ID Q42873_SOLLC Unreviewed; 859 AA.
AC Q42873;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 08-NOV-2023, entry version 139.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=LOX {ECO:0000313|EMBL:AAA74393.1};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EMBL:AAA74393.1};
RN [1] {ECO:0000313|EMBL:AAA74393.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Rutgers {ECO:0000313|EMBL:AAA74393.1};
RC TISSUE=Fruit pericarp {ECO:0000313|EMBL:AAA74393.1};
RX PubMed=7724686; DOI=10.1104/pp.107.2.669;
RA Kausch K.D., Handa A.K.;
RT "Molecular cloning and nucleotide sequence of a lipoxygenase cDNA from
RT ripening tomato fruit.";
RL Plant Physiol. 107:669-670(1995).
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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; U13681; AAA74393.1; -; mRNA.
DR PIR; T06352; T06352.
DR RefSeq; NP_001234873.2; NM_001247944.2.
DR AlphaFoldDB; Q42873; -.
DR SMR; Q42873; -.
DR ProMEX; Q42873; -.
DR GeneID; 543997; -.
DR KEGG; sly:543997; -.
DR OrthoDB; 999249at2759; -.
DR UniPathway; UPA00382; -.
DR ExpressionAtlas; Q42873; 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:SF100; LINOLEATE 9S-LIPOXYGENASE B; 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..158
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 161..859
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 213..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 97136 MW; 738DE7E070A793C8 CRC64;
MSLGGIVDAI LGKDDRPKVK GRVILMKKNV LDFINIGASV VDGISDLLGQ KVSIQLISGS
VNYDGLEGKL SNPAYLESWL TDITPITAGE STFSVTFDWD RDEFGVPGAF IIKNLHLNEF
FLKSLTLEDV PNYGKIHFVC NSWVYPAFRY KSDRIFFANQ AYLPSETPQP LRKYRENELV
ALRGDGTGKL EEWDRVYDYA CYNDLGEPDK GEEYARPILG GSSEYPYPRR GRTGREPTKA
DPNCESRNPL PMSLDIYVPR DERFGHVKKS DFLTSSLKSS LQTLLPAFKA LCDNTPNEFN
SFADVLNLYE GGIKLPEGPW LKAITDNISS EILKDILQTD GQGLLKYPTP QVIQGDKTAW
RTDEEFGREM LAGSNPVLIS RLQEFPPKSK LDPTIYGNQN STITTEHVQD KLNGLTVNEA
IKSNRLFILN HHDIVMPLLR KINMSANTKA YASRTLLFLQ DDRTLKPLAI ELSLPHPDGD
QFGTVSKVYT PADQGVEGSI WQFAKAYVAV NDMGIHQLIS HWLNTHAVIE PFVIATNRHL
SVLHPIHKLL HPHFRNTMNI NALARETLTY DGGFETSLFP AKYSMEMSAA AYKDWVFPEQ
ALPADLLKRG VAVEDLSSPH GIRLLILDYP YAVDGLEIWA AIKSWVTEYC KFYYKSDETV
EKDTELQAWW KELREEGHGD KKDEAWWPKL QTRQELRDCC TIIIWIASAL HAALHFGLYS
YAGYLPNRPT LSCNLMPEPG SVEYEELKTN PDKVFLKTFV PQLQSLLEIS IFEVSSRHAS
DEVYLGQRDS IEWTKDKEPL VAFERFGKML SDIENRIMIM NSHKSWKNRS GPVNVPYTLL
FPTSEEGLTG KGIPNSVSI
//
