A0A4P7P321 · A0A4P7P321_STAAU
- Protein5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- GenemetE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids742 (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) | ||||
Sequence: REWK | ||||||
Binding site | 21 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 112 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 117 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 420-422 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: IGS | ||||||
Binding site | 420-422 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: IGS | ||||||
Binding site | 473 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 473 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 550 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 588 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 588 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 594 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 630 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 630 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 632 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 632 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 641 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 645 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 654 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 654 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Active site | 683 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 715 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 715 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C |
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
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionA0A4P7P321
Proteomes
Structure
Family & Domains
Features
Showing features for domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-309 | Cobalamin-independent methionine synthase MetE N-terminal | ||||
Sequence: TSNLGFPRLGRKREWKKAIESYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFSLYDHILDTSLLFNIIPERFQGRTIDDDLLFDIARGNKDHVASALIKWFNTNYHYIVPEWDNVEPKVSRNVLLDRFKYAQSLNVNAHPVIVGPITFVKLSKGGHQTFEEKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTDDSESYENITREAYDYFEKAGVAKKLVIQTYFERAHLKFLSSLPVGGLGLDFVHDNGYNLKQIEAGDFDKSKTLYAGIIDGRNVWASDIEAKKVLIDKLLAH | ||||||
Coiled coil | 341-379 | |||||
Sequence: LSFATEKLDELDALRRLLNQNDSVKYDKLKARYERFQNQ | ||||||
Domain | 415-737 | Cobalamin-independent methionine synthase MetE C-terminal/archaeal | ||||
Sequence: LPTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIGLDVLVHGEFERNDMVEFFGEKLQGFLVTKFGWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPVTILNWSFERVDLPRKVVQDQIALAINEEVLALEAAGIKVIQVDEPALREGLPLRSEYHEQYLKDAVLSFKLATSSVRDETQIHTHMCYSQFGQIIHAIHDLDADVISIETSRSHGDLIKDFEDINYDLGIGLGVYDIHSPRIPTKEEITTAINRSLQQIDRSLFWVNPDCGLKTRKEEEVKDALTVLVNAVK |
Sequence similarities
Belongs to the vitamin-B12 independent methionine synthase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length742
- Mass (Da)85,042
- Last updated2019-07-31 v1
- Checksum3FC30B4DB1E463D2
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |