ID   LOX1_SOLTU              Reviewed;         861 AA.
AC   P37831;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-NOV-2008, entry version 63.
DE   RecName: Full=Lipoxygenase 1;
DE            EC=1.13.11.12;
GN   Name=LOX1.1; Synonyms=LOX1;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree; TISSUE=Tuber;
RX   MEDLINE=95175602; PubMed=7870815; DOI=10.1104/pp.107.1.265;
RA   Casey R.;
RT   "Sequence of a cDNA clone encoding a potato (Solanum tuberosum) tuber
RT   lipoxygenase.";
RL   Plant Physiol. 107:265-266(1995).
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 (By similarity).
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; X79107; CAA55724.1; -; mRNA.
DR   PIR; S44940; S44940.
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    861       Lipoxygenase 1.
FT                                /FTId=PRO_0000220722.
FT   DOMAIN       29    160       PLAT.
FT   DOMAIN      163    861       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       861    861       Iron; via carboxylate; catalytic (By
FT                                similarity).
SQ   SEQUENCE   861 AA;  96967 MW;  09732A6751DEE20D CRC64;
     MIGQITSGLF GGHDDSKKVK GTVVMMNKNV LDFTDLAGSL TGKIFDVLGQ KVSFQLISSV
     QGDPTNGLQG KHSNPAYLEN SLFTLTPLTA GSETAFGVTF DWNEEFGVPG AFIIKNMHIN
     EFFLKSLTLE DVPNHGKVHF VCNSWVYPSL NYKSDRIFFA NQPYLPSETP ELLRKYRENE
     LLTLRGDGTG KREAWDRIYD YDIYNDLGNP DQGKENVRTT LGGSAEYPYP RRGRTGRPPT
     RTDPKSESRI PLILSLDIYV PRDERFGHLK MSDFLTYALK SIVQFILPEL HALFDGTPNE
     FDSFEDVLRL YEGGIKLPQG PLFKALTAAI PLEMIRELLR TDGEGILRFP TPLVIKDSKT
     AWRTDEEFAR EMLAGVNPVI ISRLQEFPPK SKLDPEAYGN QNSTITAEHI EDKLDGLTVD
     EAMNNNKLFI LNHHDVIIPY LRRINTTITK AYASRTLLFL QDNGSLKPLA IELSFPHPDG
     DQFGVTSKVY TPSDQGVESS IWQLAKAYVA VNDVGVHQLI SHWLNTHAVI EPFVIATNRQ
     LSVLHPIHKL LYPHFRDTMN INASARQLLV NAGGVLESTV FQSKFAMEMS AVVYKDWVFP
     DQALPADLVK RGVAVEDSSS PHGVRLLIED YPYAVDGLEI WSAIKSWVTD YCSFYYGSDE
     EILKDNELQA WWKELREVGH GDKKNEPWWP EMETPQELID SCTTIIWIAS ALHAAVNFGQ
     YPYAGYLPNR PTVSRRFMPE PGTPEYEELK RNPDKAFLKT ITAQLQTLLG VSLVEILSRH
     TTDEIYLGQR ESPEWTKDKE PLAAFDRFGK KLTDIEKQII QRNGDNILTN RSGPVNAPYT
     LLFPTSEGGL TGKGIPNSVS I
//