C7018_ORYSJ
ID C7018_ORYSJ Reviewed; 510 AA.
AC Q0DBF4; A0A0N7KMA9; Q5Z5S0; Q6GZ42;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ent-sandaracopimaradiene 3-hydroxylase {ECO:0000303|PubMed:22247270};
DE EC=1.14.14.70 {ECO:0000269|PubMed:22247270, ECO:0000269|PubMed:23795884};
DE AltName: Full=Cytochrome P450 701A8 {ECO:0000303|PubMed:22247270};
DE AltName: Full=Ent-kaurene oxidase 4 {ECO:0000303|PubMed:15075394};
DE Short=OsKO4 {ECO:0000303|PubMed:15075394};
DE AltName: Full=Ent-kaurene oxidase-like 4 {ECO:0000303|PubMed:15316288};
DE Short=OsKOL4 {ECO:0000303|PubMed:15316288};
DE AltName: Full=OsKOS1 {ECO:0000303|PubMed:16299167};
DE AltName: Full=Syn-pimaradiene 3-monooxygenase {ECO:0000303|PubMed:25758958};
DE EC=1.14.14.68 {ECO:0000269|PubMed:25758958};
GN Name=CYP701A8 {ECO:0000303|PubMed:22247270};
GN Synonyms=KO1 {ECO:0000312|EMBL:AAT46567.1};
GN OrderedLocusNames=Os06g0569500 {ECO:0000312|EMBL:BAF19819.1},
GN LOC_Os06g37300 {ECO:0000305};
GN ORFNames=OSJNBa0062E01.27 {ECO:0000312|EMBL:BAD54592.1};
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 {ECO:0000312|EMBL:BAF19819.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH RICE DWARF VIRUS (RDV) P2
RP PROTEIN.
RC STRAIN=cv. Xiushui 11;
RX PubMed=16299167; DOI=10.1104/pp.105.072306;
RA Zhu S., Gao F., Cao X., Chen M., Ye G., Wei C., Li Y.;
RT "The rice dwarf virus P2 protein interacts with ent-kaurene oxidases in
RT vivo, leading to reduced biosynthesis of gibberellins and rice dwarf
RT symptoms.";
RL Plant Physiol. 139:1935-1945(2005).
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 TISSUE SPECIFICITY, AND INDUCTION BY ELICITOR.
RX PubMed=15316288; DOI=10.1023/b:plan.0000038261.21060.47;
RA Itoh H., Tatsumi T., Sakamoto T., Otomo K., Toyomasu T., Kitano H.,
RA Ashikari M., Ichihara S., Matsuoka M.;
RT "A rice semi-dwarf gene, Tan-Ginbozu (D35), encodes the gibberellin
RT biosynthesis enzyme, ent-kaurene oxidase.";
RL Plant Mol. Biol. 54:533-547(2004).
RN [6]
RP GENE FAMILY.
RX PubMed=15075394; DOI=10.1104/pp.103.033696;
RA Sakamoto T., Miura K., Itoh H., Tatsumi T., Ueguchi-Tanaka M., Ishiyama K.,
RA Kobayashi M., Agrawal G.K., Takeda S., Abe K., Miyao A., Hirochika H.,
RA Kitano H., Ashikari M., Matsuoka M.;
RT "An overview of gibberellin metabolism enzyme genes and their related
RT mutants in rice.";
RL Plant Physiol. 134:1642-1653(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION
RP BY JASMONATE.
RX PubMed=22247270; DOI=10.1104/pp.111.187518;
RA Wang Q., Hillwig M.L., Wu Y., Peters R.J.;
RT "CYP701A8: a rice ent-kaurene oxidase paralog diverted to more specialized
RT diterpenoid metabolism.";
RL Plant Physiol. 158:1418-1425(2012).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23795884; DOI=10.1042/bj20130574;
RA Wu Y., Wang Q., Hillwig M.L., Peters R.J.;
RT "Picking sides: distinct roles for CYP76M6 and CYP76M8 in rice oryzalexin
RT biosynthesis.";
RL Biochem. J. 454:209-216(2013).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25758958; DOI=10.1007/s00253-015-6496-2;
RA Kitaoka N., Wu Y., Xu M., Peters R.J.;
RT "Optimization of recombinant expression enables discovery of novel
RT cytochrome P450 activity in rice diterpenoid biosynthesis.";
RL Appl. Microbiol. Biotechnol. 99:7549-7558(2015).
CC -!- FUNCTION: Catalyzes the hydroxylation of ent-sandaracopimaradiene at
CC the C3alpha position to produce ent-3beta-hydroxy-sandaracopimaradiene,
CC an intermediates for the biosynthesis of oryzalexin D and oryzalexin E
CC phytoalexins (PubMed:22247270, PubMed:23795884). Catalyzes the
CC hydroxylation of ent-cassadiene at the C3alpha position to produce
CC 3alpha-hydroxy-ent-cassadiene, which may be an intermediate for the
CC biosynthesis of phytocassane phytoalexins (PubMed:22247270). Catalyzes
CC the hydroxylation of syn-pimaradiene (9-beta-pimara-7,15-diene) at the
CC C3beta position to produce 3-beta-syn-pimaradiene (PubMed:25758958).
CC Can hydroxylate ent-kaurene in vitro, but the product is not ent-
CC kauren-19-ol as expected for ent-kaurene oxidase activity
CC (PubMed:22247270). {ECO:0000269|PubMed:22247270,
CC ECO:0000269|PubMed:23795884, ECO:0000269|PubMed:25758958}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-sandaracopimara-8(14),15-diene + O2 + reduced [NADPH--
CC hemoprotein reductase] = ent-sandaracopimaradien-3beta-ol + H(+) +
CC H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:41464,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:50061,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78255;
CC EC=1.14.14.70; Evidence={ECO:0000269|PubMed:22247270,
CC ECO:0000269|PubMed:23795884};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9beta-pimara-7,15-diene + O2 + reduced [NADPH--hemoprotein
CC reductase] = 9beta-pimara-7,15-diene-3beta-ol + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55472, Rhea:RHEA-
CC 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:138966;
CC EC=1.14.14.68; Evidence={ECO:0000269|PubMed:25758958};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 uM for ent-cassadiene {ECO:0000269|PubMed:22247270};
CC KM=2.3 uM for ent-sandaracopimaradiene {ECO:0000269|PubMed:22247270};
CC KM=7 uM for ent-kaurene {ECO:0000269|PubMed:22247270};
CC KM=27 uM for syn-pimaradiene {ECO:0000269|PubMed:25758958};
CC Note=kcat is 1.4 sec(-1) with syn-pimaradiene as substrate.
CC {ECO:0000269|PubMed:25758958};
CC -!- SUBUNIT: Interacts with the rice dwarf virus (RDV) P2 protein.
CC {ECO:0000269|PubMed:16299167}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf blades and sheaths, stems and
CC panicles. {ECO:0000269|PubMed:15316288}.
CC -!- INDUCTION: By N-acetylchitooligosaccharide elicitor (PubMed:15316288)
CC and methyl jasmonate (PubMed:22247270). {ECO:0000269|PubMed:15316288,
CC ECO:0000269|PubMed:22247270}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000255|RuleBase:RU000461}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD54592.1; Type=Erroneous gene model prediction;
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DR EMBL; AY579214; AAT46567.1; -; mRNA.
DR EMBL; AP005471; BAD54592.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008212; BAF19819.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS98305.1; -; Genomic_DNA.
DR RefSeq; XP_015640905.1; XM_015785419.1.
DR AlphaFoldDB; Q0DBF4; -.
DR SMR; Q0DBF4; -.
DR STRING; 4530.OS06T0569500-01; -.
DR PaxDb; Q0DBF4; -.
DR PRIDE; Q0DBF4; -.
DR EnsemblPlants; Os06t0569500-01; Os06t0569500-01; Os06g0569500.
DR GeneID; 4341343; -.
DR Gramene; Os06t0569500-01; Os06t0569500-01; Os06g0569500.
DR KEGG; osa:4341343; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q0DBF4; -.
DR OMA; GHTHIIL; -.
DR OrthoDB; 702827at2759; -.
DR BRENDA; 1.14.14.68; 4460.
DR BRENDA; 1.14.14.86; 8948.
DR PlantReactome; R-OSA-1119557; GA12 biosynthesis.
DR SABIO-RK; Q0DBF4; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q0DBF4; OS.
DR GO; GO:0009707; C:chloroplast outer membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102596; F:cytochrome P450 dependent ent-sandaracopimaradiene 3-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052615; F:ent-kaurene oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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; IDA:UniProtKB.
DR GO; GO:0051502; P:diterpene phytoalexin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0010241; P:ent-kaurene oxidation to kaurenoic acid; IBA:GO_Central.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IBA:GO_Central.
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 InterPro; IPR044225; KO_chloroplastic.
DR PANTHER; PTHR47283; PTHR47283; 1.
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; Host-virus interaction; Iron; Membrane; Metal-binding; Monooxygenase;
KW NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..510
FT /note="Ent-sandaracopimaradiene 3-hydroxylase"
FT /id="PRO_0000430731"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
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|UniProtKB:P04798"
FT CONFLICT 123
FT /note="K -> E (in Ref. 1; AAT46567)"
FT CONFLICT 218
FT /note="S -> P (in Ref. 1; AAT46567)"
SQ SEQUENCE 510 AA; 56965 MW; 7FA05F6A42E664E8 CRC64;
MESMLVAGAG AAAVAAVGGL VAAAALADKL VAAPPPRKNR ANPPPAVPGL PIIGNLHQLK
EKKPHQTFAK WSETYGPIYT IKTGASPVVV LNSTEVAKEA MIDKFSSIST RKLPKAMSVL
TRKSMVAISD YGDYQKMAKR NIMIGMLGFN AQKQFRGTRE RMISNVLSTL HKLVSLDPHS
PLNFRDVYIN ELFSLSLIQS LGEDVSSVYV EEFGREISKD EIFDVLVHEM MMCAVEADWR
DYFPYLSWLP NKSFDTIVST TEFRRDAIMN ALIKKQKERI ARGEARASYI DFLLEAERSA
QLTDDQLMLL LSESILAAAD TVLVTTEWTM YEIAKNPDKQ ELLYQEIREA CGGEAVTEDD
LPRLPYLNAV FHETLRLHSP VPVLPPRFVH DDTTLAGYDI AAGTQMMINV YACHMDEKVW
ESPGEWSPER FLGEGFEVAD RYKTMAFGAG RRTCAGSLQA MNIACVAVAR LVQELEWRLR
EGDGDKEDTM QFTALKLDPL HVHLKPRGRM
