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   16-JUN-2009, entry version 43.
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; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=cv. Salome; TISSUE=Leaf;
RX   MEDLINE=22339598; PubMed=12452441;
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
CC       diverse aspects of plant physiology including growth and
CC       development, pest resistance, and senescence or responses to
CC       wounding. This enzyme exhibits linoleate 13-lipoxygenase activity.
CC   -!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,11E)-(13S)-13-
CC       hydroperoxyoctadeca-9,11-dienoate.
CC   -!- COFACTOR: Binds 1 iron ion per subunit. Iron is tightly bound (By
CC       similarity).
CC   -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family.
CC   -!- SIMILARITY: Contains 1 lipoxygenase domain.
CC   -!- SIMILARITY: Contains 1 PLAT domain.
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DR   EMBL; AJ507213; CAD45187.1; -; mRNA.
DR   HSSP; P08170; 2SBL.
DR   Gramene; Q8GSM2; -.
DR   BRENDA; 1.13.11.12; 283.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016165; F:lipoxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000907; LipOase.
DR   InterPro; IPR013819; LipOase_C.
DR   InterPro; IPR001024; LipOase_LH2.
DR   InterPro; IPR001246; LipOase_pln.
DR   Gene3D; G3DSA:2.60.60.20; Lipase_LipOase; 1.
DR   PANTHER; PTHR11771; LipOase; 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   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; Iron;
KW   Lipid synthesis; Metal-binding; Oxidoreductase; Oxylipin biosynthesis;
KW   Plastid; Transit peptide.
FT   TRANSIT       1      ?       Chloroplast (Potential).
FT   CHAIN         ?    896       Lipoxygenase 2.3, chloroplastic.
FT                                /FTId=PRO_0000018325.
FT   DOMAIN       80    199       PLAT.
FT   DOMAIN      202    896       Lipoxygenase.
FT   METAL       556    556       Iron; catalytic (By similarity).
FT   METAL       561    561       Iron; catalytic (By similarity).
FT   METAL       746    746       Iron; catalytic (By similarity).
FT   METAL       750    750       Iron; catalytic (By similarity).
FT   METAL       896    896       Iron; via carboxylate; catalytic (By
FT                                similarity).
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
//