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Entry version 67 (11 Dec 2019)
Sequence version 1 (22 Nov 2005)
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Protein

Tricetin 3',4',5'-O-trimethyltransferase

Gene

OMT2

Organism
Triticum aestivum (Wheat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Flavonoid B-ring-specific O-methyltransferase with a preference for flavones > dihydroflavones > flavonols that possess at least two B-ring hydroxyl groups. Active with tricetin, 5-hydroxyferulic acid, luteolin, quercitin, eriodictyol, quercetagetin, taxifolin, gossypetin and myricetin. No activity with naringenin, apigenin, kaempferol, 7,8-dihydroxy- or 5,7,8-trihydroxy flavones, chlorogenic acid, gallic acid or daphnetin. Catalyzes the sequential O-methylation of tricetin via 3'-O-methyltricetin, 3',5'-O-methyltricetin to 3',4',5'-O-trimethyltricetin. May also be involved in S lignin biosynthesis.2 Publications

Miscellaneous

OMT1 has a very low activity with phenylpropanoids (5-hydroxyferulic acid and caffeic acid) while OMT2 has a good activity with them.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=3.73 µM for tricetin2 Publications
  2. KM=3.33 µM for S-adenosyl-L-methionine2 Publications
  3. KM=8.36 µM for 5-hydroxyferulic acid2 Publications
  4. KM=6.59 µM for myricetin2 Publications
  5. KM=68.75 µM for caffeic acid2 Publications
  6. KM=83.04 µM for caffeoyl-CoA2 Publications
  7. KM=95.17 µM for 5-hydroxyferuloyl-CoA2 Publications
  8. KM=43.72 µM for caffeoyl aldehyde2 Publications
  9. KM=17.31 µM for 5-hydroxyconiferaldehyde2 Publications
  10. KM=84.03 µM for caffeoyl alcohol2 Publications
  11. KM=100.21 µM for 5-hydroxyconiferyl alcohol2 Publications
  1. Vmax=142.86 pmol/sec/mg enzyme with tricetin as methyl acceptor2 Publications
  2. Vmax=88.5 pmol/sec/mg enzyme with 5-hydroxyferulic acid as methyl acceptor2 Publications
  3. Vmax=45.66 pmol/sec/mg enzyme with myricetin as methyl acceptor2 Publications
  4. Vmax=2.38 nmol/sec/mg enzyme with caffeic acid as methyl acceptor2 Publications
  5. Vmax=1.26 nmol/sec/mg enzyme with caffeoyl-CoA as methyl acceptor2 Publications
  6. Vmax=1.28 nmol/sec/mg enzyme with 5-hydroxyferuloyl-CoA as methyl acceptor2 Publications
  7. Vmax=2.56 nmol/sec/mg enzyme with caffeoyl aldehyde as methyl acceptor2 Publications
  8. Vmax=1.56 nmol/sec/mg enzyme with 5-hydroxyconiferaldehyde as methyl acceptor2 Publications
  9. Vmax=3.55 nmol/sec/mg enzyme with caffeoyl alcohol as methyl acceptor2 Publications
  10. Vmax=2.67 nmol/sec/mg enzyme with 5-hydroxyconiferyl alcohol as methyl acceptor2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei201S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei224S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei244S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei245S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1
Binding sitei258S-adenosyl-L-methioninePROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei262Proton acceptorPROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMethyltransferase, Transferase
Biological processFlavonoid biosynthesis, Lignin biosynthesis
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-15895

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.1.1.104 6500
2.1.1.169 6500
2.1.1.68 6500

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Tricetin 3',4',5'-O-trimethyltransferase (EC:2.1.1.169)
Short name:
TaOMT2
Alternative name(s):
Caffeic acid 3-O-methyltransferase
Short name:
TaCM
Flavone O-methyltransferase 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:OMT2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiTriticum aestivum (Wheat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri4565 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeTriticinaeTriticum
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000019116 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004039871 – 356Tricetin 3',4',5'-O-trimethyltransferaseAdd BLAST356

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q38J50

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in roots, stems and leaves.1 Publication

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q38J50 baseline and differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. The monomer is fully active and dimerization is not required for sequential methylation.

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
4565.Traes_3B_E7624B49D.1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q38J50

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni123 – 129Substrate bindingBy similarity7
Regioni155 – 173Substrate bindingBy similarityAdd BLAST19

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K22439

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016461 O-MeTrfase_COMT
IPR001077 O_MeTrfase_dom
IPR012967 Plant_MeTrfase_dimerisation
IPR029063 SAM-dependent_MTases
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08100 Dimerisation, 1 hit
PF00891 Methyltransf_2, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005739 O-mtase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46785 SSF46785, 1 hit
SSF53335 SSF53335, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51683 SAM_OMT_II, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q38J50-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSIAAGADE DACMYALQLV SSSILPMTLK NAIELGLLET LMAAGGKFLT
60 70 80 90 100
PAEVAAKLPS AANPEAPDMV DRMLRLLASY NVVSCRTEDG KDGRLSRRYG
110 120 130 140 150
AAPVCKYLTP NEDGVSMSAL ALMNQDKVLM ESWYYLKDAV LDGGIPFNKA
160 170 180 190 200
YGMSAFEYHG TDPRFNRVFN EGMKNHSIII TKKLLESYKG FEGLGTLVDV
210 220 230 240 250
GGGVGATVAA ITAHYPTIKG INFDLPHVIS EAPPFPGVTH VGGDMFQKVP
260 270 280 290 300
SGDAILMKWI LHDWSDEHCA TLLKNCYDAL PAHGKVVLVE CILPVNPEAT
310 320 330 340 350
PKAQGVFHVD MIMLAHNPGG RERYEREFEA LAKGAGFAAM KTTYIYANAW

AIEFTK
Length:356
Mass (Da):38,570
Last modified:November 22, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5EA3037A554E13FB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti89D → E in ABP63535 (PubMed:17976886).Curated1
Sequence conflicti252G → A in ABP63535 (PubMed:17976886).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
DQ223971 mRNA Translation: ABB03907.1
EF413031 mRNA Translation: ABP63535.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:ABB03907

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ223971 mRNA Translation: ABB03907.1
EF413031 mRNA Translation: ABP63535.1

3D structure databases

SMRiQ38J50
ModBaseiSearch...

Protein-protein interaction databases

STRINGi4565.Traes_3B_E7624B49D.1

Proteomic databases

PRIDEiQ38J50

Genome annotation databases

KEGGiag:ABB03907

Phylogenomic databases

KOiK22439

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15895
BRENDAi2.1.1.104 6500
2.1.1.169 6500
2.1.1.68 6500

Gene expression databases

ExpressionAtlasiQ38J50 baseline and differential

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR016461 O-MeTrfase_COMT
IPR001077 O_MeTrfase_dom
IPR012967 Plant_MeTrfase_dimerisation
IPR029063 SAM-dependent_MTases
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF08100 Dimerisation, 1 hit
PF00891 Methyltransf_2, 1 hit
PIRSFiPIRSF005739 O-mtase, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51683 SAM_OMT_II, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFOMT2_WHEAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q38J50
Secondary accession number(s): B8LGB9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: November 22, 2005
Last modified: December 11, 2019
This is version 67 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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