ID   LOX1_LENCU              Reviewed;         866 AA.
AC   P38414;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-NOV-2008, entry version 61.
DE   RecName: Full=Lipoxygenase;
DE            EC=1.13.11.12;
GN   Name=LOX1.1;
OS   Lens culinaris (Lentil) (Cicer lens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Lens.
OX   NCBI_TaxID=3864;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seedling shoot;
RX   MEDLINE=94162308; PubMed=8117753; DOI=10.1016/0005-2760(94)90275-5;
RA   Hilbers M.P., Rossi A., Finazzi-Agro A., Veldink G.A.,
RA   Vliegenthart J.F.G.;
RT   "The primary structure of a lipoxygenase from the shoots of etiolated
RT   lentil seedlings derived from its cDNA.";
RL   Biochim. Biophys. Acta 1211:239-242(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   -!- SIMILARITY: Belongs to the lipoxygenase family.
CC   -!- SIMILARITY: Contains 1 lipoxygenase domain.
CC   -!- SIMILARITY: Contains 1 PLAT domain.
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DR   EMBL; X71344; CAA50483.1; -; mRNA.
DR   HSSP; P08170; 2SBL.
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    866       Lipoxygenase.
FT                                /FTId=PRO_0000220704.
FT   DOMAIN       42    171       PLAT.
FT   DOMAIN      174    866       Lipoxygenase.
FT   METAL       526    526       Iron; catalytic (By similarity).
FT   METAL       531    531       Iron; catalytic (By similarity).
FT   METAL       717    717       Iron; catalytic (By similarity).
FT   METAL       721    721       Iron; catalytic (By similarity).
FT   METAL       866    866       Iron; via carboxylate; catalytic (By
FT                                similarity).
SQ   SEQUENCE   866 AA;  96639 MW;  E3E5D00E84E3C89C CRC64;
     MASLLFGRGQ KLKGTVILMQ KNVLDINALT AAQSPSGIIG GAFGVVGSIA GSIIDTATAF
     LGRSVRLRLI SATVADASGK GKVSKEAFLE GLLTSIPTLG DKQSAFSVHF EWDSNMGTPG
     AFYIENFMQG GEFFLVSLTL DDVPNVGSIK FACNSWIYND KKYQSDRIFF ANKTYLPSAT
     PAPLVSYRQE ELKTLRGDGT GERQEWDRIY DYDVYNDLGA PDQKATLGRP VLGGSSTLPY
     PRRGRTGRKK TVKEPQSESR SDTVYLPRDE AFGHVKSSDF LVYILKSASQ NIVPQLRSVV
     TLQLNNPEFN TFEDVRSLYD GGIKLPTDVL SKISPIPLFS ELFRSDGEAA LKFPPPKVIQ
     VDHSAWMTDE EFAREMIAGV NPHIIKEVLS FPIKSKLDSQ LYGDNTSKIT KEHLEPNLGG
     VTVEGAIQTN RLFTPDHHDA LFPYLRKINA TATKAYATRT VLFLQDNGTL KPLAIELSTP
     HPDGDSFGPV SKVYLPASEG VEASIWLLAK AFVVVNDSCY HQLVSHWLNT HAVVEPFIIA
     TNRHLSVVHP IHKLLLPHYR DTMNINALAR NVLVNAEGII ESTFLWGNYA MEMSAVVYKD
     WVFPDQGLPN DLIKRGVAVK DPSSPHGVRL LIEDYPYASD GLEIWAAIKS WVEEYVNFYY
     KSDAAIAQDA ELQAFWKELV EVGHGDLKSA TWWFKMQNRK ELIEACSILI WIASALHAAV
     NFGQYPYGGY ILNRPTKSRK FMPEKGTPEY DDLAKNYEKA YLRTITPKND TLTDLTIIEV
     LSRHASDEQY LGERIEGDDW TTDSVPKEAF KRFGKKLAEI EEKLTQRNND ESLRNRYGPV
     KMPYTLLYPS SEEGLTCRGI PNSISI
//