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;
CC Evidence={ECO:0000255|PROSITE-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
//
