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 16-OCT-2013, entry version 85. 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; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; OC 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 CC diverse aspects of plant physiology including growth and CC development, pest resistance, and senescence or responses to CC wounding. Catalyzes the hydroperoxidation of lipids containing a CC cis,cis-1,4-pentadiene structure (By similarity). CC -!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9S,10E,12Z)-9-hydroperoxy- CC 10,12-octadecadienoate. CC -!- COFACTOR: Binds 1 iron ion per subunit. Iron is tightly bound (By CC similarity). CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the lipoxygenase family. CC -!- SIMILARITY: Contains 1 lipoxygenase domain. CC -!- SIMILARITY: Contains 1 PLAT domain. 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 ProteinModelPortal; O22508; -. DR SMR; O22508; 18-861. DR UniPathway; UPA00382; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IEA:InterPro. DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.60.60.20; -; 1. DR Gene3D; 4.10.372.10; -; 1. DR InterPro; IPR008976; Lipase_LipOase. DR InterPro; IPR000907; LipOase. DR InterPro; IPR013819; LipOase_C. DR InterPro; IPR020834; LipOase_CS. DR InterPro; IPR020833; LipOase_Fe_BS. DR InterPro; IPR001246; LipOase_pln. DR InterPro; IPR027433; Lipoxygenase_domain_3. DR InterPro; IPR001024; PLAT/LH2_dom. DR PANTHER; PTHR11771; PTHR11771; 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; SSF48484; SSF48484; 1. DR SUPFAM; SSF49723; SSF49723; 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 Complete proteome; Cytoplasm; Dioxygenase; Fatty acid biosynthesis; KW Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism; KW Metal-binding; Oxidoreductase; Oxylipin biosynthesis; KW Reference proteome. FT CHAIN 1 861 Probable linoleate 9S-lipoxygenase 8. FT /FTId=PRO_0000412926. FT DOMAIN 33 160 PLAT. FT DOMAIN 163 861 Lipoxygenase. FT METAL 522 522 Iron; catalytic (By similarity). FT METAL 527 527 Iron; catalytic (By similarity). FT METAL 713 713 Iron; catalytic (By similarity). FT METAL 717 717 Iron; catalytic (By similarity). FT METAL 861 861 Iron; via carboxylate; catalytic (By FT similarity). 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 //