A0A1G7MZJ9 · A0A1G7MZJ9_9GAMM
- ProteinSerine hydroxymethyltransferase
- GeneglyA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids421 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic activity
- (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Cofactor
Pathway
Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1.
One-carbon metabolism; tetrahydrofolate interconversion.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 121 | (6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 125-127 | (6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: GHL | ||||||
Site | 228 | Plays an important role in substrate specificity | ||||
Sequence: H | ||||||
Binding site | 246 | (6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 355-357 | (6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: SPF |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | cobalt ion binding | |
Molecular Function | glycine hydroxymethyltransferase activity | |
Molecular Function | methyltransferase activity | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | serine binding | |
Molecular Function | zinc ion binding | |
Biological Process | folic acid metabolic process | |
Biological Process | glycine biosynthetic process from serine | |
Biological Process | L-serine catabolic process | |
Biological Process | methylation | |
Biological Process | tetrahydrofolate interconversion |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine hydroxymethyltransferase
- EC number
- Short namesSHMT ; Serine methylase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Oceanospirillales > Halomonadaceae > Onishia
Accessions
- Primary accessionA0A1G7MZJ9
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 229 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-386 | Serine hydroxymethyltransferase-like | ||||
Sequence: FDDALLEAMQKEAARQEAHIELIASENYASPRVMEAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDYAKELFGASYANVQPHSGSQANGAVFQALVKPGDTVLGMSLDAGGHLTHGAKPNFSGKHYEAIQYGLDDRGLIDYEEVARLAREHQPKMIIAGFSAYSQIIDWAKFREIADEVGAYLLVDMAHVAGLVAAGVYPTPLPHAHVVTTTTHKTLRGPRGGLILSAEGSEEIEKKLQSAVFPGGQGGPLEHVIAAKAICFKEAMEPEFKAYQQQVVKNAQVMAKVFIERGFDIVSGGTEDHLFLLSLIKQGLTGKDADAALGRAHITVNKNAVPGDPQSPFVTSGLRIGTPAVTTRGFGETECRDLATWI |
Sequence similarities
Belongs to the SHMT family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length421
- Mass (Da)45,411
- Last updated2017-11-22 v1
- ChecksumEE0A904637F7A9EB
Keywords
- Technical term