ID   LOX1_ARATH              Reviewed;         859 AA.
AC   Q06327;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   16-JUN-2009, entry version 85.
DE   RecName: Full=Lipoxygenase 1;
DE            EC=1.13.11.12;
GN   Name=LOX1; OrderedLocusNames=At1g55020; ORFNames=F14C21.3, F14C21.54;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Root;
RX   MEDLINE=94105302; PubMed=7506426; DOI=10.1104/pp.101.2.441;
RA   Melan M.A., Dong X., Endara M.E., Davis K.R., Ausubel F.M.,
RA   Peterman T.K.;
RT   "An Arabidopsis thaliana lipoxygenase gene can be induced by
RT   pathogens, abscisic acid, and methyl jasmonate.";
RL   Plant Physiol. 101:441-450(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RX   MEDLINE=94137782; PubMed=8305494; DOI=10.1016/0005-2760(94)90244-5;
RA   Melan M.A., Nemhauser J.M., Peterman T.K.;
RT   "Structure and sequence of the Arabidopsis thaliana lipoxygenase 1
RT   gene.";
RL   Biochim. Biophys. Acta 1210:377-380(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
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   -!- INDUCTION: By wounding, abscisic acid (ABA) and methyl jasmonate.
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; L04637; AAA32827.1; -; mRNA.
DR   EMBL; U01843; AAA17036.1; -; Genomic_DNA.
DR   EMBL; AC069144; AAG51123.1; -; Genomic_DNA.
DR   EMBL; AY093104; AAM13103.1; -; mRNA.
DR   EMBL; BT010358; AAQ56801.1; -; mRNA.
DR   IPI; IPI00547307; -.
DR   PIR; JQ2267; JQ2267.
DR   RefSeq; NP_175900.1; -.
DR   UniGene; At.19984; -.
DR   UniGene; At.67309; -.
DR   HSSP; P08170; 1FGT.
DR   PRIDE; Q06327; -.
DR   GeneID; 841944; -.
DR   GenomeReviews; CT485782_GR; AT1G55020.
DR   KEGG; ath:AT1G55020; -.
DR   NMPDR; fig|3702.1.peg.5025; -.
DR   TAIR; At1g55020; -.
DR   OMA; Q06327; DWITTIT.
DR   BRENDA; 1.13.11.12; 302.
DR   ArrayExpress; Q06327; -.
DR   GermOnline; AT1G55020; Arabidopsis thaliana.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016165; F:lipoxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0048364; P:root development; IMP:TAIR.
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   Complete proteome; Cytoplasm; Dioxygenase; Fatty acid biosynthesis;
KW   Iron; Lipid synthesis; Metal-binding; Oxidoreductase;
KW   Oxylipin biosynthesis.
FT   CHAIN         1    859       Lipoxygenase 1.
FT                                /FTId=PRO_0000220703.
FT   DOMAIN       21    161       PLAT.
FT   DOMAIN      164    859       Lipoxygenase.
FT   METAL       519    519       Iron; catalytic (By similarity).
FT   METAL       524    524       Iron; catalytic (By similarity).
FT   METAL       711    711       Iron; catalytic (By similarity).
FT   METAL       715    715       Iron; catalytic (By similarity).
FT   METAL       859    859       Iron; via carboxylate; catalytic (By
FT                                similarity).
SQ   SEQUENCE   859 AA;  98045 MW;  49378EBACD5FF579 CRC64;
     MFGELRDLLT GGGNETTTKK VKGTVVLMKK NVLDFNDFNA SFLDRLHEFL GNKITLRLVS
     SDVTDSENGS KGKLGKAAHL EDWITTITSL TAGESAFKVT FDYETDFGYP GAFLIRNSHF
     SEFLLKSLTL EDVPGHGRVH YICNSWIYPA KHYTTDRVFF SNKTYLPHET PATLLKYREE
     ELVSLRGTGE GELKEWDRVY DYAYYNDLGV PPKNPRPVLG GTQEYPYPRR GRTGRKPTKE
     DPQTESRLPI TSSLDIYVPR DERFGHLKMS DFLAYALKAI AQFIQPALEA VFDDTPKEFD
     SFEDVLKIYE EGIDLPNQAL IDSIVKNIPL EMLKEIFRTD GQKFLKFPVP QVIKEDKTAW
     RTDEEFAREM LAGLNPVVIQ LLKEFPPKSK LDSESYGNQN STITKSHIEH NLDGLTVEEA
     LEKERLFILD HHDTLMPYLG RVNTTTTKTY ASRTLLFLKD DGTLKPLVIE LSLPHPNGDK
     FGAVSEVYTP GEGVYDSLWQ LAKAFVGVND SGNHQLISHW MQTHASIEPF VIATNRQLSV
     LHPVFKLLEP HFRDTMNINA LARQILINGG GIFEITVFPS KYAMEMSSFI YKNHWTFPDQ
     ALPAELKKRG MAVEDPEAPH GLRLRIKDYP YAVDGLEVWY AIESWVRDYI FLFYKIEEDI
     QTDTELQAWW KEVREEGHGD KKSEPWWPKM QTREELVESC TIIIWVASAL HAAVNFGQYP
     VAGYLPNRPT ISRQYMPKEN TPEFEELEKN PDKVFLKTIT AQLQTLLGIS LIEILSTHSS
     DEVYLGQRDS KEWAAEKEAL EAFEKFGEKV KEIEKNIDER NDDETLKNRT GLVKMPYTLL
     FPSSEGGVTG RGIPNSVSI
//