JAR6_NICAT
ID JAR6_NICAT Reviewed; 580 AA.
AC A0A314KSQ4; B0VXR3;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 2.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Jasmonoyl--L-amino acid synthetase JAR6 {ECO:0000305};
DE EC=6.3.2.52 {ECO:0000269|PubMed:17273867};
DE AltName: Full=Jasmonate-amino acid synthetase JAR6 {ECO:0000305};
DE AltName: Full=Jasmonic acid-amido synthetase JAR6 {ECO:0000305};
DE AltName: Full=Protein JASMONATE RESISTANT 6 {ECO:0000305};
GN Name=JAR6; ORFNames=A4A49_19048 {ECO:0000312|EMBL:OIT32368.1};
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=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).
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).
CC -!- FUNCTION: Catalyzes the synthesis of jasmonate-amino acid conjugates by
CC adenylation (PubMed:17273867). Catalyzes the conjugation of jasmonate
CC (JA) to Ile, Leu and Val (PubMed:17273867). Catalyzes the conjugation
CC of JA to Ile that may mediate defense signaling and resistance to the
CC herbivore Manduca sexta caterpillars (PubMed:17273867).
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:17273867};
CC -!- INDUCTION: Induced by wounding and oral secretion of the herbivore
CC Manduca sexta caterpillars. {ECO:0000269|PubMed:17273867}.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=OIT32368.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ359730; ABC87761.1; -; mRNA.
DR EMBL; MJEQ01001075; OIT32368.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_019225904.1; XM_019370359.1.
DR RefSeq; XP_019225905.1; XM_019370360.1.
DR AlphaFoldDB; A0A314KSQ4; -.
DR SMR; A0A314KSQ4; -.
DR STRING; 49451.A0A314KSQ4; -.
DR EnsemblPlants; OIT32368; OIT32368; A4A49_19048.
DR GeneID; 109207440; -.
DR Gramene; OIT32368; OIT32368; A4A49_19048.
DR KEGG; nau:109207440; -.
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..580
FT /note="Jasmonoyl--L-amino acid synthetase JAR6"
FT /id="PRO_0000446307"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 103
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 167..171
FT /ligand="an L-alpha-amino acid"
FT /ligand_id="ChEBI:CHEBI:59869"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 329..332
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000250|UniProtKB:Q9SKE2"
FT BINDING 332..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 CONFLICT 247
FT /note="R -> K (in Ref. 1; ABC87761)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="R -> G (in Ref. 1; ABC87761)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="F -> S (in Ref. 1; ABC87761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 64781 MW; F9B9A36EE97D7FC3 CRC64;
MKMLVEKIEK KFDQEKVIEE FEDLTKDAGK IQEETLKKIL EQNGGTEYLQ LWGLNGRTDP
QTFKNCVPIV THNDLEPYIQ RIADGDLSPI LTGKPIETIS LSSGTTQGKP KFVPFNDELM
ESTMQIFKTS FAFRNREFPI GNGKALQFIY SSKQFKTKGG LAAGTATTNV YRNAQFKKTM
KAMCTPCCSP DEVIFGPDFH QSLYCHLLCG LIFHDEVQVV SSTFAHSIVH AFRTFEQVWE
ALVVDIREGV LSSRVTVPSI RLAMSKLLKP DPELADTIYN KCSRLSNWYG LIPDLFPNTR
YIYGIMTGSM EPYLKKLRHY AGELPLLSAD YGSSEGWVGV NVNPKLPPEL VTYAVLPNIG
YFEFIPLGGN LNGIEQANSP VGLTEVKLGE EYEVVFTNFA GLYRYRLGDV VKVKGFHNGT
PELQFVCRSN LLLSINIDKN TEKDLQLAVE AAAKRLVDEK LEVVDFTSHV NVSADPGHYV
IFWELSGEAT DEMLQDCCNC LDRSFIDAGY VSSRKVNAIG ALELRIVKRG TFHKILDHFV
GLGGAVSQFK TPRCVGPKNS SLLQILSSNV VETYVSTAFC