A0AAE5V858 · A0AAE5V858_STAEP
- Protein5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- GenemetE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids748 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic activity
- 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 zinc ion per subunit.
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 18-21 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | |||
Binding site | 21 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | |||
Binding site | 112 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | |||
Binding site | 117 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | |||
Binding site | 420-422 | L-homocysteine (UniProtKB | ChEBI) | |||
Binding site | 420-422 | L-methionine (UniProtKB | ChEBI) | |||
Binding site | 473 | L-homocysteine (UniProtKB | ChEBI) | |||
Binding site | 473 | L-methionine (UniProtKB | ChEBI) | |||
Binding site | 550 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | |||
Binding site | 588 | L-homocysteine (UniProtKB | ChEBI) | |||
Binding site | 588 | L-methionine (UniProtKB | ChEBI) | |||
Binding site | 594 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | |||
Binding site | 630 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 630 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 632 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 632 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 641 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 645 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 654 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 654 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Active site | 683 | Proton donor | |||
Binding site | 715 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 715 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | methionine biosynthetic process | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionA0AAE5V858
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 6-310 | Cobalamin-independent methionine synthase MetE N-terminal | |||
Domain | 415-737 | Cobalamin-independent methionine synthase MetE C-terminal/archaeal | |||
Sequence similarities
Belongs to the vitamin-B12 independent methionine synthase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length748
- Mass (Da)85,943
- Last updated2024-05-29 v1
- Checksum8EFB4E589A3E7404
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PEJG01000002 EMBL· GenBank· DDBJ | PIH11207.1 EMBL· GenBank· DDBJ | Genomic DNA |