GH33_ORYSJ
ID GH33_ORYSJ Reviewed; 462 AA.
AC Q5NAZ7; A0A0P0UZZ7; Q0JPI4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Jasmonoyl--L-amino acid synthetase GH3.3 {ECO:0000305};
DE EC=6.3.2.52 {ECO:0000269|PubMed:24033451};
DE AltName: Full=Auxin-responsive GH3-like protein 3 {ECO:0000303|PubMed:15856348};
DE Short=OsGH3-3 {ECO:0000303|PubMed:15856348};
DE AltName: Full=Indole-3-acetic acid-amido synthetase GH3.3 {ECO:0000305};
DE AltName: Full=Jasmonate-amino acid synthetase JAR2 {ECO:0000305};
DE AltName: Full=Jasmonic acid-amido synthetase JAR2 {ECO:0000305};
DE AltName: Full=Protein JASMONATE RESISTANT 2 {ECO:0000303|PubMed:21619871};
DE Short=OsJAR2 {ECO:0000303|PubMed:21619871};
GN Name=GH3.3 {ECO:0000303|PubMed:15856348};
GN Synonyms=JAR2 {ECO:0000303|PubMed:21619871};
GN OrderedLocusNames=Os01g0221100 {ECO:0000312|EMBL:BAF04344.1},
GN LOC_Os01g12160 {ECO:0000305};
GN ORFNames=P0483F08.33-1 {ECO:0000312|EMBL:BAD81367.1};
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
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 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 [6]
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 [7]
RP FUNCTION, AND INDUCTION BY WOUNDING.
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 [8]
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).
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, Leu,
CC Met, Val and Trp (PubMed:24033451). May catalyze the synthesis of
CC indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism
CC for the plant to cope with the presence of excess auxin (By
CC similarity). {ECO:0000250|UniProtKB:O82333,
CC ECO:0000269|PubMed:21619871, ECO:0000269|PubMed:24033451}.
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 and flowers.
CC {ECO:0000269|PubMed:15856348}.
CC -!- INDUCTION: At low level by auxin. Induced by wounding
CC (PubMed:21619871). {ECO:0000269|PubMed:15856348,
CC ECO:0000269|PubMed:21619871}.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD81367.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP002094; BAD81367.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008207; BAF04344.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS71074.1; -; Genomic_DNA.
DR EMBL; AK072125; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q5NAZ7; -.
DR SMR; Q5NAZ7; -.
DR STRING; 4530.OS01T0221100-01; -.
DR PaxDb; Q5NAZ7; -.
DR PRIDE; Q5NAZ7; -.
DR EnsemblPlants; Os01t0221100-01; Os01t0221100-01; Os01g0221100.
DR EnsemblPlants; Os01t0221100-02; Os01t0221100-02; Os01g0221100.
DR Gramene; Os01t0221100-01; Os01t0221100-01; Os01g0221100.
DR Gramene; Os01t0221100-02; Os01t0221100-02; Os01g0221100.
DR eggNOG; ENOG502QTQD; Eukaryota.
DR HOGENOM; CLU_016249_0_0_1; -.
DR InParanoid; Q5NAZ7; -.
DR OMA; CISVHET; -.
DR PlantReactome; R-OSA-6787011; Jasmonic acid signaling.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q5NAZ7; 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:0102058; F:jasmonoyl-leucine synthetase activity; IDA:UniProtKB.
DR GO; GO:0102057; F:jasmonoyl-valine synthetase activity; IDA:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IC:Gramene.
DR GO; GO:0009416; P:response to light stimulus; IC:Gramene.
DR InterPro; IPR004993; GH3.
DR PANTHER; PTHR31901; PTHR31901; 1.
DR Pfam; PF03321; GH3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Jasmonic acid signaling pathway; Ligase; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..462
FT /note="Jasmonoyl--L-amino acid synthetase GH3.3"
FT /id="PRO_0000203580"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 106
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 170..174
FT /ligand="an L-alpha-amino acid"
FT /ligand_id="ChEBI:CHEBI:59869"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 334..337
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 337..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 339
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT CONFLICT 362
FT /note="P -> H (in Ref. 5; AK072125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 50511 MW; 52FB68161F2947CC CRC64;
MLEKKATRST RVDGVSGEAV IEEFERVTRD AANVQRETLR RILAENGGVE YLRGLGLAGA
TDPATFRARV PLATHADLEP YIDRIADGDA SPVLTAKPAT SISLSSGTTQ GKRKYLLFNE
ELVKSTMQIY RISYAFRNRE FPVENGKALQ FIYSSRETRT KGGLTATTAT TNVYRSEEFK
ATMRDIQSQC CSPDEVIFGP DFAQSLYCHL LAGLLAAGDV QIVSATFAHS VVLAFQTFER
AWEDLCADIR RGEVSPSRVT SPAVRRAMAA LLAAPNPGLA DEVARKCAAL SNWYGVIPAL
WPNARYVYGI MTGSMEHYVK KLRHYAGGLP LVAAEYGASE GWVGANVEPG TPPERATFTV
LPDIAYFEFI PLKPVAGDGG YAEAEPVGLT EVAAGELYEV VMTTFAGNTR SSSSCMTLVA
YYYLQSKKWM NICRFCISVH ETSRNLVTCT FAATGHIMFA QK
