ID A0A3B6IL62_WHEAT Unreviewed; 861 AA.
AC A0A3B6IL62;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=CFC21_056336 {ECO:0000313|EMBL:KAF7047402.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS4B02G037700.3};
RN [1] {ECO:0000313|EMBL:KAF7047402.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7047402.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS4B02G037700.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS4B02G037700.3};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS4B02G037700.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7047402.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7047402.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM022221; KAF7047402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6IL62; -.
DR SMR; A0A3B6IL62; -.
DR STRING; 4565.A0A3B6IL62; -.
DR EnsemblPlants; TraesCS4B02G037700.3; TraesCS4B02G037700.3; TraesCS4B02G037700.
DR Gramene; TraesCS4B02G037700.3; TraesCS4B02G037700.3; TraesCS4B02G037700.
DR Gramene; TraesCS4B03G0082200.3; TraesCS4B03G0082200.3.CDS; TraesCS4B03G0082200.
DR Gramene; TraesKAR4B01G0018530.1; cds.TraesKAR4B01G0018530.1; TraesKAR4B01G0018530.
DR OrthoDB; 462210at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000019116; Chromosome 4B.
DR Proteomes; UP000815260; Chromosome 4B.
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; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
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:UP000019116}.
FT DOMAIN 34..160
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 163..861
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 211..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 96054 MW; 816F65FCB5901B46 CRC64;
MILGGLVDSL TGANKSARLK GTVVLMRKNV LDLNDFGATI MDGIGEFIGK GVTCQLISST
LVDHDNGGRG KVGAEAELEQ WVTSLPSLTT GESKFGLTFD WEVEKLGVPG AIIVNNHHSS
EFLLKTVTLH DVPGRGNLSF VANSWIYPVG SYTYSRVFFA NDTYLPSQMP AALKPYRDDE
LRNLRGDDRQ GPYQEHDRVY RYDVYNDLGE GRPVLGGSAE HPYPRRGRTG RKPNANDPSL
ESRLSLLEQI YVPRDEKFGH LKTSDFLGYS IKAITQGILP AVRTYVDTTP GEFDSFQDII
NLYEGGIKLP NVPALEELRK QFPLQLIKDL LPVGGDSLLK LPVPHIIQAD QQAWRTDEEF
SREVLAGVNP VMITRLTEFP PKSSLDPSKF GDHTSTVTAA HIEKNLEGLT VQQALESNRL
YILDHHDRFM PFLIDVNNLP GNFIYATRTL FFLRGDGRLT PLAIELSEPV IQGGLTTAKS
KVYTPVPSGS VEGWVWEFAK AYVAVNDSGW HQLVSHWLNT HAVMEPFVIS TNRQLSVTHP
VHKLLSPHYR DTMTINALAR QTLINAGGIF EMTVFPGKFA LGMSSVVYKD WKFTEQGLPD
DLIKRGMAVE DPSSPYKVRL LVSDYPYAAD GLAIWHAIEQ YVSEYLAIYY PNDGVVQGDV
ELQAWWKEVR EVGHGDLKVA PWWPRMQAVG ELAKACTTII WIGSALHAAV NFGQYPYAGF
LPNRPTVSRR RMPEPGTEQY AELERDPERA FIHTITSQIQ TIIGISLLEV LSKHSSDELY
LGQRDTPEWT SDPKALEVFK RFSERLVEIE SKVVGMNHDP QLLNRNGPAK FPYMLLYPNT
SDHKGAAAGL TAKGIPNSIS I
//
