OMT17_ORYSJ
ID OMT17_ORYSJ Reviewed; 292 AA.
AC Q7F8T6; A0A0P0XH89; Q7F8T5;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Tricin synthase 2;
DE EC=2.1.1.175;
DE AltName: Full=Caffeoyl-CoA 3-O-methyltransferase ROMT17;
GN Name=ROMT-17; OrderedLocusNames=Os08g0498400, LOC_Os08g38910;
GN ORFNames=OsJ_27815, P0026F07.26-1, P0026F07.26-2;
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] (ISOFORMS 1 AND 2).
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, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND MUTAGENESIS OF GLU-112; ASP-208; ASP-234 AND
RP ASN-235.
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 Note=Binds 1 divalent metal cation per subunit. Fully active with
CC Mg(2+) and active at 70% with Mn(2+). Active at 40% with Co(2+) ion and
CC less than 10% with Ca(2+) or Zn(2+) ions.
CC {ECO:0000269|PubMed:17943312};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for tricetin {ECO:0000269|PubMed:17943312};
CC KM=104 uM for luteolin {ECO:0000269|PubMed:17943312};
CC KM=44 uM for myricetin {ECO:0000269|PubMed:17943312};
CC KM=72 uM for caffeoyl-CoA {ECO:0000269|PubMed:17943312};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7F8T6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7F8T6-2; Sequence=VSP_042108;
CC -!- TISSUE SPECIFICITY: Expressed in stems only.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP000364; BAD08718.1; -; Genomic_DNA.
DR EMBL; AP000364; BAD08719.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF24057.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT06084.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT06085.1; -; Genomic_DNA.
DR EMBL; CM000145; EEE68938.1; -; Genomic_DNA.
DR EMBL; AK061757; BAG88094.1; -; mRNA.
DR EMBL; AK065515; BAG89547.1; -; mRNA.
DR RefSeq; XP_015649763.1; XM_015794277.1. [Q7F8T6-1]
DR AlphaFoldDB; Q7F8T6; -.
DR SMR; Q7F8T6; -.
DR STRING; 4530.OS08T0498400-01; -.
DR PaxDb; Q7F8T6; -.
DR PRIDE; Q7F8T6; -.
DR EnsemblPlants; Os08t0498400-01; Os08t0498400-01; Os08g0498400. [Q7F8T6-1]
DR EnsemblPlants; Os08t0498400-02; Os08t0498400-02; Os08g0498400. [Q7F8T6-2]
DR GeneID; 4345935; -.
DR Gramene; Os08t0498400-01; Os08t0498400-01; Os08g0498400. [Q7F8T6-1]
DR Gramene; Os08t0498400-02; Os08t0498400-02; Os08g0498400. [Q7F8T6-2]
DR KEGG; osa:4345935; -.
DR eggNOG; KOG1663; Eukaryota.
DR HOGENOM; CLU_067676_5_0_1; -.
DR InParanoid; Q7F8T6; -.
DR OMA; ICRRICW; -.
DR OrthoDB; 1116724at2759; -.
DR SABIO-RK; Q7F8T6; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q7F8T6; OS.
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 Alternative splicing; Magnesium; Metal-binding; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..292
FT /note="Tricin synthase 2"
FT /id="PRO_0000414605"
FT REGION 21..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 132..133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 185
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 208
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 210
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 234
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT VAR_SEQ 2..103
FT /note="SMACTKVWRSTMYTPRRLKRTTPASRVSSTAMAAANGDASHGANGGIQIQSK
FT EMKTAIHSNDSPKTLLKSESLHEYMLNTMVYPRENEFMRELRLITSEHTY -> MLCCV
FT TFLLDSIS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_042108"
FT MUTAGEN 112
FT /note="E->L: 40% loss of activity."
FT /evidence="ECO:0000269|PubMed:17943312"
FT MUTAGEN 208
FT /note="D->L: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:17943312"
FT MUTAGEN 234
FT /note="D->L: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:17943312"
FT MUTAGEN 235
FT /note="N->L: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:17943312"
SQ SEQUENCE 292 AA; 32032 MW; FAE0077D09AA640E CRC64;
MSMACTKVWR STMYTPRRLK RTTPASRVSS TAMAAANGDA SHGANGGIQI QSKEMKTAIH
SNDSPKTLLK SESLHEYMLN TMVYPRENEF MRELRLITSE HTYGFMSSPP EEGQLLSLLL
NLTGAKNTIE VGVFTGCSVL ATALAIPDDG KVVAIDVSRE YFDLGLPVIK KAGVAHKVDF
REGAAMPILD NLLANEENEG KFDFAFVDAD KGNYGEYHER LLRLVRAGGV LAYDNTLWGG
SVALEDDSVL EEFDQDIRRS IVAFNAKIAG DPRVEAVQLP VSDGITLCRR LV
