LOX1_ORYSJ
ID LOX1_ORYSJ Reviewed; 863 AA.
AC Q76I22; Q10EI8; Q7G786;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Linoleate 9S-lipoxygenase 1;
DE EC=1.13.11.58;
DE AltName: Full=9-lipoxygenase;
DE AltName: Full=Lipoxygenase 1;
DE AltName: Full=r9-LOX1;
GN OrderedLocusNames=Os03g0699700, LOC_Os03g49260; ORFNames=OSJNBb0017F17.10;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=14634153; DOI=10.1093/pcp/pcg142;
RA Mizuno K., Iida T., Takano A., Yokoyama M., Fujimura T.;
RT "A new 9-lipoxygenase cDNA from developing rice seeds.";
RL Plant Cell Physiol. 44:1168-1175(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse
CC aspects of plant physiology including growth and development, pest
CC resistance, and senescence or responses to wounding. This lipoxygenase
CC introduces molecular oxygen exclusively into the C-9 position of
CC linoleic and linolenic. {ECO:0000269|PubMed:14634153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00726};
CC Note=Binds 1 Fe cation per subunit. Iron is tightly bound.
CC {ECO:0000255|PROSITE-ProRule:PRU00726};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo 1 day after inbibition,
CC and at low levels in developing seeds between 3 and 20 days after
CC flowering. {ECO:0000269|PubMed:14634153}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; AB099850; BAD02945.1; -; mRNA.
DR EMBL; AC093017; AAX95631.1; -; Genomic_DNA.
DR EMBL; AC097368; AAO38440.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98382.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12904.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS85907.1; -; Genomic_DNA.
DR EMBL; AK103565; BAG96145.1; -; mRNA.
DR RefSeq; XP_015632769.1; XM_015777283.1.
DR AlphaFoldDB; Q76I22; -.
DR SMR; Q76I22; -.
DR STRING; 4530.OS03T0699700-01; -.
DR PaxDb; Q76I22; -.
DR PRIDE; Q76I22; -.
DR EnsemblPlants; Os03t0699700-01; Os03t0699700-01; Os03g0699700.
DR GeneID; 4333818; -.
DR Gramene; Os03t0699700-01; Os03t0699700-01; Os03g0699700.
DR KEGG; osa:4333818; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; Q76I22; -.
DR OMA; KFFIRTI; -.
DR OrthoDB; 385042at2759; -.
DR BioCyc; MetaCyc:MON-12733; -.
DR BRENDA; 1.13.11.58; 4460.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q76I22; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 4.10.372.10; -; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001246; LipOase_plant.
DR InterPro; IPR027433; Lipoxygenase_dom_3.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; PTHR11771; 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 SUPFAM; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 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; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Reference proteome.
FT CHAIN 1..863
FT /note="Linoleate 9S-lipoxygenase 1"
FT /id="PRO_0000220707"
FT DOMAIN 32..158
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 161..863
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 204..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 518
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 523
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 709
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 713
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 863
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT CONFLICT 160
FT /note="N -> I (in Ref. 1; BAD02945)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="L -> P (in Ref. 1; BAD02945)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="H -> R (in Ref. 1; BAD02945)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="E -> K (in Ref. 1; BAD02945)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="T -> A (in Ref. 1; BAD02945)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="E -> A (in Ref. 1; BAD02945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 863 AA; 97499 MW; AA8309F3DBCEC2F1 CRC64;
MLGGLKDKLT GKNGNKIKGL AVLMSRKLLD PRDFTASLLD NVHEVFGNSI TCQLVSATVA
DQNNEGRGIV GSEANLEQGL TDLPSVSQGE SKLTVRFNWE MDKHGVPGAI IIKNHHSTKF
FLKTITLHDV PGCDTIVFVA NSWIYPVGKY HYNRIFFANN SYLPSQMPEA LRPYREDELR
YLRGEDRQGP YQEHDRIYRY DVYNDLGEPD RDNPRPVLGG SQKHPYPRRG RTGRIPTKKD
PNSESRLSLL EQIYVPSDER FAHLKMSDFA GYSIKAIVQG ILPAIRTYVD LTPGEFDSFE
DILKLYRGGL KLPSIPALEE LRKSFPVQLI KDLLPVGGSY LLKFPKPDII KENEVAWRTD
EEFAREILAG LNPMVIRRLT EFPPKSTLDP SKYGDQTSTI TPAHIEKNLE GLSVQQALDS
NRLYILDHHD HFMPFLIDIN SLDGIFTYAT RTLLFLRDDD TLKPLAIELS LPHIEGNLTS
AKSKVHTPAS SGIESWVWQL AKAYVAVNDS GWHQLISHWL NTHAVMEPFV IATNRQLSVT
HPVYKLLQPH YRDTMTINAL ARQTLINGGG IFEQTVFPGK HALAMSSAVY KNWNFTEQGL
PDDLIKRGIA IKDPSSPSKV KLLIKDYPYA TDGLAIWQAI EQWVTEYCAI YYPNDGVLQG
DVELQAWWKE VREVGHGDLK DADWWPKMQS LPELTKACTT IIWIASALHA AVNFGQYPYA
GYLPNRPTIS RRPMPEPGSK EYTELDENPE KFFIRTITSQ FQTILGVSLI EILSKHSADE
IYLGQRDTPE WTSDPKALEA FKRFSRQLVE IESKVLNMNK DPLLKNRVGP ANFPYTLMFP
NTSDNKGAAE GITARGIPNS ISI
