A0A2U2EA85 · A0A2U2EA85_MYCAV
- Protein5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- GenemetE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids756 (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 | 20-23 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: RELK | ||||||
Binding site | 23 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 114 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 119 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 433-435 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: IGS | ||||||
Binding site | 433-435 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: IGS | ||||||
Binding site | 486 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 486 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 517-518 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 563 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 601 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 601 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 607 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 643 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 643 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 645 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 645 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 658 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 667 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 667 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Active site | 696 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 728 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 728 | Zn2+ 1 (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 > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium avium complex (MAC)
Accessions
- Primary accessionA0A2U2EA85
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length756
- Mass (Da)81,633
- Last updated2018-07-18 v1
- Checksum218F5D3EC8D4ADC3