C76M8_ORYSJ
ID C76M8_ORYSJ Reviewed; 500 AA.
AC Q6YTF1; A0A0P0VKN5;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Oryzalexin D synthase;
DE EC=1.14.14.112 {ECO:0000269|PubMed:21985968, ECO:0000269|PubMed:22215681};
DE EC=1.14.14.123 {ECO:0000269|PubMed:23795884};
DE AltName: Full=Cytochrome P450 76M8 {ECO:0000303|PubMed:18759039};
DE AltName: Full=Ent-cassadiene C11-alpha-hydroxylase 2;
GN Name=CYP76M8 {ECO:0000303|PubMed:18759039};
GN OrderedLocusNames=Os02g0569400 {ECO:0000312|EMBL:BAF09098.1},
GN LOC_Os02g36070 {ECO:0000305};
GN ORFNames=OsJ_07203 {ECO:0000312|EMBL:EAZ23507.1},
GN OSJNBa0008E01.2 {ECO:0000312|EMBL:BAD17658.1},
GN P0025F02.31 {ECO:0000312|EMBL:BAD17786.1};
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;
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 [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=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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION
RP 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).
RN [9]
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).
CC -!- FUNCTION: Enzyme of the diterpenoid metabolism involved in the
CC biosynthesis of both phytocassane and the oryzalexin class of
CC phytoalexins. Can hydroxylate syn-pimaradiene, ent-pimaradiene, ent-
CC sandaracopimaradiene, ent-isokaurene, ent-kaurene, and ent-cassadiene,
CC but no activity with syn-stemodene, syn-stemarene, syn-labdatriene,
CC C11-alpha-hydroxy-ent-cassadiene or syn-pimadien-19-oic acid as
CC substrates. Hydroxylates 3-alpha-hydroxy-ent-sandaracopimaradiene at C-
CC 7-beta, resulting in a 3-alpha,7-beta-diol corresponding to oryzalexins
CC D. {ECO:0000269|PubMed:21985968, ECO:0000269|PubMed:22215681,
CC ECO:0000269|PubMed:23795884}.
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:21985968,
CC ECO:0000269|PubMed:22215681};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-sandaracopimaradien-3beta-ol + O2 + reduced [NADPH--
CC hemoprotein reductase] = H(+) + H2O + oryzalexin D + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:41472, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:78255, ChEBI:CHEBI:78256;
CC EC=1.14.14.123; Evidence={ECO:0000269|PubMed:23795884};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 uM for ent-cassadiene {ECO:0000269|PubMed:21985968,
CC ECO:0000269|PubMed:22215681};
CC KM=4 uM for ent-pimaradiene {ECO:0000269|PubMed:22215681};
CC KM=15 uM for ent-isokaurene {ECO:0000269|PubMed:22215681};
CC KM=7 uM for ent-sandaracopimaradiene {ECO:0000269|PubMed:22215681};
CC KM=5 uM for ent-kaurene {ECO:0000269|PubMed:22215681};
CC KM=2 uM for syn-pimaradiene {ECO:0000269|PubMed:22215681};
CC Note=kcat is 0.011 sec(-1) with ent-sandaracopimaradien as substrate.
CC kcat is 0.009 sec(-1) with ent-pimaradiene as substrate. kcat is
CC 0.015 sec(-1) with ent-isokaurene as substrate. kcat is 0.006 sec(-1)
CC with ent-cassadiene as substrate. kcat is 0.009 sec(-1) with ent-
CC kaurene as substrate. kcat is 0.006 sec(-1) with syn-pimaradiene as
CC substrate. {ECO:0000269|PubMed:22215681};
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 -!- WEB RESOURCE: Name=Cytochrome P450 Homepage;
CC URL="http://drnelson.uthsc.edu/CytochromeP450.html";
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DR EMBL; AP005835; BAD17658.1; -; Genomic_DNA.
DR EMBL; AP006069; BAD17786.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09098.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79332.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ23507.1; -; Genomic_DNA.
DR EMBL; AK069701; BAG91560.1; -; mRNA.
DR RefSeq; XP_015623630.1; XM_015768144.1.
DR AlphaFoldDB; Q6YTF1; -.
DR SMR; Q6YTF1; -.
DR STRING; 4530.OS02T0569400-01; -.
DR PaxDb; Q6YTF1; -.
DR PRIDE; Q6YTF1; -.
DR EnsemblPlants; Os02t0569400-01; Os02t0569400-01; Os02g0569400.
DR GeneID; 4329722; -.
DR Gramene; Os02t0569400-01; Os02t0569400-01; Os02g0569400.
DR KEGG; osa:4329722; -.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; Q6YTF1; -.
DR OMA; DLWKWRT; -.
DR OrthoDB; 702827at2759; -.
DR BioCyc; MetaCyc:MON-18617; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q6YTF1; baseline and differential.
DR Genevisible; Q6YTF1; 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:0102598; F:3alpha-hydroxy-ent-sandaracopimardiene 7-beta-monooxygenase activity; IEA:UniProtKB-EC.
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: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="Oryzalexin D synthase"
FT /id="PRO_0000418867"
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"
SQ SEQUENCE 500 AA; 55933 MW; DB8D1A60BC66BD58 CRC64;
MENSQMWLLW GALSVALFFY FSTLRRRYAG GKPLPPGPTP LPLIGNLHLV GGGTFHHKLR
DLARVHGPVM TLKLGLATNV VISSREAAIE AYTKYDRHLA ARATPDTFRA CGFADRSMVF
IPSSDPQWKA LRGIHASHVF TPRVLAAVRP IRERKVGDLI AYLRAHAGEE VLVGHAMYTG
ILNMVSFSYF SVDIVDMGSQ MARELREVVD DIILVVGKPN VSDFYPFLRP LDLQGLRRWT
TKRFNRVFSI MGDIIDRRLA HIRDNKPRHD DFLDSILELM AAGKIDRVNV LNMLFEAFVA
GADTMALTLE WVMAELLKNP SVMAKARAEL RDVLGDKEIV EEADAARLPY LQAVLKEAMR
LHPVGALLLP HFAMEDGVEV GGYAVPKGST VLFNAWAIMR DAAAWERPDE FVPERFVERT
PQLDFRGKDV EFMPFGSGRR LCPGLPLAER VVPFILASML HTFEWELPGG MTAEELDVSE
KFKTANVLAV PLKAVPVLIK
