JAR4_NICAT
ID JAR4_NICAT Reviewed; 577 AA.
AC A0A1J6KGJ9; A1BNG5;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Jasmonoyl--L-amino acid synthetase JAR4 {ECO:0000305};
DE EC=6.3.2.52 {ECO:0000269|PubMed:17085687};
DE AltName: Full=Jasmonate-amino acid synthetase JAR4 {ECO:0000305};
DE AltName: Full=Jasmonic acid-amido synthetase JAR4 {ECO:0000305};
DE AltName: Full=Protein JASMONATE RESISTANT 4 {ECO:0000303|PubMed:17085687};
GN Name=JAR4 {ECO:0000303|PubMed:17085687};
GN ORFNames=A4A49_35910 {ECO:0000312|EMBL:OIT21023.1};
OS Nicotiana attenuata (Coyote tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=49451;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=17085687; DOI=10.1105/tpc.106.041103;
RA Kang J.H., Wang L., Giri A., Baldwin I.T.;
RT "Silencing threonine deaminase and JAR4 in Nicotiana attenuata impairs
RT jasmonic acid-isoleucine-mediated defenses against Manduca sexta.";
RL Plant Cell 18:3303-3320(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28536194; DOI=10.1073/pnas.1700073114;
RA Xu S., Brockmoeller T., Navarro-Quezada A., Kuhl H., Gase K., Ling Z.,
RA Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA Timmermann B., Gaquerel E., Baldwin I.T.;
RT "Wild tobacco genomes reveal the evolution of nicotine biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6133-6138(2017).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=17273867; DOI=10.1007/s00425-007-0477-3;
RA Wang L., Halitschke R., Kang J.H., Berg A., Harnisch F., Baldwin I.T.;
RT "Independently silencing two JAR family members impairs levels of trypsin
RT proteinase inhibitors but not nicotine.";
RL Planta 226:159-167(2007).
CC -!- FUNCTION: Catalyzes the synthesis of jasmonate-amino acid conjugates by
CC adenylation (PubMed:17085687, PubMed:17273867). Catalyzes the
CC conjugation of jasmonate (JA) to Ile, Leu and Val (PubMed:17273867).
CC Catalyzes the conjugation of jasmonate (JA) to Ile to mediate defense
CC signaling and resistance to the herbivore Manduca sexta caterpillars
CC (PubMed:17085687). {ECO:0000269|PubMed:17085687,
CC ECO:0000269|PubMed:17273867}.
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:17085687};
CC -!- INDUCTION: Induced by wounding (PubMed:17085687, PubMed:17273867).
CC Induced by oral secretion of the herbivore Manduca sexta caterpillars
CC (PubMed:17273867). Induced by treatment with JA-Ile (PubMed:17085687).
CC {ECO:0000269|PubMed:17085687, ECO:0000269|PubMed:17273867}.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ359729; ABC87760.1; -; mRNA.
DR EMBL; MJEQ01004674; OIT21023.1; -; Genomic_DNA.
DR RefSeq; XP_019239437.1; XM_019383892.1.
DR AlphaFoldDB; A0A1J6KGJ9; -.
DR SMR; A0A1J6KGJ9; -.
DR STRING; 49451.A0A1J6KGJ9; -.
DR EnsemblPlants; OIT21023; OIT21023; A4A49_35910.
DR GeneID; 109219431; -.
DR Gramene; OIT21023; OIT21023; A4A49_35910.
DR OMA; DEKIMID; -.
DR OrthoDB; 374623at2759; -.
DR BRENDA; 6.3.2.52; 9729.
DR Proteomes; UP000187609; Unassembled WGS sequence.
DR GO; GO:0102053; F:(-)-jasmonoyl-isoleucine synthetase activity; IDA:UniProtKB.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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 Plant defense; Reference proteome.
FT CHAIN 1..577
FT /note="Jasmonoyl--L-amino acid synthetase JAR4"
FT /id="PRO_0000446306"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 102
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 166..170
FT /ligand="an L-alpha-amino acid"
FT /ligand_id="ChEBI:CHEBI:59869"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 328..331
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 331..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 531..535
FT /ligand="an L-alpha-amino acid"
FT /ligand_id="ChEBI:CHEBI:59869"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT CONFLICT 359
FT /note="G -> D (in Ref. 1; ABC87760)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="N -> K (in Ref. 1; ABC87760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 64648 MW; 67398E1F1D6F3E49 CRC64;
MKMVVEKTEK FDPEEVIEEF EVLTKDAGKI QEETLQKILE ENGGTEYLQQ WGLNGKTDSL
SFKNCIPIVT HKDLEPYIHR IADGDLSPIL TGKPITTISL SSGTTQGKPK FVPFNEELME
STMQIFKTSF VFRNREFPVV NGKALQFIYG SKQFKTKGGL AAGTATTNVY RNAQFKKTMK
AMQTPCCSPD EVIFGPDFQQ SLYCHLLCGL IFRDEVQVVS STFAHSIVHA FRNFEQIWQE
LVTNIREGVL SSRVIVPSMR AAMSKLLKPD PELADTIFNK CSRLSNWYGL IPELFPNTRY
IYGIMTGSME PYLKKLRHYA GDLPLLSADY GSSEGWIGAN VNPELPPELV TYAVLPNIGY
FEFIPLMENL DGLEPMPVGL TEVKLGEEYE IVVTNFAGLY RYRLGDVVKI KGFHNGTPEL
QFICRRNLLL SINIDKNTEK DLQLAVEAAA KILSDEKLEV VDFTSHVNVS ADPGHYVIFW
ELNGEASEEI LKECCNCLDK SFVDAGYVGS RKVHAIGALE LRIVKRGTFH KILDHFVGLG
AAVSQFKTPR CVGPTNLSVL QILSSNVVES YFSTAFC
