ID A0A0D3FMV1_9ORYZ Unreviewed; 866 AA.
AC A0A0D3FMV1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART03G30840.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART03G30840.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART03G30840.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART03G30840.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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; A0A0D3FMV1; -.
DR STRING; 65489.A0A0D3FMV1; -.
DR PaxDb; 65489-OBART03G30840-1; -.
DR EnsemblPlants; OBART03G30840.1; OBART03G30840.1; OBART03G30840.
DR Gramene; OBART03G30840.1; OBART03G30840.1; OBART03G30840.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000026960; 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:SF49; LINOLEATE 9S-LIPOXYGENASE 3-RELATED; 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:UP000026960}.
FT DOMAIN 33..161
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 164..866
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 206..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 96221 MW; 1054774A9CD18982 CRC64;
MLGGIIDTIT GSSKQSRLKG TVVLMRKNVL DLNDFGATVI DGLGEFLGKG VTCQLISSTA
VDPNNGNRGK VGAEASLEQW LTSSLPSLTT GESRFGVTFD WDVDKLGVPG AIIVKNHHSN
EFFLKTITLD DVPGRAGAVV FLANSWVYPA DKYRYDRVFF ANDAYLPSQM PAALKPYRDD
ELRNLRGDDQ QGPYEEHDRV YRYDVYNDLG SPDSGNPRPI LGGSPDTPYP RRGRTGRKPT
TTDPDSESRL SLVEQIYVPR DERFGHLKMA DFLGYSIKAI AEGIVPAIRT YVDTTPGEFD
SFQDILDLYE GGLKLPDVPA LEELRKRFPL QLVKDLLPAA GDYILKLPMP QIIKQDKEAW
RTDEEFAREV LAGVNPMMIT RLTEFPPKSS LDPSKFGDHT STITAAHIGS NLEGLTVQQA
LDSNRLYILD HHDRFMPFLI DVNGLEGNFI YATRTLFFLR GDGTLAPLAI ELSEPMIQGD
VTAAKSTVYT PASTGVEAWV WQLAKAYVAV NDSGWHQLIS HWLNTHAVME PFVIATNRQL
SVTHPVHKLL SPHYRDTMTI NALARQTLIN AGGIFEMTVF PGKYALWMSS MVYKNWNFTE
QGLPADLIKR GVAVEDATSP YKVRLLIKDY PYAADGLEIW HAIEQWVGEY LAIYYTDDGV
LRGDAELQAW WAEVREVGHG DLKGAAWWPR MDAVSELRDA CTTIIWIASA LHAAVNFGQY
PYAGYLPNRP TVSRRRMPEP GTEAYGELGR DPERAFIRTI TSQLQTIIGI SLIEVLSKHS
SDEVYLGQRD TPAWTSDARA LEAFRRFSDR LVEIEGKVVG MNGDAGLKNR NGPAEFPYML
LYPNTSDVTG AAAGITAKGI PNSISI
//