ID   LOX17_SOLTU             Reviewed;         861 AA.
AC   O22507;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Probable linoleate 9S-lipoxygenase 7;
DE            EC=1.13.11.58;
GN   Name=LOX1.7; Synonyms=PLOX1;
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], TISSUE SPECIFICITY, AND INDUCTION BY PATHOGEN;
RP   JASMONATE AND ARACHIDONATE.
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   -!- TISSUE SPECIFICITY: Expressed in tubers. Detected in sprouts and
CC       flowers. but not in leaves or stems. {ECO:0000269|Ref.1}.
CC   -!- INDUCTION: Up-regulated by pathogen infection, and by jasmonate or
CC       arachidonate treatments. No induction by linoleic acid.
CC       {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR   EMBL; AF019613; AAB81594.1; -; mRNA.
DR   AlphaFoldDB; O22507; -.
DR   SMR; O22507; -.
DR   PRIDE; O22507; -.
DR   InParanoid; O22507; -.
DR   UniPathway; UPA00382; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; O22507; 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 7"
FT                   /id="PRO_0000412925"
FT   DOMAIN          29..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..246
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;  97065 MW;  2438BA73CED18275 CRC64;
     MIGQITSGLF GGHDDSKKVK GTVVMMNKNV LDFTDLAGSL TGKIFDVLGQ KVSFQLISSV
     QGDPTNGLQG KHSNPAYLEN SLFTLTPLTA GSETAFGVTF DWNEEFGVPG AFIIKNMHIN
     EFFLKSLTLE DVPNHGKVHF VCNSWVYPSL NYKSDRIFFA NQPYLPSETP ELLRKYRENE
     LLTLRGDGTG KREAWDRIYD YDIYNDLGNP DQGKENVRTT LGGSAEYPYP RRGRTGRPPT
     RTDPKSESRI PLILSLDIYV PRDERFGHLK MSDFLTYALK SIVQFILPEL HALFDGTPNE
     FDSFEDVLRL YEGRDQLPQG PLFKALTAAI PLEMIRELLR TDGEGILRFP TPLVIKDSKT
     AWRTDEEFAR EMLAGVNPII ISRLQEFPPK SKLDPEAYGN QNSTITAEHI EDKLDGLTVD
     EAMNNNKLFI LNHHDVIIPY LRRINTTITK TYASRTLLFL QDNGSLKPLA IELSLPHPDG
     DQFGVTSKVY TPSDQGVESS IWQLAKAYVA VNDTGVHQLI SHWLNTHAVI EPFVIATNRQ
     LSVLHPIHKL LYPHFRDTMN INASARQILV NAGGVLESTV FQSKFAMEMS AVVYKDWVFP
     DQALPADLVK RGVAVEDSSS PHGVRLLIED YPYAVDGLEI WSAIKSWVTD YCSFYYGSDE
     EILKDNELQA WWKELREVGH GDKKNEPWWP EMKTPQELID SCTTIIWIAS ALHAAVNFGQ
     YPYAGYLPNR PTVSRRFMPE PGTPDYEELK RNPDKAFLKT ITAQLQTLLG VSLVEILSRH
     TTDEIYLGQR ESPEWTKDKE PLAAFDRFGK KLTDIEKQII QRNGDNILTN RSGPVNAPYT
     LLFPTSEGGL TGKGIPNSVS I