A0AAD0KTH4 · A0AAD0KTH4_MYCLR
- Protein5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- GenemetE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids760 (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 = L-methionine + tetrahydropteroyltri-L-glutamate
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 | 24-27 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: RELK | ||||||
Binding site | 27 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 118 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 123 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 437-439 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: IGS | ||||||
Binding site | 437-439 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: IGS | ||||||
Binding site | 490 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 490 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 521-522 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 567 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 605 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 605 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 611 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 647 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 647 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 649 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 649 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 662 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 671 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 671 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Active site | 700 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 732 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 732 | 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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium
Accessions
- Primary accessionA0AAD0KTH4
Proteomes
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 12-315 | Cobalamin-independent methionine synthase MetE N-terminal | ||||
Sequence: ATVTGSPRIGPRRELKRATEGYWAKRTSRSELESVASTLRRDMWSDLAAAGLDSVPVNTFSYYDQMLDTAFMLGALPARVAQVSDDLDQYFALARGNNDIKPLEMTKWFDTNYHYLVPEIEPATTFSLNPGKILGELKEALEQRIPSRPVIIGPVTFLLLSKGINGGGAPIQRLEELVGIYCTLLSLLAENGARWVQFDEPALVTDLSPDAPALAEAVYTALGSVSKRPAIYVATYFGNPGASLAGLARTPIEAIGVDFVCGADTSVAAVPELAGKTLVAGIVDGRNIWRTDLESALSKLATLL | ||||||
Domain | 432-754 | Cobalamin-independent methionine synthase MetE C-terminal/archaeal | ||||
Sequence: LPTTTIGSYPQTSAIRKARAALQDAEIDEAEYISRMKKEVADAIKLQEQLGLDVLVHGEPERNDMVQYFAEQLGGFFATQNGWVQSYGSRCVRPPILYGDVSRPHPMTIEWITYAQSLTDKPVKGMLTGPVTILAWSFVRDDQPLADTANQVALAIRDETVDLQSAGIAIIQVDEPALRELLPLRRADQDEYLCWAVKAFRLATSGVADSTQIHTHLCYSEFGEVIGAIADLDADVTSIEAARSHMEVLDDLNAVGFANSIGPGVYDIHSPRVPSTDEIAKSLRAALKAIPMQRLWVNPDCGLKTRSVDEVSASLQNMVAAAR |
Sequence similarities
Belongs to the vitamin-B12 independent methionine synthase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length760
- Mass (Da)82,235
- Last updated2024-05-29 v1
- Checksum1E92FA570B9ACC97