LOXA_SOLLC
ID LOXA_SOLLC Reviewed; 860 AA.
AC P38415;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Linoleate 9S-lipoxygenase A;
DE EC=1.13.11.58;
DE AltName: Full=Lipoxygenase A;
GN Name=LOX1.1; Synonyms=LOXA;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Caruso; TISSUE=Pericarp;
RX PubMed=7972514; DOI=10.1104/pp.106.1.109;
RA Ferrie B.J., Beaudoin N., Burkhart W., Bowsher C.G., Rothstein S.J.;
RT "The cloning of two tomato lipoxygenase genes and their differential
RT expression during fruit ripening.";
RL Plant Physiol. 106:109-118(1994).
CC -!- FUNCTION: Plant lipoxygenase 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. It 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.
CC -!- TISSUE SPECIFICITY: Expressed in germinating seeds as well as in
CC ripening fruit.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; U09026; AAA53184.1; -; mRNA.
DR RefSeq; NP_001234856.1; NM_001247927.2.
DR AlphaFoldDB; P38415; -.
DR SMR; P38415; -.
DR STRING; 4081.Solyc08g014000.2.1; -.
DR PaxDb; P38415; -.
DR PRIDE; P38415; -.
DR EnsemblPlants; Solyc08g014000.3.1; Solyc08g014000.3.1; Solyc08g014000.3.
DR GeneID; 543994; -.
DR Gramene; Solyc08g014000.3.1; Solyc08g014000.3.1; Solyc08g014000.3.
DR KEGG; sly:543994; -.
DR eggNOG; ENOG502QVKD; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; P38415; -.
DR OMA; ENWLTTI; -.
DR OrthoDB; 385042at2759; -.
DR PhylomeDB; P38415; -.
DR BRENDA; 1.13.11.58; 3101.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000004994; Chromosome 8.
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..860
FT /note="Linoleate 9S-lipoxygenase A"
FT /id="PRO_0000220705"
FT DOMAIN 29..159
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 162..860
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 209..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 521
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 526
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 712
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 716
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 860
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 860 AA; 96765 MW; 43D1091853469426 CRC64;
MLGQLVGGLI GGHHDSKKVK GTVVMMKKNA LDFTDLAGSL TDKIFEALGQ KVSFQLISSV
QSDPANGLQG KHSNPAYLEN FLLTLTPLAA GETAFGVTFD WNEEFGVPGA FVIKNMHINE
FFLKSLTLED VPNHGKVHFV CNSWVYPSFR YKSDRIFFAN QPYLPSETPE LLRKYRENEL
VTLRGDGTGK REAWDRIYDY DVYNDLGNPD QGKENVRTTL GGSADYPYPR RGRTGRPPTR
TDPKSESRIP LILSLDIYVP RDERFGHLKM SDFLTYALKS IVQFILPELH ALFDGTPNEF
DSFEDVLRLY EGGIKLPQGP LFKALTDAIP LEMIRELLRT DGEGILRFPT PLVIKDSKTA
WRTDEEFARE MLAGVNPVII SRLEEFPPKS KLDPELYGNQ NSTITAEHIE GKLDGLTIDE
AINSNKLFIL NHHDVLIPYL RRINTTTTKT YASRTLLFLQ DNGSLKPLAI ELSLPHPDGD
QFGVTSKVYT PSDQGVEGSI WQLAKAYVAV NDSGVHQLIS HWLNTHAVIE PFVIATNRQL
SVLHPIHKLL YPHFRDTMNI NALARQILIN AGGVLESTVF PSKFAMEMSA VVYKDWVFPD
QALPADLVKR GVAVEDSSSP HGVRLLIDDY PYAVDGLEIW SAIKSWVTDY CSFYYGSNEE
ILKDNELQAW WKEVREVGHG DKKNEPWWAE METPQELIDS CTTIIWIASA LHAAVNFGQY
PYAGYLPNRP TVSRKFMPEP GTPEYEELKK NPDKAFLKTI TAQLQTLLGV SLIEILSRHT
TDEIYLGQRE SPEWTKDKEP LAAFERFGNK LTDIEKQIMQ RNGNNILTNR TGPVNAPYTL
LFPTSEGGLT GKGIPNSVSI
