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C76M5_ORYSJ
ID   C76M5_ORYSJ             Reviewed;         501 AA.
AC   Q6YTF5; A0A0P0VKM0; A3A866;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Cytochrome P450 76M5 {ECO:0000305};
DE            EC=1.14.14.122 {ECO:0000269|PubMed:22215681};
GN   Name=CYP76M5 {ECO:0000303|PubMed:22215681};
GN   OrderedLocusNames=Os02g0569000 {ECO:0000312|EMBL:BAF09097.1},
GN   LOC_Os02g36030 {ECO:0000305};
GN   ORFNames=OsJ_07201 {ECO:0000312|EMBL:EAZ23505.1},
GN   P0025F02.20 {ECO:0000312|EMBL:BAD17782.1};
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   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 the oryzalexin class of phytoalexins. Hydroxylates ent-
CC       sandaracopimaradien. {ECO:0000269|PubMed:22215681}.
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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAZ23505.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP006069; BAD17782.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF09097.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS79330.1; -; Genomic_DNA.
DR   EMBL; CM000139; EAZ23505.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK059010; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015624125.1; XM_015768639.1.
DR   AlphaFoldDB; Q6YTF5; -.
DR   SMR; Q6YTF5; -.
DR   STRING; 4530.OS02T0569000-01; -.
DR   PaxDb; Q6YTF5; -.
DR   PRIDE; Q6YTF5; -.
DR   EnsemblPlants; Os02t0569000-01; Os02t0569000-01; Os02g0569000.
DR   GeneID; 4329721; -.
DR   Gramene; Os02t0569000-01; Os02t0569000-01; Os02g0569000.
DR   KEGG; osa:4329721; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_2_1; -.
DR   InParanoid; Q6YTF5; -.
DR   OMA; TEDCIKW; -.
DR   OrthoDB; 702827at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6YTF5; 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..501
FT                   /note="Cytochrome P450 76M5"
FT                   /id="PRO_0000430727"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         443
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        296
FT                   /note="I -> T (in Ref. 5; AK059010)"
SQ   SEQUENCE   501 AA;  55244 MW;  DF3AFB25FDAF391F CRC64;
     METRELWVLA AALAVSLLYY LAALMRYAGG GCSRSSRPPL PPGPTPLPLI GNLLSLRGVL
     HHRLASLARV HGPVMALRLG LTTAVVVSSR DAAAEAFTKH DRRLAARVVP DSNRAHGFSD
     RSIIWLPSSD PRWKALRGIQ ATHLFSPRGL AAVRSVRESK VRDIVAYFRS RAGEEVVFGE
     AIYSGVLNLV SSSFFSVNMA GVGSEEAHGL RELVEDLVEA IAKPNVSDLF PFLRQLDLQG
     LRRRTEERMA RAFGILDGII DRRLANRTHG DRHGDFLDAL LDLVSEGKMA RDHVTIMLFE
     VFGAGSDTMS VSLEWAMAEL LRNPRAMRKA RAELEDAAAV VEESDAARLP YLQAVVKEAM
     RLHPVGPILL PHRAVEDGVE IGGYAVPRGA MVIFNAWAIM RDPAAWERPD EFVPERFMET
     TTAIDFRGKE YEYLPFGSGR RLCPGLPLAE RVVPFVLASL LRAFEWRLPD GVSAEDLDVS
     ERFNTANVLA VPLKVVPVIV N
 
 
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