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A0A2Z6EY78 · A0A2Z6EY78_9BURK

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 site379methylcob(III)alamin (UniProtKB | ChEBI)
Binding site448-452methylcob(III)alamin (UniProtKB | ChEBI)
Binding site451Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site496methylcob(III)alamin (UniProtKB | ChEBI)
Binding site500methylcob(III)alamin (UniProtKB | ChEBI)
Binding site556methylcob(III)alamin (UniProtKB | ChEBI)
Binding site642S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site841S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site895-896S-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
      MCB1EB_2206

Organism names

  • Taxonomic identifier
  • Strain
    • B1-EB
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Mycoavidus

Accessions

  • Primary accession
    A0A2Z6EY78

Proteomes

Subcellular Location

Family & Domains

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    928
  • Mass (Da)
    102,510
  • Last updated
    2018-10-10 v1
  • MD5 Checksum
    75EE7679D43A8BD50C0378F3E5D81F6A
MTDATDLNRRAPHQIGLEPALRLAGLEAFNIGAQTRFVNIGERTNVTGSKAFARMILNDEFDAALSVARQQVENGAQIIDINMDEAMLDSKAAMVRFLNLIAAEPDIARVPIMLDSSKWEVLEAGLKCVQGKAIVNSISLKEGVEIFKQQAQSIRRYGAAAVVMAFDETGQADSFARKITICERSYRILVEEVGFAPEDIIFDPNIFAIATGIDEHNNYAVDFIEATRWIKAHLPYAKVSGGVSNVSFSFRGNDAVREAIHTVFLYHAISAGMDMGIVNAGQLGIYAELDPTLRERVEDVVLNRSVQTANGMSATERLLEITEHFKQGGGAKNQEALLWRQLSVKDRLAHALVHGITEFIIEDTEEARQQYARPIQVIEGPLMDGMNRVGDLFGAGKMFLPQVVKSARVMKQAVAHLLPFIEAEKNLLTAQGGDAKPKGKMVIATVKGDVHDIGKNIVSVVLQCNNFEVINMGVMVPCSEILAKAKAENADMIGLSGLITPSLEEMAYVAAEIQRDEILRARNIPLLIGGATTSRVHTAVKIAPQYGGPVIYVPDASRAVSVASSLLSETHSATYIAELKTNYERIREQHANKKTQPMVSLSQARANRHRINWTTTSPTKPKLIGRRVLKNYDLAELARYIDWGPFFQTWDLAGPFPAILTDAIVGEAARRVYEDAQNMLAQLIAGRWLTAHGVFALLPANTVNDDDIEIYTDETRKQIALTWHTLRQQSERPVIEGPNQEKIRRPNRALADFIAPKETQIDDYIGLFAVTAGLNIDKKVQQFEQAQDDYSAIMLKALADRLAESFAERLHERIRTEFWGYAAAEQLSHNELINEKYVGIRPAPGYPACPDHLVKQAMFSLMHCDEIDMQLTESLAMLPAASVSGFYLAHPDSTYFSVGKIGTDQLDDYARRTGLSITDAQRALAASL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP018150
EMBL· GenBank· DDBJ
BBE10367.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
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