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A0A2Z5WGS8 · A0A2Z5WGS8_KOMEU

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 site225Zn2+ (UniProtKB | ChEBI)
Binding site291Zn2+ (UniProtKB | ChEBI)
Binding site292Zn2+ (UniProtKB | ChEBI)
Binding site734-738methylcob(III)alamin (UniProtKB | ChEBI)
Binding site737Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site782methylcob(III)alamin (UniProtKB | ChEBI)
Binding site840methylcob(III)alamin (UniProtKB | ChEBI)
Binding site1112S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1166-1167S-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

    • Name
      metH

Organism names

Accessions

  • Primary accession
    A0A2Z5WGS8

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-306Hcy-binding
Domain346-602Pterin-binding
Domain631-724B12-binding N-terminal
Domain724-861B12-binding
Domain885-1169AdoMet 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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,169
  • Mass (Da)
    128,638
  • Last updated
    2018-10-10 v1
  • MD5 Checksum
    1C3EF81D42496B3A48DBF619A3F5686D
MTTRPHLLDALRDQVLLCDGGMGSRVQLLDLEVERDYWGQENCTEILNLSRPELVREIHRGYFEAGADMVETNSFGGSPITLAEFGLADRAREINRTAGHLAREAAETFADGRHRYVVGSIGPGTKLPSLGNIDYDTLEAGLTEQCRGLIEGGVDCFLIETCQDTLQIKAAVNGAKIARAEMGVDTPIFVQVTVETTGTLLVGPDIAAAATVINALDVPLMGLNCATGPQEMAEHVRWLSENWPGLISVQPNAGLPELVNGTTHYPLTPAEMASWVERFITEDGLNLIGGCCGTSTPHTQALDQMLRKRAEGTGRIRPAPVPRRPVWIPSVASLYSQVPLRQENSYFSIGERCNANGSKKWRQLQEAGDWDGCVALGREQVAEGSNALDICTAFVGRDEMREMNAVVTRFTSSVNAPLVIDSTETPVIEAALKLHGGKPIINSINFEDGEAIANERMLLARKFGASVIALTIDEAGMAKTAEDKLRIATRLVEFACEKHGLPQSDLMIDPLTFTIGTGTEDDRKLGEWTLEGIRLIRERFPDIQIVLGLSNISFGLNPAARAVLNSVFLDHAVRAGMTAAIVHVSKIRPLHLIPADEVKVAEDLIFDRRAEGYDPLQRILEIFADRKAADAVKKTRAETAPERLKDRIVDGDRKGLEDDLAEAMRDMAPLDIINTVLLDGMKVVGELFGAGKMQLPFVLQSAETMKAAVAWLEPHMERTEGQARGTMVLATVKGDVHDIGKNLVDIILTNNGYQVINLGIKVPVADMIAAAREHRADAIGMSGLLVKSTVIMRENLEEMQRQGLDVPVMLGGAALTRNYVEEDCTAAYGEAGRVAYARDAFDGLSLMDKVVQGEFDTYLAAIQSRRAGKASRSNRTQDIEDAATRGFGPVDKVAARARREKLTADEPVLTPPFWGPRVLEATPEAVLPFLNERSLYQFQWGFRKQGRSLDDFMVWARKELRPVLRHMLALCAEQDILHPKASYGYWKAAGEGNDLVLFGEDGATEVARFTLPRQPRADGACIADFVRDIDDARRDVIGLQVVTVGQDASDRAREWFEADRYKDYLYLHGLSVEMAEAMAEYTHKRMRAEMGFAAEDDRDMAKLLQQGYRGSRYSFGYPACPRLEEQEPILKLLDAQKIGVSLTDGFQLHPEQSTSALVIFNPHAKYFSI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LC202824
EMBL· GenBank· DDBJ
BBB89266.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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