ID A0A3B6HM35_WHEAT Unreviewed; 923 AA.
AC A0A3B6HM35;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=CFC21_050875 {ECO:0000313|EMBL:KAF7041035.1};
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:TraesCS4A02G009400.1};
RN [1] {ECO:0000313|EMBL:KAF7041035.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7041035.1};
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:TraesCS4A02G009400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS4A02G009400.1};
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:TraesCS4A02G009400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7041035.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7041035.1};
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; CM022220; KAF7041035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6HM35; -.
DR SMR; A0A3B6HM35; -.
DR STRING; 4565.A0A3B6HM35; -.
DR PaxDb; 4565-Traes_4AS_4A582A66D-1; -.
DR EnsemblPlants; TraesCS4A02G009400.1; TraesCS4A02G009400.1; TraesCS4A02G009400.
DR Gramene; TraesCAD_scaffold_012100_01G000500.1; TraesCAD_scaffold_012100_01G000500.1; TraesCAD_scaffold_012100_01G000500.
DR Gramene; TraesCLE_scaffold_011885_01G000100.1; TraesCLE_scaffold_011885_01G000100.1; TraesCLE_scaffold_011885_01G000100.
DR Gramene; TraesCS4A02G009400.1; TraesCS4A02G009400.1; TraesCS4A02G009400.
DR Gramene; TraesCS4A03G0015900.1; TraesCS4A03G0015900.1.CDS; TraesCS4A03G0015900.
DR Gramene; TraesKAR4A01G0004050.1; cds.TraesKAR4A01G0004050.1; TraesKAR4A01G0004050.
DR Gramene; TraesPAR_scaffold_012396_01G000100.1; TraesPAR_scaffold_012396_01G000100.1; TraesPAR_scaffold_012396_01G000100.
DR Gramene; TraesRN4A0100017100.1; TraesRN4A0100017100.1; TraesRN4A0100017100.
DR Gramene; TraesROB_scaffold_027995_01G000100.1; TraesROB_scaffold_027995_01G000100.1; TraesROB_scaffold_027995_01G000100.
DR Gramene; TraesWEE_scaffold_008664_01G000100.1; TraesWEE_scaffold_008664_01G000100.1; TraesWEE_scaffold_008664_01G000100.
DR OMA; QRTHAIM; -.
DR OrthoDB; 462210at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000019116; Chromosome 4A.
DR Proteomes; UP000815260; Chromosome 4A.
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; LIPOXYGENASE; 1.
DR PANTHER; PTHR11771:SF113; LIPOXYGENASE 6-RELATED; 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 84..221
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 226..923
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 8..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 923 AA; 102154 MW; 2D5050A727EEDE88 CRC64;
MAASCRELAG AGLARPATSS SQPGRSRNDL CFAPLRQEGR GHQGRIRRRG VKVVAAVSEE
LPRLASAGKG AGAAARPPQG KVALRAAVTV RRKQKEDLKE AVAGHLDALW DMVGRGVLLE
LVSTKIDPRT SKAVRSGGAS IKDWCAKRGA RGEHVVYTAE FTVDAGFGEP GAVVVANRHH
REFFLESVVV EGALPCGTVY FDCNSWVQTT GELPGDGNRV FFSNKPYLPS QTPPGLREIR
EKVLRDLRGD GTGVRKISDQ IYDYAMYNDL GNPDRGKEFI RPILGGDKIP YPRRCRTGRP
PTDTNMLSES RVEKPHRIYV PRDETFEELK QGAFISGRLR AVLHTLIPSL IASISAETHN
FQGFHHVDNL YKEGLRLKLG LQEHLFQKIP FVQKIQESSE GMLRYDTPSI LSKDKFAWLR
DDEFARQAVA GINPVSIERL TVFPPVSKLD PATYGPPESS ITEQHIAGQL NGLTVQEAID
KEKLFIVDHH DVYMPFLDRI NAIEGRKAYA TRAIFFLTQG GTLKPVAIEL SLPPAQSGEP
QPSKVLTPAC DATSNWIWML GKAHVSSNDA GVHQLVNHWL RTHAIMEPFI LAAHRRMSAM
HPIFKLLHPH MRYTLEINAL ARQSLINAEG VIESCFTPGP VSGEISSAYY GNHWRFDLEG
LPADLLRRGV AVEDATQPHG IRLLIEDYPY ANDGLLLWSA IGNWVESYVQ LYYPDAGTVQ
SDDELQEWYH ESIHVGHADL RDAPWWPPLS TPRDLANILT TLVWLASAQH AALNFGQYPL
GGYVPNRPPL MRRLLPDPER DAAEYAMFLA DPHRFFLNAM PGVLEATKFM AVVDTLSTHS
PDEEYLGESL DEGAAPWTGD EEALAAHGMF AADVRRAEET IERRNADHGR RNRCGAGVLP
YELLAPSSPP GVTCRGVPNS ISI
//
