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A0A4D7JF80 · A0A4D7JF80_9BACT

  • Protein
    Methionine synthase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site362methylcob(III)alamin (UniProtKB | ChEBI)
Binding site427-431methylcob(III)alamin (UniProtKB | ChEBI)
Binding site430Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site475methylcob(III)alamin (UniProtKB | ChEBI)
Binding site479methylcob(III)alamin (UniProtKB | ChEBI)
Binding site531methylcob(III)alamin (UniProtKB | ChEBI)
Binding site618S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site804methylcob(III)alamin (UniProtKB | ChEBI)
Binding site859-860S-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
      DCC35_09010

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 9dcg1
  • Taxonomic lineage
    Bacteria > Bacteroidota > Cytophagia > Cytophagales > Roseivirgaceae > Roseivirga

Accessions

  • Primary accession
    A0A4D7JF80

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain, coiled coil.

Type
IDPosition(s)Description
Domain27-288Pterin-binding
Domain318-412B12-binding N-terminal
Domain417-552B12-binding
Coiled coil544-571
Domain568-897AdoMet activation

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
    903
  • Mass (Da)
    101,637
  • Last updated
    2019-07-31 v1
  • MD5 Checksum
    57FD9EAEEFEAFCDF9863567CFFE38D62
MSENNFTYKPLRLSGLEPLYVTPNANFINIGERTNVTGSRKFLRLIREDKYEEALDVALDQVRGGAQVIDVNMDEAMIDGKAAMVKFLHLMASEPEIARIPIMIDSSKWEIIEAGLQCIQGKGIVNSISLKEGEEQFLEQARLIKKYGAAVVVMAFDEDGQADNYHRRIEICERSYKLLTEIADFPAQDIIFDPNIFPVATGMEEHRRNALDFFEATAWIKQHLHGAKVSGGVSNVSFSFRGNNKVREAMHAAFLYHAIKHGMDMGIVNPTMLEVYDEIPDDLLERVEDVLLNRREDATERLLEFAETVKNDKREDKKAEEWRSGTVEERLSHALVKGIIDHIEEDTEEAFQKLGRPLKVIEGPLMDGMNIVGDLFGSGKMFLPQVVKSARVMKRAVAYLTPYLEAEKKANPNQKPKAKILLATVKGDVHDIGKNIVSVVLACNNFDVVDLGVMVPAEKILQAAIDEKVDAIGLSGLITPSLDEMVHVAKEMERSGFDMPLLIGGATTSRIHTAVKIDPHYSGVVTHVLDASRCVSVCTNALSDERKEEFKQNLKEEYEKARADHANKKQIKKYISYEEAVLNAERQDWEGYEPPAPNKTGTFVFNDINIEELIPYIDWTPFFSAWMLKGKFPQILNHEVVGVEASKLYSDAQDMLAEVVENRSLKAHGVVGIYPAVRTGADTVSVMDESGKPHFNFEFLRQQGQKGKGLPNLSLADFISPSDAGKTDYIGGFAVTAGDGIEDLIQEYELDDYKQIMIKALADRLAEAFAEYLHEKVRKEIWGYAAGENYENEELIKERYIGIRPAPGYPACPDHTEKIKLFDWLKVPENTGITLTESMAMYPTAAVSGYYFSHPESRYFGLGKIERDQVEEYSKRKGWDIETTEKWLAPNLNYDPEKLVIQN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP028923
EMBL· GenBank· DDBJ
QCK14869.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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