LOX23_HORVU
ID LOX23_HORVU Reviewed; 896 AA.
AC Q8GSM2;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Lipoxygenase 2.3, chloroplastic;
DE EC=1.13.11.12;
DE AltName: Full=LOX2:Hv:3;
DE Flags: Precursor;
GN Name=LOX2.3;
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], AND CHARACTERIZATION.
RC STRAIN=cv. Salome; TISSUE=Leaf;
RX PubMed=12452441; DOI=10.1515/bc.2002.185;
RA Bachmann A., Hause B., Maucher H., Garbe E., Voeroes K., Weichert H.,
RA Wasternack C., Feussner I.;
RT "Jasmonate-induced lipid peroxidation in barley leaves initiated by
RT distinct 13-LOX forms of the chloroplast.";
RL Biol. Chem. 383:1645-1657(2002).
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
CC exhibits linoleate 13-lipoxygenase activity.
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 -!- 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;
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 -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; AJ507213; CAD45187.1; -; mRNA.
DR AlphaFoldDB; Q8GSM2; -.
DR SMR; Q8GSM2; -.
DR PRIDE; Q8GSM2; -.
DR KEGG; ag:CAD45187; -.
DR UniPathway; UPA00382; -.
DR ExpressionAtlas; Q8GSM2; baseline and differential.
DR GO; GO:0009507; C:chloroplast; TAS:AgBase.
DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IEA:UniProtKB-EC.
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:0010597; P:green leaf volatile biosynthetic process; TAS:AgBase.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009753; P:response to jasmonic acid; TAS:AgBase.
DR GO; GO:0009751; P:response to salicylic acid; TAS:AgBase.
DR CDD; cd01751; PLAT_LH2; 1.
DR Gene3D; 4.10.372.10; -; 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; PTHR11771; 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; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 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; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Plastid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..896
FT /note="Lipoxygenase 2.3, chloroplastic"
FT /id="PRO_0000018325"
FT DOMAIN 80..199
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 202..896
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 249..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 556
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 561
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 746
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 750
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 896
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 896 AA; 101234 MW; 31511189946B866A CRC64;
MIHLKQPLVL SAQSSNVASP LFVAGGQQRR ASGAGRTCSG RRLSARRISC ASTEEAVGVS
TSVTTKERAL TVTAIVTAQV PTSVYVARGL DDIQDLFGKT LLLELVSSEL DPKTGRERER
VKGFAHMTLK EGTYEAKMSV PASFGPVGAV LVENEHHREM FIKDIKLITG GDESTAITFD
VASWVHSKFD DPEPRAFFTV KSYLPSQTPP GIEALRKKEL ETLRGDGHSE RKFHERVYDY
DTYNDLGDPD KNIDHKRPVL GTKEHPYPRR CRTGRPKTLY DPETETRSSP VYVPRDEQFS
DVKGRTFSAT TLRSGLHAIL PAVAPLLNNS HGFSHFPAID ALYSDGIPLP VDGHGGNSFN
VINDVIPRVV QMIEDTTEHV LRFEVPEMLE RDRFSWFRDE EFARQTLAGL NPICIRRLTE
FPIVSKLDPA VYGPAESALS KEILEKMMNG RMTVEEAMEK KRLFLLDYHD VFLPYVHRVR
ELPDTTLYGS RTVFFLSDEG TLMPLAIELT RPQSPTKPQW KRAFTHGSDA TESWLWKLAK
AHVLTHDTGY HQLVSHWLRT HACVEPYIIA TNRQLSRMHP VYRLLHPHFR YTMEINALAR
EALINADGII EEAFLAGKYS IELSSVAYGA AWQFNTEALP EDLINRGLAV RRDDGELELA
IKDYPYADDG LLIWGSIKQW ASDYVDFYYK SDGDVAGDEE LRAWWEEVRT KGHADKKDEP
WWPVCDTKEN LVQILTIIMW VTSGHHAAVN FGQYHYAGYF PNRPTVVRRN IPVEENRDDE
MKKFMARPEE VLLQSLPSQM QAIKVMATLD ILSSHSPDEE YMGEYAEPAW LAEPMVKAAF
EKFSGRLKEA EGTIDMRNNN PENKNRCGAG IVPYELLKPF SEPGVTGRGI PNSISI
