A0AAE5V858 · A0AAE5V858_STAEP

  • Protein
    5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
  • Gene
    metE
  • 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 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
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 )

Note: Binds 1 zinc ion per subunit.
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.

Type
IDPosition(s)Description
Binding site18-215-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI)
Binding site215-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI)
Binding site1125-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI)
Binding site1175-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI)
Binding site420-422L-homocysteine (UniProtKB | ChEBI)
Binding site420-422L-methionine (UniProtKB | ChEBI)
Binding site473L-homocysteine (UniProtKB | ChEBI)
Binding site473L-methionine (UniProtKB | ChEBI)
Binding site5505-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI)
Binding site588L-homocysteine (UniProtKB | ChEBI)
Binding site588L-methionine (UniProtKB | ChEBI)
Binding site5945-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI)
Binding site630Zn2+ (UniProtKB | ChEBI); catalytic
Binding site630Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site632Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site632Zn2+ (UniProtKB | ChEBI); catalytic
Binding site641Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site645Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site654Zn2+ (UniProtKB | ChEBI); catalytic
Binding site654Zn2+ 1 (UniProtKB | ChEBI); catalytic
Active site683Proton donor
Binding site715Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site715Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Molecular Function5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
Molecular Functionzinc ion binding
Biological Processmethionine biosynthetic process
Biological Processmethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
  • EC number
  • Alternative names
    • Cobalamin-independent methionine synthase
    • Methionine synthase, vitamin-B12 independent isozyme

Gene names

    • Name
      metE
    • ORF names
      CTJ08_02565

Organism names

  • Taxonomic identifier
  • Strain
    • SCH-17
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Accessions

  • Primary accession
    A0AAE5V858

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain6-310Cobalamin-independent methionine synthase MetE N-terminal
Domain415-737Cobalamin-independent methionine synthase MetE C-terminal/archaeal

Sequence similarities

Belongs to the vitamin-B12 independent methionine synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    748
  • Mass (Da)
    85,943
  • Last updated
    2024-05-29 v1
  • Checksum
    8EFB4E589A3E7404
MTTIKTSNLGFPRLGRKREWKKAIENYWAHKIDKAELDQTLTDLHKENLLLQKNYHLDSIPVGDFSLYDHILDTSLLFNIIPERFQGREVNDDLLFDIARGNKEHVASALIKWFNTNYHYIVPEWDNVEPKIEKNTLLERFKYAQSINVNAHPVIVGPITFVKLSKGGHQSFEEKVETLLPLYKEVLQSLVDAGAKYIQIDEPILVTDDSESYEDITRKAYDYFANEGLGKYLVIQTYFERVHLKFLSSLPVGGLGLDLVHDNGYNLKQIEDGDFDQSKALYAGIIDGRNVWAADIEAKKQLIETLQQHTQQLVIQPSSSLLHVPVSLDDETLDESIAEGLSFATEKLDELDALRRLFNDNDLSKYEHYKARYERFQSQSFKNLEYDFESVPTHRKSPFAKRKQLQNQRLNLPDLPTTTIGSFPQTREVRKFRADWKNNRITDAEYQEFLQNEIARWIKIQEDIGLDVLVHGEFERNDMVEFFGEKLQGFLVTKFGWVQSYGSRAVKPPVIYGDVKWTAPLTVKETVYAQSLTDKPVKGMLTGPVTILNWSFERVDVPRKVVQDQIALAIDEEVLALEEAGIKVIQVDEPALREGLPLRSEYHEQYLEDAVHSFKLATSSVHDETQIHTHMCYSQFGQIIHAIHDLDADVISIETSRSHGDLIQDFEDINYDLGIGLGVYDIHSPRIPTEEEITTAINRSLQQIDRSLFWVNPDCGLKTRKEDEVKDALTVLVNAVKKKRQESESTTA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PEJG01000002
EMBL· GenBank· DDBJ
PIH11207.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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