LOX15_SOLTU
ID LOX15_SOLTU Reviewed; 862 AA.
AC Q43191;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable linoleate 9S-lipoxygenase 5;
DE EC=1.13.11.58;
DE AltName: Full=Leaf lipoxygenase;
GN Name=LOX1.5; Synonyms=POTLX-3;
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. Berolina;
RA Kolomiets M.V., Hannapel D.J., Gladon R.J.;
RT "Nucleotide sequence of a cDNA clone for a lipoxygenase from abscisic acid-
RT treated potato leaves.";
RL (er) Plant Gene Register PGR96-069(1996).
RN [2]
RP INDUCTION BY PATHOGEN; ETHYLENE AND JASMONATE, AND 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. May contribute to
CC cell death during the hypersensitive response (HR) by the massive
CC production of free fatty acid hydroperoxides. 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 -!- TISSUE SPECIFICITY: Not detected in leaves, stems, flowers, roots,
CC tubers and stolons during normal growth and development.
CC {ECO:0000269|PubMed:11080289}.
CC -!- INDUCTION: Up-regulated within 6 hours after pathogen infection,
CC ethylene or jasmonate treatments. Not induced by wounding.
CC {ECO:0000269|PubMed:11080289}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; U60202; AAB67865.1; -; mRNA.
DR PIR; T07775; T07775.
DR RefSeq; NP_001274916.1; NM_001287987.1.
DR AlphaFoldDB; Q43191; -.
DR SMR; Q43191; -.
DR STRING; 4113.PGSC0003DMT400028158; -.
DR BindingDB; Q43191; -.
DR ChEMBL; CHEMBL2189149; -.
DR EnsemblPlants; RHC08H1G1067.2.1; RHC08H1G1067.2.1; RHC08H1G1067.2.
DR GeneID; 102577714; -.
DR Gramene; RHC08H1G1067.2.1; RHC08H1G1067.2.1; RHC08H1G1067.2.
DR KEGG; sot:102577714; -.
DR eggNOG; ENOG502QVKD; Eukaryota.
DR InParanoid; Q43191; -.
DR OrthoDB; 385042at2759; -.
DR UniPathway; UPA00382; -.
DR PRO; PR:Q43191; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q43191; baseline and differential.
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..862
FT /note="Probable linoleate 9S-lipoxygenase 5"
FT /id="PRO_0000412923"
FT DOMAIN 36..161
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 164..862
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 523
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 528
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 714
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 718
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 862
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 862 AA; 97778 MW; 94667A9F56041E89 CRC64;
MLLEKIVEAI SGRSEDNGKK VKGTIVLMKK NVLDFNDVNA SLLDGVLEFL GKRVSLQLIS
VVHADPGNSL QGKRSNPAYL EKWLTTGTSL VAGESAFDVT FDWDEDIGVP GAFIINNFHF
NEFYLKSLTL EDVPNHGNVH FVCNSWVYPA KKYKSERIFF ANQAYLPGET PEPLRNYREK
ELVNLRGNGN GKLEEWDRVY DYALYNDLGD PEKGKQYART ILGGSAEYPY PRRGRTGRKP
TKADPKSESR IPLLMSLDIY VPRDERFGHI KLSDFLTYAL KSIVQFLIPE FQALFDSTPD
EFDSFEDVLK LYEGGIKLPQ GPFLKALTDS IPLEILKEII RTDGEGKFKF PTPQVIQEDK
SSWRTDEEFA REMLAGVNPV IISRLQEFPP KSQLDSEVYG NQNSTITKEH IENTLDGLTI
DDAIKTNRLY ILNHHDILMP YVRRINTTNT KLYASRTLLF LQDDGTMKPV AIELSLPHPD
GDELGAVSKV YTPADQGVEG SIWQLAKAYV AVNDSGVHQL ISHWLNTHAA IEPFVIATNR
QLSVLHPIHK LLHPHFRDTM NINALARQIL INAGGVLEMT VFPAKYAMEM SAVVYKSWVF
PEQALPADLI KRGVAVEDSS SPHGVRLLIQ DYPYAVDGLE IWSAIKSWVT EYCNFYYKSD
ELVLKDNELQ AWWKELREEG HGDKKDEPWW PKMQTRQELK DSCTIIIWIA SALHAAVNFG
QYPYAGYLPN RPTLSRRFMP EPGTPEYEEL KTNPDKAYLK TITPQLQTLL GISLIEILSR
HASDEIYLGQ RDSSEWTKDQ EPIAAFERFG KKLSEIEDQI IQMNGDKKWK NRSGPVNVPY
TLLFPTSEQG LTGKGIPNSV SI
