D5WYV1 · D5WYV1_THIK1
- Protein5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- GenemetE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids793 (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 | 16-19 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: RELK | ||||||
Binding site | 19 | 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 | 440-442 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: IGS | ||||||
Binding site | 440-442 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: IGS | ||||||
Binding site | 493 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 493 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 524-525 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 570 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 608 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 608 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 614 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 650 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 650 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 652 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 652 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 674 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 674 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Active site | 703 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 735 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 735 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Thiomonas
Accessions
- Primary accessionD5WYV1
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-313 | Cobalamin-independent methionine synthase MetE N-terminal | ||||
Sequence: THILGYPRIGPQRELKFALENFWQGKSSASELQATAAQLRAANWAKQRDAGLHFAAVGDFALYDHMLDTAALLGALPARFGFDARTLGLEQYFALARGNAAQPAMEMTKWFDTNYHYLVPELDSATTFDGGFDALFDRVREAQEAGHAPKPVLVGPLTFLWLSKSHQPGFDRLSLAPALSRAYARVLARLAELGVEWVQLDEPALTLDLDTSWRDLLPTLYAALPVQAGALRPKLLLSTYFESISFAPATLAGLPVDGVHLDLVRAPQQIDLWREALPAQWVLSAGIIDGRNVWRSDLAAALRVLRPLHA | ||||||
Domain | 435-757 | Cobalamin-independent methionine synthase MetE C-terminal/archaeal | ||||
Sequence: LPTTTIGSFPQTAEIRAGRAAWRRGELRHTDYLQKMREEIAAVIRKQEDIGLDVLVHGEAERNDMVEFFGEQLWGYTFSAGGWVQSYGSRCVKPPIIWGDVWRPEPMTVDTARHAQALTPRPVKGMLTGPITLLQWSFVRDDLPRDQVALQLALAVRDEVSDLQNAGIAIIQIDEPAFREGLPLKRDNWPQYLSWAVRAFGVSAGVARDDTQIHTHMCYSEFNDILPSIAAMDADVITIETSRSNMELLDGFGAFAYPNDIGPGVYDIHSPRVPSAADMARLLRRAAQLIAPERLWVNPDCGLKTRAWPETEAALRHMVQAAR |
Sequence similarities
Belongs to the vitamin-B12 independent methionine synthase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length793
- Mass (Da)87,618
- Last updated2010-07-13 v1
- ChecksumF156F57417E2AF14
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002021 EMBL· GenBank· DDBJ | ADG32278.1 EMBL· GenBank· DDBJ | Genomic DNA |