LOX18_SOLTU
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 03-AUG-2022, entry version 116.
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}.
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DR EMBL; AF019614; AAB81595.1; -; mRNA.
DR AlphaFoldDB; O22508; -.
DR SMR; O22508; -.
DR PRIDE; O22508; -.
DR InParanoid; O22508; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; O22508; baseline.
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; 4.10.372.10; -; 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; 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 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