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A0A8H9XDR1 · A0A8H9XDR1_9CAUL

  • 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.

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 site345methylcob(III)alamin (UniProtKB | ChEBI)
Binding site409-413methylcob(III)alamin (UniProtKB | ChEBI)
Binding site412Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site457methylcob(III)alamin (UniProtKB | ChEBI)
Binding site461methylcob(III)alamin (UniProtKB | ChEBI)
Binding site514methylcob(III)alamin (UniProtKB | ChEBI)
Binding site601S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site789S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site844-845S-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
      H2041_00540

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MCMED-G08
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Caulobacterales > Caulobacteraceae > Phenylobacterium

Accessions

  • Primary accession
    A0A8H9XDR1

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-266Pterin-binding
Domain301-395B12-binding N-terminal
Domain399-535B12-binding
Domain551-881AdoMet 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
    881
  • Mass (Da)
    96,650
  • Last updated
    2022-01-19 v1
  • MD5 Checksum
    CBBB8C71465B65A5B2CBC947E8DBDC45
MRPTFINIGERTNVTGSAKFRKLIVEGDFAEALSVARQQVEAGAAVIDVNMDEGLLDSKQAMVTFLNLMAAEPDIARVPVMIDSSKWEVIEAGLQCVQGKSIVNSISLKEGEEAFVRQAKACLRYGAAVVVMAFDEQGQADTAARKIEICTRAYRKLVDDIGFPPEDIIFDPNIFAVATGIEEHDNYAVDFIEATRAIKESLPGARVSGGVSNVSFSFRGNEPVRRAIHSVFLYHAIAAGMDMGIVNAGDLPVYDEIEPELREAVEDVILNRPQRTNISNTERLVELAPKYKGGKGQSKGPDLAWREGSVEERLKHALVKGITEFIEEDTEAARQQAERPLHVIEGPLMAGMDVVGDLFGSGKMFLPQVVKSARVMKQAVAYLMPFMEAEKEGKPREAAGKVLMATVKGDVHDIGKNIVGVVLQCNNYEVIDLGVMVPADRILDEAEKHNVDIIGLSGLITPSLDEMVFVASEMERRGFDIPLLIGGATTSKTHTAVKIQPAYKRGSTTYVLDASRAVSVVSGLLSPTERERIQAETAAEYERVREQYARGQTNRARASLEEARAKAFSIDWADYDPPRPHVTGLQVFEDYDLADLAAHIDWTPFFASWELVGRFPQILDDDVVGEAARSLYADAQAMLAKIVEEKWFTAKGVVGFWPANADGDDVVVYADESRVTELARFHTLRQQIAKADGKPNVALADFIAPIGTKPDWIGGFAVTAGHGEAEIAARYKAAGDDYNAILAAALADRLAEAFAEAMHRKVRTELWGFSPDEPFDIDALIAEKYQGIRPAAGYPAQPDHTEKRTLFALLDAEARVGVKLTESFAMTPASSVSGLYFAHPQSHYFGVGRIEKDQVEDYARRKGWAVTEAERWLAPILNYQP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACESE010000001
EMBL· GenBank· DDBJ
MBA4792136.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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