ID   LOX13_SOLTU             Reviewed;         861 AA.
AC   Q43189;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Probable linoleate 9S-lipoxygenase 3;
DE            EC=1.13.11.58;
GN   Name=LOX1.3; Synonyms=POTLX-1;
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], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Superior;
RA   Kolomiets M.V., Hannapel D.J., Gladon R.J.;
RT   "Potato lipoxygenase genes expressed during the early stages of
RT   tuberization.";
RL   (er) Plant Gene Register PGR96-065(1996).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=11080289; DOI=10.1104/pp.124.3.1121;
RA   Kolomiets M.V., Chen H., Gladon R.J., Braun E.J., Hannapel D.J.;
RT   "A leaf lipoxygenase of potato induced specifically by pathogen
RT   infection.";
RL   Plant Physiol. 124:1121-1130(2000).
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 and roots. Not detected in
CC       leaves, flowers, stems, shoot tips, or axillary buds.
CC       {ECO:0000269|PubMed:11080289, ECO:0000269|Ref.1}.
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; U60200; AAB67858.1; -; mRNA.
DR   AlphaFoldDB; Q43189; -.
DR   SMR; Q43189; -.
DR   PRIDE; Q43189; -.
DR   InParanoid; Q43189; -.
DR   BRENDA; 1.13.11.58; 5757.
DR   UniPathway; UPA00382; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; Q43189; 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 3"
FT                   /id="PRO_0000412921"
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..247
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;  96974 MW;  11AA977F04FF1C56 CRC64;
     MIGQITSGLF GGHDDSKKVK GTVVMMNKNV LDFTDLASSL TGKIFDVLGQ KVSFQLISSV
     QGDPTNGLQG KHSNPAYLEN SLFTLTPLTA GSETAFGVTF DWNEEFGVPG AFIIKNMHIT
     EFFLKSLTLE DVPNHGKVHF VCNSWVYPSL NYKSDRIFFA NQPYLPSDTP ELLRKYRENE
     LLTLRGDGTG KREAWDRIYD YDIYNDLGNP DQGKENVRTT LGGSAEYPYP RRGRTGRPPT
     RTDPKSESRI PLILSTDIYV PRDERFGHLK MSDFLTYALK SIVQFILPEL HALFDGTPNE
     FDSFEDVLRL YEGGIKLPQG PLFKALTAAI PLEMIRELLR TDGEGILRFP TPLVIKDSKT
     AWRTDEEFAR EMLAGTNPVI ISRLQEFPPK SKLDPEAYGN QNSTITAEHI EDKLDGLTVD
     EAMNNNKLFI LNHHDLLIPY LRRINTTITK TYASRTLLFL QDNGSLKPLA IELSLPHPDG
     DQFGVTSKVY TPSDQGVESS IWQLAKAYVA VNDSGVHQLI SHWLNTHAVI EPFVIATNRQ
     LSVLHPIHKL LYPHFRDTMN INALARQILI NAAGVFESTV FQSKFALEMS AVVYKDWVFP
     DQALPADLVK RGVAVEDSSS PHGVRLLIED YPYAVDGLEI WSAIKSWVTD YCSFYYGSDE
     EILKDNELQA WWKELREVGH GDKKNEPWWP EMETPQELID SCTTIIWIAS ALHAAVNFGQ
     YPYAGYLPNR ATVSRRFMPE PGTPEYEELK KNPDKAFLKT ITAQLQTLLG VSLVEILSRH
     TTDEIYLGQR ESPEWTKDKE PLAAFDRFGK KLTDIEKQII QRNGDNILTN RSGPVNAPYT
     LLFPTSEGGL TGKGIPNSVS I