LOXC1_ORYSJ
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 03-AUG-2022, entry version 145.
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;
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 -!- 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; 4530.OS08T0508800-01; -.
DR PaxDb; P38419; -.
DR PRIDE; 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; 385042at2759; -.
DR BioCyc; MetaCyc:MON-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 Genevisible; P38419; 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: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; 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..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
