A0A0D2Y8Z1 · A0A0D2Y8Z1_FUSOF

Function

function

Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.

Features

Showing features for binding site, active site.

1766100200300400500600700
Type
IDPosition(s)Description
Binding site195-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI)
Binding site1205-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI)
Binding site440-442L-homocysteine (UniProtKB | ChEBI)
Binding site440-442L-methionine (UniProtKB | ChEBI)
Binding site493L-methionine (UniProtKB | ChEBI)
Binding site524-5255-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI)
Binding site5705-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI)
Binding site608L-homocysteine (UniProtKB | ChEBI)
Binding site608L-methionine (UniProtKB | ChEBI)
Binding site651Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site653Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site662Zn2+ 2 (UniProtKB | ChEBI)
Binding site675Zn2+ 1 (UniProtKB | ChEBI); catalytic
Active site704Proton donor
Binding site736Zn2+ 1 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Molecular Function5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
Molecular Functionzinc ion binding
Biological ProcessL-methionine biosynthetic process from homoserine via O-acetyl-L-homoserine and cystathionine
Biological Processmethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
  • EC number

Gene names

    • Name
      28954061
    • ORF names
      FOXB_12227

Organism names

Accessions

  • Primary accession
    A0A0D2Y8Z1
  • Secondary accessions
    • F9G0P5

Proteomes

Organism-specific databases

PTM/Processing

Proteomic databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain4-317Cobalamin-independent methionine synthase MetE N-terminal
Region385-420Disordered
Compositional bias389-419Basic and acidic residues
Domain435-758Cobalamin-independent methionine synthase MetE C-terminal/archaeal

Sequence similarities

Belongs to the vitamin-B12 independent methionine synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    766
  • Mass (Da)
    86,552
  • Last updated
    2015-04-29 v1
  • MD5 Checksum
    E891FDFD19C55C2B02DF888F2F6C5D40
MVQSAILGFPRMGVNRDLKKATEAYWGGKISQSDLLAEAKRLRLAHWKIQQDAGVDIIPSNDFALYDQVLHQIQDFGAVPERYTKDGLDPIDQYFAMGRGHQKEGVDVPSLEMVKWFDSNYHYVKPTLQDNQTFKLTDSPKAVAEFKEAKEAGINTRPVLVGPVSFLHLGKADRGQSVEPIDLLEKLLPVYEQILTQLKEAGAETVQIDEPVLVFDLPQKTKAAFKPAYEKFASLGDKIPKIVFTTYFGDIVHNLDLLPKDVYGVHIDLVRNPEQLEKVLGAIGPNTILSAGVVDGRNIWKTNLKRAIETVETAIQKLGKDRVIAATSSSLLHTPHTLASEKKLDPEIADWFSFATEKASEIALIAKAVTEGPASVREQLEANAKSIKARADSPRTNDPQVKERQSKVTQKDYERKSEFTTRISQQQKKLNLPLFPTTTIGSFPQTKEIRVQRNKFTKGEITAEEYDRFIEKEIEENIKIQEELDLDVFVHGEPERNDMVQFFGERFQGYAFTTHAWVQSYGSRCVRPPIIVGDISRPQPMTVKESKYAVSVSKKPMKGMLTGPVTCLRWSFPRDDVHQSVQAEQLALALRDEVVDLEKAGIDVIQVDEPALREGLPLRSGEERDAYLKWAVQAFRLSTAGVEDATQIHSHFCYSEFQDFFHAIAALDADVLSIENSKSDAKLLRVFVDSEYPRHIGPGVYDIHSPRVPSEQEIKDRIEEMLQFLKPEQLWIDPDCGLKTRQWKETKEALANMVNAAKYFRAKYAK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias389-419Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AFQF01003011
EMBL· GenBank· DDBJ
EGU77267.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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