A0A2V6EH34 · A0A2V6EH34_UNCVE
- ProteinSerine hydroxymethyltransferase
- GeneglyA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids595 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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 active site, binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 8 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 14 | |||||
Sequence: R | ||||||
Active site | 122 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 301 | (6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 305-307 | (6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: GHL | ||||||
Site | 409 | Plays an important role in substrate specificity | ||||
Sequence: H | ||||||
Binding site | 424 | (6S)-5,6,7,8-tetrahydrofolate (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | cobalt ion binding | |
Molecular Function | glycine hydroxymethyltransferase activity | |
Molecular Function | methyltransferase activity | |
Molecular Function | protein tyrosine phosphatase 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 | protein dephosphorylation | |
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
- Taxonomic lineageBacteria > Verrucomicrobiota
Accessions
- Primary accessionA0A2V6EH34
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 410 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-151 | Phosphotyrosine protein phosphatase I | ||||
Sequence: KSVLFVCTGNVCRSPIAEGLFRRLLGNRKDIEVASAGVHAVRGQPPSSHAIEVCAEEGAEISNLRSQPLTGALVERATHIFAMTGAHVEAIQMLFPNAADKTFLLREFEEAGATCWRDVSDPIGLGRDVYNSCAETIKNALPSVLAFVEE | ||||||
Compositional bias | 160-183 | Polar residues | ||||
Sequence: GRSGGASTYLMSDLPHSTEPSLSA | ||||||
Region | 160-189 | Disordered | ||||
Sequence: GRSGGASTYLMSDLPHSTEPSLSAPSGGLR |
Sequence similarities
Belongs to the SHMT family.
Belongs to the low molecular weight phosphotyrosine protein phosphatase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length595
- Mass (Da)64,671
- Last updated2018-09-12 v1
- Checksum8C4CE1381226BA09
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 160-183 | Polar residues | ||||
Sequence: GRSGGASTYLMSDLPHSTEPSLSA |