ID LOXA_PHAVU Reviewed; 862 AA. AC P27480; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 24-JAN-2024, entry version 118. DE RecName: Full=Linoleate 9S-lipoxygenase 1; DE EC=1.13.11.58; DE AltName: Full=Lipoxygenase 1; DE EC=1.13.11.12; GN Name=LOXA; Synonyms=LOX1; OS Phaseolus vulgaris (Kidney bean) (French bean). 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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus. OX NCBI_TaxID=3885; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Red Mexican; TISSUE=Leaf; RX PubMed=8130796; DOI=10.1046/j.1365-313x.1994.5010123.x; RA Eiben H.G., Slusarenko A.J.; RT "Complex spatial and temporal expression of lipoxygenase genes during RT Phaseolus vulgaris (L.) development."; RL Plant J. 5:123-135(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 = (13S)-hydroperoxy-(9Z,11E)- CC octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13S)-hydroperoxy- CC (9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:34495, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:58757; CC EC=1.13.11.12; 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. 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; X63525; CAA45088.1; -; Genomic_DNA. DR PIR; S22153; S22153. DR AlphaFoldDB; P27480; -. DR SMR; P27480; -. DR ProMEX; P27480; -. DR eggNOG; ENOG502QQSP; Eukaryota. DR SABIO-RK; P27480; -. DR UniPathway; UPA00382; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IEA:UniProtKB-EC. DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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-UniPathway. 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:SF101; 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 Cytoplasm; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism; KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase; KW Oxylipin biosynthesis. FT CHAIN 1..862 FT /note="Linoleate 9S-lipoxygenase 1" FT /id="PRO_0000220715" FT DOMAIN 44..171 FT /note="PLAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152" FT DOMAIN 174..862 FT /note="Lipoxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT REGION 225..257 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 522 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 527 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 713 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 862 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" SQ SEQUENCE 862 AA; 97155 MW; 24D56D1CEE3C191E CRC64; MFGILNRGHK IKGTVVLMTK NVFDFNEFVS TTRGGIVGAA GGLFGAATDI VGGIVDGATA IFSRNIAIQL ISATKTDGLG NGKVGKQTFL EKHLPSLPNL GDRQDAFNVY FEWDENFGIP EAFYIKNFMQ SEFFLVSLTL EDIPNHGTIH FVCNSWVYNA KSYKRDRIFF ANKTYLPNET PASLVKYRKE ELENLRGDGT GERKEYDRIY DYAVYNDLGN PDKNKNLART TLGGSSDFPY PRRGRTGRKS TRKDPKCEIP TSDTYIPRDE NFGHLKSGDF LTYAIKSLTQ NVLPTFQKAF GFNNEFDTFE DVRGLFEGGL YLPTDVISKI SPIPVLKEIL RTDGEQVLKF PPPHVIRVTK SAWMTDEEFG REMLAGVNPC LIQRLQEFPP KSKLDVTVYG DQTSTMTKEH LEINLGGLTV EEALHGNRLF ILDHHDAFIP YLERINDLPT AKCYATRTIL FLKDDNTLKP LAIELSLPNP GGKGANSRVI LPADGGAEST IWLLAKAYVV VNDSCYHQLM SHWLNTHAVM EPFVIATNRH LSVLHPIYKL LLPHYRDTMN INALARQSLI NAGGVIERSF LPGEFAVEMS SAVYKSWVFT DQALPADLIK RGMAVEDPSS PYGLRLVVED YPYAVDGLEI WDTIQTWVKD YVSLYYPTND AVKKDTELQA WWKEAVEKGH GDLKDKPWWP KLNTPQDLIH TCSIIIWIAS ALHAAVNFGQ YPYGGFILNR PTITRRLLPE PGTKEYGELT SNYQKAYLRT ITGKVEAIVD LSVIEILSRH ASDEVYLGQR DNPNWTNNIK ALQAFKRFGQ KLKEIEEKIM GRNKDSSLRN RNGPVKMPYT VLLPTCEDEG LTFRGIPNSI SI //