ID LOXB_PHAVU Reviewed; 741 AA. AC P27481; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 24-JAN-2024, entry version 115. DE RecName: Full=Linoleate 9S-lipoxygenase; DE EC=1.13.11.58; DE AltName: Full=Lipoxygenase; DE EC=1.13.11.12; DE Flags: Fragment; 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 [MRNA]. RC STRAIN=cv. Red Mexican; TISSUE=Leaf; RX PubMed=8400375; DOI=10.1094/mpmi-6-453; RA Slusarenko A.J., Meier B.M., Shaw N.; RT "Spatial and temporal accumulation of defense gene transcripts in bean RT (Phaseolus vulgaris) leaves in relation to bacteria-induced hypersensitive RT cell death."; RL Mol. Plant Microbe Interact. 6:453-466(1993). 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 -!- 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 -!- 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; X63521; CAA45086.1; -; mRNA. DR PIR; S18906; S18906. DR AlphaFoldDB; P27481; -. DR SMR; P27481; -. DR eggNOG; ENOG502QQSP; Eukaryota. 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 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; IPR027433; Lipoxygenase_dom_3. DR InterPro; IPR001024; PLAT/LH2_dom. DR InterPro; IPR036392; PLAT/LH2_dom_sf. DR PANTHER; PTHR11771:SF122; LINOLEATE 9S-LIPOXYGENASE-4; 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 Cytoplasm; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism; KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase; KW Oxylipin biosynthesis. FT CHAIN <1..>741 FT /note="Linoleate 9S-lipoxygenase" FT /id="PRO_0000220716" FT DOMAIN <1..53 FT /note="PLAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152" FT DOMAIN 56..741 FT /note="Lipoxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT REGION 108..144 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 407 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 412 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 598 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT BINDING 602 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT NON_TER 1 FT NON_TER 741 SQ SEQUENCE 741 AA; 84197 MW; 2F2CDD5979606AC1 CRC64; IPGAFYIKNF MQVEFYLKSL TLEDIPNHGT IHFICNSWIY NSKVYKSDRI FFANNTYLPS ETPAPLLKYR EEELKNVRGD GSGERKEWDR VYDYDVYNDL GNPDKGAALA RPVLGGSTLP YPRRGRTGRP KTKKDPNSEK PSDFVYLPRD EAFGHLKSSD FLAYGLKSVS QDVLPVLTDA FDGNLLSLEF DNFAEVHKLY EGGVTLPTNF LSKYAPIPIV KEIFRSDGEQ FLKYPPPKVM QVNKSAWMTD EEFARETIAG VNPNVIKSLE EFPPRSKLDT QSFGDHTSII TKEHLEINLG GLTVEQAIQS KKLFILDHHD YLIPYLRRIN ASATKTYATR TIFFLKSDGT LAPLAIELSK PHPQGDEHGP VSEVYVPAYE GVEAYIWLLA KAYVVVNDSC YHQLVSHWLN THAVVEPFVL ATNRQLSVVH PVYKLLFPHY RDTMNINSLA RKSLVNADGI IEKTFLWGRY ALELSAVIYK DWSLHDQALP NDLVKRGVAV KDPSAPHGVK LVIEDYPYAS DGLEIWDAIK SWVVEYVAFY YKSDEVLQQD SELQAWWKEL VQVGHGDLKD KPWWPKMQSR ENLVEVSTTL IWIASALHAA VNFGQYPYGG LILNRPTISR RFMPEKGSAE YAALAKNPEK EFLKTITGKK ETLIDLTVIE ILSRHASDEI YLGERDGGDH WTSDAGPLEA FKRFGKKLAE IEKKLVQKNN DETLRNRTGP AKMPYTLLYP SSEEGLTFRG I //