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 27-MAR-2024, entry version 129. 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; Evidence={ECO:0000255|PROSITE- CC 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 39947.Q8H016; -. DR PaxDb; 39947-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; ILIWNAS; -. DR OrthoDB; 462210at2759; -. 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 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; 3.10.450.60; -; 1. DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 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; LIPOXYGENASE; 1. DR PANTHER; PTHR11771:SF113; LIPOXYGENASE 6-RELATED; 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; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1. DR SUPFAM; SSF48484; Lipoxigenase; 1. DR PROSITE; PS00711; LIPOXYGENASE_1; 1. DR PROSITE; PS00081; LIPOXYGENASE_2; 1. DR PROSITE; PS51393; LIPOXYGENASE_3; 1. DR PROSITE; PS50095; PLAT; 1. DR Genevisible; Q8H016; OS. 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 //