ID   LOX11_SOLTU             Reviewed;         861 AA.
AC   P37831;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Linoleate 9S-lipoxygenase 1;
DE            EC=1.13.11.58;
DE   AltName: Full=Lipoxygenase 1;
DE            Short=StLOX1;
GN   Name=LOX1.1; Synonyms=LOX1;
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. Desiree; TISSUE=Tuber;
RX   PubMed=7870815; DOI=10.1104/pp.107.1.265;
RA   Casey R.;
RT   "Sequence of a cDNA clone encoding a potato (Solanum tuberosum) tuber
RT   lipoxygenase.";
RL   Plant Physiol. 107:265-266(1995).
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.
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; X79107; CAA55724.1; -; mRNA.
DR   PIR; S44940; S44940.
DR   AlphaFoldDB; P37831; -.
DR   SMR; P37831; -.
DR   STRING; 4113.PGSC0003DMT400054145; -.
DR   PRIDE; P37831; -.
DR   InParanoid; P37831; -.
DR   BRENDA; 1.13.11.58; 5757.
DR   UniPathway; UPA00382; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P37831; 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="Linoleate 9S-lipoxygenase 1"
FT                   /id="PRO_0000220722"
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;  96967 MW;  09732A6751DEE20D 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 YEGGIKLPQG PLFKALTAAI PLEMIRELLR TDGEGILRFP TPLVIKDSKT
     AWRTDEEFAR EMLAGVNPVI ISRLQEFPPK SKLDPEAYGN QNSTITAEHI EDKLDGLTVD
     EAMNNNKLFI LNHHDVIIPY LRRINTTITK AYASRTLLFL QDNGSLKPLA IELSFPHPDG
     DQFGVTSKVY TPSDQGVESS IWQLAKAYVA VNDVGVHQLI SHWLNTHAVI EPFVIATNRQ
     LSVLHPIHKL LYPHFRDTMN INASARQLLV NAGGVLESTV FQSKFAMEMS AVVYKDWVFP
     DQALPADLVK RGVAVEDSSS PHGVRLLIED YPYAVDGLEI WSAIKSWVTD YCSFYYGSDE
     EILKDNELQA WWKELREVGH GDKKNEPWWP EMETPQELID SCTTIIWIAS ALHAAVNFGQ
     YPYAGYLPNR PTVSRRFMPE PGTPEYEELK RNPDKAFLKT ITAQLQTLLG VSLVEILSRH
     TTDEIYLGQR ESPEWTKDKE PLAAFDRFGK KLTDIEKQII QRNGDNILTN RSGPVNAPYT
     LLFPTSEGGL TGKGIPNSVS I