C76M6_ORYSJ
ID C76M6_ORYSJ Reviewed; 512 AA.
AC Q6Z5I7; A0A0P0VKN1;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Oryzalexin E synthase {ECO:0000305};
DE EC=1.14.14.122 {ECO:0000269|PubMed:22215681, ECO:0000269|PubMed:23795884};
DE AltName: Full=Cytochrome P450 76M6 {ECO:0000303|PubMed:22215681};
GN Name=CYP76M6 {ECO:0000303|PubMed:22215681};
GN OrderedLocusNames=Os02g0571900 {ECO:0000312|EMBL:BAF09106.1},
GN LOC_Os02g36280 {ECO:0000305};
GN ORFNames=OsJ_07213 {ECO:0000312|EMBL:EAZ23517.1},
GN P0689H05.39 {ECO:0000312|EMBL:BAD17279.1};
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 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 [6]
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 the oryzalexin class of phytoalexins. Can use ent-
CC sandaracopimaradien and syn-stemodene as substrates, but no activity
CC with syn-stemoden-19-oic acid. Hydroxylates 3-alpha-hydroxy-ent-
CC sandaracopimaradiene at C-9-beta, resulting in a 3-alpha,9-beta-diol
CC corresponding to oryzalexins E. {ECO:0000269|PubMed:22215681,
CC ECO:0000269|PubMed:23795884}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-sandaracopimaradien-3beta-ol + O2 + reduced [NADPH--
CC hemoprotein reductase] = H(+) + H2O + oryzalexin E + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:41468, 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:78259;
CC EC=1.14.14.122; Evidence={ECO:0000269|PubMed:22215681,
CC 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=17 uM for ent-sandaracopimaradien {ECO:0000269|PubMed:22215681};
CC KM=7 uM for syn-stemodene {ECO:0000269|PubMed:22215681};
CC Note=kcat is 0.046 sec(-1) with ent-sandaracopimaradien as substrate.
CC kcat is 0.020 sec(-1) with syn-stemodene as substrate.
CC {ECO:0000269|PubMed:22215681};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Up-regulated by methyl jasmonate.
CC {ECO:0000269|PubMed:22215681}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000255|RuleBase:RU000461}.
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DR EMBL; AP005114; BAD17279.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09106.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79349.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ23517.1; -; Genomic_DNA.
DR RefSeq; XP_015625955.1; XM_015770469.1.
DR AlphaFoldDB; Q6Z5I7; -.
DR SMR; Q6Z5I7; -.
DR STRING; 4530.OS02T0571900-01; -.
DR PaxDb; Q6Z5I7; -.
DR PRIDE; Q6Z5I7; -.
DR EnsemblPlants; Os02t0571900-01; Os02t0571900-01; Os02g0571900.
DR GeneID; 4329730; -.
DR Gramene; Os02t0571900-01; Os02t0571900-01; Os02g0571900.
DR KEGG; osa:4329730; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_2_1; -.
DR InParanoid; Q6Z5I7; -.
DR OMA; RRRTEYH; -.
DR OrthoDB; 702827at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6Z5I7; 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:0102597; F:3alpha-hydroxy-ent-sandaracopimardiene 9-beta-monooxygenase 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 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..512
FT /note="Oryzalexin E synthase"
FT /id="PRO_0000430728"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 452
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 512 AA; 56363 MW; 0CF74FFE6BC983CB CRC64;
MEKLKSELWM TAVATCMSLL LYLTILRRRH ASGGRSLALP PGPTPLPLIG NLLCLGGIFH
QTLAKLARVH GPVMTLKLGL TTAVVVSSAE AAREAYTKHD QRLAARPVPD AFRANGFSER
SIVFSPSSDP QWKNLRGIHA THIFSPRALA ALRGIRERKV RDIVGYIRTV AGEEMCVREV
VHNGVLNLIS TSFFSMDMAD VRSESARGLR GLIEDIIATV AGPNVSDFFP FLRQLDLQGL
RRQTGSHLGI VFGLLDDIID RRMAETRDHP DKQRHGDFLD ALISLASAGK IPRYHITYLL
FDVFAAGADT MTTTVEWAMA ELLRNPRVMA KVRAEVTDAL GGRESFDEGD AASLTYLQCV
FKEAMRLHPV GSILVPHLAV QDGVEIGGYA VPKGTTVIFN AWAIMRDPAA WESPDQFLPE
RFLHKEESSS PPLELRGKDY EYIPFGSGRR LCPGLPLAER AVPFILASLL HAFEWRLPDG
MSPDDMDMTE KFATANVLAT PLKAVPVASH TS
