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Entry version 153 (02 Jun 2021)
Sequence version 1 (01 Mar 2001)
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Protein

Flavone 3'-O-methyltransferase 1

Gene

OMT1

Organism
Arabidopsis thaliana (Mouse-ear cress)
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

Methylates OH residues of flavonoid compounds. Converts quercetin into isorhamnetin. Dihydroquercetin is not a substrate. Catalyzes the methylation of monolignols, the lignin precursors. Does not contribute to the phenylpropanoid pattern of the pollen tryphine, but is probably confined to isorhamnetin glycoside biosynthesis (PubMed:10700397, PubMed:12777055, PubMed:20652169, PubMed:22258746).

Involved in melatonin biosynthesis. Can function as acetylserotonin O-methyltransferase. Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine) (PubMed:25039887).

5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Does not require magnesium. Completely inhibited by 5 mM of either NiSO4 or p-chloromercuribenzoate (pCMB). Acetylserotonin O-methyltransferase activity is inhibited by caffeate (PubMed:25039887).2 Publications

<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=1.76 µM for quercetin (at 30 degrees Celsius)1 Publication
  2. KM=3.38 µM for myricetin (at 30 degrees Celsius)1 Publication
  3. KM=24.2 µM for caffeic acid (at pH 7.5)1 Publication
  4. KM=233 µM for N-acetylserotonin (at pH 7.8 and 37 degrees Celsius)1 Publication
  5. KM=32 µM for 5-OH ferulic acid (at pH 7.5)1 Publication
  6. KM=19.7 µM for caffeyl aldehyde (at pH 7.5)1 Publication
  7. KM=17.9 µM for 5-OH coniferyl aldehyde (at pH 7.5)1 Publication
  8. KM=51.5 µM for caffeyl alcohol (at pH 7.5)1 Publication
  9. KM=31.6 µM for 5-OH coniferyl alcohol (at pH 7.5)1 Publication
  10. KM=23.7 µM for quercetin (at pH 7.5)1 Publication
  1. Vmax=384.6 pmol/sec/mg enzyme with quercetin as substrate1 Publication
  2. Vmax=227.3 pmol/sec/mg enzyme with myricetin as substrate1 Publication
  3. Vmax=3.8 pmol/sec/µg enzyme with quercetin as substrate (at pH 7.5)1 Publication
  4. Vmax=51.9 pmol/sec/µg enzyme with 5-OH coniferyl alcohol as substrate (at pH 7.5)1 Publication
  5. Vmax=35.3 pmol/sec/µg enzyme with caffeyl alcohol as substrate (at pH 7.5)1 Publication
  6. Vmax=66.2 pmol/sec/µg enzyme with 5-OH coniferyl aldehyde as substrate (at pH 7.5)1 Publication
  7. Vmax=35.9 pmol/sec/µg enzyme with caffeyl aldehyde as substrate (at pH 7.5)1 Publication
  8. Vmax=30.1 pmol/sec/µg enzyme with 5-OH ferulic acid as substrate (at pH 7.5)1 Publication
  9. Vmax=14.6 pmol/sec/µg enzyme with caffeic acid as substrate (at pH 7.5)1 Publication
  10. Vmax=1800 pmol/min/mg enzyme with N-acetylserotonin as substrate (at pH 7.8 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 7.5 (PubMed:10700397, PubMed:20652169). Optimum pH is 7.8 for acetylserotonin O-methyltransferase activity (PubMed:25039887).3 Publications

Temperature dependencei

Optimum temperature is 37 degrees Celsius for acetylserotonin O-methyltransferase activity.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: quercetin degradation

This protein is involved in the pathway quercetin degradation, which is part of Flavonoid metabolism.
View all proteins of this organism that are known to be involved in the pathway quercetin degradation and in Flavonoid metabolism.

Pathwayi: melatonin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes melatonin from serotonin.Curated This subpathway is part of the pathway melatonin biosynthesis, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes melatonin from serotonin, the pathway melatonin biosynthesis and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei129SubstrateBy similarity1
Binding sitei206S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei229S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei249S-adenosyl-L-methionineBy similarity1
Binding sitei250S-adenosyl-L-methionine; via amide nitrogenBy similarity1
Binding sitei263S-adenosyl-L-methionineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei267Proton acceptorPROSITE-ProRule annotation1
Active sitei2951 Publication1
Active sitei3271 Publication1

<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 processMelatonin biosynthesis
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.1.1.42, 399
2.1.1.68, 399
2.1.1.76, 399

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00724
UPA00837;UER00815

<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%5Fand%5Ftaxonomy%5Fsection">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:
Flavone 3'-O-methyltransferase 1 (EC:2.1.1.42)
Short name:
AtOMT1
Alternative name(s):
Acetylserotonin O-methyltransferase OMT1Curated (EC:2.1.1.41 Publication)
Caffeate O-methyltransferase 1 (EC:2.1.1.68)
Quercetin 3'-O-methyltransferase 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:OMT1
Synonyms:COMT1
Ordered Locus Names:At5g54160
ORF Names:K18G13.3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiArabidopsis thaliana (Mouse-ear cress)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri3702 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000006548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Chromosome 5

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT5G54160

The Arabidopsis Information Resource

More...
TAIRi
locus:2153423, AT5G54160

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Reduced levels of syringyl (S) units in lignins that contain more 5-hydroxyguaiacyl units (5-OH-G), the precursors of S-units. Substitution of sinapyl (S) alcohol-derived substructures by 5-hydroxyconiferyl alcohol (5OHG)-derived moieties in fiber cell walls. No effect on hydroxycinnamic acid amides in pollen.3 Publications

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000632171 – 363Flavone 3'-O-methyltransferase 1Add BLAST363

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9FK25

PRoteomics IDEntifications database

More...
PRIDEi
Q9FK25

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
248754

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9FK25

<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 seedlings, leaves, stems, flowers and siliques, mostly in vascular tissues. Mostly expressed in the apical part of the stems and in roots. Expressed in the endothecium and the epidermal anther, but not in the tapetum. Also detected in all epidermal tissues of flower organs, including petals, sepals and the tip of the stigma.2 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Observed in young seedling and progressively restricted to vascular tissues. Present in whole blade of young leaves but confined to the vascular tissues of mature leaves. In stems, mostly present in xylem, mature phloem and differentiating fibers. In siliques, only present in the lignified extremities. Expressed during early and late stages of flower development.2 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9FK25, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9FK25, AT

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
20748, 6 interactors

Protein interaction database and analysis system

More...
IntActi
Q9FK25, 4 interactors

STRING: functional protein association networks

More...
STRINGi
3702.AT5G54160.1

<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
Q9FK25

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3178, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_005533_12_1_1

Identification of Orthologs from Complete Genome Data

More...
OMAi
ELPHACE

Database of Orthologous Groups

More...
OrthoDBi
817726at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9FK25

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, COMT-like
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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q9FK25-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSTAETQLT PVQVTDDEAA LFAMQLASAS VLPMALKSAL ELDLLEIMAK
60 70 80 90 100
NGSPMSPTEI ASKLPTKNPE APVMLDRILR LLTSYSVLTC SNRKLSGDGV
110 120 130 140 150
ERIYGLGPVC KYLTKNEDGV SIAALCLMNQ DKVLMESWYH LKDAILDGGI
160 170 180 190 200
PFNKAYGMSA FEYHGTDPRF NKVFNNGMSN HSTITMKKIL ETYKGFEGLT
210 220 230 240 250
SLVDVGGGIG ATLKMIVSKY PNLKGINFDL PHVIEDAPSH PGIEHVGGDM
260 270 280 290 300
FVSVPKGDAI FMKWICHDWS DEHCVKFLKN CYESLPEDGK VILAECILPE
310 320 330 340 350
TPDSSLSTKQ VVHVDCIMLA HNPGGKERTE KEFEALAKAS GFKGIKVVCD
360
AFGVNLIELL KKL
Length:363
Mass (Da):39,618
Last modified:March 1, 2001 - 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:iB4380028D89C43DC
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 conflicti229D → N in AAB96879 (PubMed:9349713).Curated1
Sequence conflicti295E → V in CAA81580 (PubMed:8580968).Curated1
Sequence conflicti301T → S in CAA81580 (PubMed:8580968).Curated1
Sequence conflicti348V → C in CAA81580 (PubMed:8580968).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
U70424 mRNA Translation: AAB96879.1
AB013387 Genomic DNA Translation: BAB11578.1
CP002688 Genomic DNA Translation: AED96460.1
AY062837 mRNA Translation: AAL32915.1
AY081565 mRNA Translation: AAM10127.1
AY087297 mRNA Translation: AAM64849.1
Z27062 mRNA Translation: CAA81580.1

NCBI Reference Sequences

More...
RefSeqi
NP_200227.1, NM_124796.4

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT5G54160.1; AT5G54160.1; AT5G54160

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
835504

Gramene; a comparative resource for plants

More...
Gramenei
AT5G54160.1; AT5G54160.1; AT5G54160

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT5G54160

<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
U70424 mRNA Translation: AAB96879.1
AB013387 Genomic DNA Translation: BAB11578.1
CP002688 Genomic DNA Translation: AED96460.1
AY062837 mRNA Translation: AAL32915.1
AY081565 mRNA Translation: AAM10127.1
AY087297 mRNA Translation: AAM64849.1
Z27062 mRNA Translation: CAA81580.1
RefSeqiNP_200227.1, NM_124796.4

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
1NIImodel-A1-363[»]
SMRiQ9FK25
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi20748, 6 interactors
IntActiQ9FK25, 4 interactors
STRINGi3702.AT5G54160.1

PTM databases

iPTMnetiQ9FK25

Proteomic databases

PaxDbiQ9FK25
PRIDEiQ9FK25
ProteomicsDBi248754

Genome annotation databases

EnsemblPlantsiAT5G54160.1; AT5G54160.1; AT5G54160
GeneIDi835504
GrameneiAT5G54160.1; AT5G54160.1; AT5G54160
KEGGiath:AT5G54160

Organism-specific databases

AraportiAT5G54160
TAIRilocus:2153423, AT5G54160

Phylogenomic databases

eggNOGiKOG3178, Eukaryota
HOGENOMiCLU_005533_12_1_1
OMAiELPHACE
OrthoDBi817726at2759
PhylomeDBiQ9FK25

Enzyme and pathway databases

UniPathwayiUPA00724
UPA00837;UER00815
BRENDAi2.1.1.42, 399
2.1.1.68, 399
2.1.1.76, 399

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9FK25

Gene expression databases

ExpressionAtlasiQ9FK25, baseline and differential
GenevisibleiQ9FK25, AT

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR016461, COMT-like
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

MobiDB: a database of protein disorder and mobility annotations

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<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 nameiOMT1_ARATH
<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: Q9FK25
Secondary accession number(s): O49964, Q42170
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: March 1, 2001
Last modified: June 2, 2021
This is version 153 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, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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