ID   LOX21_HORVU             Reviewed;         936 AA.
AC   P93184;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   22-FEB-2023, entry version 118.
DE   RecName: Full=Lipoxygenase 2.1, chloroplastic;
DE            EC=1.13.11.12;
DE   AltName: Full=LOX-100;
DE   AltName: Full=LOX2:Hv:1;
DE   Flags: Precursor;
GN   Name=LOX2.1;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 213-227, CATALYTIC
RP   ACTIVITY, FUNCTION, AND INDUCTION.
RC   STRAIN=cv. Salome; TISSUE=Leaf;
RX   PubMed=9492266; DOI=10.1046/j.1432-1327.1998.2510036.x;
RA   Voeroes K., Feussner I., Kuehn H., Lee J., Graner A., Loebler M.,
RA   Parthier B., Wasternack C.;
RT   "Characterization of a methyljasmonate-inducible lipoxygenase from barley
RT   (Hordeum vulgare cv. Salome) leaves.";
RL   Eur. J. Biochem. 251:36-44(1998).
CC   -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse
CC       aspects of plant physiology including growth and development, pest
CC       resistance, and senescence or responses to wounding. This enzyme is
CC       possibly involved in jasmonic acid synthesis. It exhibits linoleate 13-
CC       lipoxygenase and arachidonate 15-lipoxygenase activity.
CC       {ECO:0000269|PubMed:9492266}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-
CC         octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12;
CC         Evidence={ECO:0000269|PubMed:9492266};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13S)-hydroperoxy-
CC         (9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:34495,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:58757;
CC         EC=1.13.11.12; Evidence={ECO:0000269|PubMed:9492266};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00726};
CC       Note=Binds 1 Fe cation per subunit. Iron is tightly bound.
CC       {ECO:0000255|PROSITE-ProRule:PRU00726};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.;
CC   -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC       ProRule:PRU00726}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- INDUCTION: Transient induction by exogenous methyl jasmonate, reaching
CC       a maximum 48 hours after treatment. Not induced by endogenous jasmonic
CC       acid resulting from sorbitol stress. {ECO:0000269|PubMed:9492266}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR   EMBL; U56406; AAC12951.1; -; mRNA.
DR   PIR; T06190; T06190.
DR   AlphaFoldDB; P93184; -.
DR   SMR; P93184; -.
DR   BRENDA; 1.13.11.12; 2687.
DR   BRENDA; 1.13.11.33; 2687.
DR   UniPathway; UPA00382; -.
DR   ExpressionAtlas; P93184; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IDA:CACAO.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0034440; P:lipid oxidation; IEA:InterPro.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009753; P:response to jasmonic acid; IDA:CACAO.
DR   CDD; cd01751; PLAT_LH2; 1.
DR   Gene3D; 3.10.450.60; -; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   InterPro; IPR000907; LipOase.
DR   InterPro; IPR013819; LipOase_C.
DR   InterPro; IPR036226; LipOase_C_sf.
DR   InterPro; IPR020834; LipOase_CS.
DR   InterPro; IPR020833; LipOase_Fe_BS.
DR   InterPro; IPR001246; LipOase_plant.
DR   InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR   InterPro; IPR027433; Lipoxygenase_dom_3.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR   PANTHER; PTHR11771:SF128; LIPOXYGENASE; 1.
DR   Pfam; PF00305; Lipoxygenase; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   PRINTS; PR00087; LIPOXYGENASE.
DR   PRINTS; PR00468; PLTLPOXGNASE.
DR   SMART; SM00308; LH2; 1.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   SUPFAM; SSF48484; Lipoxigenase; 1.
DR   PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR   PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR   PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Dioxygenase; Direct protein sequencing;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Iron; Lipid biosynthesis;
KW   Lipid metabolism; Metal-binding; Oxidoreductase; Oxylipin biosynthesis;
KW   Plastid; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..936
FT                   /note="Lipoxygenase 2.1, chloroplastic"
FT                   /id="PRO_0000018323"
FT   DOMAIN          88..217
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DOMAIN          220..936
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         587
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         592
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         777
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         781
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         936
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ   SEQUENCE   936 AA;  105864 MW;  567B8519E0B5D959 CRC64;
     MLTATKPLVG GACAAPSSSA RRRTFVVPEA RRKPGNGRRT SVSKVGSTST STTTTTTTTL
     SADSNGAAVG TVTRPDVHVQ DRTHATEMKA TVTVHMSKAA GVRDFLYDLI LKTWLHVDLV
     SSELDPQTGQ EREPISGAVK HSGRVDDEWD MYEATFKVPA SFGPIGAVQV TNYHHSEMLL
     GDIEVFPTGQ EESAVTFHCK SWIDPSHCTP DKRVFFPAHS YLPSQTPKGV EGLRKRELEI
     LRGTGCGERK EHDRIYDYDV YNDLGNPDDD NNPTTRPVLG GKEHPYPRRC RTGRPRSKKD
     PFSEERSHKE HIYVPRDEAF TERKMGAFDT KKFMSQLHAL TTGLKTAKHK SQSFPSLSAI
     DQLYDDNFRN QPVQPEGGKL RFVIDLLETE LLHLFKLEGA AFLEGIRRVF KFETPEIHDR
     DKFAWFRDEE FARQTIAGMN PMSIQLVTEF PIKSNLDEAT YGPADSLITK EVVEEQIRRV
     MTADEAVQNK KLFMLDYHDL LLPYVHKVRK LDGTTLYGSR ALFFLTADGT LRPIAIELTR
     PKSKKKPQWR QVFTPGCDGS VTGSWLWQLA KAHILAHDAG VHQLVSHWLR THACTEPYII
     AANRQLSQMH PVYRLLHPHF RFTMEINAQA RAMLINAGGI IEGSFVPGEY SLELSSVAYD
     QQWRFDMEAL PEDLIRRGMA VRNPNGELEL AIEDYPYAND GLLVWDAIKQ WALTYVQHYY
     PCAADIVDDE ELQAWWTEVR TKGHADKQDE PWWPELDSHE NLAQTLATIM WVTSGHHAAV
     NFGQYPMAGY IPNRPTMARR NMPTEIGGDD MRDFVEAPEK VLLDTFPSQY QSAIVLAILD
     LLSTHSSDEE YMGTHEEPAW TKDGVINQAF EEFKESTRKI VEQVDEWNND PDRKNRHGAG
     MVPYVLLRPS DGDPTDGDPT DEKMVMEMGI PNSISI
//