ID   LOX22_HORVU             Reviewed;         932 AA.
AC   Q8GSM3;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-NOV-2008, entry version 41.
DE   RecName: Full=Lipoxygenase 2.2, chloroplastic;
DE            EC=1.13.11.12;
DE   AltName: Full=LOX2:Hv:2;
DE   Flags: Precursor;
GN   Name=LOX2.2;
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; AJ507212; CAD45186.1; -; mRNA.
DR   HSSP; P08170; 2SBL.
DR   Gramene; Q8GSM3; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016165; F:lipoxygenase activity; IEA:InterPro.
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         ?    932       Lipoxygenase 2.2, chloroplastic.
FT                                /FTId=PRO_0000018324.
FT   DOMAIN       79    219       PLAT.
FT   DOMAIN      223    932       Lipoxygenase.
FT   METAL       588    588       Iron; catalytic (By similarity).
FT   METAL       593    593       Iron; catalytic (By similarity).
FT   METAL       778    778       Iron; catalytic (By similarity).
FT   METAL       782    782       Iron; catalytic (By similarity).
FT   METAL       932    932       Iron; via carboxylate; catalytic (By
FT                                similarity).
SQ   SEQUENCE   932 AA;  106493 MW;  64D80DF4370F30E0 CRC64;
     MQTATKPLVG ARAVPLSRRA SFLVAEARRK PSTNARRTRV GSTSTTTTTT TILTDVNGPA
     LTTVAKPGHQ YDLKQTVEMK ATVSVHMKSF WWSDEKKERA RDWAYDLILG SWLTLELVSS
     ELDPKTGQEH DVISGKLKHS RETEKDYDLY EAIFTCRHRL APSGAVRLVN YHHTEMLLGE
     VKIFPAGEDP TKSSAVTLFH CQSWIDPSHC SPDKRTFFPV EKSYIPSQTP KGVEKLRKSE
     LEALRGNGCG ERKKHDRIYD YDVYNDLGKP ESKRPVLGGK EHPYPRRCRT GRPRSKTDPS
     SEEESHKKGE MYVPRDETFT ERKEQAFLTK QLLSQLHGLC TGLKVNKDIL PSFPTLASID
     ALYDDDFRNQ PVQPEGGKVR LILDLLAKEL VHLVKLEGAE FVEGIRRVFK FETPEIHDMD
     KLAWFRDEEF ARQTLAGMNP LSIQLVTELP IVSKLDELKY GPADSLITKE LIEKQINRIM
     TAEEAVAQKK LFMLDYHDLL LPYVHRVRKL DNKTMYGSRT LFFLADDGTL RPIAIELTRP
     KSPHKQQWRK VFTPGSGYSG SVTGSWEWQL AKIHVLSHDT GYHQLVSHWL RTHCCVEPYV
     IAANRQLSQM HPIYRLLHPH FRFTMEINAQ ARGMLICADG IIEKTFSPGE FSMEISSAAY
     DKQWRFDMEA LPEDLIRRGM AVRGEDGKLE LAIEDYPYAN DGLLVWDAIK QWASDYVAHY
     YPCAVDIVDD EELQDWWTEV RTKGHPDKQD EPWWPELDCH ESLVQVLATI MWVTSAHHAA
     VNFGQYPMAG YVPNHPSIAR RNMPCEMGPE EMLAFKAAPE KVWLDTLPSQ LQTVMVMATL
     DLLSSHASDE EYMGTHQEPA WQRDGEVDKA FQVFQKKMRD IAEQVEEWNK DDSRRNRHGA
     GVVPYVLLRP LNGNPMDAKT VMEMGIPNSI SI
//