ID I3NM23_WHEAT Unreviewed; 861 AA.
AC I3NM23;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 28-JUN-2023, entry version 73.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=Lpx {ECO:0000313|EMBL:AHG59317.1};
GN ORFNames=4K11.1 {ECO:0000313|EMBL:ADP02185.1};
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|EMBL:ADP02185.1};
RN [1] {ECO:0000313|EMBL:ADP02185.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22592657; DOI=10.1007/s10142-012-0283-2;
RA Duan J., Wu J., Liu Y., Xiao J., Zhao G., Gu Y., Jia J., Kong X.;
RT "New cis-regulatory elements in the Rht-D1b locus region of wheat.";
RL Funct. Integr. Genomics 12:489-500(2012).
RN [2] {ECO:0000313|EMBL:AHG59317.1}
RP NUCLEOTIDE SEQUENCE.
RA Garbus I., Romero J.R., Echenique V.C.;
RT "Triticum aestivum lipoxygenases-1.";
RL Submitted (FEB-2013) 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; HQ435327; ADP02185.1; -; Genomic_DNA.
DR EMBL; KC679302; AHG59317.1; -; Genomic_DNA.
DR AlphaFoldDB; I3NM23; -.
DR Gramene; TraesKAR4D01G0013080.1; cds.TraesKAR4D01G0013080.1; TraesKAR4D01G0013080.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR OrthoDB; 462210at2759; -.
DR UniPathway; UPA00382; -.
DR ExpressionAtlas; I3NM23; baseline and differential.
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}.
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..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 95979 MW; 12422DC009D0F245 CRC64;
MILGGLIDSL TGANKNARLK GTAVLMRKNV LDLTDFGATI MDGIGDFLGK GVTCQLISST
LIDHDNGGRG KVGAEAELEQ WVTSLPSLTT GESKFGLTFD WEVEKLGVPG AIVVNNYHSS
EFLLKTVTLH DVPGRGNLSF VANSWIYPAA TYTYSRVFFA NDTYLPSQMP AALKPYRDDE
LRNLRGDDRQ GPYQEHDRVY RYDVYNDLGE GRPVLGGSAE HPYPRRGRTG RKPNASDPSL
ESRLSLLEQI YVPRDEKFGH LKTSDFLGYS IKAITQGILP AVRTYVDTTP GEFDSFQDIM
NLYEGGIKLP MVPALEELRK QFPLQLIKDL LPVGGDSLLK LPVPHIIQAD QQAWRTDEEF
AREVLAGVNP VMITRLTEFP PKSSLDPSKF GDHTSTITAA HIQKNLEGLT VQQALESNRL
YILDHHDRFM PFLIEVNNLP GNFIYATRTL FFLRGDGRLT PLAIELSEPV ILGGLTTAKS
KVYTPVPSGS VEGWVWEFAK AYVAVNDSGW HQLVSHWLNT HAVMEPFVIS TNRHLSVTHP
VHKLLSPHYR DTMTINALAR QTLINAGGIF EMTVFPGKFA LGMSSVVYKD WKFTEQGLPD
DLIKRGMAVE DLSSPYKVRL LVSDYPYAAD GLAIWHAIEQ YVGEYLAIYY PDDGVLRGDT
ELQAWWKEAR EVGHGDLKDA PWWPRMQGVG ELAKACTTII WIGSALHAAV NFGQYPYAGF
LPNRPTVSRR RMPEPGTDAY AELERDPERA FIHTITSQIQ TIIGISLLEV LSKHSSDELY
LGQRDTPEWT SDPKALEVFK RFSERLVEIE SKVVGMNHDP QLLNRNGPAK LPYMLLYPNT
SDHKGAAAGL TAKGIPNSIS I
//
