LOXC2_ORYSJ
ID LOXC2_ORYSJ Reviewed; 941 AA.
AC Q84YK8; Q0J4K1; Q7EXZ6; Q9XHM6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable lipoxygenase 8, chloroplastic;
DE EC=1.13.11.12;
DE Flags: Precursor;
GN Name=CM-LOX2; OrderedLocusNames=Os08g0509100, LOC_Os08g39850;
GN ORFNames=B1168A08.28-1, B1168A08.28-2, OSJNBa0016N23.103-1,
GN OSJNBa0016N23.103-2;
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=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 [2]
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 [3]
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 [4]
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 259-941.
RC STRAIN=cv. Aichi asahi; TISSUE=Seedling leaf;
RA Peng Y., Hou Z.;
RT "Purification and cDNA cloning of two rice lipoxygenases induced by blast
RT fungus.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
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. It 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD10669.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD10729.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005816; BAD10668.1; -; Genomic_DNA.
DR EMBL; AP005816; BAD10669.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP006049; BAC57390.1; -; Genomic_DNA.
DR EMBL; AP006049; BAD10729.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008214; BAF24114.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT06179.1; -; Genomic_DNA.
DR EMBL; AK066825; BAG90142.1; -; mRNA.
DR EMBL; AF095896; AAD42043.1; -; mRNA.
DR RefSeq; XP_015650450.1; XM_015794964.1.
DR AlphaFoldDB; Q84YK8; -.
DR SMR; Q84YK8; -.
DR STRING; 4530.OS08T0509100-01; -.
DR PaxDb; Q84YK8; -.
DR PRIDE; Q84YK8; -.
DR EnsemblPlants; Os08t0509100-01; Os08t0509100-01; Os08g0509100.
DR GeneID; 4345994; -.
DR Gramene; Os08t0509100-01; Os08t0509100-01; Os08g0509100.
DR KEGG; osa:4345994; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR HOGENOM; CLU_004282_0_0_1; -.
DR InParanoid; Q84YK8; -.
DR OMA; GVVTYEA; -.
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 8.
DR Proteomes; UP000059680; Chromosome 8.
DR ExpressionAtlas; Q84YK8; baseline and differential.
DR Genevisible; Q84YK8; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 Chloroplast; Dioxygenase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW Oxylipin biosynthesis; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..941
FT /note="Probable lipoxygenase 8, chloroplastic"
FT /id="PRO_0000018328"
FT DOMAIN 100..236
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 242..941
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 598
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 603
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 790
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 794
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT BINDING 941
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT CONFLICT 590
FT /note="A -> T (in Ref. 5; AAD42043)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="A -> T (in Ref. 5; AAD42043)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="A -> T (in Ref. 5; AAD42043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 941 AA; 104494 MW; BE3C7BA515137C32 CRC64;
MLRPQLNPSS SHHHTTTTSS SSSTQLYFAS SSCIASLRRP SPPSLIAGAG CRTTRRRQQG
RQRVVVRCAS SSAASSASEA ARRGTGSSDM APAAVVKVKA VATIKVTVEG LLNSLRPSKA
IDNIRDLIGR SLFLELVSSE LEAKTGKKKA TVHSYAHKVD DDDHGVVTYE ADFDVPTGFG
PIGAVVVTNE LGQEMFLEDL NLTAGDGAGN STVLPIRCNS WVQPKSSIDE GTPGKRIFFA
KAYLPGQTPA GLRSYREEDL KQKRGNGAGQ READDRVYDY DVYNDLGNPD SNGDLARPVL
GGSKQFPYPR RCRTGRPPSK KDPKSETRKG NVYVPRDEEF SEVKNAQFLL KTLQSVLHAA
VPAAQSALID NLSLNLPFPS FFVIDKLFED GVELPGVEKL GFLHSIVPRL LELLRDSPGD
KILLFDTPAN VQKDKFAWLR DEEFARETLA GINPYAIELV REFPLKSKLD PAVYGPAESA
ITADLLEEQM RRVMTVEEAI SQKRLFMLDF HDLFLPYVHK IRSLKHTTMY GSRTIFFLTD
DGTLRLLAIE LTRPASPSQP QWRQVFTPST DTTKSWLWRM AKAHVRAHDA GHHELITHWL
RTHCAVEPYI IAANRQLSEM HPIYQLLHPH FRYTMRINAL ARSRLISAAG IIELSFSPQK
YSMELSSVAY DKLWRFDMEA LPADLVRRGM AEEDPTAEHG LRLAIEDYPF ANDGLLIWDA
IKTWVQAYVA RFYPDADSVA GDEELQAFWT EVRTKGHGDK KDAPWWPKLD SPESLAHTLT
TIVWVAAAHH AAVNFGQYDF GGYFPNRPSI ARTVMPVEEP VDGAAMERFL DNPDQALREC
FPSQVQATVV MAVLDVLSTH STDEEYLGGE QTRPWNSDAA VQAAYAGFTA RLKEIEGVID
GRNKDRKLKN RCGAGILPYQ LMKPFSDAGV TGMGIPNSTS I
