ID E5F115_TRITD Unreviewed; 861 AA.
AC E5F115;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 22-FEB-2023, entry version 61.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=Lpx-B1.2 {ECO:0000313|EMBL:ADR71857.1};
OS Triticum turgidum subsp. durum (Durum wheat) (Triticum durum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4567 {ECO:0000313|EMBL:ADR71857.1};
RN [1] {ECO:0000313|EMBL:ADR71857.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PRI1.2 {ECO:0000313|EMBL:ADR71857.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:ADR71857.1}, and Mature grains
RC {ECO:0000313|EMBL:ADR71862.1};
RX PubMed=21110856; DOI=10.1186/1471-2229-10-263;
RA Verlotta A., De Simone V., Mastrangelo A.M., Cattivelli L., Papa R.,
RA Trono D.;
RT "Insight into durum wheat Lpx-B1: a small gene family coding for the
RT lipoxygenase responsible for carotenoid bleaching in mature grains.";
RL BMC Plant Biol. 10:263-263(2010).
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; HM126467; ADR71857.1; -; Genomic_DNA.
DR EMBL; HM126472; ADR71862.1; -; mRNA.
DR AlphaFoldDB; E5F115; -.
DR UniPathway; UPA00382; -.
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 2: Evidence at transcript level;
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..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 96026 MW; 3E646B87C03ECB2D CRC64;
MILGGLVDSL TGANKSARLQ 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 RFSERLAEIE SKVVGMNHDP QLLNRNGPAK FPYMLLYPNT
SDHKGAAAGL TAKGIPNSIS I
//
