A0AA96XS88 · A0AA96XS88_9PSED

  • Protein
    Methionine synthase
  • Gene
    metH
  • 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 site250Zn2+ (UniProtKB | ChEBI)
Binding site313Zn2+ (UniProtKB | ChEBI)
Binding site314Zn2+ (UniProtKB | ChEBI)
Binding site695methylcob(III)alamin (UniProtKB | ChEBI)
Binding site758-762methylcob(III)alamin (UniProtKB | ChEBI)
Binding site761Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site806methylcob(III)alamin (UniProtKB | ChEBI)
Binding site810methylcob(III)alamin (UniProtKB | ChEBI)
Binding site863methylcob(III)alamin (UniProtKB | ChEBI)
Binding site950S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1138S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1199-1200S-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
      QOM08_17815

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • P105
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0AA96XS88

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain8-328Hcy-binding
Domain359-620Pterin-binding
Domain651-745B12-binding N-terminal
Domain748-884B12-binding
Domain900-1236AdoMet 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
    1,236
  • Mass (Da)
    135,510
  • Last updated
    2024-03-27 v1
  • Checksum
    36E0F6B4F3E58757
MSDRSARLYLLQQALKERILILDGGMGTMIQSYKLEEQDYRGKRFADWPSDVKGNNDLLVLSRPDVIGAIEKAYLDAGADILETNTFNATQVSQADYGMQGLAYELNLEGARLARKVADAKTLETPDKPRFVAGVLGPTSRTCSLSPDVNNPGYRNVTFDELVENYTEATKGLIEGGADLILIETIFDTLNAKAAIFAVQGVYEELGVELPIMISGTITDASGRTLSGQTTEAFWNSVAHAKPISVGLNCALGASELRPYLEELSNKASTHVSAHPNAGLPNEFGEYDELPVDTAKVIEEFAQSGFLNIVGGCCGTTPAHIEAIAKAVAGYAPRQIPEIPRACRLSGLEPFTIDRNSLFVNVGERTNITGSAKFARLIREDNYTEALEVALQQVEAGAQVIDINMDEGMLDSKKAMVTFLNLIAGEPDISRVPIMIDSSKWEVIEAGLKCIQGKGIVNSISMKEGVEQFIHHAKLCKRYGAAVVVMAFDEAGQADTEARKKEICKRSYDILVNEVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFINACAYIRDELPYALTSGGVSNVSFSFRGNNPVREAIHSVFLLYAIRSGLTMGIVNAGQLEIYDQIPVELRDAVEDVILNRTPEGTDALLAIADKYKGDGSVKEAETEEWRGWEVNKRLEHALVKGITTHIVEDTEESRLSFARPIEVIEGPLMAGMNIVGDLFGAGKMFLPQVVKSARVMKQAVAHLIPFIEAEKGDKPEAKGKILMATVKGDVHDIGKNIVGVVLGCNGYDVVDLGVMVPAEKILQVAKEQKCDIIGLSGLITPSLDEMVHVAREMQRQDFHLPLMIGGATTSKAHTAVKIEPKYSNDAVIYVTDASRAVGVATQLLSKELKPAFVEKTRLEYIDVRERTANRSARTERLSYPAAVAKKPQFDWSSYQPVKPTFTGAKVLDNIDLNVLAEYIDWTPFFISWDLAGKYPRILTDEVVGEAATALYADARAMLRKLIDEKLISARAVFGFWPANQVHDDDLEVYGEDGKPLARLHHLRQQIIKTDGKPNFSLADFVAPKDSGVTDYVGGFITTAGIGAEEVAKAYQEAGDDYNSIMVKALADRLAEACAEWLHQQVRKEHWGYAKDESLDNDALIKEQYTGIRPAPGYPACPDHTEKATLFRLLDPEASELKAGRSGVFLTEHYAMFPAAAVSGWYFAHPHAQYFAVGKIDKDQVQSYTARKGQDLSVTERWLAPNLGYDN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP126693
EMBL· GenBank· DDBJ
WNZ76577.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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