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Entry version 33 (11 Dec 2019)
Sequence version 1 (05 Sep 2012)
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Protein

Scoulerine-9-O-methyltransferase 1

Gene

SOMT1

Organism
Papaver somniferum (Opium poppy)
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

Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine (PubMed:22535422, PubMed:22653730, PubMed:29610307). Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine (PubMed:22535422, PubMed:22653730). Can convert (S)-tetrahydrocolumbamine to tetrahydropalmatine (PubMed:22535422). Can convert (S)-norreticuline to (S)-norcodamine (PubMed:22535422). Can convert (S)-reticuline to (S)-codamine (PubMed:22535422). Substrate preference is (S)-scoulerine > (S)-tetrahydrocolumbamine > (S)-norreticuline > (S)-reticuline (PubMed:22535422).3 Publications

<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=28.5 µM for (S)-scoulerine1 Publication
  2. KM=70.3 µM for (S)-reticuline1 Publication
  3. KM=19 µM for S-adenosyl-L-methionine1 Publication
  1. Vmax=2036 nmol/min/mg enzyme with (S)-scoulerine as substrate1 Publication
  2. Vmax=184.4 nmol/min/mg enzyme with (S)-reticuline as substrate1 Publication
  3. Vmax=1290 nmol/min/mg enzyme with S-adenosyl-L-methionine as substrate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Alkaloid biosynthesis

This protein is involved in Alkaloid biosynthesis.Curated
View all proteins of this organism that are known to be involved in Alkaloid biosynthesis.

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 sitei153SubstrateCombined sources1
Binding sitei207S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei211S-adenosyl-L-methionineCombined sources1 Publication1
Binding sitei235S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
Binding sitei258S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources1 Publication1
Binding sitei292S-adenosyl-L-methionineCombined sources1 Publication1
<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 sitei296Proton acceptorPROSITE-ProRule annotation1 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 processAlkaloid metabolism
LigandS-adenosyl-L-methionine

<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:
Scoulerine-9-O-methyltransferase 11 Publication (EC:2.1.1.1173 Publications)
Short name:
PsSOMT11 Publication
Alternative name(s):
Norreticuline 3-O-methyltransferase SOMT1Curated (EC:2.1.1.-1 Publication)
O-methyltransferase 11 Publication
Reticuline 3-O-methyltransferase SOMT1Curated (EC:2.1.1.-1 Publication)
Tetrahydrocolumbamine 2-O-methyltransferase SOMT1Curated (EC:2.1.1.891 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:SOMT11 Publication
Synonyms:PSMT11 Publication
<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>OrganismiPapaver somniferum (Opium poppy)
<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 identifieri3469 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaRanunculalesPapaveraceaePapaveroideaePapaver

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi296H → A: Loss of enzymatic activity. 1 Publication1

<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_00004475911 – 390Scoulerine-9-O-methyltransferase 1Add BLAST390

<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

Highly expressed in capsules (PubMed:22653730). Expressed is stems (PubMed:22653730, PubMed:22535422). Expressed at low levels in roots (PubMed:22535422).2 Publications

<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

1390
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
I3V6A7

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

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>Regioni278 – 279S-adenosyl-L-methionine bindingCombined sources1 Publication2
Regioni296 – 297Substrate bindingCombined sources1 Publication2

<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

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.

I3V6A7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATNGEIFNT YGHNRQTATV TKITASNESS NGVCYLSETA NLGKLICIPM
60 70 80 90 100
ALRAAMELNV FQLISKFGTD AKVSASEIAS KMPNAKNNPE AAMYLDRILR
110 120 130 140 150
LLGASSILSV STTKKSINRG GDDVVVHEKL YGLTNSSCCL VPRQEDGVSL
160 170 180 190 200
VEELLFTSDK VVVDSFFKLK CVVEEKDSVP FEVAHGAKIF EYAATEPRMN
210 220 230 240 250
QVFNDGMAVF SIVVFEAVFR FYDGFLDMKE LLDVGGGIGT SVSKIVAKYP
260 270 280 290 300
LIRGVNFDLP HVISVAPQYP GVEHVAGDMF EEVPKGQNML LKWVLHDWGD
310 320 330 340 350
ERCVKLLKNC WNSLPVGGKV LIIEFVLPNE LGNNAESFNA LIPDLLLMAL
360 370 380 390
NPGGKERTIS EYDDLGKAAG FIKTIPIPIS NGLHVIEFHK
Length:390
Mass (Da):42,699
Last modified:September 5, 2012 - 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:iC3E59F1D7F78BE01
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 conflicti15 – 17RQT → HQS in AFB74611 (PubMed:22653730).Curated3
Sequence conflicti221F → V in AFB74611 (PubMed:22653730).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
JN185323 mRNA Translation: AFK73709.1
JQ658999 Genomic DNA Translation: AFB74611.1

<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
JN185323 mRNA Translation: AFK73709.1
JQ658999 Genomic DNA Translation: AFB74611.1

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
6I5QX-ray3.05A/B/C/D1-390[»]
6I5ZX-ray3.00A/B/C/D1-390[»]
6I6KX-ray1.49A/B1-390[»]
6I6LX-ray1.29A/B1-390[»]
6I6MX-ray1.20A/B1-390[»]
6I6NX-ray1.50A/B1-390[»]
SMRiI3V6A7
ModBaseiSearch...
PDBe-KBiSearch...

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 nameiSOMT1_PAPSO
<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: I3V6A7
Secondary accession number(s): I3PLQ5
<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 3, 2019
Last sequence update: September 5, 2012
Last modified: December 11, 2019
This is version 33 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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