Q99028 · COMT_PIG
- ProteinCatechol O-methyltransferase
- GeneCOMT
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids186 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
Catalytic activity
- a catechol + S-adenosyl-L-methionine = a guaiacol + H+ + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
- 2-hydroxyestrone + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-estrone + H+ + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
- 4-hydroxyestrone + S-adenosyl-L-methionine = 4-methoxyestrone + H+ + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
- 2-hydroxyestrone + S-adenosyl-L-methionine = 2-methoxyestrone + H+ + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
- 4-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 4-methoxy-17beta-estradiol + H+ + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
- 2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-17beta-estradiol + H+ + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
- 2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-methoxy-17beta-estradiol + H+ + S-adenosyl-L-homocysteineThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 7 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 29 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 37 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 55 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 56 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 82-85 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GASQ | ||||||
Binding site | 84 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 106 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 106 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 109 | substrate | ||||
Sequence: K | ||||||
Binding site | 134 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 135 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 135 | substrate | ||||
Sequence: N | ||||||
Binding site | 164 | substrate | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cytosol | |
Cellular Component | dendrite | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | catechol O-methyltransferase activity | |
Molecular Function | magnesium ion binding | |
Biological Process | catecholamine catabolic process | |
Biological Process | developmental process | |
Biological Process | dopamine metabolic process | |
Biological Process | lipid metabolic process | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCatechol O-methyltransferase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus
Accessions
- Primary accessionQ99028
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type II membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000090016 | 1-186 | Catechol O-methyltransferase | |||
Sequence: KERAMHVGRKKGQIVDTVVQEQRPSVLLELGAYCGYSAVRMARLLLPSARLLTIELNPDNAAIAQQVVDFAGLQDRVTVVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGCGRFECTHFSSYLEYSQMVDGLEKAVYKGPGSPAQP | ||||||
Modified residue | 182 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Structure
Family & Domains
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length186
- Mass (Da)20,587
- Last updated1994-06-01 v1
- Checksum493B8801F06C6262
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: K |
Keywords
- Technical term