ID LOX1_LENCU Reviewed; 866 AA. AC P38414; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 02-SEP-2026, entry version 115. DE RecName: Full=Linoleate 9S-lipoxygenase; DE EC=1.13.11.58; DE AltName: Full=Lipoxygenase; GN Name=LOX1.1; OS Lens culinaris (Lentil) (Cicer lens). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Lens. OX NCBI_TaxID=3864; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Seedling shoot; RX PubMed=8117753; DOI=10.1016/0005-2760(94)90275-5; RA Hilbers M.P., Rossi A., Finazzi-Agro A., Veldink G.A., Vliegenthart J.F.G.; RT "The primary structure of a lipoxygenase from the shoots of etiolated RT lentil seedlings derived from its cDNA."; RL Biochim. Biophys. Acta 1211:239-242(1994). 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. It catalyzes the CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene CC structure. CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)- CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00726}; CC Note=Binds 1 Fe cation per subunit. Iron is tightly bound. CC {ECO:0000255|PROSITE-ProRule:PRU00726}; CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE- CC ProRule:PRU00726}. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}. 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; X71344; CAA50483.1; -; mRNA. DR AlphaFoldDB; P38414; -. DR SMR; P38414; -. DR UniPathway; UPA00382; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-ARBA. DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0034440; P:lipid oxidation; IEA:InterPro. DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01751; PLAT_LH2; 1. DR FunFam; 1.20.245.10:FF:000002; Lipoxygenase; 1. DR FunFam; 3.10.450.60:FF:000002; Lipoxygenase; 1. DR FunFam; 4.10.375.10:FF:000001; Lipoxygenase; 1. DR Gene3D; 3.10.450.60; -; 1. DR Gene3D; 4.10.375.10; Lipoxygenase-1, Domain 2; 1. DR Gene3D; 4.10.372.10; Lipoxygenase-1, Domain 3; 1. DR Gene3D; 1.20.245.10; Lipoxygenase-1, Domain 5; 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 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 Cytoplasm; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism; KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase; KW Oxylipin biosynthesis. FT CHAIN 1..866 FT /note="Linoleate 9S-lipoxygenase" FT /id="PRO_0000220704" FT DOMAIN 42..171 FT /note="PLAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152" FT DOMAIN 174..866 FT /note="Lipoxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT REGION 226..262 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 242..251 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 252..262 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 526 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 531 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 717 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 721 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 866 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" SQ SEQUENCE 866 AA; 96639 MW; E3E5D00E84E3C89C CRC64; MASLLFGRGQ KLKGTVILMQ KNVLDINALT AAQSPSGIIG GAFGVVGSIA GSIIDTATAF LGRSVRLRLI SATVADASGK GKVSKEAFLE GLLTSIPTLG DKQSAFSVHF EWDSNMGTPG AFYIENFMQG GEFFLVSLTL DDVPNVGSIK FACNSWIYND KKYQSDRIFF ANKTYLPSAT PAPLVSYRQE ELKTLRGDGT GERQEWDRIY DYDVYNDLGA PDQKATLGRP VLGGSSTLPY PRRGRTGRKK TVKEPQSESR SDTVYLPRDE AFGHVKSSDF LVYILKSASQ NIVPQLRSVV TLQLNNPEFN TFEDVRSLYD GGIKLPTDVL SKISPIPLFS ELFRSDGEAA LKFPPPKVIQ VDHSAWMTDE EFAREMIAGV NPHIIKEVLS FPIKSKLDSQ LYGDNTSKIT KEHLEPNLGG VTVEGAIQTN RLFTPDHHDA LFPYLRKINA TATKAYATRT VLFLQDNGTL KPLAIELSTP HPDGDSFGPV SKVYLPASEG VEASIWLLAK AFVVVNDSCY HQLVSHWLNT HAVVEPFIIA TNRHLSVVHP IHKLLLPHYR DTMNINALAR NVLVNAEGII ESTFLWGNYA MEMSAVVYKD WVFPDQGLPN DLIKRGVAVK DPSSPHGVRL LIEDYPYASD GLEIWAAIKS WVEEYVNFYY KSDAAIAQDA ELQAFWKELV EVGHGDLKSA TWWFKMQNRK ELIEACSILI WIASALHAAV NFGQYPYGGY ILNRPTKSRK FMPEKGTPEY DDLAKNYEKA YLRTITPKND TLTDLTIIEV LSRHASDEQY LGERIEGDDW TTDSVPKEAF KRFGKKLAEI EEKLTQRNND ESLRNRYGPV KMPYTLLYPS SEEGLTCRGI PNSISI //