C74A2_ORYSJ
ID C74A2_ORYSJ Reviewed; 478 AA.
AC Q7XYS3; Q10PQ1; Q8H7R3; Q8VZX5; Q940D7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Allene oxide synthase 2;
DE EC=4.2.1.92;
DE AltName: Full=Cytochrome P450 74A2;
DE AltName: Full=Hydroperoxide dehydrase 2;
GN Name=CYP74A2; Synonyms=AOS2;
GN OrderedLocusNames=Os03g0225900, LOC_Os03g12500; ORFNames=OSJNBa0081P02.18;
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], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12596875; DOI=10.1271/bbb.66.2719;
RA Ha S.-B., Lee B.-C., Lee D.-E., Kuk Y.I., Lee A.-Y., Han O., Back K.;
RT "Molecular characterization of the gene encoding rice allene oxide synthase
RT and its expression.";
RL Biosci. Biotechnol. Biochem. 66:2719-2722(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Nipponbare; TISSUE=Seedling leaf;
RA Agrawal G.K., Rakwal R., Jwa N.-S., Han K.-S., Agrawal V.P.;
RT "Molecular cloning and mRNA expression analysis of the first rice jasmonate
RT biosynthetic pathway gene allene oxide synthase.";
RL Plant Physiol. Biochem. 40:771-782(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare;
RA Mei C., Qi M., Yang Y.;
RT "Characterization of rice allene oxide synthase gene.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP TISSUE SPECIFICITY, INDUCTION, AND NOMENCLATURE.
RX PubMed=14988482; DOI=10.1093/pcp/pch025;
RA Haga K., Iino M.;
RT "Phytochrome-mediated transcriptional up-regulation of ALLENE OXIDE
RT SYNTHASE in rice seedlings.";
RL Plant Cell Physiol. 45:119-128(2004).
CC -!- FUNCTION: Involved in the biosynthesis of jasmonic acid, a growth
CC regulator that is implicated also as a signaling molecule in plant
CC defense. Converts 13-hydroperoxylinolenic acid to 12,13-epoxylinolenic
CC acid. {ECO:0000269|PubMed:12596875}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate =
CC (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O;
CC Xref=Rhea:RHEA:25074, ChEBI:CHEBI:15377, ChEBI:CHEBI:36438,
CC ChEBI:CHEBI:58757; EC=4.2.1.92;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC -!- TISSUE SPECIFICITY: Weakly expressed in roots, shoots, leaves and
CC flowers. {ECO:0000269|PubMed:12596875, ECO:0000269|PubMed:14988482,
CC ECO:0000269|Ref.2}.
CC -!- INDUCTION: By jasmonic acid, salicylic acid, hydrogen peroxide, copper
CC and by the protein phosphatases cantharidin, endothall and okadaic acid
CC in light-grown seedling leaves. By incompatible rice blast fungus
CC M.grisea. Not induced by red (R) light or abrasion in dark-grown
CC seedlings. {ECO:0000269|PubMed:12596875, ECO:0000269|PubMed:14988482,
CC ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AY055775; AAL17675.1; -; mRNA.
DR EMBL; AY062258; AAL38184.1; -; Genomic_DNA.
DR EMBL; AY310358; AAP75620.1; -; mRNA.
DR EMBL; AC107226; AAN52753.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF94742.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11350.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83058.1; -; Genomic_DNA.
DR EMBL; AK061758; BAG88095.1; -; mRNA.
DR RefSeq; XP_015628763.1; XM_015773277.1.
DR AlphaFoldDB; Q7XYS3; -.
DR SMR; Q7XYS3; -.
DR STRING; 4530.OS03T0225900-01; -.
DR PaxDb; Q7XYS3; -.
DR PRIDE; Q7XYS3; -.
DR EnsemblPlants; Os03t0225900-01; Os03t0225900-01; Os03g0225900.
DR EnsemblPlants; Os03t0225900-02; Os03t0225900-02; Os03g0225900.
DR GeneID; 4332121; -.
DR Gramene; Os03t0225900-01; Os03t0225900-01; Os03g0225900.
DR Gramene; Os03t0225900-02; Os03t0225900-02; Os03g0225900.
DR KEGG; osa:4332121; -.
DR eggNOG; ENOG502QQNS; Eukaryota.
DR HOGENOM; CLU_045757_0_0_1; -.
DR InParanoid; Q7XYS3; -.
DR OMA; NIRNAPA; -.
DR OrthoDB; 759497at2759; -.
DR PlantReactome; R-OSA-1119332; Jasmonic acid biosynthesis.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q7XYS3; OS.
DR GO; GO:0009978; F:allene oxide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Heme; Iron;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Metal-binding;
KW Oxylipin biosynthesis; Reference proteome.
FT CHAIN 1..478
FT /note="Allene oxide synthase 2"
FT /id="PRO_0000052125"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277..278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344..347
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CONFLICT 65
FT /note="D -> E (in Ref. 3; AAP75620)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="E -> Q (in Ref. 1; AAL17675)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="E -> K (in Ref. 1; AAL17675)"
FT /evidence="ECO:0000305"
FT CONFLICT 197..201
FT /note="PTKAA -> LDQGR (in Ref. 1; AAL17675)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="R -> T (in Ref. 3; AAP75620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 52271 MW; FB67CBCB5BA80CB4 CRC64;
MELGVPLPRR PVPGSYGVPF VSAVRDRLDF YYLQGQDKYF ESRAERYGST VVRINVPPGP
FMARDPRVVA LLDAKSFPVL FDVAKVEKRD VFTGTFMPST SLTGGYRVCA YLDPSEPNHA
KIKQLLLSLL VSRKDAFVPV FRSNFGALLD TVESQLASGG GKSDFTALND ATSFEFIGEA
YFGVRPSASS SLGTGGPTKA ALWLLWQLAP LTTLGLPMII EDPLLHTLPL PPFLISSDYK
ALYAYFAAAA SQALDAAEGL GLSREEACHN LLFATVFNSY GGFKLLLPQI LSRVAQAGEK
LHERLAAEIR SAVADAGGNV TLAALEKMEL TRSVVWEALR LDPPVRFQYG RAKADLEIES
HDASFAIKKG EMLFGYQPCA TRDPRVFGAT AREFVGDRFV GEEGRKLLQY VYWSNGRETE
NPSVDNKQCP GKNLVVLVGR LLLVELFLRY DTFTAEAGKK VVITGVTKAS TSAVNRTA
