ID W1PUB1_AMBTC Unreviewed; 906 AA.
AC W1PUB1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=AMTR_s00022p00208630 {ECO:0000313|EMBL:ERN11648.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN11648.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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 EMBL; KI392687; ERN11648.1; -; Genomic_DNA.
DR RefSeq; XP_006850067.1; XM_006850004.2.
DR AlphaFoldDB; W1PUB1; -.
DR STRING; 13333.W1PUB1; -.
DR EnsemblPlants; ERN11648; ERN11648; AMTR_s00022p00208630.
DR GeneID; 18439847; -.
DR Gramene; ERN11648; ERN11648; AMTR_s00022p00208630.
DR KEGG; atr:18439847; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR OMA; CRITASQ; -.
DR OrthoDB; 462210at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
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:SF89; LIPOXYGENASE 2, CHLOROPLASTIC; 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:UP000017836}.
FT DOMAIN 72..205
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 208..906
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 255..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 102247 MW; B0D93EC9DC57B184 CRC64;
MMNSQVQAGS RSALLVVPNP ILRPSRDSLV RLNRPGSWPG NRRKVGMGKV FAVIWDRSVS
KKTGDNVITV KAKATVKVTV GGELTNVGLG RGVGDLLEVL GKSVRLELVS EELDPQTGLE
KPTMKGYLHR KIGLNGLDVV EYEGEFKVSP SFGAVGAVLV RNEHHKEMYF ESIVLNGFDQ
GPIQITCNSW VHARSDNPED RVFFSDKSYL PPVTPAGLKK LREKELETLR GNGQGERKDF
ERIYDYDKYN DLGNPDDADT ARPVLGGKDH PYPRRCRTGR PMTRTDPLSE SRLKILVDSP
YVPRDEAFSE LKQAQFGLKT LKSVLHALIP GVEAFVEDKN MGFDFFTDID LLFKHGVKFH
KTDGEGSVLN SLLLPRLVKK AVDGGSDVLQ FEMPSIMDRD KFSWMRDEEF ARQTIAGINP
YCIELVKEFP FVSTLDPKIY GPTESAITKE IIEREIKGVM TVEEAVAQKK LFVLDYHDIL
MPYVNKVRAL EGTTLYASRT VFFLTHLGTL QPVAIELVRP RSETEDAWRK VFTQGIDHTT
AWLWKLAKCH VAAHDSGMHQ LVSHWLRTHC CTEPYVIAAN RQLSAMHPIY RLLQPHFRYT
MEINALARQS LINADGIIES CFSPMKYSIE LSSYAYDLTW RFDKEALPAD LIKRGLAEED
PTAEHGVKLV IEDYPFANDG LLIWSAIKQW VTDYVSYYYS NPGSVQSDTE LQAFWEEVRT
KGHEDKKDEP WWPVLKTNDD LIQVLSTIVW VVSGHHAAVN FGQYPYGGYF PNRPTITRNN
LPVENESCAE FKRFLEKPET TLLSSFPSQL QATKVMTILD VLSSHSPEEE YLGGQVEPEW
ALVPEIRAAF EKFSGRMKEI EGIIDQRNTD LELRNRTGAG VVPYELLKPF SEPGVTGKGV
PTSISI
//
