ile accumulation (PubMed:23621526). Involved in
CC the production of JA-Ile in response to wounding (PubMed:21619871,
CC PubMed:23621526, PubMed:24033451). Required for modulation of light and
CC JA signaling in photomorphogenesis (PubMed:18266905). Required for
CC normal seed development (PubMed:18266905, PubMed:23621526). Required
CC for optimal flower opening and closing and anther dehiscence
CC (PubMed:24947835). May catalyze the synthesis of indole-3-acetic acid
CC (IAA)-amino acid conjugates, providing a mechanism for the plant to
CC cope with the presence of excess auxin (By similarity).
CC {ECO:0000250|UniProtKB:O82333, ECO:0000269|PubMed:18266905,
CC ECO:0000269|PubMed:21619871, ECO:0000269|PubMed:23621526,
CC ECO:0000269|PubMed:23832371, ECO:0000269|PubMed:24033451,
CC ECO:0000269|PubMed:24947835}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a jasmonate + an L-alpha-amino acid + ATP = a jasmonyl-L-amino
CC acid + AMP + diphosphate + H(+); Xref=Rhea:RHEA:55772,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59869, ChEBI:CHEBI:136183, ChEBI:CHEBI:136184,
CC ChEBI:CHEBI:456215; EC=6.3.2.52;
CC Evidence={ECO:0000269|PubMed:24033451};
CC -!- TISSUE SPECIFICITY: Expressed in green shoots, roots and flowers.
CC {ECO:0000269|PubMed:15856348}.
CC -!- INDUCTION: At low level by auxin. Induced by methyl jasmonate (MeJA),
CC red light, far-red light and blue light (PubMed:18266905). Induced by
CC wounding and infection by the rice blast fungus Magnaporthe oryzae
CC (PubMed:21619871). Induced by elicitors from oral secretions of
CC armyworm caterpillars (Spodoptera mauritia) (PubMed:23621526).
CC {ECO:0000269|PubMed:15856348, ECO:0000269|PubMed:18266905,
CC ECO:0000269|PubMed:21619871, ECO:0000269|PubMed:23621526}.
CC -!- DISRUPTION PHENOTYPE: Open-husk phenotype after pollination and
CC malformed seeds with low fertility (PubMed:18266905, PubMed:23621526,
CC PubMed:24947835). Increased susceptibility to infection by the rice
CC blast fungus Magnaporthe oryzae (PubMed:23832371).
CC {ECO:0000269|PubMed:18266905, ECO:0000269|PubMed:23621526,
CC ECO:0000269|PubMed:23832371, ECO:0000269|PubMed:24947835}.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {ECO:0000305}.
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DR EMBL; AC137608; AAT47070.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF18374.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS95574.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64857.1; -; Genomic_DNA.
DR EMBL; AK071721; BAG92652.1; -; mRNA.
DR RefSeq; XP_015639715.1; XM_015784229.1.
DR AlphaFoldDB; Q6I581; -.
DR SMR; Q6I581; -.
DR STRING; 4530.OS05T0586200-01; -.
DR PaxDb; Q6I581; -.
DR PRIDE; Q6I581; -.
DR EnsemblPlants; Os05t0586200-01; Os05t0586200-01; Os05g0586200.
DR GeneID; 4339756; -.
DR Gramene; Os05t0586200-01; Os05t0586200-01; Os05g0586200.
DR KEGG; osa:4339756; -.
DR eggNOG; ENOG502QTQD; Eukaryota.
DR HOGENOM; CLU_016249_2_1_1; -.
DR InParanoid; Q6I581; -.
DR OMA; DEKIMID; -.
DR OrthoDB; 374623at2759; -.
DR PlantReactome; R-OSA-6787011; Jasmonic acid signaling.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q6I581; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0102053; F:(-)-jasmonoyl-isoleucine synthetase activity; IDA:UniProtKB.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0080123; F:jasmonate-amino synthetase activity; IEA:InterPro.
DR GO; GO:0102058; F:jasmonoyl-leucine synthetase activity; IDA:UniProtKB.
DR GO; GO:0102057; F:jasmonoyl-valine synthetase activity; IDA:UniProtKB.
DR GO; GO:0009864; P:induced systemic resistance, jasmonic acid mediated signaling pathway; IEA:InterPro.
DR GO; GO:0009694; P:jasmonic acid metabolic process; IEA:InterPro.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009733; P:response to auxin; IC:Gramene.
DR GO; GO:0009416; P:response to light stimulus; IC:Gramene.
DR GO; GO:0009611; P:response to wounding; IEA:InterPro.
DR InterPro; IPR004993; GH3.
DR InterPro; IPR031110; JAR1.
DR PANTHER; PTHR31901; PTHR31901; 1.
DR PANTHER; PTHR31901:SF50; PTHR31901:SF50; 1.
DR Pfam; PF03321; GH3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Growth regulation;
KW Jasmonic acid signaling pathway; Ligase; Nucleotide-binding; Plant defense;
KW Reference proteome; Stress response.
FT CHAIN 1..581
FT /note="Jasmonoyl--L-amino acid synthetase GH3.5"
FT /id="PRO_0000203582"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 95
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 159..163
FT /ligand="an L-alpha-amino acid"
FT /ligand_id="ChEBI:CHEBI:59869"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 321..324
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 324..329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 326
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 534..538
FT /ligand="an L-alpha-amino acid"
FT /ligand_id="ChEBI:CHEBI:59869"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 561
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
SQ SEQUENCE 581 AA; 65095 MW; 4AFB20349ABB6818 CRC64;
MTICSCEETI NEFEMLTRDA ARVQKDTLKK ILEINASAEY LQNFGLGGRT DAESYKSCIP
LCVHNDIEPY IQRIVDGDTS PVVTGEPITN LSLSSGTTHG KPKFIPFNDE LLETTLQIYR
TSYAFRNREY PIGQGKALQF VYGSKQVITK GGILATTATT NLYRRQRYKE GMKDIQSQCC
SPDEVIFGPD FHQSLYCHLL CGLIYSEEVH SVFSTFAHSL VHAFQTFEEV WEDLCTDIRD
GVLSKKVTAP SIREAVSKIL KPNPELADSI YKKCIGLSNW YGVIPALWPN AKYVYGIMTG
SMEPYLKKLR HYAGNLPLIS ADYGASEGWV GSNIDPTVPP EQVTYAVLPQ VGYFEFIPLE
KPIGEETENS ASIHYIESDP VGLTEVEVGK IYEVVITNFA GLYRYRLGDV VKIARFHNST
PELQFICRRS LVLSINIDKN TEKDLQLAVE EASKFLEGEK LEVMDFTSFV ERSSDPGRYV
IFWELSGDAS DEVLSSCANA LDLAFIDAGY TGSRKIKTIG PLELRILRKG TFKEILDHFL
SLGGAVSQFK TPRFVNPSNS KVLQILSRNV TQSYFSTAYG F
