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C74A4_ORYSJ
ID   C74A4_ORYSJ             Reviewed;         510 AA.
AC   Q6Z6K9; Q0E2R6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Allene oxide synthase 4;
DE            EC=4.2.1.92;
DE   AltName: Full=Cytochrome P450 74A4;
DE   AltName: Full=Hydroperoxide dehydrase 4;
GN   Name=CYP74A4; Synonyms=AOS4;
GN   OrderedLocusNames=Os02g0218800, LOC_Os02g12690; ORFNames=P0027A02.15;
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=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   [2]
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   [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).
RN   [4]
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   [5]
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 (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   -!- TISSUE SPECIFICITY: Expressed in dark-grown seedlings.
CC       {ECO:0000269|PubMed:14988482}.
CC   -!- INDUCTION: By red (R) light and far-red (FR) light in dark-grown
CC       seedlings. Not induced by abrasion. {ECO:0000269|PubMed:14988482}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AP004996; BAD17184.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF08222.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS77679.1; -; Genomic_DNA.
DR   EMBL; AK105964; BAG97469.1; -; mRNA.
DR   RefSeq; XP_015623380.1; XM_015767894.1.
DR   AlphaFoldDB; Q6Z6K9; -.
DR   SMR; Q6Z6K9; -.
DR   STRING; 4530.OS02T0218800-01; -.
DR   PaxDb; Q6Z6K9; -.
DR   PRIDE; Q6Z6K9; -.
DR   EnsemblPlants; Os02t0218800-01; Os02t0218800-01; Os02g0218800.
DR   GeneID; 4328743; -.
DR   Gramene; Os02t0218800-01; Os02t0218800-01; Os02g0218800.
DR   KEGG; osa:4328743; -.
DR   eggNOG; ENOG502QQNS; Eukaryota.
DR   HOGENOM; CLU_045757_0_0_1; -.
DR   InParanoid; Q6Z6K9; -.
DR   OMA; YKIFLPH; -.
DR   OrthoDB; 485250at2759; -.
DR   PlantReactome; R-OSA-1119332; Jasmonic acid biosynthesis.
DR   UniPathway; UPA00382; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6Z6K9; 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; 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   Fatty acid biosynthesis; Fatty acid metabolism; Heme; Iron;
KW   Lipid biosynthesis; Lipid metabolism; Lyase; Metal-binding;
KW   Oxylipin biosynthesis; Reference proteome.
FT   CHAIN           1..510
FT                   /note="Allene oxide synthase 4"
FT                   /id="PRO_0000052127"
FT   BINDING         299..300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         367..370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         454
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   510 AA;  55330 MW;  93EE98E53F02DEAE CRC64;
     MAPPRANSGD GNDGAVGGQS KLSPSGLLIR EIPGGYGVPF LSPLRDRLDY YYFQGADEFF
     RSRVARHGGA TVLRVNMPPG PFLAGDPRVV ALLDARSFRV LLDDSMVDKA DTLDGTFMPS
     LALFGGHRPL AFLDAADPRH AKIKRVVMSL AAARMHHVAP AFRAAFAAMF DEVDAGLVAG
     GPVEFNKLNM RYMLDFTCAA LFGGAPPSKA MGDAAVTKAV KWLIFQLHPL ASKVVKPWPL
     EDLLLHTFRL PPFLVRREYG EITAYFAAAA AAILDDAEKN HPGIPRDELL HNLVFVAVFN
     AYGGFKIFLP HIVKWLARAG PELHAKLASE VRAAAPAGGG EITISAVEKE MPLVKSVVWE
     ALRMNPPVEF QYGRARRDMV VESHDAAYEV RKGELLFGYQ PLATRDEKVF DRAGEFVPDR
     FVSGAGSAAR PLLEHVVWSN GPETGTPSEG NKQCPGKDMV VAVGRLMVAG LFRRYDTFAA
     DVEELPLEPV VTFTSLTRAA DGDGAARRGV
 
 
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