FOMT2_WHEAT
ID FOMT2_WHEAT Reviewed; 356 AA.
AC Q38J50; B8LGB9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Tricetin 3',4',5'-O-trimethyltransferase;
DE Short=TaOMT2;
DE EC=2.1.1.169;
DE AltName: Full=Caffeic acid 3-O-methyltransferase;
DE Short=TaCM;
DE AltName: Full=Flavone O-methyltransferase 2;
GN Name=OMT2;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Norstar;
RX PubMed=16730127; DOI=10.1016/j.bbagen.2006.02.008;
RA Zhou J.M., Gold N.D., Martin V.J., Wollenweber E., Ibrahim R.K.;
RT "Sequential O-methylation of tricetin by a single gene product in wheat.";
RL Biochim. Biophys. Acta 1760:1115-1124(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. H4564;
RX PubMed=17976886; DOI=10.1016/j.biochi.2007.09.016;
RA Ma Q.H., Xu Y.;
RT "Characterization of a caffeic acid 3-O-methyltransferase from wheat and
RT its function in lignin biosynthesis.";
RL Biochimie 90:515-524(2008).
RN [3]
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=18397325; DOI=10.1111/j.1742-4658.2008.06377.x;
RA Kornblatt J.A., Zhou J.M., Ibrahim R.K.;
RT "Structure-activity relationships of wheat flavone O-methyltransferase: a
RT homodimer of convenience.";
RL FEBS J. 275:2255-2266(2008).
CC -!- FUNCTION: Flavonoid B-ring-specific O-methyltransferase with a
CC preference for flavones > dihydroflavones > flavonols that possess at
CC least two B-ring hydroxyl groups. Active with tricetin, 5-
CC hydroxyferulic acid, luteolin, quercitin, eriodictyol, quercetagetin,
CC taxifolin, gossypetin and myricetin. No activity with naringenin,
CC apigenin, kaempferol, 7,8-dihydroxy- or 5,7,8-trihydroxy flavones,
CC chlorogenic acid, gallic acid or daphnetin. Catalyzes the sequential O-
CC methylation of tricetin via 3'-O-methyltricetin, 3',5'-O-methyltricetin
CC to 3',4',5'-O-trimethyltricetin. May also be involved in S lignin
CC biosynthesis. {ECO:0000269|PubMed:16730127,
CC ECO:0000269|PubMed:17976886}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 S-adenosyl-L-methionine + tricetin = 3',4',5'-O-
CC trimethyltricetin + 3 H(+) + 3 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:32351, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:60020, ChEBI:CHEBI:60045;
CC EC=2.1.1.169; Evidence={ECO:0000269|PubMed:16730127,
CC ECO:0000269|PubMed:17976886, ECO:0000269|PubMed:18397325};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.73 uM for tricetin {ECO:0000269|PubMed:16730127,
CC ECO:0000269|PubMed:17976886};
CC KM=3.33 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:16730127,
CC ECO:0000269|PubMed:17976886};
CC KM=8.36 uM for 5-hydroxyferulic acid {ECO:0000269|PubMed:16730127,
CC ECO:0000269|PubMed:17976886};
CC KM=6.59 uM for myricetin {ECO:0000269|PubMed:16730127,
CC ECO:0000269|PubMed:17976886};
CC KM=68.75 uM for caffeic acid {ECO:0000269|PubMed:16730127,
CC ECO:0000269|PubMed:17976886};
CC KM=83.04 uM for caffeoyl-CoA {ECO:0000269|PubMed:16730127,
CC ECO:0000269|PubMed:17976886};
CC KM=95.17 uM for 5-hydroxyferuloyl-CoA {ECO:0000269|PubMed:16730127,
CC ECO:0000269|PubMed:17976886};
CC KM=43.72 uM for caffeoyl aldehyde {ECO:0000269|PubMed:16730127,
CC ECO:0000269|PubMed:17976886};
CC KM=17.31 uM for 5-hydroxyconiferaldehyde
CC {ECO:0000269|PubMed:16730127, ECO:0000269|PubMed:17976886};
CC KM=84.03 uM for caffeoyl alcohol {ECO:0000269|PubMed:16730127,
CC ECO:0000269|PubMed:17976886};
CC KM=100.21 uM for 5-hydroxyconiferyl alcohol
CC {ECO:0000269|PubMed:16730127, ECO:0000269|PubMed:17976886};
CC Vmax=142.86 pmol/sec/mg enzyme with tricetin as methyl acceptor
CC {ECO:0000269|PubMed:16730127, ECO:0000269|PubMed:17976886};
CC Vmax=88.5 pmol/sec/mg enzyme with 5-hydroxyferulic acid as methyl
CC acceptor {ECO:0000269|PubMed:16730127, ECO:0000269|PubMed:17976886};
CC Vmax=45.66 pmol/sec/mg enzyme with myricetin as methyl acceptor
CC {ECO:0000269|PubMed:16730127, ECO:0000269|PubMed:17976886};
CC Vmax=2.38 nmol/sec/mg enzyme with caffeic acid as methyl acceptor
CC {ECO:0000269|PubMed:16730127, ECO:0000269|PubMed:17976886};
CC Vmax=1.26 nmol/sec/mg enzyme with caffeoyl-CoA as methyl acceptor
CC {ECO:0000269|PubMed:16730127, ECO:0000269|PubMed:17976886};
CC Vmax=1.28 nmol/sec/mg enzyme with 5-hydroxyferuloyl-CoA as methyl
CC acceptor {ECO:0000269|PubMed:16730127, ECO:0000269|PubMed:17976886};
CC Vmax=2.56 nmol/sec/mg enzyme with caffeoyl aldehyde as methyl
CC acceptor {ECO:0000269|PubMed:16730127, ECO:0000269|PubMed:17976886};
CC Vmax=1.56 nmol/sec/mg enzyme with 5-hydroxyconiferaldehyde as methyl
CC acceptor {ECO:0000269|PubMed:16730127, ECO:0000269|PubMed:17976886};
CC Vmax=3.55 nmol/sec/mg enzyme with caffeoyl alcohol as methyl acceptor
CC {ECO:0000269|PubMed:16730127, ECO:0000269|PubMed:17976886};
CC Vmax=2.67 nmol/sec/mg enzyme with 5-hydroxyconiferyl alcohol as
CC methyl acceptor {ECO:0000269|PubMed:16730127,
CC ECO:0000269|PubMed:17976886};
CC -!- SUBUNIT: Homodimer. The monomer is fully active and dimerization is not
CC required for sequential methylation. {ECO:0000269|PubMed:18397325}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and leaves.
CC {ECO:0000269|PubMed:17976886}.
CC -!- MISCELLANEOUS: OMT1 has a very low activity with phenylpropanoids (5-
CC hydroxyferulic acid and caffeic acid) while OMT2 has a good activity
CC with them.
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}.
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DR EMBL; DQ223971; ABB03907.1; -; mRNA.
DR EMBL; EF413031; ABP63535.1; -; mRNA.
DR AlphaFoldDB; Q38J50; -.
DR SMR; Q38J50; -.
DR STRING; 4565.Traes_3B_E7624B49D.1; -.
DR PRIDE; Q38J50; -.
DR KEGG; ag:ABB03907; -.
DR eggNOG; KOG3178; Eukaryota.
DR BioCyc; MetaCyc:MON-15895; -.
DR BRENDA; 2.1.1.104; 6500.
DR BRENDA; 2.1.1.169; 6500.
DR BRENDA; 2.1.1.68; 6500.
DR SABIO-RK; Q38J50; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q38J50; baseline and differential.
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:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
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 Flavonoid biosynthesis; Lignin biosynthesis; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..356
FT /note="Tricetin 3',4',5'-O-trimethyltransferase"
FT /id="PRO_0000403987"
FT REGION 155..173
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 123..129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 244
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 245
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT CONFLICT 89
FT /note="D -> E (in Ref. 2; ABP63535)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="G -> A (in Ref. 2; ABP63535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 38570 MW; 5EA3037A554E13FB CRC64;
MGSIAAGADE DACMYALQLV SSSILPMTLK NAIELGLLET LMAAGGKFLT PAEVAAKLPS
AANPEAPDMV DRMLRLLASY NVVSCRTEDG KDGRLSRRYG AAPVCKYLTP NEDGVSMSAL
ALMNQDKVLM ESWYYLKDAV LDGGIPFNKA YGMSAFEYHG TDPRFNRVFN EGMKNHSIII
TKKLLESYKG FEGLGTLVDV GGGVGATVAA ITAHYPTIKG INFDLPHVIS EAPPFPGVTH
VGGDMFQKVP SGDAILMKWI LHDWSDEHCA TLLKNCYDAL PAHGKVVLVE CILPVNPEAT
PKAQGVFHVD MIMLAHNPGG RERYEREFEA LAKGAGFAAM KTTYIYANAW AIEFTK
