A0A2Z6EY78 · A0A2Z6EY78_9BURK
- ProteinMethionine synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids928 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
Catalytic activity
- (6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine
Cofactor
Protein has several cofactor binding sites:
Pathway
Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 379 | methylcob(III)alamin (UniProtKB | ChEBI) | |||
Binding site | 448-452 | methylcob(III)alamin (UniProtKB | ChEBI) | |||
Binding site | 451 | Co (UniProtKB | ChEBI) of methylcob(III)alamin (UniProtKB | ChEBI); axial binding residue | |||
Binding site | 496 | methylcob(III)alamin (UniProtKB | ChEBI) | |||
Binding site | 500 | methylcob(III)alamin (UniProtKB | ChEBI) | |||
Binding site | 556 | methylcob(III)alamin (UniProtKB | ChEBI) | |||
Binding site | 642 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 841 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 895-896 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | cobalamin binding | |
Molecular Function | methionine synthase activity | |
Molecular Function | zinc ion binding | |
Biological Process | homocysteine metabolic process | |
Biological Process | methylation | |
Biological Process | tetrahydrofolate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMethionine synthase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Mycoavidus
Accessions
- Primary accessionA0A2Z6EY78
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Domain
Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin.
Sequence similarities
Belongs to the vitamin-B12 dependent methionine synthase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length928
- Mass (Da)102,510
- Last updated2018-10-10 v1
- MD5 Checksum75EE7679D43A8BD50C0378F3E5D81F6A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP018150 EMBL· GenBank· DDBJ | BBE10367.1 EMBL· GenBank· DDBJ | Genomic DNA |