LOX6_ORYSJ
ID LOX6_ORYSJ Reviewed; 918 AA.
AC Q8H016; A0A0P0VTS2; Q10QX5; Q8H7L4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable lipoxygenase 6;
DE EC=1.13.11.12;
GN OrderedLocusNames=Os03g0179900 {ECO:0000312|EMBL:BAF11072.1},
GN LOC_Os03g08220 {ECO:0000312|EMBL:ABF94297.1};
GN ORFNames=OSJNBa0050H14.14, OSJNBb0076N15.1;
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 [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 [2]
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 [3]
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 [4]
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 [5]
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. Catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-
CC octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13S)-hydroperoxy-
CC (9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:34495,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:58757;
CC EC=1.13.11.12;
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 -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN65431.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAO13474.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC125472; AAO13474.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC126223; AAN65431.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF94297.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11072.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS82610.1; -; Genomic_DNA.
DR EMBL; AK121637; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015630875.1; XM_015775389.1.
DR AlphaFoldDB; Q8H016; -.
DR SMR; Q8H016; -.
DR STRING; 4530.OS03T0179900-01; -.
DR PaxDb; Q8H016; -.
DR PRIDE; Q8H016; -.
DR EnsemblPlants; Os03t0179900-01; Os03t0179900-01; Os03g0179900.
DR GeneID; 4331824; -.
DR Gramene; Os03t0179900-01; Os03t0179900-01; Os03g0179900.
DR KEGG; osa:4331824; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; Q8H016; -.
DR OMA; QGILKYD; -.
DR OrthoDB; 385042at2759; -.
DR PlantReactome; R-OSA-1119332; Jasmonic acid biosynthesis.
DR PlantReactome; R-OSA-1119566; Divinyl ether biosynthesis II (13-LOX).
DR PlantReactome; R-OSA-1119618; 13-LOX and 13-HPL pathway.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q8H016; baseline and differential.
DR Genevisible; Q8H016; OS.
DR GO; GO:0016165; F:linoleate 13S-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 CDD; cd01751; PLAT_LH2; 1.
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; IPR042057; Lipoxy_PLAT/LH2.
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 Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Reference proteome.
FT CHAIN 1..918
FT /note="Probable lipoxygenase 6"
FT /id="PRO_0000220712"
FT DOMAIN 90..218
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 221..918
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 56..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 573
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 578
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 765
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 769
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 918
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ SEQUENCE 918 AA; 101959 MW; 25BB8DD1E7906CF8 CRC64;
MELTGLTRAA AAATVTPPAP RRGWGELRFA PLLPGERHGR RKVVVAAISE EVPRLAASPS
SGIKGGGAGE RRPAPEKVAL RAALTVRRKQ KEDIKEAVAG HLDALWDMVG RNVVLELIST
KIHPRTKKPM QSGRVSIKDW CQKRGAKGDH VVYTAEFTVD ADFGEPGAIA VANRHNREFF
LESIVVEGGG LPCGPVHFAC NSWVQSTREL PTKRVFFSNK PYLPSETPPG LRELREKELK
DLRGDGTGVR KLSDRIYDYA TYNDLGNPDK GKEFIRPILG GEKIPYPRRC RTGRPPTDTN
MLAESRVEKP HPIYVPRDEA FEELKQGAFS SGRLRAVLHT LIPSLIASIS AETHNFQGFH
HIDNLYKEGL RLKLGLQEHL FQKIPLVQKI QESSEGMLRY DTPSILSKDK FAWLRDDEFA
RQAVAGINPV NIERLQVFPP VSKLDPAIYG PPESSITETH IAGHLNGLTV QQAMDEAKLF
IVDYHDAYLP FLDRINAIDG RKAYATRTIF FLTEAGTLKP IAIELSLPPA KPGEPRPSKV
LTPPYDATSN WLWMLAKAHV SSNDAGVHQL VNHWLRTHAT MEPFILAAHR HMSAMHPIFK
LLHPHMRYTL EINALARQSL INADGVIESC FTPGPVSGEI SAAYYRNHWR FDLEGLPSDL
IRRGVAVEDA TQPHGVRLLI EDYPYANDGL LLWSAIRSWV ESYVQLYYPD AGTVQCDLEL
QGWYHESIHV GHGDLRHAPW WPPLSTPVDL ASILTTLVWL ASAQHAALNF GQYPLGGYVP
NRPPLIRRLL PDLERDAAEY AAFLADPHRF FLNAMPGVLE ATKFMAVVDT LSTHSPDEEY
LGEGRDEGGV PWTADEAAVA AHGMFAADVR RAEETIERRN ADHGRKNRCG AGVLPYELLA
PSSPPGVTCR GVPNSISI
