A0A4P7P321 · A0A4P7P321_STAAU

  • 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.

TypeIDPosition(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+ 1 (UniProtKB | ChEBI); catalytic
Binding site654Zn2+ (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
      G0Z31_05045
      , GQX52_00745
      , M1K003_0398
      , SAMEA4552975_01416
      , SAMEA70153168_00656

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • M1K003
    • UP89
    • UP127
    • A13
    • MOS114
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Accessions

  • Primary accession
    A0A4P7P321

Proteomes

Family & Domains

Features

Showing features for domain, coiled coil.

TypeIDPosition(s)Description
Domain6-309Cobalamin-independent methionine synthase MetE N-terminal
Coiled coil341-379
Domain415-737Cobalamin-independent methionine synthase MetE C-terminal/archaeal

Sequence similarities

Belongs to the vitamin-B12 independent methionine synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    742
  • Mass (Da)
    85,042
  • Last updated
    2019-07-31 v1
  • Checksum
    3FC30B4DB1E463D2
MTTIKTSNLGFPRLGRKREWKKAIESYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFSLYDHILDTSLLFNIIPERFQGRTIDDDLLFDIARGNKDHVASALIKWFNTNYHYIVPEWDNVEPKVSRNVLLDRFKYAQSLNVNAHPVIVGPITFVKLSKGGHQTFEEKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTDDSESYENITREAYDYFEKAGVAKKLVIQTYFERAHLKFLSSLPVGGLGLDFVHDNGYNLKQIEAGDFDKSKTLYAGIIDGRNVWASDIEAKKVLIDKLLAHTNELVIQPSSSLLHVPVSLDDETLDTSVGEGLSFATEKLDELDALRRLLNQNDSVKYDKLKARYERFQNQSFKNLDYDFESVRTSRQSPFAQRIEQQQKRLNLPDLPTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIGLDVLVHGEFERNDMVEFFGEKLQGFLVTKFGWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPVTILNWSFERVDLPRKVVQDQIALAINEEVLALEAAGIKVIQVDEPALREGLPLRSEYHEQYLKDAVLSFKLATSSVRDETQIHTHMCYSQFGQIIHAIHDLDADVISIETSRSHGDLIKDFEDINYDLGIGLGVYDIHSPRIPTKEEITTAINRSLQQIDRSLFWVNPDCGLKTRKEEEVKDALTVLVNAVKAKRQE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAIHOM010000002
EMBL· GenBank· DDBJ
CAC7001092.1
EMBL· GenBank· DDBJ
Genomic DNA
CAIIGN010000002
EMBL· GenBank· DDBJ
CAC8219814.1
EMBL· GenBank· DDBJ
Genomic DNA
BDVT01000002
EMBL· GenBank· DDBJ
GBV19426.1
EMBL· GenBank· DDBJ
Genomic DNA
JAAJIY010000011
EMBL· GenBank· DDBJ
NGK20883.1
EMBL· GenBank· DDBJ
Genomic DNA
JAANDN010000003
EMBL· GenBank· DDBJ
NUY67197.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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