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

metal ion binding Source: UniProtKB-KW
O-methyltransferase activity Source: PomBase

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

catecholamine metabolic process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

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

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
PaxDbⁱ	O42898
PRIDEⁱ	O42898

PTM databases

iPTMnetⁱ	O42898

iPTMnetⁱ

O42898

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	2766121 interactor.
STRINGⁱ	4896.SPBC119.03.1

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	IDAYSHT
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

Similar proteinsⁱ

50% Identity

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
O42898	Q8NKC1 G8BKS4 H8XA70 A3LY58 C4YT58 A0A1D8PRK7 G1UAD2 G3AVK8 B9WJY7 Q6BVD9 +8	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis) Candida orthopsilosis (strain 90-125) (Yeast) Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis) Candida albicans (strain WO-1) (Yeast) Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) Candida albicans (Yeast) Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1) Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast) Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) And more	281	UniRef50_Q8NKC1	Cluster: Probable catechol O-methyltransferase 2	19

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	2766121 interactor.
STRINGⁱ	4896.SPBC119.03.1

PTM databases

iPTMnetⁱ	O42898

iPTMnetⁱ

O42898

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O42898
PaxDbⁱ	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	IDAYSHT
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:	March 28, 2018
	This is version 100 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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - O42898 (COMT1_SCHPO)

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Probable catechol O-methyltransferase 1

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<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

Nucleus

Other locations

Cytosol

Mitochondrion

Nucleus

<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

PTM 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

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

PTM 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

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ