ID   LOXC1_ORYSJ             Reviewed;         924 AA.
AC   P38419; Q6YVT0; Q9XHM7;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Lipoxygenase 7, chloroplastic;
DE            EC=1.13.11.12;
DE   Flags: Precursor;
GN   Name=CM-LOX1; Synonyms=LOX2.1;
GN   OrderedLocusNames=Os08g0508800, LOC_Os08g39840; ORFNames=B1168A08.24;
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], AND FUNCTION.
RC   STRAIN=cv. Aichi asahi; TISSUE=Leaf;
RX   PubMed=7508918; DOI=10.1016/s0021-9258(17)41924-7;
RA   Peng Y.L., Shirano Y., Ohta H., Hibino T., Tanaka K., Shibata D.;
RT   "A novel lipoxygenase from rice. Primary structure and specific expression
RT   upon incompatible infection with rice blast fungus.";
RL   J. Biol. Chem. 269:3755-3761(1994).
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=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).
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-13 position of
CC       linoleic and linolenic acids. {ECO:0000269|PubMed:7508918}.
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   -!- INDUCTION: By fungal infection.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR   EMBL; D14000; BAA03102.1; -; mRNA.
DR   EMBL; AF095895; AAD39093.1; -; mRNA.
DR   EMBL; AP005816; BAD10665.1; -; Genomic_DNA.
DR   EMBL; AP014964; BAT06178.1; -; Genomic_DNA.
DR   RefSeq; XP_015650717.1; XM_015795231.1.
DR   AlphaFoldDB; P38419; -.
DR   SMR; P38419; -.
DR   STRING; 39947.P38419; -.
DR   PaxDb; 39947-P38419; -.
DR   EnsemblPlants; Os08t0508800-01; Os08t0508800-01; Os08g0508800.
DR   GeneID; 4345993; -.
DR   Gramene; Os08t0508800-01; Os08t0508800-01; Os08g0508800.
DR   KEGG; osa:4345993; -.
DR   eggNOG; ENOG502QQSP; Eukaryota.
DR   HOGENOM; CLU_004282_0_0_1; -.
DR   InParanoid; P38419; -.
DR   OMA; ANIQSRH; -.
DR   OrthoDB; 462210at2759; -.
DR   BioCyc; MetaCyc:MONOMER-16718; -.
DR   BRENDA; 1.13.11.12; 4460.
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; P38419; 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:0016166; F:phytoene dehydrogenase activity; IDA:Gramene.
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   GO; GO:0051707; P:response to other organism; IDA:Gramene.
DR   GO; GO:0009611; P:response to wounding; IDA:Gramene.
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; P38419; 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..61
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           62..924
FT                   /note="Lipoxygenase 7, chloroplastic"
FT                   /id="PRO_0000018327"
FT   DOMAIN          88..218
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DOMAIN          225..924
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   REGION          231..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..315
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         581
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         586
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         773
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         777
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         924
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   CONFLICT        143
FT                   /note="D -> E (in Ref. 1; AAD39093)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        342..343
FT                   /note="AA -> P (in Ref. 1; AAD39093)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350..352
FT                   /note="LLL -> CSS (in Ref. 1; BAA03102)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        450
FT                   /note="S -> T (in Ref. 1; AAD39093)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        484
FT                   /note="S -> N (in Ref. 1; BAA03102)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        540
FT                   /note="P -> L (in Ref. 1; BAA03102)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        625..628
FT                   /note="RSAL -> ARV (in Ref. 1; BAA03102)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        682
FT                   /note="H -> Q (in Ref. 1; BAA03102)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        764
FT                   /note="T -> N (in Ref. 1; BAA03102)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        819
FT                   /note="A -> R (in Ref. 1; AAD39093)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        858..864
FT                   /note="WNSDAAV -> GTATRRL (in Ref. 1; BAA03102)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   924 AA;  102819 MW;  E2142F9775751FEB CRC64;
     MLRPQLNPSS HTTTTSSSSS TQLFASSSCI ASLRRPSSSS SSVVAAARRT RGQGSSRVVV
     VCASSSATAS RGDSSSDMAA AAAVRVKAVA TIKVTVGELI NRSIDIRDLI GRSLSLELVS
     SELDAKTGKE KATVRSYAHN VDDDDHSVVT YEADFDVPSG FGPIGAIIVT NELRQEMFLE
     DINLTASDGA GNSTVLPIRC NSWVQPKSVG DEGTPSKRIF FANKTYLPGQ TPAGLRSYRK
     NDLQQKRGDG TGEREADDRV YDYDVYNDLG NPDSNGDLAR PVLGGNKQFP YPRRCRTGRP
     PSKKDPKSET RKGNVYVPRD EEFSPEKEDY FLRKTVGSVL QAAVPAAQSL LLDKLKWNLP
     FPSFFVIDKL FEDGVELPGV DKLNFLESVV PRLLEHLRDT PAEKILRFET PANIQKDKFA
     WLRDEEFARE TLAGINPYAI ELVREFPLKS KLDPAVYGPA ESAITADLLE EQMRRVMTVE
     EAISQKRLFM LDFHDLFLPY VHKIRSLDHT TMYGSRTVFF LTDDGTLQLL AIELTRPASP
     SQPQWRQVFT PSTDATMSWL WRMAKAHVRA HDAGHHELIT HWLRTHCAVE PYIIAANRQL
     SEMHPIYQLL RPHFRYTMRI NARARSALIS AGGIIERSFS PQKYSMELSS VAYDKLWRFD
     TEALPADLVR RGMAEEDPTA EHGLKLAIED YPFANDGLLI WDAIKTWVQA YVARFYPDAD
     SVAGDEELQA FWTEVRTKGH GDKKDAPWWP KLDSPESLAH TLTTIVWVAA AHHAAVNFGQ
     YDFGGYFPNR PSIARTVMPV EEPVDGAAME RFLDNPDQAL RECFPSQVQA TVVMAVLDVL
     SSHSTDEEYL GGEQTRPWNS DAAVQAAYDG FAARLKEIEG VIDGRNKDRK LKNRCGAGIL
     PYQLMKPFSD SGVTGMGIPN STSI
//