C99A2_ORYSJ
ID C99A2_ORYSJ Reviewed; 532 AA.
AC Q7X7X4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cytochrome P450 99A2;
DE EC=1.14.-.-;
GN Name=CYP99A2; OrderedLocusNames=Os04g0180400, LOC_Os04g10160;
GN ORFNames=OSJNBa0027O01.2, OSJNBa0052P16.24;
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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-532.
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, AND INDUCTION.
RX PubMed=17872948; DOI=10.1074/jbc.m703344200;
RA Shimura K., Okada A., Okada K., Jikumaru Y., Ko K.-W., Toyomasu T.,
RA Sassa T., Hasegawa M., Kodama O., Shibuya N., Koga J., Nojiri H.,
RA Yamane H.;
RT "Identification of a biosynthetic gene cluster in rice for momilactones.";
RL J. Biol. Chem. 282:34013-34018(2007).
CC -!- FUNCTION: Involved in momilactone phytoalexins biosynthesis.
CC Participates in the biosynthetic steps between 9-beta-pimara-7,15-diene
CC and 3-beta-hydroxy-9-beta-pimara-7,15-dien-19,6-beta-olide.
CC {ECO:0000269|PubMed:17872948}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By chitin oligosaccharide elicitor.
CC {ECO:0000269|PubMed:17872948}.
CC -!- MISCELLANEOUS: 3-beta-hydroxy-9-beta-pimara-7,15-dien-19,6-beta-olide
CC is a precursor of the phytoalexins momilactones A and B. Phytoalexins
CC are diterpenoid secondary metabolites involved in the defense mechanism
CC of the plant and produced in response to attack (by a pathogen,
CC elicitor or UV irradiation). Momilactone B can also act as an
CC allochemical (an antimicrobial and allelopathic agent), being
CC constitutively produced in the root of the plant and secreted to the
CC rhizosphere where it suppresses the growth of neighboring plants and
CC soil microorganisms.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF14091.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD39530.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD39708.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL662934; CAD39530.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL662936; CAD39708.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008210; BAF14091.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK071546; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015633968.1; XM_015778482.1.
DR AlphaFoldDB; Q7X7X4; -.
DR SMR; Q7X7X4; -.
DR STRING; 4530.OS04T0180400-01; -.
DR PaxDb; Q7X7X4; -.
DR GeneID; 4335096; -.
DR KEGG; osa:4335096; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_1_1; -.
DR InParanoid; Q7X7X4; -.
DR OrthoDB; 702827at2759; -.
DR PlantReactome; R-OSA-1119308; Momilactone biosynthesis.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q7X7X4; OS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..532
FT /note="Cytochrome P450 99A2"
FT /id="PRO_0000349106"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 468
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"
SQ SEQUENCE 532 AA; 59533 MW; C5EAB30AE62BFB24 CRC64;
MQFFAKQNCQ VNLLTNNPSS NPRFIMEINS AATLTLVSLL TLPILLALLT RKSSSKKRRP
PGPWNLPLVG GLLHLLRSHP QVALRELASK YGPVMFLRMG QIDTVVVSSP AAAQEVLRDK
DVMFASRPSL LVSEIFCYDN LDVGFAPYGA YWRMLRKLCT VELLSTKVVR QLAPVRNDET
LTLVRNIKAA SSGHGGGGGK KPVTLARLLT TCTNTITAKA AFGQACGVEL QEQFLTALDV
GLKFSGGFCF GDLFPSLRFI DAMTGLRSRL WRARGQLDSV FDKIIAQCEE HQGDSLVNVL
LRIRDQGDLE FPFGTTNIKA IILDMFTGGT ETTSSAAEWV MSELMRNPEV MAKVQAEVRR
VFDNKSPQDH EGLIDNLRYM KMVIKETMRL NPVLPLLMPH LCRETCDIGG YEVVEGTRVV
INSWAMARSP EYWDDAEEFK PERFEDGMAD YKGSRFEYLP FGTGRRRCPG DTFGMVLLEL
IVARLLYYFD WSLPAGMQPD DVDMDFVVTA TTRRKNHLQL VASPYKLAPI QI
