ID LOXB_SOLLC Reviewed; 859 AA. AC P38416; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 02-SEP-2026, entry version 135. DE RecName: Full=Linoleate 9S-lipoxygenase B; DE EC=1.13.11.58; DE AltName: Full=Lipoxygenase B; GN Name=LOX1.2; Synonyms=LOXB; 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; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Caruso; TISSUE=Pericarp; RX PubMed=7972514; DOI=10.1104/pp.106.1.109; RA Ferrie B.J., Beaudoin N., Burkhart W., Bowsher C.G., Rothstein S.J.; RT "The cloning of two tomato lipoxygenase genes and their differential RT expression during fruit ripening."; RL Plant Physiol. 106:109-118(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 -!- TISSUE SPECIFICITY: Fruit specific. 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; U09025; AAA53183.1; -; mRNA. DR PIR; T06339; T06339. DR AlphaFoldDB; P38416; -. DR SMR; P38416; -. DR FunCoup; P38416; 97. DR STRING; 4081.P38416; -. DR PaxDb; 4081-P38416; -. DR eggNOG; ENOG502QQSP; Eukaryota. DR InParanoid; P38416; -. DR UniPathway; UPA00382; -. DR Proteomes; UP000004994; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IEA:UniProtKB-ARBA. DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. 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; 4.10.372.10:FF:000001; 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..859 FT /note="Linoleate 9S-lipoxygenase B" FT /id="PRO_0000220706" FT DOMAIN 34..158 FT /note="PLAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152" FT DOMAIN 161..859 FT /note="Lipoxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT REGION 213..246 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 233..244 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 521 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" 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 711 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 859 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" SQ SEQUENCE 859 AA; 97122 MW; DAD79B10AE627434 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 PFVVATNRHL 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 //