A0A1V1V6C0 · A0A1V1V6C0_PHODP

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 site245Zn2+ (UniProtKB | ChEBI)
Binding site308Zn2+ (UniProtKB | ChEBI)
Binding site309Zn2+ (UniProtKB | ChEBI)
Binding site691methylcob(III)alamin (UniProtKB | ChEBI)
Binding site753-757methylcob(III)alamin (UniProtKB | ChEBI)
Binding site756Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site801methylcob(III)alamin (UniProtKB | ChEBI)
Binding site805methylcob(III)alamin (UniProtKB | ChEBI)
Binding site857methylcob(III)alamin (UniProtKB | ChEBI)
Binding site944S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1132S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1187-1188S-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
    • ORF names
      IC627_01560
      , PDPUS_1_02939

Organism names

Accessions

  • Primary accession
    A0A1V1V6C0

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-323Hcy-binding
Domain354-615Pterin-binding
Domain647-741B12-binding N-terminal
Domain743-878B12-binding
Domain894-1221AdoMet 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
    1,221
  • Mass (Da)
    135,256
  • Last updated
    2017-06-07 v1
  • MD5 Checksum
    44D461E208EBAB7FFEC92062B982662C
MVKGLNLLQQRLAEQILIIDGGMGTMIQGYKLTESDYRGERFANWHCDIKGNNDLLVLTQPQIITDIHQQYLAAGADILETNTFNATTIAMADYDMADLSAEINLVAAQLARQAADKWSTPDKPRFVAGVLGPTNRTCSISPDVNDPGFRNITFDQLVIAYSESTRALIKGGVDLILIETIFDTLNAKACAFAVESVFDELGYQLPIMISGTITDASGRTLSGQTTEAFYNALRHVKPISFGLNCALGPDELRQYVAELSRLAECSVSAHPNAGLPNAFGEYDLEPEEMAEHIAEWAQSGFLNLVGGCCGTTPEHIRQMAAVTQNIKPRTPPSIPVACRLSGLEPLNIEKNSLFINVGERTNVTGSARFKRLIKEELYDEALEVARQQVEAGAQIIDINMDEGMLDAKAAMVRFLNLCATEPEIAKVPIMVDSSKWEVIEAGLQCVQGKPIVNSISLKEGKAKFIEQAKLIQRYGAAVIVMAFDEEGQADTRERKVEICTQAYRILVDEVGFAPEDIIFDPNIFAVATGIEEHNNYAVDFIEAVGEIKATLPHAMISGGVSNVSFSFRGNDPVREAIHAVFLYYCFQKGMDMGIVNAGQLAIYDDLPQELRQAVEDVVLNLREDSTERLLDIAEKYRGTGKVEEDRSAQEWRSWPIEKRLEHALVKGITEFIVEDTEQARVLAAKPLEVIEGPLMAGMNVVGDLFGEGRMFLPQVVKSARVMKQAVAYLEPFINAEKQAGSSNGKILLATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVSCEQILKVAKEEQVDIVGLSGLITPSLDEMVHVAKEMERQGFELPLLIGGATTSKAHTAVKIEQNYHAPVVYVSNASRAVGVCSVLLSETQREDFIARLDKEYEVVRDQHSRKKPRSAPITLEQARENCAHIDWQSYQPPQPKSKGIHTIIDCSVATLRQYIDWTPFFITWSLSGKYPTILRHEVVGEEATKLFNEANVLLDKIEQEGIIKANGVCGFFPANSVGDDIEVYTDESRQHVLTRLHHLRQQTAKPKGANYCLSDFIAPKSSRHPDWIGAFAVTGGIGESELAAQFKAQGDDYNAILIQAVADRLAEAFAEYLHQQVRTQLWGYSPNEDLSNDDLIREKYQGIRPAPGYPACPEHTEKGTLWQLLDVEERTGMSLTESYAMWPGASVSGWYFSHPEARYFAVAQIQQDQALDYANRKGWNEREIEKWLGPNLN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP018045
EMBL· GenBank· DDBJ
BAX54313.1
EMBL· GenBank· DDBJ
Genomic DNA
CP061854
EMBL· GenBank· DDBJ
QOD56796.1
EMBL· GenBank· DDBJ
Genomic DNA

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