ID A0A0E0P9S6_ORYRU Unreviewed; 916 AA.
AC A0A0E0P9S6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 22-FEB-2023, entry version 43.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI04G15410.2, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI04G15410.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-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; A0A0E0P9S6; -.
DR EnsemblPlants; ORUFI04G15410.2; ORUFI04G15410.2; ORUFI04G15410.
DR Gramene; ORUFI04G15410.2; ORUFI04G15410.2; ORUFI04G15410.
DR HOGENOM; CLU_004282_0_0_1; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
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; LIPOXYGENASE; 1.
DR PANTHER; PTHR11771:SF95; LIPOXYGENASE 4, CHLOROPLASTIC; 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:UP000008022}.
FT DOMAIN 91..227
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 230..916
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 281..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 101771 MW; 1B0B51E2BDCF7397 CRC64;
MASLELLGRR MSSCSWGGGS AAAMRGGAGM CFASMEAAGS RGMGKGASRR RTARSTAPVG
ALVERVVVAP APVEQQRGAG RPEAHPQSVA ARAVVTVRRR RKEDAKDRFA EQLDALADRV
GRSVLLELVS TETDPRKGTP KKSKPSALVG WFDKKDVKAE RVVYTAEFAV DAGFGEPGAV
TVLNRHQREF YIESIVVEGF PTGPAHFTCN SWVQPTRVSR DRRVFFSNRP YLPSETPPGL
RELRLRELAD LRGDGTGERR ITDRVYDYDV YNDLGNPDKG VASARPVLGG EQMPYPRRMR
TGHASAESRV EYPEPIYVSR DEEFEEGKNE MLSEGAIKAL LHNFMPLLVS SVSPDIRDFA
GFHDVDNLFK EGLRLKQALH DQLFQKIPFV RKIQENSEGL LRYDTPDIIK KDKFAWLRDD
EFARQALAGI NPVNIERLQA FPPVSKLDPA VYGPPESAIT EEHIIGHLDG MSVQEAVEGS
RLYMLDYHDI FLPFLDRINA QDGRKAYGTR AVFFLTAAGT LKPIAIELCL PPMTDGCKRA
KRVFTPPADA TSNWLWQLAK AHVCSNDAGV HQLINHWLRT HACMEPFIIA AHRQMSAMHP
IFKLLKPHMR YTLKINALAR QILINGDGVI ESGFTPGNVC MEMSAFAYRE LWRLDQEGLP
ADLIRRGMAV EDPSQPHGLR LLIEDYPYAA DGLLLWSAIS RWCEAYVAAY YPSDEAVQAD
YELQSWYAEA VQSGHADKRG APWWPRLSTP GDLASLLTTL VWLCSAQHAA LNFGQYPLGG
YIPNRPPLMR RLVPAEGDPE YAHLVADPHR FFLSALPSLT QTTTFMTVID TLSTHSADEE
YLGERPDEAW TADPAALAAA REFAADVRRA EEEIERRNAD PSRRNRCGAG VLPYELMAPS
SGPGITCRGV PNSVTI
//
