ID LOX18_SOLTU Reviewed; 861 AA. AC O22508; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 08-NOV-2023, entry version 120. DE RecName: Full=Probable linoleate 9S-lipoxygenase 8; DE EC=1.13.11.58; GN Name=LOX1.8; Synonyms=PLOX2; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Lemhi Russet; TISSUE=Tuber; RX DOI=10.1034/j.1399-3054.1998.1020214.x; RA Fidantsef A.L., Bostock R.M.; RT "Characterization of potato tuber lipoxygenase cDNAs and lipoxygenase RT expression in potato tubers and leaves."; RL Physiol. Plantarum 102:257-271(1998). CC -!- FUNCTION: Plant lipoxygenases 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. Catalyzes the CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene CC structure. {ECO:0000255|PROSITE-ProRule:PRU00726}. 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; CC Evidence={ECO:0000255|PROSITE-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 {ECO:0000255|PROSITE-ProRule:PRU00726}. 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; AF019614; AAB81595.1; -; mRNA. DR AlphaFoldDB; O22508; -. DR SMR; O22508; -. DR InParanoid; O22508; -. DR UniPathway; UPA00382; -. DR Proteomes; UP000011115; Unassembled WGS sequence. DR ExpressionAtlas; O22508; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central. 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:SF178; LINOLEATE 9S-LIPOXYGENASE A; 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; Reference proteome. FT CHAIN 1..861 FT /note="Probable linoleate 9S-lipoxygenase 8" FT /id="PRO_0000412926" FT DOMAIN 33..160 FT /note="PLAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152" FT DOMAIN 163..861 FT /note="Lipoxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" FT REGION 220..245 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 861 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726" SQ SEQUENCE 861 AA; 97020 MW; 92C31F6EAF55FB58 CRC64; MIGQITSGLF GGHDDSKKVK GTVVMMNKNV LDFTDLASSL TGKIFDVLGQ KVSFQLISSV QGDPTNGLQG KHSNPAYLEN SLFTLTPLTA GSETAFGVTF DWNEEFGVPG AFIIKNMHIT EFFLKSLTLE DVPNHGKVHF VCNSWVYPSL NYKSDRIFFA NQPYLPSETP ELLRKYRENE LLTLRGDGTG KREAWDRIYD YDIYNDLGNP DQGKENVRTT LGGSAEYPYP RRGRTGRPPT RTDPKVKSRI PLILSLDIYV PRDERFGHLK MSDFLTYALK SIVQFILPEL HALFDGTPNE FDSFEDVLRL YEGGIKLPQG PLFKALTAAI PLEMIRELLR TDGEGILRFP TPLVIKDSKT AWRTDEEFAR EMLAGVNPII ISRLQEFPPK SKLDPEAYGN QNSTITAEHI EDKLDGLTVD EAMNNNKLFI LNHHDVIIPY LRRINTTITK TYASRTLLFL QDNGSLKPLA IELSLPHPDG DQFGVTSKVY TPTDQGVESS IWQLAKAYVA VNDTGVHQLI SHWLNTHAVI EPFVIATNRQ LSVLHPIHKL LYPHFRDTMN INASARQILV NAGGVLESTV FQSKFAMEMS AVVYKDWVFP DQALPADLVK RGVAVEDSSS PHGVRLLIED YPYAVDGLEI WSAIKSWVTD YCSFYYGSDE EILKDNELQA WWKELREVGH GDKKNEPWWP EMKTPQELID SCTTIIWIAS ALHAAVNFGQ YPYAGYLPNR PTVSRRFMPE PGTPEYEELK RNPDKAFLKT ITAQLQTLLG VSLVEILSRH TTDEIYLGQR ESPEWTKDKE PLAAFDRFGK KLTDIEKQII QRNGDNILTN RSGPVNAPYT LLFPTSEGGL TGKGIPNSVS I //