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   25-NOV-2008, entry version 66.
DE   RecName: Full=Lipoxygenase A;
DE            EC=1.13.11.12;
GN   Name=LOX1.1; Synonyms=LOXA;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum; Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Caruso; TISSUE=Pericarp;
RX   MEDLINE=95062736; 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
CC       diverse aspects of plant physiology including growth and
CC       development, pest resistance, and senescence or responses to
CC       wounding. It catalyzes the hydroperoxidation of lipids, containing
CC       a cis,cis-1,4-pentadiene structure.
CC   -!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,11E)-(13S)-13-
CC       hydroperoxyoctadeca-9,11-dienoate.
CC   -!- COFACTOR: Binds 1 iron ion per subunit. Iron is tightly bound (By
CC       similarity).
CC   -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC   -!- SUBUNIT: Monomer (By similarity).
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.
CC   -!- SIMILARITY: Contains 1 lipoxygenase domain.
CC   -!- SIMILARITY: Contains 1 PLAT domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U09026; AAA53184.1; -; mRNA.
DR   UniGene; Les.3668; -.
DR   HSSP; P08170; 1FGT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016165; F:lipoxygenase activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000907; LipOase.
DR   InterPro; IPR013819; LipOase_C.
DR   InterPro; IPR001024; LipOase_LH2.
DR   InterPro; IPR001246; LipOase_pln.
DR   Gene3D; G3DSA:2.60.60.20; Lipase_LipOase; 1.
DR   PANTHER; PTHR11771; LipOase; 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   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; Iron;
KW   Lipid synthesis; Metal-binding; Oxidoreductase; Oxylipin biosynthesis.
FT   CHAIN         1    860       Lipoxygenase A.
FT                                /FTId=PRO_0000220705.
FT   DOMAIN       29    159       PLAT.
FT   DOMAIN      162    860       Lipoxygenase.
FT   METAL       521    521       Iron; catalytic (By similarity).
FT   METAL       526    526       Iron; catalytic (By similarity).
FT   METAL       712    712       Iron; catalytic (By similarity).
FT   METAL       716    716       Iron; catalytic (By similarity).
FT   METAL       860    860       Iron; via carboxylate; catalytic (By
FT                                similarity).
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
//