A0A2Z6GFU9 · A0A2Z6GFU9_9PROT

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 site258Zn2+ (UniProtKB | ChEBI)
Binding site323Zn2+ (UniProtKB | ChEBI)
Binding site324Zn2+ (UniProtKB | ChEBI)
Binding site704methylcob(III)alamin (UniProtKB | ChEBI)
Binding site769-773methylcob(III)alamin (UniProtKB | ChEBI)
Binding site772Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site817methylcob(III)alamin (UniProtKB | ChEBI)
Binding site821methylcob(III)alamin (UniProtKB | ChEBI)
Binding site874methylcob(III)alamin (UniProtKB | ChEBI)
Binding site961S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1151S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1206-1207S-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
      OYT1_ch2523

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • OYT1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Nitrosomonadales > Gallionellaceae > Ferriphaselus

Accessions

  • Primary accession
    A0A2Z6GFU9

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain18-338Hcy-binding
Domain369-630Pterin-binding
Domain660-754B12-binding N-terminal
Domain759-895B12-binding
Domain911-1241AdoMet 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
    1,241
  • Mass (Da)
    135,998
  • Last updated
    2018-12-05 v1
  • Checksum
    B83BB7959D326A84
MVKFPLIFSRTAAMTRTPHRIETLIQQRILILDGAMGTMIQRYKLTEADYRGTRFADWHRDLKGNNDLLVITKPEVIRAIHEEYLAAGADIIETNTFGANATTLHAYGMSSLNYELNVAGARVAREACDKYASADKPRFVAGVLGPTDKTATISPDVNDPAARNISFDQLVADYSDATRGLMDGGADTILIETIFDTLNAKAAIFAVQSVFEERGTSLPIMISGTITDASGRTLTGQVTEAFYNSLAHAKPLSIGLNCALGAEELRQYVAELSRVSNCYVSAHPNAGLPNPLAESGYDDTPENMAGHLKEWAESGFLNIIGGCCGTSPAFIKAIAETVKGIAPRKIPANPVECRLSGLEPFNIGEGSLFVNVGERANVTGSAKFKRLILEGKFDEALEVAKQQVETGAQVIDVNMDEAMLDGEAAMVKFLNLIASEPDISKVPLMIDSSKWSIIEAGLKCVQGKSIVNSISLKEGEENFIKYATLVRRYGAAAVVMAFDEAGQADTYQRKIEICQRSYDILVNKVGFPPEDIIFDPNIFAVATGIEEHNNYAVDFIEACAWIRKNLPYAKISGGVSNVSFSFRGNEPVREAIHTVFLYHAIKAGMSMGIVNAGQLGVYEELPKDLREAVEDVVLNRHPDAGEKLVTLAENFKGGGKAQVEDLEWRKGTVQERLTHALVRGITTYIVEDTEEARLQAKLPVEVIEGPLMTGMNVVGDLFGAGKMFLPQVVKSARVMKQAVAHLIPYIEAEKLRSGDTSTKGKILMATVKGDVHDIGKNIVTVVLQCNNFEVINMGVMVPCQQILDMAREHKVDIIGLSGLITPSLEEMAHVAKEMERQGFTIPLLIGGATTSRVHTAVKIEPNYPSGTVVYVTDASRAVGVCSNLLSDTLRDGYIAEIKSDYQAAREQHEGRKGKASYVSLGEARAHGFKTDWANYVPPKPAFTGVKELRDYPLSEIAQYIDWTPFFQAWELAGRYPKILKDEVVGEEATKLFADAQAMLKRIVDERWLTANAVFGLFPANSVNADDIEIYTDESRSSVAMTWHNLRQQTKKPESIPNYCLADFVAPKDSGLADYLGAFAVTTGLGIDARVAEFEKQNDDYNAILLKALADRLAEAFAELLHARVRREFWGYAADEGLDNDSLIEEKYRGIRPAPGYPACPDHTEKGALFDLLQAPQNADITLTESYAMLPTAAVSGFYFSHPKAQYFATGKVDKEQVADYAQRKGWTAEEAERWLAPVLSY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP018738
EMBL· GenBank· DDBJ
BBE52035.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp