ID   LOXA_PHAVU              Reviewed;         862 AA.
AC   P27480;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-NOV-2008, entry version 61.
DE   RecName: Full=Lipoxygenase 1;
DE            EC=1.13.11.12;
GN   Name=LOXA; Synonyms=LOX1;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae;
OC   Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Red Mexican; TISSUE=Leaf;
RX   MEDLINE=94177173; PubMed=8130796;
RA   Eiben H.G., Slusarenko A.J.;
RT   "Complex spatial and temporal expression of lipoxygenase genes during
RT   Phaseolus vulgaris (L.) development.";
RL   Plant J. 5:123-135(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.
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; X63525; CAA45088.1; -; Genomic_DNA.
DR   PIR; S22153; S22153.
DR   HSSP; P08170; 1F8N.
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   3: Inferred from homology;
KW   Cytoplasm; Dioxygenase; Fatty acid biosynthesis; Iron;
KW   Lipid synthesis; Metal-binding; Oxidoreductase; Oxylipin biosynthesis.
FT   CHAIN         1    862       Lipoxygenase 1.
FT                                /FTId=PRO_0000220715.
FT   DOMAIN       44    171       PLAT.
FT   DOMAIN      174    862       Lipoxygenase.
FT   METAL       522    522       Iron; catalytic (By similarity).
FT   METAL       527    527       Iron; catalytic (By similarity).
FT   METAL       713    713       Iron; catalytic (By similarity).
FT   METAL       717    717       Iron; catalytic (By similarity).
FT   METAL       862    862       Iron; via carboxylate; catalytic (By
FT                                similarity).
SQ   SEQUENCE   862 AA;  97155 MW;  24D56D1CEE3C191E CRC64;
     MFGILNRGHK IKGTVVLMTK NVFDFNEFVS TTRGGIVGAA GGLFGAATDI VGGIVDGATA
     IFSRNIAIQL ISATKTDGLG NGKVGKQTFL EKHLPSLPNL GDRQDAFNVY FEWDENFGIP
     EAFYIKNFMQ SEFFLVSLTL EDIPNHGTIH FVCNSWVYNA KSYKRDRIFF ANKTYLPNET
     PASLVKYRKE ELENLRGDGT GERKEYDRIY DYAVYNDLGN PDKNKNLART TLGGSSDFPY
     PRRGRTGRKS TRKDPKCEIP TSDTYIPRDE NFGHLKSGDF LTYAIKSLTQ NVLPTFQKAF
     GFNNEFDTFE DVRGLFEGGL YLPTDVISKI SPIPVLKEIL RTDGEQVLKF PPPHVIRVTK
     SAWMTDEEFG REMLAGVNPC LIQRLQEFPP KSKLDVTVYG DQTSTMTKEH LEINLGGLTV
     EEALHGNRLF ILDHHDAFIP YLERINDLPT AKCYATRTIL FLKDDNTLKP LAIELSLPNP
     GGKGANSRVI LPADGGAEST IWLLAKAYVV VNDSCYHQLM SHWLNTHAVM EPFVIATNRH
     LSVLHPIYKL LLPHYRDTMN INALARQSLI NAGGVIERSF LPGEFAVEMS SAVYKSWVFT
     DQALPADLIK RGMAVEDPSS PYGLRLVVED YPYAVDGLEI WDTIQTWVKD YVSLYYPTND
     AVKKDTELQA WWKEAVEKGH GDLKDKPWWP KLNTPQDLIH TCSIIIWIAS ALHAAVNFGQ
     YPYGGFILNR PTITRRLLPE PGTKEYGELT SNYQKAYLRT ITGKVEAIVD LSVIEILSRH
     ASDEVYLGQR DNPNWTNNIK ALQAFKRFGQ KLKEIEEKIM GRNKDSSLRN RNGPVKMPYT
     VLLPTCEDEG LTFRGIPNSI SI
//