Q99028 · COMT_PIG

  • Protein
    Catechol O-methyltransferase
  • Gene
    COMT
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

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-homocysteine
    This reaction proceeds in the forward direction.
    EC:2.1.1.6 (UniProtKB | ENZYME | Rhea)
  • 2-hydroxyestrone + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-estrone + H+ + S-adenosyl-L-homocysteine
    This reaction proceeds in the forward direction.
  • 4-hydroxyestrone + S-adenosyl-L-methionine = 4-methoxyestrone + H+ + S-adenosyl-L-homocysteine
    This reaction proceeds in the forward direction.
  • 2-hydroxyestrone + S-adenosyl-L-methionine = 2-methoxyestrone + H+ + S-adenosyl-L-homocysteine
    This reaction proceeds in the forward direction.
  • 4-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 4-methoxy-17beta-estradiol + H+ + S-adenosyl-L-homocysteine
    This reaction proceeds in the forward direction.
  • 2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-17beta-estradiol + H+ + S-adenosyl-L-homocysteine
    This reaction proceeds in the forward direction.
  • 2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-methoxy-17beta-estradiol + H+ + S-adenosyl-L-homocysteine
    This reaction proceeds in the forward direction.

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site7S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site29S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site37S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site55S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site56S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site82-85S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site84S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site106Mg2+ (UniProtKB | ChEBI)
Binding site106S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site109substrate
Binding site134Mg2+ (UniProtKB | ChEBI)
Binding site135Mg2+ (UniProtKB | ChEBI)
Binding site135substrate
Binding site164substrate

GO annotations

AspectTerm
Cellular Componentaxon
Cellular Componentcytosol
Cellular Componentdendrite
Cellular Componentmembrane
Cellular Componentplasma membrane
Molecular Functioncatechol O-methyltransferase activity
Molecular Functionmagnesium ion binding
Biological Processcatecholamine catabolic process
Biological Processdevelopmental process
Biological Processdopamine metabolic process
Biological Processlipid metabolic process
Biological Processmethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Catechol O-methyltransferase
  • EC number

Gene names

    • Name
      COMT

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus

Accessions

  • Primary accession
    Q99028

Proteomes

Subcellular Location

Cytoplasm
Cell membrane
; Single-pass type II membrane protein

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000900161-186Catechol O-methyltransferase
Modified residue182Phosphoserine

Keywords

Proteomic databases

Interaction

Protein-protein interaction databases

Chemistry

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    186
  • Mass (Da)
    20,587
  • Last updated
    1994-06-01 v1
  • Checksum
    493B8801F06C6262
KERAMHVGRKKGQIVDTVVQEQRPSVLLELGAYCGYSAVRMARLLLPSARLLTIELNPDNAAIAQQVVDFAGLQDRVTVVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGCGRFECTHFSSYLEYSQMVDGLEKAVYKGPGSPAQP

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Keywords

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp