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A0A2T3KA05 · A0A2T3KA05_9GAMM

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site247Zn2+ (UniProtKB | ChEBI)
Binding site310Zn2+ (UniProtKB | ChEBI)
Binding site311Zn2+ (UniProtKB | ChEBI)
Binding site693methylcob(III)alamin (UniProtKB | ChEBI)
Binding site755-759methylcob(III)alamin (UniProtKB | ChEBI)
Binding site758Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site803methylcob(III)alamin (UniProtKB | ChEBI)
Binding site807methylcob(III)alamin (UniProtKB | ChEBI)
Binding site859methylcob(III)alamin (UniProtKB | ChEBI)
Binding site946S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1134S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1189-1190S-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
      C9J27_25950

Organism names

  • Taxonomic identifier
  • Strain
    • FS-7.2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Vibrionales > Vibrionaceae > Photobacterium

Accessions

  • Primary accession
    A0A2T3KA05

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-325Hcy-binding
Domain356-617Pterin-binding
Domain649-743B12-binding N-terminal
Domain745-880B12-binding
Domain896-1222AdoMet 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
    1,222
  • Mass (Da)
    135,118
  • Last updated
    2018-07-18 v1
  • MD5 Checksum
    D7C76BD8FD586C61ACDF5791F7053448
MLKSKDVLHKRLEQQILIIDGGMGTMIQGYKLDEQDYRGQRFSDWHADLKGNNDLLVLTQPQLIKDIHLEYLEAGADILETNTFNATTIAMADYDMESLSAEINFAAATLAREAADEWTAQTPDKPRFVAGVLGPTNRTCSISPDVNDPGFRNVTFDQLVIAYSESTHALIKGGVDIILIETIFDTLNAKACAFAVTGVFEELGYELPVMISGTITDASGRTLSGQTTEAFYNSLRHVKPISFGLNCALGPDELRQYVAELSRISECAVSAHPNAGLPNAFGEYDLEAEEMAEHIKEWAQQGFLNLVGGCCGTTPEHIRQMYQVTKNIKPRLLPEIKIACRLSGLEPLIIEADSLFVNVGERTNVTGSARFKRLIKDELYDAALEVARQQVEAGAQIIDINMDEGMLDAKAAMVRFLNLCATEPEIAKVPIMVDSSKWEIIEAGLKCVQGKPIVNSISLKEGKENFIAQAKLLRRYGAAVIVMAFDEVGQADTRERKIEICTNAYHILVDEVGFPAEDIIFDPNIFAVATGIEEHNNYAVDFIEAVADIKRTLPHAMVSGGVSNVSFSFRGNNPVREAIHAVFLYYCFKNGMDMGIVNAGQLAIYDDLSDELRNAVEDVVLNRRDDSTDRLLDIAANYRDSGAVEEDRSQQEWRSWSVEKRLEHALVKGITEFIIEDTEQARVNATKPLDVIEGPLMAGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAHLEPYINAEKQVGYTNGKILLATVKGDVHDIGKNIVGVVLQCNNYEIIDLGVMVSCDQILQVAQEQNVDIIGLSGLITPSLDEMVHVAKEMQRRGFDIPLLIGGATTSKAHTAVKIEQNYQQPVVYVSNASRAVGVCSALLSEQQKPAFVERLTAEYDVVREQHARKKPRTAPITLDQARANAVALDWVNYTPPAPKQAGVHTFTDFPIAELRKYIDWTPFFMTWSLSGKYPTILRHEVVGVEATKLFEDANKILDDIERTGMIKANGVCGLFPANNIGDDVEVYTDETRTEVLTVLHGLRQQTKKPKGPNYCLSDYIAPKESGKADWIGAFAVTGGIGEYEIAAQFKAQGDDYNAIMIQAVADRLAEAFAECMHQIVRKQIWGYAADEDLGNDDLIREKYQGIRPAPGYAACPEHTEKGAIWQLLDAEANIGMVLTESYAMWPGAAVSGWYFSHPDARYFAVAQIQHDQLASYADRKGWNMIEAEKWLGPNL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PYNF01000061
EMBL· GenBank· DDBJ
PSU87846.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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