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C76M7_ORYSJ
ID   C76M7_ORYSJ             Reviewed;         500 AA.
AC   Q69X58; A0A0P0WYD0; A3BDA8;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Ent-cassadiene C11-alpha-hydroxylase 1;
DE            EC=1.14.14.112 {ECO:0000269|PubMed:19825834, ECO:0000269|PubMed:21985968, ECO:0000269|PubMed:22215681};
DE   AltName: Full=Cytochrome P450 76M7 {ECO:0000303|PubMed:19825834};
GN   Name=CYP76M7 {ECO:0000303|PubMed:19825834};
GN   OrderedLocusNames=Os06g0599200 {ECO:0000312|EMBL:BAF19912.1},
GN   LOC_Os06g39780 {ECO:0000305};
GN   ORFNames=OsJ_07204, OsJ_21875 {ECO:0000312|EMBL:EAZ37547.1},
GN   OSJNBa0008E01.17, P0025F02.46, P0642B07.53 {ECO:0000312|EMBL:BAD32943.1};
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=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 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RG   The rice full-length cDNA consortium;
RT   "Oryza sativa full length cDNA.";
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19825834; DOI=10.1105/tpc.108.063677;
RA   Swaminathan S., Morrone D., Wang Q., Fulton D.B., Peters R.J.;
RT   "CYP76M7 is an ent-cassadiene C11alpha-hydroxylase defining a second
RT   multifunctional diterpenoid biosynthetic gene cluster in rice.";
RL   Plant Cell 21:3315-3325(2009).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=21985968; DOI=10.1016/j.febslet.2011.09.038;
RA   Wu Y., Hillwig M.L., Wang Q., Peters R.J.;
RT   "Parsing a multifunctional biosynthetic gene cluster from rice: Biochemical
RT   characterization of CYP71Z6 & 7.";
RL   FEBS Lett. 585:3446-3451(2011).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY METHYL JASMONATE.
RX   PubMed=22215681; DOI=10.1074/jbc.m111.305599;
RA   Wang Q., Hillwig M.L., Okada K., Yamazaki K., Wu Y., Swaminathan S.,
RA   Yamane H., Peters R.J.;
RT   "Characterization of CYP76M5-8 indicates metabolic plasticity within a
RT   plant biosynthetic gene cluster.";
RL   J. Biol. Chem. 287:6159-6168(2012).
CC   -!- FUNCTION: Enzyme of the diterpenoid metabolism involved in the
CC       biosynthesis of antibacterial oryzalides such as phytocassane. Can use
CC       ent-cassadiene as substrate, but not C11-alpha-hydroxy-ent-cassadiene,
CC       ent-pimaradiene, ent-sandaracopimaradiene, ent-kaurene, ent-isokaurene,
CC       syn-pimaradiene, syn-stemarene, syn-stemodene.
CC       {ECO:0000269|PubMed:19825834, ECO:0000269|PubMed:21985968,
CC       ECO:0000269|PubMed:22215681}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ent-cassa-12,15-diene + O2 + reduced [NADPH--hemoprotein
CC         reductase] = ent-11beta-hydroxycassa-12,15-diene + H(+) + H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:31967,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:50060,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:63662;
CC         EC=1.14.14.112; Evidence={ECO:0000269|PubMed:19825834,
CC         ECO:0000269|PubMed:21985968, ECO:0000269|PubMed:22215681};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=39 uM for Ent-cassa-12,15-diene {ECO:0000269|PubMed:19825834};
CC         Vmax=0.13 umol/min/mg enzyme {ECO:0000269|PubMed:19825834};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Up-regulated by methyl jasmonate.
CC       {ECO:0000269|PubMed:22215681}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAZ37547.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Cytochrome P450 Homepage;
CC       URL="http://drnelson.uthsc.edu/CytochromeP450.html";
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DR   EMBL; AP003623; BAD32943.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF19912.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS98483.1; -; Genomic_DNA.
DR   EMBL; CM000143; EAZ37547.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK318614; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015641474.1; XM_015785988.1.
DR   AlphaFoldDB; Q69X58; -.
DR   SMR; Q69X58; -.
DR   STRING; 4530.OS06T0599200-01; -.
DR   PaxDb; Q69X58; -.
DR   PRIDE; Q69X58; -.
DR   EnsemblPlants; Os06t0599200-01; Os06t0599200-01; Os06g0599200.
DR   GeneID; 4341447; -.
DR   Gramene; Os06t0599200-01; Os06t0599200-01; Os06g0599200.
DR   KEGG; osa:4341447; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_2_1; -.
DR   InParanoid; Q69X58; -.
DR   OMA; GKDAEFM; -.
DR   OrthoDB; 702827at2759; -.
DR   BioCyc; MetaCyc:MON-18619; -.
DR   SABIO-RK; Q69X58; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000007752; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   Genevisible; Q69X58; OS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0036202; F:ent-cassa-12,15-diene 11-hydroxylase 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:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0051502; P:diterpene phytoalexin biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic 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..500
FT                   /note="Ent-cassadiene C11-alpha-hydroxylase 1"
FT                   /id="PRO_0000418866"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         442
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|UniProtKB:P04798"
FT   CONFLICT        372
FT                   /note="F -> C (in Ref. 4; EAZ37547)"
SQ   SEQUENCE   500 AA;  55522 MW;  61DDD8E96F912132 CRC64;
     MENSQVWLLW GALSVAVLFY LSTLRRRHAG GKPLPPGPTP LPLIGNLHLA GGTSFHHKLR
     DLARVHGPVM TLKLGLATNV VISSREAAIE AYTKYDRHLA ARATPDTFRA CGFADRSMVF
     IPSSDPRWKA LRGIQGSHVF TPRGLAAVRP IRERKVGDLM AYLRAHAGEE VLLGQAMHTG
     LLNLVSFSYF SIDIVDMGSQ MARDLREVVD DIISVVGKPN ISDFYPFLRP LDLQGLRRWT
     TKRFNRVFSI MGDIIDRRLA HIRDNKPSHN DFLDSLLELM AAGKIDRVNV LDMLFEAFVA
     GADTMALTLE WVMAELLKNP GVMAKARAEL RDVLGDKEVV EEADAARLPY LQAVLKEAMR
     LHPVGALLLP HFAVEDGVEV GGYAVPKGST VLFNAWAIMR DPAAWERPDE FVPERFVERA
     PLLDFRGKDA EFMPFGSGRR LCPGLPLAER VMPFILASML HTFEWKLPGG MTAEDVDVSE
     KFKSANVLAV PLKAVPVLIK
 
 
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