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   27-MAR-2024, entry version 122.
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; 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   -!- 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; 39947.Q84YK8; -.
DR   PaxDb; 39947-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; HSYAHKV; -.
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 8.
DR   Proteomes; UP000059680; Chromosome 8.
DR   ExpressionAtlas; Q84YK8; baseline and differential.
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; 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:SF127; LIPOXYGENASE 7, CHLOROPLASTIC; 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; Q84YK8; OS.
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
//