ID A0A0D9ZCV5_9ORYZ Unreviewed; 870 AA.
AC A0A0D9ZCV5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM03G33150.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM03G33150.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM03G33150.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0D9ZCV5; -.
DR STRING; 40148.A0A0D9ZCV5; -.
DR EnsemblPlants; OGLUM03G33150.1; OGLUM03G33150.1; OGLUM03G33150.
DR Gramene; OGLUM03G33150.1; OGLUM03G33150.1; OGLUM03G33150.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblPlants.
DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IEA:EnsemblPlants.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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 GO; GO:0051707; P:response to other organism; IEA:EnsemblPlants.
DR GO; GO:0009611; P:response to wounding; IEA:EnsemblPlants.
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:SF54; LINOLEATE 9S-LIPOXYGENASE 2; 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:UP000026961}.
FT DOMAIN 32..158
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 161..870
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 203..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 97326 MW; 4ACC1482566D5312 CRC64;
MLGGIIGGLT GNKNARLKGS LVLMRKNALD INDFGATVID GISEFLGRGV TCQLVSSSLV
DPNNGNRGRV GTEASLEQWL TSLPSLTTGE SKFGVTFEWE VEKMGIPGAI IVKNNHAAEF
FLKTITLDNV PGHGAVVFVA NSWIYPASKY RYNRVFFSND TSLPSKMPAA LKPYRDDELR
NLRGDDQQGP YQEHDRVYRY DVYNDLGEPD SGNPRPVLGG SPDRPYPRRG RTGRKPTKTD
PTAESRLSLL ENIYVPRDER FGHLKMADFL GYSIKALVDG IVPAIRTYVD LTPGEFDSFK
DILKLYEGGL KLPSIPALEE LRKRFPLQLV KDLIPAGGDY LLKLPMPHVI REDKKAWMTD
DEFAREILAG VNPMVIARLT EFPPRSRLDP ARYGDQTSTI TAAHVERGLE RLTVQQAIDG
NRLYVVDHHD HFMPYLLDIN SLDDNFIYAT RTLLFLRGDG TLAPLAIELS LPHLQDDGLI
TARSTVYTPA ARGGTGAGAV EWWVWQLAKA YVNVNDYCWH QLISHWLNTH AVMEPFVIAT
NRQLSVAHPV HKLLLPHYRD TMTINALARQ TLINGGGIFE MTVFPRKHAL AMSSAFYKDW
SFADQALPDD LVKRGVAVPD PASPYKVRLL IEDYPYANDG LAVWHAIEQW ATEYLAIYYP
NDGVLQGDAE LQAWWKEVRE VGHGDIKDAT WWPEMKTVAE LVKACATIIW IGSALHAAVN
FGQYPYAGYL PNRPSVSRRP MPEPGTKEYD ELARDPEKVF VRTITKQMQA IVGISLLEIL
SKHSSDEVYL GQRDTPEWTS DAKALEAFKR FGARLTEIES RVVAMNKDPH RKNRVGPTNF
PYTLLYPNTS DLKGDAAGLS ARGIPNSISI
//
