ID   LOX5_ORYSJ              Reviewed;         899 AA.
AC   Q7XV13;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   24-JAN-2024, entry version 107.
DE   RecName: Full=Putative lipoxygenase 5;
DE            EC=1.13.11.12;
GN   OrderedLocusNames=Os04g0447100, LOC_Os04g37430;
GN   ORFNames=OSJNBa0064H22.1;
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=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
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. 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}.
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DR   EMBL; AL606448; CAD40882.2; -; Genomic_DNA.
DR   EMBL; AP014960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q7XV13; -.
DR   SMR; Q7XV13; -.
DR   STRING; 39947.Q7XV13; -.
DR   PaxDb; 39947-Q7XV13; -.
DR   eggNOG; ENOG502QQSP; Eukaryota.
DR   HOGENOM; CLU_004282_0_0_1; -.
DR   InParanoid; Q7XV13; -.
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 4.
DR   Proteomes; UP000059680; Chromosome 4.
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:SF95; LIPOXYGENASE 4, 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; Q7XV13; OS.
PE   3: Inferred from homology;
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..899
FT                   /note="Putative lipoxygenase 5"
FT                   /id="PRO_0000220711"
FT   DOMAIN          68..204
FT                   /note="PLAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT   DOMAIN          207..899
FT                   /note="Lipoxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   REGION          15..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         559
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         564
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         751
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         755
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT   BINDING         899
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
SQ   SEQUENCE   899 AA;  100082 MW;  02FDC5545BBAE928 CRC64;
     MRGGAGMCFA SMEAAGSRGM GKGASRRRTA RSTAPVGALV ERVVVAPAPV EQQRGAGRPE
     AHPQSVAARA VVTVRRRRKE DAKDRFAEQL DALADRVGRS VLLELVSTET DPRKGTPKKS
     KPSALVGWFD KKDVKAERVV YTAEFAVDAG FGEPGAVTVL NRHQREFYIE SIVVEGFPTG
     PAHFTCNSWV QPTRVSRDRR VFFSNRPYLP SETPPGLREL RLRELADLRG DGTGERRITD
     RVYDYDVYND LGNPDKGVAS ARPVLGGEQM PYPRRMRTGR PSTATDASAE SRVEYPEPIY
     VSRDEEFEEG KNEMLSEGAI KALLHNFMPL LVSSVSPDIR DFAGFHDVDN LFKEGLRLKQ
     ALHDQLFQKI PFVRKIQENS EGLLRYDTPD IIKKDKFAWL RDDEFARQAL AGINPVNIER
     LQAFPPVSKL DPAVYGPPES AITEEHIIGH LDGMSVQEAV EGSRLYMLDY HDIFLPFLDR
     INAQDGRKAY GTRAVFFLTA AGTLKPIAIE LCLPPMTDGC KRAKRVFTPP ADATSNWLWQ
     LAKAHVCSND AGVHQLINHW LRTHACMEPF IIAAHRQMSA MHPIFKLLKP HMRYTLKINA
     LARQILINGD GVIESGFTPG NVCMEMSAFA YRELWRLDQE GLPADLIRRG MAVEDPSQPH
     GLRLLIEDYP YAADGLLLWS AISRWCEAYV AAYYPSDEAV QADYELQSWY AEAVQSGHAD
     KRGAPWWPRL STPGDLASLL TTLVWLCSAQ HAALNFGQYP LGGYIPNRPP LMRRLVPAEG
     DPEYAHLVAD PHRFFLSALP SLTQTTTFMT VIDTLSTHSA DEEYLGERPD EAWTADPAAL
     AAAREFAADV RRAEEEIERR NADPSRRNRC GAGVLPYELM APSSGPGITC RGVPNSVTI
//