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C99A3_ORYSJ
ID   C99A3_ORYSJ             Reviewed;         502 AA.
AC   Q0JF01; A0A0P0W6Z1; A3ARJ3; B7EK40; Q5JQE4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=9-beta-pimara-7,15-diene oxidase;
DE            EC=1.14.14.111 {ECO:0000269|PubMed:21175892};
DE   AltName: Full=Cytochrome P450 99A3;
GN   Name=CYP99A3; OrderedLocusNames=Os04g0178400, LOC_Os04g09920;
GN   ORFNames=OsJ_013415, OSJNBa0096F01.14;
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=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   [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).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
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   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18759039; DOI=10.1360/02yc9056;
RA   Zhong L., Wang K., Tan J., Li W., Li S.;
RT   "Putative cytochrome P450 genes in rice genome (Oryza sativa L. ssp.
RT   indica) and their EST evidence.";
RL   Sci. China, Ser. C, Life Sci. 45:512-517(2002).
RN   [8]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=17872948; DOI=10.1074/jbc.m703344200;
RA   Shimura K., Okada A., Okada K., Jikumaru Y., Ko K.-W., Toyomasu T.,
RA   Sassa T., Hasegawa M., Kodama O., Shibuya N., Koga J., Nojiri H.,
RA   Yamane H.;
RT   "Identification of a biosynthetic gene cluster in rice for momilactones.";
RL   J. Biol. Chem. 282:34013-34018(2007).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION
RP   BY JASMONIC ACID.
RX   PubMed=21175892; DOI=10.1111/j.1365-313x.2010.04408.x;
RA   Wang Q., Hillwig M.L., Peters R.J.;
RT   "CYP99A3: functional identification of a diterpene oxidase from the
RT   momilactone biosynthetic gene cluster in rice.";
RL   Plant J. 65:87-95(2011).
CC   -!- FUNCTION: Involved in momilactone phytoalexins biosynthesis; acts as a
CC       multifunctional diterpene oxidase. Participates in the biosynthetic
CC       steps between 9-beta-pimara-7,15-diene and 3-beta-hydroxy-9-beta-
CC       pimara-7,15-dien-19,6-beta-olide. Catalyzes also consecutive oxidations
CC       at C19 of syn-stemod-13(17)-ene. {ECO:0000269|PubMed:17872948,
CC       ECO:0000269|PubMed:21175892}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9beta-pimara-7,15-diene + 3 O2 + 3 reduced [NADPH--hemoprotein
CC         reductase] = 9beta-pimara-7,15-dien-19-oate + 4 H(+) + 4 H2O + 3
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:31951,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:50067,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:63659;
CC         EC=1.14.14.111; Evidence={ECO:0000269|PubMed:21175892};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2 uM for syn-pimaradiene {ECO:0000269|PubMed:21175892};
CC         KM=9 uM for syn-stemodene {ECO:0000269|PubMed:21175892};
CC         Note=kcat is 46 sec(-1) with syn-pimaradiene as substrate and 49
CC         sec(-1) with syn-stemodene as substrate.
CC         {ECO:0000269|PubMed:21175892};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: By chitin oligosaccharide elicitor and jasmonic acid (MeJA).
CC       {ECO:0000269|PubMed:17872948, ECO:0000269|PubMed:21175892}.
CC   -!- MISCELLANEOUS: 3-beta-hydroxy-9-beta-pimara-7,15-dien-19,6-beta-olide
CC       is a precursor of the phytoalexins momilactones A and B. Phytoalexins
CC       are diterpenoid secondary metabolites involved in the defense mechanism
CC       of the plant and produced in response to attack (by a pathogen,
CC       elicitor or UV irradiation). Momilactone B can also act as an
CC       allochemical (an antimicrobial and allelopathic agent), being
CC       constitutively produced in the root of the plant and secreted to the
CC       rhizosphere where it suppresses the growth of neighboring plants and
CC       soil microorganisms.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE04106.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=EAZ29932.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Cytochrome P450 Homepage;
CC       URL="http://drnelson.uthsc.edu/CytochromeP450.html";
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DR   EMBL; AL662933; CAE04106.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP008210; BAF14086.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS87950.1; -; Genomic_DNA.
DR   EMBL; CM000141; EAZ29932.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK071864; BAG92737.1; -; mRNA.
DR   RefSeq; XP_015634021.1; XM_015778535.1.
DR   AlphaFoldDB; Q0JF01; -.
DR   SMR; Q0JF01; -.
DR   STRING; 4530.OS04T0178400-01; -.
DR   PaxDb; Q0JF01; -.
DR   PRIDE; Q0JF01; -.
DR   EnsemblPlants; Os04t0178400-01; Os04t0178400-01; Os04g0178400.
DR   GeneID; 4335091; -.
DR   Gramene; Os04t0178400-01; Os04t0178400-01; Os04g0178400.
DR   KEGG; osa:4335091; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_1_1; -.
DR   InParanoid; Q0JF01; -.
DR   OMA; LINSWAM; -.
DR   OrthoDB; 702827at2759; -.
DR   BioCyc; MetaCyc:MON-18613; -.
DR   BRENDA; 1.14.14.111; 4460.
DR   SABIO-RK; Q0JF01; -.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000007752; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   Genevisible; Q0JF01; OS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0036209; F:9beta-pimara-7,15-diene oxidase activity; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR   GO; GO:0071395; P:cellular response to jasmonic acid stimulus; IEP:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0016101; P:diterpenoid metabolic process; IDA:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..502
FT                   /note="9-beta-pimara-7,15-diene oxidase"
FT                   /id="PRO_0000349107"
FT   TRANSMEM        4..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         438
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   502 AA;  55892 MW;  FB572E00D9997A01 CRC64;
     MMEINSEATV TLVSVVTLPI LLALLTRKSS SKKRRPPGPW NLPLVGGLLH LLRSQPQVAL
     RDLAGKYGPV MFLRTGQVDT VVISSPAAAQ EVLRDKDVTF ASRPSLLVSE IFCYGNLDIG
     FAPYGAYWRM LRKLCTVELL STKMVRQLAP IRDGETLALV RNIEAAAGGK KPFTLATLLI
     SCTNTFTAKA AFGQACGGEL QEQFLTALDE ALKFSNGFCF GDLFPSLRFI DAMTGLRSRL
     ERLRLQLDTV FDKIVAQCES NPGDSLVNVL LRIKDQGELD FPFSSTHVKA IILDMFTGGT
     ETTSSTTEWL MSELMRNPEV MAKVQAEVRG VFDNKSPQDH EGLLENLSYM KLVIKETLRL
     NPVLPLLLPH LCRETCEIGG YEIVEGTRVL INSWAMARSP EYWDDAEKFI PERFEDGTAD
     FKGSRFEYLP FGTGRRRCPG DIFAMATLEL IVARLLYYFD WSLPDGMQPG DIDMELVVGA
     TARRKNHLQL VASPYKPISM QS
 
 
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