A6TGK9 · METE_KLEP7
- Protein5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- GenemetE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids754 (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
Note: Binds 1 zinc ion 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 | 17-20 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: RELK | ||||||
Binding site | 117 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 431-433 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: IGS | ||||||
Binding site | 431-433 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: IGS | ||||||
Binding site | 484 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 484 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 515-516 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 561 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 599 | L-homocysteine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 599 | L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 605 | 5-methyltetrahydropteroyltri-L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 641 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 643 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 665 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Active site | 694 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 726 | 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 > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Klebsiella
Accessions
- Primary accessionA6TGK9
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000017249 | 1-754 | 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase | |||
Sequence: MTIINHTLGFPRVGLRRELKKAQESYWAGNATREELLAVGRELRARHWEQQKQAGVDLLPVGDFAWYDHVLTTSLLLGNVPARHQNKDGSIDIDTLFRIGRGRAPTGEPAAAAEMTKWFNTNYHYMVPEFVKGQQFKLSWTQLLDEVDEALALGHKIKPVLLGPVTYLWLGKVKGEPFDRLTLLNTILPVYQQVLAELAKRGIDWVQIDEPALVLELPPAWLEAFQPAYDALQGQVKLLLTTYFEGVSDNLATIAALPVQGLHVDLVHGKDDVAELHNRLPADWLLSAGLINGRNVWRADLTEKYAQIKDLVGKRELWVASSCSLLHSPIDLSVETRLDAEVKSWFAFALQKCGELALLRDALNSGDTAAITEWSAPIQARRHSTRVHNAEVEKRLAAITAQDSQRASPYEVRAQAQRQRFNLPKWPTTTIGSFPQTTEIRGLRLDFKKGNLDASHYRTGIAEHIKQAIVEQERLGLDVLVHGEAERNDMVEYFGEHLDGFIFTQNGWVQSYGSRCVKPPVVIGDVSRPQAITVDWAKYAQSLTAKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVADLEAAGIGIIQIDEPALREGLPLKRSDWDAYLQWGVEAFRLNAAVAKDDTQIHTHMCYCEFNDIMDSIAALDADVITIETSRSDMELLESFEAFEYPNEIGPGVYDIHSPNVPSVEWIEALLKKAAQRIPVERLWVNPDCGLKTRGWPETRAALANMVQAARNLRQSA |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length754
- Mass (Da)84,504
- Last updated2007-08-21 v1
- ChecksumA2A602DD35DC090F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000647 EMBL· GenBank· DDBJ | ABR79693.1 EMBL· GenBank· DDBJ | Genomic DNA |