FOMT1_WHEAT
ID FOMT1_WHEAT Reviewed; 360 AA.
AC Q84N28;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Flavone O-methyltransferase 1;
DE EC=2.1.1.-;
DE AltName: Full=Caffeic acid O-methyltransferase;
DE Short=TaCOMT1;
GN Name=OMT1; Synonyms=COMT1;
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], AND INDUCTION BY PATHOGEN; METHYL JASMONATE;
RP SALICYLIC ACID; ETHYLENE; HYDROGEN PEROXIDE AND WOUNDING.
RX DOI=10.1016/j.plantsci.2005.01.014;
RA Jang C.S., Johnson J.W., Seo Y.W.;
RT "Differential expression of TaLTP3 and TaCOMT1 induced by Hessian fly
RT larval infestation in a wheat line possessing H21 resistance gene.";
RL Plant Sci. 168:1319-1326(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19211254; DOI=10.1016/j.plaphy.2008.11.011;
RA Zhou J.M., Seo Y.W., Ibrahim R.K.;
RT "Biochemical characterization of a putative wheat caffeic acid O-
RT methyltransferase.";
RL Plant Physiol. Biochem. 47:322-326(2009).
CC -!- FUNCTION: Flavone-specific O-methyltransferase with a preference for
CC flavones > flavonols. Active with tricetin, luteolin, quercitin and
CC eriodictyol. Very low activity with phenylpropanoids (5-hydroxyferulic
CC acid and caffeic acid). Catalyzes the sequential O-methylation of
CC tricetin via 3'-O-methyltricetin, 3',5'-O-methyltricetin to 3',4',5'-O-
CC trimethyltricetin. {ECO:0000269|PubMed:19211254}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.07 uM for tricetin {ECO:0000269|PubMed:19211254};
CC Vmax=11.64 pmol/sec/mg enzyme with tricetin as methyl acceptor
CC {ECO:0000269|PubMed:19211254};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by Hessian fly larval infestation, salicylic
CC acid, ethylene, H(2)O(2) and wounding. Not induced by methyl jasmonate.
CC {ECO:0000269|Ref.1}.
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; AY226581; AAP23942.1; -; mRNA.
DR AlphaFoldDB; Q84N28; -.
DR SMR; Q84N28; -.
DR STRING; 4565.Traes_7DL_930094B08.1; -.
DR PRIDE; Q84N28; -.
DR EnsemblPlants; TraesCAD_scaffold_063459_01G000100.1; TraesCAD_scaffold_063459_01G000100.1; TraesCAD_scaffold_063459_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_139309_01G000100.1; TraesCLE_scaffold_139309_01G000100.1; TraesCLE_scaffold_139309_01G000100.
DR EnsemblPlants; TraesCS7B02G245500.1; TraesCS7B02G245500.1; TraesCS7B02G245500.
DR EnsemblPlants; TraesPAR_scaffold_050390_01G000100.1; TraesPAR_scaffold_050390_01G000100.1; TraesPAR_scaffold_050390_01G000100.
DR EnsemblPlants; TraesROB_scaffold_057321_01G000100.1; TraesROB_scaffold_057321_01G000100.1; TraesROB_scaffold_057321_01G000100.
DR Gramene; TraesCAD_scaffold_063459_01G000100.1; TraesCAD_scaffold_063459_01G000100.1; TraesCAD_scaffold_063459_01G000100.
DR Gramene; TraesCLE_scaffold_139309_01G000100.1; TraesCLE_scaffold_139309_01G000100.1; TraesCLE_scaffold_139309_01G000100.
DR Gramene; TraesCS7B02G245500.1; TraesCS7B02G245500.1; TraesCS7B02G245500.
DR Gramene; TraesPAR_scaffold_050390_01G000100.1; TraesPAR_scaffold_050390_01G000100.1; TraesPAR_scaffold_050390_01G000100.
DR Gramene; TraesROB_scaffold_057321_01G000100.1; TraesROB_scaffold_057321_01G000100.1; TraesROB_scaffold_057321_01G000100.
DR KEGG; ag:AAP23942; -.
DR eggNOG; KOG3178; Eukaryota.
DR OMA; ANIRPAM; -.
DR BRENDA; 2.1.1.169; 6500.
DR SABIO-RK; Q84N28; -.
DR Proteomes; UP000019116; Unplaced.
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:0032259; P:methylation; IBA:GO_Central.
DR GO; GO:0009723; P:response to ethylene; IDA:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
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; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..360
FT /note="Flavone O-methyltransferase 1"
FT /id="PRO_0000403986"
FT REGION 159..177
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 127..133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 249
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 360 AA; 38860 MW; AEDF183EC84737C9 CRC64;
MGSTAADMAA SADEEACMYA LQLVSSSILP MTLKNAIELG LLETLVAAGG KLLTPAEVAA
KLPSTANPAA ADMVDRMLRL LASYNVVSCT MEEGKDGRLS RRYRAAPVCK FLTPNEDGVS
MAALALMNQD KVLMESWYYL KDAVLDGGIP FNKAYGMSAF EYHGTDPRFN RVFNEGMKNH
SIIITKKLLE VYKGFEGLGT IVDVGGGVGA TVGAITAAYP AIKGINFDLP HVISEAQPFP
GVTHVGGDMF QKVPSGDAIL MKWILHDWSD EHCATLLKNC YDALPAHGKV VLVECILPVN
PEATPKAQGV FHVDMIMLAH NPGGRERYER EFEALAKGAG FKAIKTTYIY ANAFAIEFTK
