P33018 · SFGH2_ECOLI
- ProteinS-formylglutathione hydrolase YeiG
- GeneyeiG
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids278 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against alpha-naphthyl acetate, lactoylglutathione, palmitoyl-CoA and several pNP-esters of short chain fatty acids.
Catalytic activity
- H2O + S-formylglutathione = formate + glutathione + H+
Activity regulation
Inhibited by the sulfhydryl inhibitors (N-ethylmaleimide, iodoacetate, ZnCl2 and CuCl2).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.43 mM | S-formylglutathione | |||||
1.03 mM | alpha-naphthyl acetate | |||||
0.45 mM | pNP-acetate | |||||
0.7 mM | pNP-butyrate | |||||
0.95 mM | pNP-caproate | |||||
0.48 mM | pNP-propionate | |||||
0.58 mM | S-lactoylglutathione |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
12.6 μmol/min/mg | with S-formylglutathione as substrate | ||||
9.79 μmol/min/mg | with alpha-naphthyl acetate as substrate | ||||
0.5 μmol/min/mg | with pNP-acetate as substrate | ||||
0.7 μmol/min/mg | with pNP-butyrate as substrate | ||||
0.64 μmol/min/mg | with pNP-caproate as substrate | ||||
0.71 μmol/min/mg | with pNP-propionate as substrate | ||||
1.97 μmol/min/mg | with S-lactoylglutathione as substrate |
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 145 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 223 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 256 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | protein-containing complex | |
Molecular Function | carboxylic ester hydrolase activity | |
Molecular Function | hydroxyacylglutathione hydrolase activity | |
Molecular Function | identical protein binding | |
Molecular Function | S-formylglutathione hydrolase activity | |
Biological Process | formaldehyde catabolic process | |
Biological Process | protein homotetramerization |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameS-formylglutathione hydrolase YeiG
- EC number
- Short namesFGH
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP33018
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 26 | Reduces catalytic efficiency, but has no effect on affinity for substrate. | ||||
Sequence: C → A | ||||||
Mutagenesis | 54 | Reduces affinity for substrate and catalytic efficiency. | ||||
Sequence: C → A | ||||||
Mutagenesis | 80 | Increases affinity for substrate, but reduces catalytic efficiency. | ||||
Sequence: D → A | ||||||
Mutagenesis | 145 | Loss of activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 199 | Reduces catalytic efficiency, but has no effect on affinity for substrate. | ||||
Sequence: D → A | ||||||
Mutagenesis | 218 | Reduces affinity for substrate and catalytic efficiency. | ||||
Sequence: D → A | ||||||
Mutagenesis | 223 | Loss of activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 255 | Increases affinity for substrate, but reduces catalytic efficiency. | ||||
Sequence: D → A | ||||||
Mutagenesis | 256 | Loss of activity. | ||||
Sequence: H → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000210345 | 1-278 | S-formylglutathione hydrolase YeiG | |||
Sequence: MEMLEEHRCFEGWQQRWRHDSSTLNCPMTFSIFLPPPRDHTPPPVLYWLSGLTCNDENFTTKAGAQRVAAELGIVLVMPDTSPRGEKVANDDGYDLGQGAGFYLNATQPPWATHYRMYDYLRDELPALVQSQFNVSDRCAISGHSMGGHGALIMALKNPGKYTSVSAFAPIVNPCSVPWGIKAFSSYLGEDKNAWLEWDSCALMYASNAQDAIPTLIDQGDNDQFLADQLQPAVLAEAARQKAWPMTLRIQPGYDHSYYFIASFIEDHLRFHAQYLLK |
Proteomic databases
Expression
Induction
Constitutively expressed.
Structure
Sequence
- Sequence statusComplete
- Length278
- Mass (Da)31,259
- Last updated1994-02-01 v1
- Checksum69292AD902EF3E72
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U00007 EMBL· GenBank· DDBJ | AAA60510.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC75215.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76631.1 EMBL· GenBank· DDBJ | Genomic DNA |