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C74A1_ORYSJ
ID   C74A1_ORYSJ             Reviewed;         512 AA.
AC   Q7Y0C8;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Allene oxide synthase 1, chloroplastic;
DE            EC=4.2.1.92;
DE   AltName: Full=Cytochrome P450 74A1;
DE   AltName: Full=Hydroperoxide dehydrase 1;
DE   Flags: Precursor;
GN   Name=CYP74A1; Synonyms=AOS1;
GN   OrderedLocusNames=Os03g0767000, LOC_Os03g55800;
GN   ORFNames=OSJNBa0079B15.7, OSJNBb0106M04.24;
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], TISSUE SPECIFICITY, INDUCTION, AND
RP   NOMENCLATURE.
RC   STRAIN=cv. Nipponbare; TISSUE=Seedling leaf;
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).
RN   [2]
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   [3]
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   [4]
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: 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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in coleoptiles, and at lower level in
CC       leaves of dark-grown seedlings. {ECO:0000269|PubMed:14988482}.
CC   -!- INDUCTION: Transiently induced by red (R) light, far-red (FR) light and
CC       abrasion in dark-grown seedlings. Not induced by FR light in
CC       phytochrome A (phyA) mutant. {ECO:0000269|PubMed:14988482}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB116527; BAD08330.1; -; mRNA.
DR   EMBL; AC099043; AAP50956.1; -; Genomic_DNA.
DR   EMBL; AC107207; AAR87328.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS86563.1; -; Genomic_DNA.
DR   RefSeq; XP_015631686.1; XM_015776200.1.
DR   AlphaFoldDB; Q7Y0C8; -.
DR   SMR; Q7Y0C8; -.
DR   STRING; 4530.OS03T0767000-01; -.
DR   PaxDb; Q7Y0C8; -.
DR   PRIDE; Q7Y0C8; -.
DR   EnsemblPlants; Os03t0767000-01; Os03t0767000-01; Os03g0767000.
DR   GeneID; 4334233; -.
DR   Gramene; Os03t0767000-01; Os03t0767000-01; Os03g0767000.
DR   KEGG; osa:4334233; -.
DR   eggNOG; ENOG502QQNS; Eukaryota.
DR   HOGENOM; CLU_045757_0_0_1; -.
DR   InParanoid; Q7Y0C8; -.
DR   OMA; KVTMAAM; -.
DR   OrthoDB; 485250at2759; -.
DR   PlantReactome; R-OSA-1119332; Jasmonic acid biosynthesis.
DR   UniPathway; UPA00382; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   ExpressionAtlas; Q7Y0C8; baseline and differential.
DR   Genevisible; Q7Y0C8; OS.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
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:0050832; P:defense response to fungus; IEA:EnsemblPlants.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009695; P:jasmonic acid biosynthetic process; IEA:EnsemblPlants.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009753; P:response to jasmonic acid; IEA:EnsemblPlants.
DR   GO; GO:0009611; P:response to wounding; IEA:EnsemblPlants.
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; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Heme; Iron;
KW   Lipid biosynthesis; Lipid metabolism; Lyase; Membrane; Metal-binding;
KW   Oxylipin biosynthesis; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..512
FT                   /note="Allene oxide synthase 1, chloroplastic"
FT                   /id="PRO_0000003627"
FT   REGION          23..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         314..315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         381..384
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         465
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"
SQ   SEQUENCE   512 AA;  56504 MW;  27B86DCE56157AAF CRC64;
     MATAAACISF ASPSPARVVI RRQTRASASA SATDRQEVVS PKRRLPLRKV PGDYGPPVVG
     AIRDRYEYFY GPGGRDGFFA ARVRAHRSTV VRLNMPPGPF VARDPRVVAL LDAASFPVLF
     DTSLVDKTDL FTGTFMPSTD LTGGYRVLSY LDPSEPNHAP LKTLLFYLLS HRRQQVIPKF
     REVYGDLFGL MENDLARVGK ADFGVHNDAA AFGFLCQGLL GRDPAKSALG RDGPKLITKW
     VLFQLSPLLS LGLPTLVEDT LLHSLRLPPA LVKKDYDRLA DFFRDAAKAV VDEGERLGIA
     REEAVHNILF ALCFNSFGGM KILFPTLVKW LGRAGARVHG RLATEVRGAV RDNGGEVTMK
     ALAEMPLVKS AVYEALRIEP PVAMQYGRAK RDMVVESHDY GYEVREGEML FGYQPMATKD
     PRVFARPEEY VPDRFLGEDG ARLLRHVVWS NGPETAAPTL HDKQCAGKDF VVLVARLLLV
     ELFLRYDSFD VEVGTSTLGS SVTVTSLKKA TF
 
 
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