Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 67 (11 Dec 2019)
Sequence version 1 (04 Apr 2006)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Isoflavone 4'-O-methyltransferase

Gene

HI4'OMT

Organism
Medicago truncatula (Barrel medic) (Medicago tribuloides)
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

2-hydroxyisoflavanone 4'-O-methyltransferase involved in the biosynthesis of the phytoalexin medicarpin. Has also an in vitro (+)-6a-hydroxymaackiain-3-0-methyltransferase activity, converting the pterocarpan 6a-hydroxymaackiain into pisatin. No activity with di- or trihydroxylated isoflavones, including daidzein and genistein, or with (-)-medicarpin and maackiain. The dual activity for either 3- or 4'-O-methylation depends upon substrate availability.1 Publication

<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=73.3 µM for 2,7,4'-trihydroxyisoflavanone1 Publication
  2. KM=62.1 µM for 6a-hydroxymaackiain1 Publication
  3. KM=99.8 µM for S-adenosyl-L-methionine1 Publication
  1. Vmax=4.0 nmol/min/mg enzyme with 2,7,4'-trihydroxyisoflavanone as substrate1 Publication
  2. Vmax=17.9 nmol/min/mg enzyme with 6a-hydroxymaackiain as substrate1 Publication
  3. Vmax=23.9 nmol/min/mg enzyme toward S-adenosyl-L-methionine for the 4'-O-methyltransferase activity1 Publication

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 sitei230S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei264S-adenosyl-L-methionine1
<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 sitei268Proton 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
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.1.1.212 3201
2.1.1.270 3201

<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:
Isoflavone 4'-O-methyltransferase (EC:2.1.1.461 Publication)
Short name:
MtHI4'OMT
Alternative name(s):
2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase (EC:2.1.1.2121 Publication)
<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:HI4'OMT
<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>OrganismiMedicago truncatula (Barrel medic) (Medicago tribuloides)
<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 identifieri3880 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladeNPAAA cladeHologaleginaIRL cladeTrifolieaeMedicago

<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_00004119771 – 364Isoflavone 4'-O-methyltransferaseAdd BLAST364

Proteomic databases

Protein Mass spectra EXtraction

More...
ProMEXi
Q29U70

<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

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q29U70 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.

1 Publication

GO - Molecular functioni

<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

Secondary structure

1364
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q29U70

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q29U70

<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>Regioni206 – 209S-adenosyl-L-methionine binding4
Regioni230 – 231S-adenosyl-L-methionine binding2
Regioni250 – 251S-adenosyl-L-methionine binding2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi96 – 99Poly-Glu4

<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
K13259

Database of Orthologous Groups

More...
OrthoDBi
817726at2759

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.

Q29U70-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAFSTNGSEE SELYHAQIHL YKHVYNFVSS MALKSAMELG IADAIHNHGK
60 70 80 90 100
PMTLSELASS LKLHPSKVNI LHRFLRLLTH NGFFAKTIVK GKEGDEEEEI
110 120 130 140 150
AYSLTPPSKL LISGKPTCLS SIVKGALHPS SLDMWSSSKK WFNEDKEQTL
160 170 180 190 200
FECATGESFW DFLNKDSESS TLSMFQDAMA SDSRMFKLVL QENKRVFEGL
210 220 230 240 250
ESLVDVGGGT GGVTKLIHEI FPHLKCTVFD QPQVVGNLTG NENLNFVGGD
260 270 280 290 300
MFKSIPSADA VLLKWVLHDW NDEQSLKILK NSKEAISHKG KDGKVIIIDI
310 320 330 340 350
SIDETSDDRG LTELQLDYDL VMLTMFLGKE RTKQEWEKLI YDAGFSSYKI
360
TPISGFKSLI EVYP
Length:364
Mass (Da):40,754
Last modified:April 4, 2006 - 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:iC7C83C858A4BC9E5
GO

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
AY942158 mRNA Translation: AAY18581.1

NCBI Reference Sequences

More...
RefSeqi
XP_013456930.1, XM_013601476.1

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
KEH30961; KEH30961; MTR_4g088190

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25493072

Gramene; a comparative resource for plants

More...
Gramenei
KEH30961; KEH30961; MTR_4g088190

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:AAY18581
mtr:MTR_4g088190

<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
AY942158 mRNA Translation: AAY18581.1
RefSeqiXP_013456930.1, XM_013601476.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZG3X-ray2.35A7-364[»]
1ZGAX-ray2.35A8-364[»]
1ZGJX-ray2.50A11-364[»]
1ZHFX-ray2.50A8-364[»]
SMRiQ29U70
ModBaseiSearch...
PDBe-KBiSearch...

Proteomic databases

ProMEXiQ29U70

Genome annotation databases

EnsemblPlantsiKEH30961; KEH30961; MTR_4g088190
GeneIDi25493072
GrameneiKEH30961; KEH30961; MTR_4g088190
KEGGiag:AAY18581
mtr:MTR_4g088190

Phylogenomic databases

KOiK13259
OrthoDBi817726at2759

Enzyme and pathway databases

BRENDAi2.1.1.212 3201
2.1.1.270 3201

Miscellaneous databases

EvolutionaryTraceiQ29U70

Gene expression databases

ExpressionAtlasiQ29U70 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 nameiI4OMT_MEDTR
<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: Q29U70
<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: July 27, 2011
Last sequence update: April 4, 2006
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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again