OMT15_ORYSJ
ID OMT15_ORYSJ Reviewed; 252 AA.
AC Q9XGP7; A0A0P0XHD0; A3BUH5; Q7XXS6;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Tricin synthase 1;
DE EC=2.1.1.175;
DE AltName: Full=Caffeoyl-CoA 3-O-methyltransferase ROMT15;
GN Name=ROMT-15; Synonyms=COA20;
GN OrderedLocusNames=Os08g0498100, LOC_Os08g38900;
GN ORFNames=OsJ_27813, P0026F07.24;
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 [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Panicle;
RX PubMed=15659629; DOI=10.1105/tpc.104.028456;
RA Moriguchi K., Suzuki T., Ito Y., Yamazaki Y., Niwa Y., Kurata N.;
RT "Functional isolation of novel nuclear proteins showing a variety of
RT subnuclear localizations.";
RL Plant Cell 17:389-403(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhao H.Y., Shen Q.X., Lv S.Y., Wang T., Song Y.R.;
RT "Characterization of three rice CCoAOMT genes.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND MUTAGENESIS OF GLU-69; ASP-168; ASP-194 AND
RP ASN-195.
RX PubMed=17943312; DOI=10.1007/s00425-007-0646-4;
RA Lee Y.J., Kim B.G., Chong Y., Lim Y., Ahn J.H.;
RT "Cation dependent O-methyltransferases from rice.";
RL Planta 227:641-647(2008).
CC -!- FUNCTION: Catalyzes the stepwise methylation of tricetin to its 3'-
CC mono- and 3',5'-dimethyl ethers. No 3',4',5'-trimethylated ester
CC derivatives are produced. Can use caffeoyl-CoA, 5-hydroxyferulic acid,
CC luteolin, tricetin, quercetin, myrcetin and 7,8-dihydroxyflavone as
CC substrates, but not naringenin, apigenin or kaempferol. The 2,3-double
CC bond and the O-dihydroxyl group of the substrate are both required for
CC catalytic activity of the enzyme. {ECO:0000269|PubMed:17943312}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 S-adenosyl-L-methionine + tricetin = 3',5'-di-O-
CC methyltricetin + 2 H(+) + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:32347, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:60016, ChEBI:CHEBI:60045;
CC EC=2.1.1.175; Evidence={ECO:0000269|PubMed:17943312};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17943312};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17943312};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:17943312};
CC Note=Binds 1 divalent metal cation per subunit. Fully active with
CC Mg(2+). Active at 80% with Mn(2+) or Co(2+) ions. Active at less than
CC 10% with Ca(2+) or Zn(2+) ions. {ECO:0000269|PubMed:17943312};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=72 uM for tricetin {ECO:0000269|PubMed:17943312};
CC KM=90 uM for luteolin {ECO:0000269|PubMed:17943312};
CC KM=80 uM for myricetin {ECO:0000269|PubMed:17943312};
CC KM=76 uM for caffeoyl-CoA {ECO:0000269|PubMed:17943312};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15659629}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in stems and roots.
CC {ECO:0000269|PubMed:17943312}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family. CCoAMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01019}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAZ43214.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB110168; BAC78560.1; -; mRNA.
DR EMBL; AY644637; AAT68023.1; -; Genomic_DNA.
DR EMBL; AP000364; BAA81774.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF24056.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT06083.1; -; Genomic_DNA.
DR EMBL; CM000145; EAZ43214.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK071482; BAG92518.1; -; mRNA.
DR EMBL; AK104326; BAG96600.1; -; mRNA.
DR EMBL; AK104801; BAG96961.1; -; mRNA.
DR RefSeq; XP_015649764.1; XM_015794278.1.
DR AlphaFoldDB; Q9XGP7; -.
DR SMR; Q9XGP7; -.
DR STRING; 4530.OS08T0498100-01; -.
DR PaxDb; Q9XGP7; -.
DR PRIDE; Q9XGP7; -.
DR EnsemblPlants; Os08t0498100-01; Os08t0498100-01; Os08g0498100.
DR GeneID; 4345934; -.
DR Gramene; Os08t0498100-01; Os08t0498100-01; Os08g0498100.
DR KEGG; osa:4345934; -.
DR eggNOG; KOG1663; Eukaryota.
DR HOGENOM; CLU_067676_5_0_1; -.
DR InParanoid; Q9XGP7; -.
DR OMA; LPHEPEC; -.
DR OrthoDB; 1116724at2759; -.
DR BioCyc; MetaCyc:MON-20528; -.
DR BRENDA; 2.1.1.104; 4460.
DR BRENDA; 2.1.1.175; 4460.
DR BRENDA; 2.1.1.267; 4460.
DR SABIO-RK; Q9XGP7; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q9XGP7; OS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..252
FT /note="Tricin synthase 1"
FT /id="PRO_0000414604"
FT BINDING 65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 89..90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 168
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 194
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 195
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT MUTAGEN 69
FT /note="E->L: 14% loss of activity."
FT /evidence="ECO:0000269|PubMed:17943312"
FT MUTAGEN 168
FT /note="D->L: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:17943312"
FT MUTAGEN 194
FT /note="D->L: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:17943312"
FT MUTAGEN 195
FT /note="N->L: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:17943312"
SQ SEQUENCE 252 AA; 27772 MW; E4FC076B47483926 CRC64;
MTTGNGDAPV IKNAHSDIDS TNKTLLKSDA LYKYVLDTTV LPREPECMRD LRLITDKHQW
GFMQSSADEA QLLGMLLKMA GAKRTIEVGV FTGYSLLATA LALPEDGKVV AIDPDRESYE
IGRPFLEKAG VAHKVDFREG KGLEKLDELL AEEAAAGREA AFDFAFVDAD KPNYVKYHEQ
LLQLVRVGGH IVYDNTLWAG TVALPPDTPL SDLDRRFSVA IRDLNSRLAA DPRIDVCQLA
IADGITICRR LV
