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Q99028

- COMT_PIG

UniProt

Q99028 - COMT_PIG

Protein

Catechol O-methyltransferase

Gene

COMT

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    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 activityi

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

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei7 – 71S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei29 – 291S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei37 – 371S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei55 – 551S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei56 – 561S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
    Binding sitei84 – 841S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
    Metal bindingi106 – 1061MagnesiumBy similarity
    Binding sitei106 – 1061S-adenosyl-L-methioninePROSITE-ProRule annotation
    Binding sitei109 – 1091SubstrateBy similarity
    Metal bindingi134 – 1341MagnesiumBy similarity
    Metal bindingi135 – 1351MagnesiumBy similarity
    Binding sitei135 – 1351SubstrateBy similarity
    Binding sitei164 – 1641SubstrateBy similarity

    GO - Molecular functioni

    1. catechol O-methyltransferase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. catecholamine metabolic process Source: UniProtKB-KW
    2. neurotransmitter catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Catecholamine metabolism, Neurotransmitter degradation

    Keywords - Ligandi

    Magnesium, Metal-binding, S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Catechol O-methyltransferase (EC:2.1.1.6)
    Gene namesi
    Name:COMT
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity; Single-pass type II membrane protein By similarity; Extracellular side By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 186›186Catechol O-methyltransferasePRO_0000090016Add
    BLAST

    Proteomic databases

    PaxDbiQ99028.
    PRIDEiQ99028.

    Interactioni

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000010805.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99028.
    SMRiQ99028. Positions 1-180.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni82 – 854S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG4122.
    HOGENOMiHOG000046392.
    HOVERGENiHBG005376.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR025782. Catechol_O-MeTrfase.
    IPR002935. O-MeTrfase_3.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR10509. PTHR10509. 1 hit.
    PfamiPF01596. Methyltransf_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51682. SAM_OMT_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Q99028-1 [UniParc]FASTAAdd to Basket

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    KERAMHVGRK KGQIVDTVVQ EQRPSVLLEL GAYCGYSAVR MARLLLPSAR    50
    LLTIELNPDN AAIAQQVVDF AGLQDRVTVV VGASQDIIPQ LKKKYDVDTL 100
    DMVFLDHWKD RYLPDTLLLE ECGLLRKGTV LLADNVICPG APDFLAHVRG 150
    CGRFECTHFS SYLEYSQMVD GLEKAVYKGP GSPAQP 186
    Length:186
    Mass (Da):20,587
    Last modified:June 1, 1994 - v1
    Checksum:i493B8801F06C6262
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Cross-referencesi

    3D structure databases

    ProteinModelPortali Q99028.
    SMRi Q99028. Positions 1-180.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000010805.

    Chemistry

    ChEMBLi CHEMBL2176837.

    Proteomic databases

    PaxDbi Q99028.
    PRIDEi Q99028.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG4122.
    HOGENOMi HOG000046392.
    HOVERGENi HBG005376.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR025782. Catechol_O-MeTrfase.
    IPR002935. O-MeTrfase_3.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR10509. PTHR10509. 1 hit.
    Pfami PF01596. Methyltransf_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51682. SAM_OMT_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human catechol-O-methyltransferase: cloning and expression of the membrane-associated form."
      Bertocci B., Miggiano V., da Prada M., Dembic Z., Lahm H.-W., Malherbe P.
      Proc. Natl. Acad. Sci. U.S.A. 88:1416-1420(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Immunoaffinity purification and partial amino acid sequence analysis of catechol-O-methyltransferase from pig liver."
      Bertocci B., Garotta G., da Prada M., Lahm H.-W., Zurcher G., Virgallita G., Miggiano V.
      Biochim. Biophys. Acta 1080:103-109(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.

    Entry informationi

    Entry nameiCOMT_PIG
    AccessioniPrimary (citable) accession number: Q99028
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3