A0A292Z069 · A0A292Z069_9PSEU

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 site235Zn2+ (UniProtKB | ChEBI)
Binding site301Zn2+ (UniProtKB | ChEBI)
Binding site302Zn2+ (UniProtKB | ChEBI)
Binding site742-746methylcob(III)alamin (UniProtKB | ChEBI)
Binding site745Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site790methylcob(III)alamin (UniProtKB | ChEBI)
Binding site848methylcob(III)alamin (UniProtKB | ChEBI)
Binding site941S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1136S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site1190-1191S-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
      TOK_5062

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • N23
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Pseudonocardia

Accessions

  • Primary accession
    A0A292Z069

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain14-316Hcy-binding
Domain347-610Pterin-binding
Domain639-732B12-binding N-terminal
Domain732-869B12-binding
Region862-913Disordered
Compositional bias863-896Basic and acidic residues
Domain894-1194AdoMet 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
    1,194
  • Mass (Da)
    129,874
  • Last updated
    2017-12-20 v1
  • Checksum
    15ED32DA319BF443
MPAQNPNRLPDGHDTSLLHTLAERVVVADGAMGTMLQDADLTLDDFAGLEGCNEILNDTRPDVVRHIHTAYLEAGADAVETNTFGANLPNLAEYDIPERIRELAEKGARLARQAADEASTADRPRYVLGSVGPGTKLPTLGHESFARLRDAYTECGIGLLAGGADAFVVETCQDLLQVKAAVLGVQRAMVAEGRRIPIITQVTVETTGTMLLGSEIGAALTALEPLGIDLIGLNCATGPAEMSEHLRTLSKHARIPLSVMPNAGLPQLGPNGAVYPLSAEELAEALSTFVRDYGLRLVGGCCGTTPAHVRAVADAVAAVTPAQRDPRPEPGVSSLYAPVPFRQDTSVLMVGERTNANGSKAFRDAMIEERWDDCVAIAREQTRDGAHMIDLNIDYVGRDGVADMAEMAGRLATASTLPIMIDSTEPEVLQAGLERLGGRCIVNSVNYEDGDGPESRFQRAMALVREHGAAVVALCIDEEGQARTADWKVRVADRLITDLTTNHGMHVEDIVVDTLTFPITTGQEEVRRDALETIEAIRDLKRLHPTVQTTLGISNVSFGLNAAARQVLNSVFLHECVNAGLDTAIVHASKILPMAKIADEQRSVALDLVYDRRREGYDPLSRFMELFEGVTASSAKAGRAEQLAALPLFERLERRIVDGERVGLEADLDSGLDERPALEIINDTLLAGMKTVGELFGSGQMQLPFVLQSAEVMKAAVAHLEPHMEKTDSDGKGTIVLATVKGDVHDIGKNLVDIILSNNGYTVVNLGIKQPISTILTAAEEHRAHAVGMSGLLVKSTVIMKENLQEMNSRGVAKKLPVLLGGAALTRSYVENDLSDVYDGRVSYARDAFEGLRLMDATMARARGDAPEVDPEEEAKAAERRARHERSKRIAAKRKAAEAEAAGPLPERSDVALDNPLPTPPFWGTRVVKGIAVSEYAGMVDERALFLGQWGLRGAKGGSGPSYEELVETEGRPRVRYWLDRLATEGVLANAAVVYGYFPAVAVRDELVVLTEPRADAPERYRFAFPRQRRDRNLCLADFWRPRDVAITNSEVDVLPLQLVTMGRPIADYANELFAKNAYRDYLEVHGLSVQLTEALAEFWHKRVREELTWSTGRNLAEEDPENVEEFFKLGYRGARYSLGYGACPNLEDRTKIVDMLEPGRIGVGLSEELQLHPEQSTDALVAHHPEAKYFNAG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias863-896Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BEGX01000061
EMBL· GenBank· DDBJ
GAY10701.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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