SPBC119.03

Functionⁱ

Catalytic activityⁱ

S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol.

Cofactorⁱ

Mg²⁺By similarityNote: Binds 1 Mg²⁺ ion per subunit.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	56	S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation	1
Binding siteⁱ	78	S-adenosyl-L-methioninePROSITE-ProRule annotation	1
Binding siteⁱ	86	S-adenosyl-L-methioninePROSITE-ProRule annotation	1
Binding siteⁱ	106	S-adenosyl-L-methioninePROSITE-ProRule annotation	1
Binding siteⁱ	107	S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation	1
Binding siteⁱ	135	S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation	1
Metal bindingⁱ	162	MagnesiumBy similarity	1
Binding siteⁱ	162	S-adenosyl-L-methioninePROSITE-ProRule annotation	1
Binding siteⁱ	165	SubstrateBy similarity	1
Metal bindingⁱ	190	MagnesiumBy similarity	1
Metal bindingⁱ	191	MagnesiumBy similarity	1
Binding siteⁱ	191	SubstrateBy similarity	1

GO - Molecular functionⁱ

catechol O-methyltransferase activity Source: UniProtKB-EC
L-dopa O-methyltransferase activity Source: UniProtKB-EC
metal ion binding Source: UniProtKB-KW

Complete GO annotation...

GO - Biological processⁱ

catecholamine metabolic process Source: UniProtKB-KW

Complete GO annotation...

Keywordsⁱ

Molecular function	Methyltransferase, Transferase
Biological process	Catecholamine metabolism
Ligand	Magnesium, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

Reactomeⁱ	R-SPO-156581. Methylation. R-SPO-379397. Enzymatic degradation of dopamine by COMT. R-SPO-379398. Enzymatic degradation of Dopamine by monoamine oxidase.

Reactomeⁱ

R-SPO-156581. Methylation.
R-SPO-379397. Enzymatic degradation of dopamine by COMT.
R-SPO-379398. Enzymatic degradation of Dopamine by monoamine oxidase.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Probable catechol O-methyltransferase 1 (EC:2.1.1.6)
Gene namesⁱ	ORF Names:SPBC119.03
Organismⁱ	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifierⁱ	284812 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe
Proteomesⁱ	UP000002485 Componentⁱ: Chromosome II

Organism-specific databases

EuPathDBⁱ	FungiDB:SPBC119.03.
PomBaseⁱ	SPBC119.03.

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol
Source: PomBase
Inferred from direct assayⁱ
- 16823372
nucleus
Source: PomBase
Inferred from direct assayⁱ
- 16823372

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000318148	1 – 266	Probable catechol O-methyltransferase 1Add BLAST		266

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O42898.
PRIDEⁱ	O42898.

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	276612. 1 interactor.
Molecular INTeraction database More...MINTⁱ	MINT-4673835.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	O42898.
SMRⁱ	O42898.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMⁱ	HOG000171638.
InParanoidⁱ	O42898.
KEGG Orthology (KO) More...KOⁱ	K00545.
OMAⁱ	NDGREQE.
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C4KCD.
PhylomeDBⁱ	O42898.

Family and domain databases

InterProⁱ	View protein in InterPro IPR002935. O-MeTrfase_3. IPR029063. SAM-dependent_MTases.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01596. Methyltransf_3. 1 hit.
SUPFAMⁱ	SSF53335. SSF53335. 1 hit.
PROSITEⁱ	View protein in PROSITE PS51682. SAM_OMT_I. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

O42898-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MPHMEDNGSE KEQLFLQHIQ NLPQERLDAI RGHPELVLKE IDEFTYPDGS 
        60         70         80         90        100
GVRMCIGDVK GGFIVGKIRE RKPKIMVELG GYLGYSAILF GNEISKIPGG 
       110        120        130        140        150
RYYSLEVNED YAKIAYELVK LAGLDEIVTI MIGKACDSLV ELQQKLLHKD 
       160        170        180        190        200
LGFQALDMVF IDHWKDLYVP DLRVIESLNM IAPGTLLVAD NIITPGAPEY 
       210        220        230        240        250
HKYVNMSPEE RRGYQAKVRN VNGFDFIGRW DLIYKTETKE FEGVIRNKHR 
       260 
KDAVDVTECV GYAKKD

Length:266

Mass (Da):30,267

Last modified:June 1, 1998 - v1

Checksum:ⁱ99316BCF4FAED5EA

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CU329671 Genomic DNA. Translation: CAA17918.1.
PIRⁱ	T39301.
NCBI Reference Sequences More...RefSeqⁱ	NP_595284.1. NM_001021191.2.

Genome annotation databases

EnsemblFungiⁱ	SPBC119.03.1; SPBC119.03.1:pep; SPBC119.03.
GeneIDⁱ	2540074.
KEGGⁱ	spo:SPBC119.03.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CU329671 Genomic DNA. Translation: CAA17918.1.
PIRⁱ	T39301.
NCBI Reference Sequences More...RefSeqⁱ	NP_595284.1. NM_001021191.2.

3D structure databases

ProteinModelPortalⁱ	O42898.
SMRⁱ	O42898.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	276612. 1 interactor.
Molecular INTeraction database More...MINTⁱ	MINT-4673835.

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O42898.
PRIDEⁱ	O42898.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblFungiⁱ	SPBC119.03.1; SPBC119.03.1:pep; SPBC119.03.
GeneIDⁱ	2540074.
KEGGⁱ	spo:SPBC119.03.

Organism-specific databases

EuPathDBⁱ	FungiDB:SPBC119.03.
PomBaseⁱ	SPBC119.03.

Phylogenomic databases

HOGENOMⁱ	HOG000171638.
InParanoidⁱ	O42898.
KEGG Orthology (KO) More...KOⁱ	K00545.
OMAⁱ	NDGREQE.
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C4KCD.
PhylomeDBⁱ	O42898.

Enzyme and pathway databases

Reactomeⁱ	R-SPO-156581. Methylation. R-SPO-379397. Enzymatic degradation of dopamine by COMT. R-SPO-379398. Enzymatic degradation of Dopamine by monoamine oxidase.

Reactomeⁱ

R-SPO-156581. Methylation.
R-SPO-379397. Enzymatic degradation of dopamine by COMT.
R-SPO-379398. Enzymatic degradation of Dopamine by monoamine oxidase.

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:O42898.

PROⁱ

PR:O42898.

Family and domain databases

InterProⁱ	View protein in InterPro IPR002935. O-MeTrfase_3. IPR029063. SAM-dependent_MTases.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01596. Methyltransf_3. 1 hit.
SUPFAMⁱ	SSF53335. SSF53335. 1 hit.
PROSITEⁱ	View protein in PROSITE PS51682. SAM_OMT_I. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	COMT1_SCHPO
Accessionⁱ	O42898Primary (citable) accession number: O42898
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
	Last sequence update:	June 1, 1998
	Last modified:	June 7, 2017
	This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

Schizosaccharomyces pombe
Schizosaccharomyces pombe: entries and gene names
SIMILARITY comments
Index of protein domains and families

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - O42898 (COMT1_SCHPO)

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Probable catechol O-methyltransferase 1

Select a section on the left to see content.

<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

Sites

<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

<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 - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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>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 - Cellular componenti

<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

Proteomic databases

<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

Protein-protein interaction databases

<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

<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

Family and domain databases

<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 length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ