ID   LOXB_PHAVU              Reviewed;         741 AA.
AC   P27481;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-NOV-2008, entry version 60.
DE   RecName: Full=Lipoxygenase;
DE            EC=1.13.11.12;
DE   Flags: Fragment;
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 [MRNA].
RC   STRAIN=cv. Red Mexican; TISSUE=Leaf;
RX   MEDLINE=94003416; PubMed=8400375;
RA   Slusarenko A.J., Meier B.M., Shaw N.;
RT   "Spatial and temporal accumulation of defense gene transcripts in bean
RT   (Phaseolus vulgaris) leaves in relation to bacteria-induced
RT   hypersensitive cell death.";
RL   Mol. Plant Microbe Interact. 6:453-466(1993).
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; X63521; CAA45086.1; -; mRNA.
DR   PIR; S18906; S18906.
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   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   >741       Lipoxygenase.
FT                                /FTId=PRO_0000220716.
FT   DOMAIN       <1     53       PLAT.
FT   DOMAIN       56    741       Lipoxygenase.
FT   METAL       407    407       Iron; catalytic (By similarity).
FT   METAL       412    412       Iron; catalytic (By similarity).
FT   METAL       598    598       Iron; catalytic (By similarity).
FT   METAL       602    602       Iron; catalytic (By similarity).
FT   NON_TER       1      1
FT   NON_TER     741    741
SQ   SEQUENCE   741 AA;  84197 MW;  2F2CDD5979606AC1 CRC64;
     IPGAFYIKNF MQVEFYLKSL TLEDIPNHGT IHFICNSWIY NSKVYKSDRI FFANNTYLPS
     ETPAPLLKYR EEELKNVRGD GSGERKEWDR VYDYDVYNDL GNPDKGAALA RPVLGGSTLP
     YPRRGRTGRP KTKKDPNSEK PSDFVYLPRD EAFGHLKSSD FLAYGLKSVS QDVLPVLTDA
     FDGNLLSLEF DNFAEVHKLY EGGVTLPTNF LSKYAPIPIV KEIFRSDGEQ FLKYPPPKVM
     QVNKSAWMTD EEFARETIAG VNPNVIKSLE EFPPRSKLDT QSFGDHTSII TKEHLEINLG
     GLTVEQAIQS KKLFILDHHD YLIPYLRRIN ASATKTYATR TIFFLKSDGT LAPLAIELSK
     PHPQGDEHGP VSEVYVPAYE GVEAYIWLLA KAYVVVNDSC YHQLVSHWLN THAVVEPFVL
     ATNRQLSVVH PVYKLLFPHY RDTMNINSLA RKSLVNADGI IEKTFLWGRY ALELSAVIYK
     DWSLHDQALP NDLVKRGVAV KDPSAPHGVK LVIEDYPYAS DGLEIWDAIK SWVVEYVAFY
     YKSDEVLQQD SELQAWWKEL VQVGHGDLKD KPWWPKMQSR ENLVEVSTTL IWIASALHAA
     VNFGQYPYGG LILNRPTISR RFMPEKGSAE YAALAKNPEK EFLKTITGKK ETLIDLTVIE
     ILSRHASDEI YLGERDGGDH WTSDAGPLEA FKRFGKKLAE IEKKLVQKNN DETLRNRTGP
     AKMPYTLLYP SSEEGLTFRG I
//