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Database: UniProt
Entry: J3LRV8_ORYBR
LinkDB: J3LRV8_ORYBR
Original site: J3LRV8_ORYBR 
ID   J3LRV8_ORYBR            Unreviewed;       863 AA.
AC   J3LRV8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE            EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN   Name=102722753 {ECO:0000313|EnsemblPlants:OB03G37840.1};
OS   Oryza brachyantha (malo sina).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB03G37840.1};
RN   [1] {ECO:0000313|EnsemblPlants:OB03G37840.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB03G37840.1};
RX   PubMed=23481403;
RA   Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA   Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA   Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA   An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA   Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA   Chen M.;
RT   "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT   Oryza genome evolution.";
RL   Nat. Commun. 4:1595-1595(2013).
RN   [2] {ECO:0000313|EnsemblPlants:OB03G37840.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2013) to UniProtKB.
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.
CC       {ECO:0000256|RuleBase:RU003975}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962,
CC         ECO:0000256|RuleBase:RU003974};
CC   -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC       {ECO:0000256|RuleBase:RU003975}.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family.
CC       {ECO:0000256|ARBA:ARBA00009419, ECO:0000256|RuleBase:RU003974}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR   RefSeq; XP_006650442.1; XM_006650379.2.
DR   AlphaFoldDB; J3LRV8; -.
DR   STRING; 4533.J3LRV8; -.
DR   EnsemblPlants; OB03G37840.1; OB03G37840.1; OB03G37840.
DR   GeneID; 102722753; -.
DR   Gramene; OB03G37840.1; OB03G37840.1; OB03G37840.
DR   KEGG; obr:102722753; -.
DR   eggNOG; ENOG502QQSP; Eukaryota.
DR   HOGENOM; CLU_004282_0_0_1; -.
DR   OMA; TESWVWQ; -.
DR   OrthoDB; 462210at2759; -.
DR   UniPathway; UPA00382; -.
DR   Proteomes; UP000006038; Chromosome 3.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
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-UniRule.
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; IPR027433; Lipoxygenase_dom_3.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   PANTHER; PTHR11771:SF207; LINOLEATE 9S-LIPOXYGENASE 1; 1.
DR   PANTHER; PTHR11771; 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   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW   ECO:0000256|RuleBase:RU003975};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003974};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU003975};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003974};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003974};
KW   Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767,
KW   ECO:0000256|RuleBase:RU003975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006038}.
FT   DOMAIN          32..158
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          161..863
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51393"
FT   REGION          204..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  97457 MW;  A1E62D37D23CB0F2 CRC64;
     MLGGLKDKLT GKNANKIKGT AVLMSRKILD PRDFTASLFD NIQELVGNSI TCQLVSATVT
     DPNNGGRGIV GSEAKMEQGL SNLPSLTHAE SNFKVRFDWD MDKHGVPGAI IVKNHHSTKF
     FLKTIILNDV PGCGTIVFVA NSWIYPLEKY HYNRIFFANN SYLPSQMPKA LSPYREDELR
     YLRGEDRQGP YQEHDRIYRY DVYNDLGEPD RDNPRPVLGG SQKHPYPRRG RTGRSPTKKD
     PNSESRLSLL DQIYLPSDER FARLKMSDFA GHSLKAIVQG ILPAIRTYVD LTPGEFDSFE
     DIMKLYKGGL KLPNIPALEE LRKNFPVQLI KDLLPVGGSY LHKLPKPDII KENEVAWRTD
     EEFAREILAG LNPMVIRRLT EFPPKSTLDP SKYGDQTSTI TPAHIEKNLE GLSVQQALDN
     NRLYILDHHD NFMPFLIEIN SLDGIFTYAT RTLLFLRGDD TLKPLAIELS LPHIEGNLTT
     AKSKVYTPAS SGTESWVWQL AKAYVAVNDS GWHQLISHWL NTHAVMEPFV IATNRQLSVA
     HPLYKILQPH YRDTMTINAL ARQTLINAGG IFEQTVFPGK HALAMSSAVY RSWNFTEQGL
     PDDLIKRGIA IKDPSSPSKV QLLIKDYPYA TDGLEVWQAI EQWVTEYCAI YYPNDGVLQG
     DVELQAWWKE VREVGHGDLK DADWWPKMQT VPELTKACTT IIWIASALHA AVNFGQYPYA
     GYLPNRPTVS RRPMPDPGSK EYTELEQNPE KFFIRTITSQ FQTILGISLI EVLSQHSSDE
     IYLGQRDTPE WTSDLKALEA FKRFSRKLVE IESKVLSMNK DPRLKNRVGP ANFPYTLLFP
     NTSDNKGAAA GITARGIPNS ISI
//
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