ID A0A0E0KHV5_ORYPU Unreviewed; 877 AA.
AC A0A0E0KHV5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC03G28110.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC03G28110.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC03G28110.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) 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 AlphaFoldDB; A0A0E0KHV5; -.
DR STRING; 4537.A0A0E0KHV5; -.
DR EnsemblPlants; OPUNC03G28110.1; OPUNC03G28110.1; OPUNC03G28110.
DR Gramene; OPUNC03G28110.1; OPUNC03G28110.1; OPUNC03G28110.
DR eggNOG; ENOG502QVKD; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR OMA; WWTELRN; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000026962; 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 CDD; cd01751; PLAT_LH2; 1.
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; 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:SF112; LINOLEATE 9S-LIPOXYGENASE 5; 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:UP000026962}.
FT DOMAIN 38..165
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 168..877
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 215..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 877 AA; 98727 MW; 6EE35373C35B97FD CRC64;
MQVQGFFDRL TGRNKEAWKE GRIRGTAVLV KKDVLDLGDF HASLLDGVHN ILGHKEGVAF
RLVSATARDP SNGGRGKLGK PAHLEELMVT MKSTAAGESV FRVAFEWDES QGIPGAVVVT
NSNRSEFFLK TLTLDGVPGK GTVVFVANSW IYPAGNYHSD RVFFANDTYL PSKMPAPLIP
YRQEELNILR GDGKIGPYKE HDRIYRYDYY NDLGQPDKGS EQVRPVLGGT QERPYPRRGR
TGRAPTETDP NTESRLPLLD LNIYVPRDER FGHLKMSDFL GYSLKAIIEG VLPIIRTYVD
TTPKEFDSFE DIMELYEGGL KVTDASALAE IKKRIPIDLI KSLLPVAGDQ LLKLPLPHVI
KEDKFAWRTD EEFAREMLAG VNPVMIKRLT DFPAKSTLDP NVYGDHTSKI TEAHIKNNME
GLTVQNALKG NRLFILDHHD HFMPFLDKIN KLDGNFIYAS RTLLLLKDDG TLKPLAIELS
LPHPDGQQHG AVSKVYTPAN TGVESQIWQL AKAYASVNDS AWHQLISHWL NTHAVIEPFV
IATNRQLSVV HPVHKLLSPH YRDTMNINAL ARQTLINADG IFEKTVFPGK YALEMSSVVY
KNWKFTEQAL PVDLVKRGVA VPDPTSPYNV RLLIKDYPYA VDGLVIWWAI ERWVGDYLAI
YYPNDSVLRG DEELQAWWKE VREVGHGDLK DQDWWPKMDT VKELTRACTI IIWIASALHA
AVNFGQYPYA GFLPNRPTVS RRPMPEPGTE EYAKLERGGD EADLVFIHTI TSQFQSILGV
SLIEILSKHS SDEVYLGQRD TPEWTSDAKA LDAFKRFGSR LVMIENRIKE MNVDPALKNR
NGPVKMPYML LYPNTSDVTG EKGQGLTAMG IPNSISI
//
