A0A1X9YVQ9 · A0A1X9YVQ9_9BACT

Function

function

Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

methylcob(III)alamin (UniProtKB | Rhea| CHEBI:28115 )

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site246Zn2+ (UniProtKB | ChEBI)
Binding site309Zn2+ (UniProtKB | ChEBI)
Binding site310Zn2+ (UniProtKB | ChEBI)
Binding site691methylcob(III)alamin (UniProtKB | ChEBI)
Binding site757-761methylcob(III)alamin (UniProtKB | ChEBI)
Binding site760Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site805methylcob(III)alamin (UniProtKB | ChEBI)
Binding site809methylcob(III)alamin (UniProtKB | ChEBI)
Binding site861methylcob(III)alamin (UniProtKB | ChEBI)
Binding site947S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1137S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1192-1193S-adenosyl-L-methionine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functioncobalamin binding
Molecular Functionmethionine synthase activity
Molecular Functionzinc ion binding
Biological Processhomocysteine metabolic process
Biological Processmethylation
Biological Processtetrahydrofolate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Methionine synthase
  • EC number
  • Alternative names
    • 5-methyltetrahydrofolate--homocysteine methyltransferase

Gene names

    • ORF names
      CA264_16785

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 19842
  • Taxonomic lineage
    Bacteria > Bacteroidota > Cytophagia > Cytophagales > Hymenobacteraceae > Pontibacter

Accessions

  • Primary accession
    A0A1X9YVQ9

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain4-324Hcy-binding
Domain355-616Pterin-binding
Domain647-741B12-binding N-terminal
Domain747-882B12-binding
Domain897-1230AdoMet activation
Region1210-1237Disordered

Domain

Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin.

Sequence similarities

Belongs to the vitamin-B12 dependent methionine synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,237
  • Mass (Da)
    136,813
  • Last updated
    2017-08-30 v1
  • Checksum
    AF84642637A2FE3B
MTKLHPIHKLLQERVLVLDGAMGTMIQRYQLQEADFRGERFQDHASDLKGNNDLLSITRPDVIKAIHAEYLEAGADIIETNTFSGTSIAMADYHLEHIVYELNYESARLAREAADEIEAKVPGKPRFVAGAIGPTNRTASLSPDVNNPGYRAITFDQLVEAYCEQVRGLVDGGSNLLLVETVFDTLNCKAALFAIDQYVQDGGKALPIMVSGTITDASGRTLSGQTVEAFWNSISHAPILSIGFNCALGARQLKTHIKELSRISDCYISAYPNAGLPNAFGGYDETAQQMGEIVEEYLKEGLVNILGGCCGTTPVHTKVISDLVQKYKPHVPTPVAPLPRYSGLEPLTIYPESLFVNVGERTNVTGSKKFARLIVEEKFEEALSVAQQQVEGGAQIIDVNMDEGMLDSEQAMTNFLNLIASEPDISKLPIMIDSSKWSVIEAGLKCVQGKSIVNSISLKEGEENFKKVARKVRQYGAAVVVMAFDEQGQADTFERRIEICEKSYRILVDEVGFPPQDIIFDPNILAIATGIEEHNNYAVDYIETIKWIKANLPHALVSGGVSNLSFSFRGNDVVREAMHTVFLYYAVQAGMDMGIVNAGMMGVYSEIPTELRDLIEDVIFNRHPDATEKLVTYAETIKGKGKGAAQADNSWREAPVEERLKHALVKGIVEFIEEDTEEARQKATKTLEVIEGPLMAGMTVVGDLFGAGKMFLPQVVKSARVMKKSVAYLLPFMEAEKLASDTSKSTAGTILMATVKGDVHDIGKNIVGVVLACNNYEVIDLGVMVSLDKILAEAEAQQVDIIGLSGLITPSLDEMVYVAQEMERRGMKIPLLIGGATTSRVHTAVKIAPQYSGPVVHVHDASRSVTVVSSLLGSDRENYIAEIKAEYEKLREDHLNRTKDRAFASIGEARANKYKVDWAATRPTKPSFLGNKVYTNYPLSEIVPFIDWTPFFHTWELKRQYPKILDDAELGTEARKLFADAQQMLQEIVDNQLLEARAVVGFYPANVEADDTIEVYADDSRENELTEFHTLRQQGKKGQGVPNMAFSDFIAPKETGVQDYIGGFVVSAGFGIEKMLEQYEAEHDDYRSIMAKALADRLAEAFAELMHLKVRRELWGYSPEEQLSNEDLIKEQYKGIRPAPGYPGCPDHTEKITLFNLLNAEEQTGIILTENLAMYPASSVSGLYFSHPESKYFGLGKIGEDQVADLAQRKNMPQEELERWLSPNLNYEPKPLAQQTA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP021235
EMBL· GenBank· DDBJ
ARS36949.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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