NOMT_ORYSJ
ID NOMT_ORYSJ Reviewed; 375 AA.
AC Q0IP69; Q2QV72; Q2QV73;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Naringenin 7-O-methyltransferase;
DE Short=NOMT;
DE Short=OsNOMT;
DE EC=2.1.1.232;
GN OrderedLocusNames=Os12g0240900, LOC_Os12g13810;
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=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=22493492; DOI=10.1074/jbc.m112.351270;
RA Shimizu T., Lin F., Hasegawa M., Okada K., Nojiri H., Yamane H.;
RT "Purification and identification of naringenin 7-o-methyltransferase, a key
RT enzyme in biosynthesis of flavonoid phytoalexin sakuranetin in rice.";
RL J. Biol. Chem. 287:19315-19325(2012).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase involved
CC in the biosynthesis of the sakuranetin, an inducible defense mechanism
CC of O.sativa against pathogen attack. {ECO:0000269|PubMed:22493492}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-naringenin + S-adenosyl-L-methionine = (2S)-sakuranetin +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:31539,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17846, ChEBI:CHEBI:28927,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.232;
CC Evidence={ECO:0000269|PubMed:22493492};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 uM for naringenin {ECO:0000269|PubMed:22493492};
CC Note=kcat is 25 sec(-1) with naringenin as substrate.;
CC -!- INDUCTION: By jasmonic acid (JA). Up-regulated in leaves infected by
CC the pathogen M.oryzae. {ECO:0000269|PubMed:22493492}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA96874.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
CC Sequence=ABA96875.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
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DR EMBL; DP000011; ABA96874.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000011; ABA96875.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008218; BAF29496.2; -; Genomic_DNA.
DR EMBL; AP014968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q0IP69; -.
DR SMR; Q0IP69; -.
DR STRING; 4530.OS12T0240900-00; -.
DR PaxDb; Q0IP69; -.
DR PRIDE; Q0IP69; -.
DR EnsemblPlants; Os12t0240900-01; Os12t0240900-01; Os12g0240900.
DR Gramene; Os12t0240900-01; Os12t0240900-01; Os12g0240900.
DR eggNOG; KOG3178; Eukaryota.
DR InParanoid; Q0IP69; -.
DR BioCyc; MetaCyc:MON-11973; -.
DR BRENDA; 2.1.1.232; 4460.
DR PlantReactome; R-OSA-1119316; Phenylpropanoid biosynthesis.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q0IP69; OS.
DR GO; GO:0008168; F:methyltransferase activity; IDA:CACAO.
DR GO; GO:0102766; F:naringenin 7-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF08100; Dimerisation; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..375
FT /note="Naringenin 7-O-methyltransferase"
FT /id="PRO_0000418734"
FT REGION 168..188
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 136..142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 276
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 375 AA; 39702 MW; 7AD1AE02B04A89C7 CRC64;
MVSPVVHRHA AGGGSGGDDD DQACMYALEL LGGSVVSMTL KAAIELGLVD ELLAAAGAAV
TAEELAARLR LPAAVAAAAA VDRMLRLLAS YGVVRCATEA GPDGKARRSY AAAPVCKWLA
AGSSSGEGSM APLGLLNLDK VFMENWYYLK EAVSEGGTAF DKAYGTSLFQ YLGQDGNEPS
NTLFNQAMAS HSVVITNKLL QFFRGFDAGA GVDVLVDVGG GVGATLRMIT ARHPHLRGVN
YDLPHVIAQA PPVEGVEHIG GSMFDHVPSG SAILLKWILH LWGDEECVKI LKNCYKALPA
KGKVILVEYV LPASPEATLA AQEAFRLDVM MLNRLAGGKE RTQQEFTDLA VDAGFSGDCK
PTYIFTNVWA LEFTK
