ID A0A2J6JKI5_LACSA Unreviewed; 799 AA.
AC A0A2J6JKI5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=LSAT_9X86541 {ECO:0000313|EMBL:PLY63334.1};
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY63334.1};
RN [1] {ECO:0000313|EMBL:PLY63334.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28401891; DOI=10.1038/ncomms14953;
RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT "Genome assembly with in vitro proximity ligation data and whole-genome
RT triplication in lettuce.";
RL Nat. Commun. 8:14953-14953(2017).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLY63334.1}.
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; NBSK01011025; PLY63334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6JKI5; -.
DR STRING; 4236.A0A2J6JKI5; -.
DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_9X86541_mrna; cds-PLY63334.1; gene-LSAT_9X86541.
DR Gramene; rna-gnl|WGS:NBSK|LSAT_9X86541_mrna; cds-PLY63334.1; gene-LSAT_9X86541.
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; 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 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; 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:SF150; 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 1..98
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 101..799
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 148..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 91747 MW; 9671DB37F1E4FCD0 CRC64;
MFTERNLKGK VGKPARLEDW ITTITPLTDG ESTYKVTFEW DEDTEVPGAF LVQNHHHSEF
YLKTLTLEDV PGHGHVHFVC NSWVYPTKRY KKDRIFFTNK AYLPSETPEF LRSYRDEELE
ILRGDGTGML EEWDRVYDYA FYNDLGNPDK DPDDARPVLG GSSEYPYPRR GRTGRPPTKS
DPNTESRLPL LMSLNIYVPR DERFGHLKLS DFLAYGLKSI VQFLLPEFQA LCDTTHDEFD
SFEDIYKLYE GGFKLPGGPL LDRIRENIPL ELLKIVLETD SDGIAKFPKP QVIKEDKSAW
RTDEEFAREM LAGVNPVKIC LLKEFPPTSK LDVKIYGNQN SSIKPHHIEK NLNGLKVDEV
LKANRLFILD HHDSLMPYLR RINATTNKIY ASRTLLLLQN DGTLKPLVIE LSLPHPDGDN
LGAISNVYTP AENGVEGSIW KLAKAYVAVN DSGIHQLISH WLHTHAVVEP FVIAANRQLS
VLHPIYKLLY PHFRDTMNIN AFARQILING GGILELTVFP GKYSMELSSV LYKDWVFPEQ
ALPVDLVKRG MAIEDSDSHH GLRLLIDDYP YAVDGLEIWS AIKSWVEDYC KFYYKNDDMI
QNDTELQSWW KELREEGHGD KKHEPWWPKM DSCQELINIC TTFIWVASAL HASVNYGQYP
YAGFLPNRPT LSRRFMPEPN TPEYDELKEN PDDVFLKTIT PQLQTLLGIA LIELLSRHSS
DEVYLGQREC PEWTMDAEPL KAFEKFGKKL KDIEEKIVKM NNDEKLKNRI GPVNVPYTLL
YPTSEEGLTG KGIPNSTSM
//
