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   03-AUG-2022, entry version 99.
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; 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; AJ507212; CAD45186.1; -; mRNA.
DR   AlphaFoldDB; Q8GSM3; -.
DR   SMR; Q8GSM3; -.
DR   PRIDE; Q8GSM3; -.
DR   KEGG; ag:CAD45186; -.
DR   UniPathway; UPA00382; -.
DR   ExpressionAtlas; Q8GSM3; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
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   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           ?..932
FT                   /note="Lipoxygenase 2.2, chloroplastic"
FT                   /id="PRO_0000018324"
FT   DOMAIN          79..219
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DOMAIN          223..932
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   REGION          270..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         588
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         593
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         778
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         782
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         932
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
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