ID LOX2_SOYBN Reviewed; 865 AA. AC P09439; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 02-SEP-2026, entry version 144. DE RecName: Full=Seed linoleate 9S-lipoxygenase-2; DE EC=1.13.11.58; DE AltName: Full=Lipoxygenase-2; DE Short=L-2; GN Name=LOX1.2; Synonyms=LOX2; OS Glycine max (Soybean) (Glycine hispida). 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; Glycine; OC Glycine subgen. Soja. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2834391; DOI=10.1016/s0021-9258(18)68716-2; RA Shibata D., Steczko J., Dixon J.E., Andrews P.C., Hermodson M., Axelrod B.; RT "Primary structure of soybean lipoxygenase L-2."; RL J. Biol. Chem. 263:6816-6821(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-865. RX AGRICOLA=IND87003970; DOI=10.1007/BF00020127; RA Start W.G., Ma Y., Polacco J.C., Hildebrand D.F., Freyer G.A., RA Altschuler M.; RT "Two soybean seed lipoxygenase nulls accumulate reduced levels of RT lipoxygenase transcripts."; RL Plant Mol. Biol. 7:11-23(1986). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 859-865. RX PubMed=1909908; DOI=10.1007/bf00020569; RA Shibata D., Kato T., Tanaka K.; RT "Nucleotide sequences of a soybean lipoxygenase gene and the short RT intergenic region between an upstream lipoxygenase gene."; RL Plant Mol. Biol. 16:353-359(1991). 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. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: Soybean contains at least 4 distinct isoenzymes, L-1, L- CC 2, L-3a and L-3b in dry seeds, and at least two distinct isozymes in CC the hypocotyl/radicle region of the seedling stem. CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=Ref.2; Type=Frameshift; Evidence={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; J03211; AAA33987.1; -; mRNA. DR EMBL; X56139; CAA39605.1; -; Genomic_DNA. DR PIR; A28161; DASYL1. DR AlphaFoldDB; P09439; -. DR SMR; P09439; -. DR STRING; 3847.P09439; -. DR PaxDb; 3847-P09439; -. DR eggNOG; ENOG502QQSP; Eukaryota. DR InParanoid; P09439; -. DR UniPathway; UPA00382; -. DR Proteomes; UP000008827; Unplaced. 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; Reference proteome. FT CHAIN 1..865 FT /note="Seed linoleate 9S-lipoxygenase-2" FT /id="PRO_0000220718" FT DOMAIN 50..175 FT /note="PLAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152" FT DOMAIN 178..865 FT /note="Lipoxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT REGION 234..265 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 255..265 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 532 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 718 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 722 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 865 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT CONFLICT 263..264 FT /note="KP -> NL (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="D -> Y (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 400 FT /note="L -> P (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 428 FT /note="L -> H (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 486 FT /note="D -> G (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 502 FT /note="V -> G (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 534 FT /note="V -> L (in Ref. 2)" FT /evidence="ECO:0000305" SQ SEQUENCE 865 AA; 97146 MW; 74CBD32E3E4A0C85 CRC64; MFSVPGVSGI LNRGGGHKIK GTVVLMRKNV LDFNSVADLT KGNVGGLIGT GLNVVGSTLD NLTAFLGRSV ALQLISATKP LANGKGKVGK DTFLEGIIVS LPTLGAGESA FNIQFEWDES MGIPGAFYIK NYMQVEFYLK SLTLEDVPNQ GTIRFVCNSW VYNTKLYKSV RIFFANHTYV PSETPAALVG YREEELKNLR GDGKGERKEH DRIYDYDVYN DLGNPDHGEN FARPILGGSS THPYPRRGRT GRYPTRKDQN SEKPGEVYVP RDENFGHLKS SDFLAYGIKS LSQYVLPAFE SVFDLNFTPN EFDSFQDVRD LHEGGIKLPT EVISTIMPLP VVKELFRTDG EQVLKFPPPH VIQVSKSAWM TDEEFAREMV AGVNPCVIRG LQEFPPKSNL DPTIYGEQTS KITADALDLD GYTVDEALAS RRLFMLDYHD VFMPYIRRIN QTYAKAYATR TILFLRENGT LKPVAIELSL PHPAGDLSGA VSQVILPAKE GVESTIWLLA KAYVVVNDSC YHQLMSHWLN THAVIEPFII ATNRHLSALH PIYKLLTPHY RDTMNINALA RQSLINADGI IEKSFLPSKH SVEMSSAVYK NWVFTDQALP ADLIKRGVAI KDPSAPHGLR LLIEDYPYAV DGLEIWAAIK TWVQEYVSLY YARDDDVKPD SELQQWWKEA VEKGHGDLKD KPWWPKLQTI EELVEICTII IWTASALHAA VNFGQYPYGG FILNRPTSSR RLLPEKGTPE YEEMVKSHQK AYLRTITSKF QTLVDLSVIE ILSRHASDEV YLGQRDNPHW TSDSKALQAF QKFGNKLKEI EEKLARKNND QSLSNRLGPV QLPYTLLHPN SEGLTCRGIP NSISI //