ID   LOXB_SOLLC              Reviewed;         859 AA.
AC   P38416;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-NOV-2008, entry version 64.
DE   RecName: Full=Lipoxygenase B;
DE            EC=1.13.11.12;
GN   Name=LOX1.2; Synonyms=LOXB;
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: Fruit specific.
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; U09025; AAA53183.1; -; mRNA.
DR   PIR; T06339; T06339.
DR   HSSP; P09186; 1NO3.
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    859       Lipoxygenase B.
FT                                /FTId=PRO_0000220706.
FT   DOMAIN       34    158       PLAT.
FT   DOMAIN      161    859       Lipoxygenase.
FT   METAL       521    521       Iron; catalytic (By similarity).
FT   METAL       526    526       Iron; catalytic (By similarity).
FT   METAL       711    711       Iron; catalytic (By similarity).
FT   METAL       859    859       Iron; via carboxylate; catalytic (By
FT                                similarity).
SQ   SEQUENCE   859 AA;  97122 MW;  DAD79B10AE627434 CRC64;
     MSLGGIVDAI LGKDDRPKVK GRVILMKKNV LDFINIGASV VDGISDLLGQ KVSIQLISGS
     VNYDGLEGKL SNPAYLESWL TDITPITAGE STFSVTFDWD RDEFGVPGAF IIKNLHLNEF
     FLKSLTLEDV PNYGKIHFVC NSWVYPAFRY KSDRIFFANQ AYLPSETPQP LRKYRENELV
     ALRGDGTGKL EEWDRVYDYA CYNDLGEPDK GEEYARPILG GSSEYPYPRR GRTGREPTKA
     DPNCESRNPL PMSLDIYVPR DERFGHVKKS DFLTSSLKSS LQTLLPAFKA LCDNTPNEFN
     SFADVLNLYE GGIKLPEGPW LKAITDNISS EILKDILQTD GQGLLKYPTP QVIQGDKTAW
     RTDEEFGREM LAGSNPVLIS RLQEFPPKSK LDPTIYGNQN STITTEHVQD KLNGLTVNEA
     IKSNRLFILN HHDIVMPLLR KINMSANTKA YASRTLLFLQ DDRTLKPLAI ELSLPHPDGD
     QFGTVSKVYT PADQGVEGSI WQFAKAYVAV NDMGIHQLIS HWLNTHAVIE PFVVATNRHL
     SVLHPIHKLL HPHFRNTMNI NALARETLTY DGGFETSLFP AKYSMEMSAA AYKDWVFPEQ
     ALPADLLKRG VAVEDLSSPH GIRLLILDYP YAVDGLEIWA AIKSWVTEYC KFYYKSDETV
     EKDTELQAWW KELREEGHGD KKDEAWWPKL QTRQELRDCC TIIIWIASAL HAALHFGLYS
     YAGYLPNRPT LSCNLMPEPG SVEYEELKTN PDKVFLKTFV PQLQSLLEIS IFEVSSRHAS
     DEVYLGQRDS IEWTKDKEPL VAFERFGKML SDIENRIMIM NSHKSWKNRS GPVNVPYTLL
     FPTSEEGLTG KGIPNSVSI
//