A0A6A7XXM2 · A0A6A7XXM2_9HYPH

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 site357methylcob(III)alamin (UniProtKB | ChEBI)
Binding site424-428methylcob(III)alamin (UniProtKB | ChEBI)
Binding site427Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site472methylcob(III)alamin (UniProtKB | ChEBI)
Binding site476methylcob(III)alamin (UniProtKB | ChEBI)
Binding site529methylcob(III)alamin (UniProtKB | ChEBI)
Binding site614S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site803S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site858-859S-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
      F0357_01580

Organism names

  • Taxonomic identifier
  • Strain
    • Sp-1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Segnochrobactraceae > Segnochrobactrum

Accessions

  • Primary accession
    A0A6A7XXM2

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain21-282Pterin-binding
Domain313-407B12-binding N-terminal
Domain414-550B12-binding
Domain564-896AdoMet 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
    903
  • Mass (Da)
    99,346
  • Last updated
    2020-06-17 v1
  • Checksum
    6D5CD7EAF25E16F0
MSDPVSSEDVAVERSETRAVFINVGERTNVTGSARFRKLVKEGDYSAALDVAREQVESGAQIIDVNMDEGLLDSEKAMVTFLNLVAAEPDIARVPVMVDSSKWSVIEAGLKCLQGKGIVNSISLKEGEEAFIRQARLVKRYGAAVVVMAFDETGQADTYQRKIDICRRCYDVLTKKVGFAPEDIIFDPNIFAVATGIDEHNNYGVDFIEATRWIRRNLPGAHVSGGVSNLSFSFRGNEPVRAAMHSVFLYHAIAAGMDMGIVNAGQLSVYDDIDPELRELCEDVVLNRRSDATERLVEAAARFKGDGAAKREVDLAWRALPVEKRLEHALVNGITEFIEVDTEEARAAADRPLHVIEGPLMAGMNVVGDLFGAGKMFLPQVVKSARVMKQAVAYLMPFMEEEKQRLGLTEQSAAAKVLLATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVPTATILERARAEKVDVIGLSGLITPSLDEMCHVAAEMEREGFDVPLLIGGATTSRIHTAVKISPNYHRGQAVYVTDASRAVGVVSRLMGDREAFVGEVRTEYAVIAEGHARSQEDRRRLPLTEARAKRFKIDWSGYQPVRPRFLGPRVFRDVPLGDIVPYIDWTPFLSAWEIKGTYPLVLDDPKVGPAARNLIRDAQAMLKQLVRERWLTASGVIGFWPANADGDDIVLYTDDSRTERLTTLHTLRQQMARTTDRGNVALADFVAPVGSGVADYVGGFAVTAGIGEDAVIERFSRANDDYSKILSQSLADRLAEAFAEAMHARVRREFWGYAAGENLAPAELIAEAYQGIRPAPGYPAQPDHTEKRTLFDLLGAESEIGLKLTESYAMWPASAVSGLYFAHPQSHYFGVGRIERDQIEDYAARKGWDIAEAERWLAPILAYDPATVRTRAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VWNA01000001
EMBL· GenBank· DDBJ
MQT11384.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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