Q9UYV8 · NITR_PYRAB
- ProteinNitrilase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids262 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Nitrilase that hydrolyzes preferentially aliphatic nitriles like malononitrile and fumaronitrile in vitro. These dinitriles are converted to the corresponding monoacid mononitriles, showing the enzyme is regioselective. Cannot hydrolyze compounds with a nitrile group bound to an aromatic ring or amino acid. Its biological role is unknown.
Catalytic activity
- a nitrile + 2 H2O = a carboxylate + NH4+
Activity regulation
Enzymatic activity is inhibited in the presence of acetone, methanol and metal ions such as Ag2+ and Hg2+. Is also inhibited by various thiol reagents such as DTNB, p-chloromercuribenzoate, p-hydroxymercuribenzoate, iodacetamide and iodacetate. EDTA has no influence on activity.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.47 mM | malononitrile | |||||
9.48 mM | fumaronitrile |
pH Dependence
Optimum pH is 7.4. Active within the pH range of 4.5-8.5.
Temperature Dependence
Optimum temperature is 80 degrees Celsius. Active at a broad temperature range (60-90 degrees Celsius). Highly thermostable with a half-life of 25 hours at 70 degrees Celsius, 9 hours at 80 degrees Celsius, and 6 hours at 90 degrees Celsius. Shows a Tm of 112.7 degrees Celsius.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 42 | Proton acceptor | ||||
Sequence: E | ||||||
Active site | 113 | Proton donor | ||||
Sequence: K | ||||||
Active site | 146 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 173-174 | substrate | ||||
Sequence: VM |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | indole-3-acetonitrile nitrilase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNitrilase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Thermococci > Thermococcales > Thermococcaceae > Pyrococcus
Accessions
- Primary accessionQ9UYV8
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000429328 | 1-262 | Nitrilase | |||
Sequence: MVKVAYVQMNPQILEPDKNYSKAEKLIKEASKQGAQLVVLPELFDTGYNFETREEVFEIAQKIPEGETTTFLMDVARDTGVYIVAGTAEKDGDVLYNSAVVVGPRGFIGKYRKIHLFYREKFFFEPGDLGFRVFDLGFMKVGVMICFDWFFPESARTLALKGADVIAHPANLVMPYAPRAMPIRALENKVYTVTADRVGEERGLKFIGKSLIASPKAEVLSMASETEEEVGVAEIDLYLVRNKRINDLNDIFKDRREEYYFR |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-237 | CN hydrolase | ||||
Sequence: VKVAYVQMNPQILEPDKNYSKAEKLIKEASKQGAQLVVLPELFDTGYNFETREEVFEIAQKIPEGETTTFLMDVARDTGVYIVAGTAEKDGDVLYNSAVVVGPRGFIGKYRKIHLFYREKFFFEPGDLGFRVFDLGFMKVGVMICFDWFFPESARTLALKGADVIAHPANLVMPYAPRAMPIRALENKVYTVTADRVGEERGLKFIGKSLIASPKAEVLSMASETEEEVGVAEIDL |
Sequence similarities
Belongs to the carbon-nitrogen hydrolase superfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length262
- Mass (Da)29,798
- Last updated2000-05-01 v1
- ChecksumC2EFA86AACF51D4F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ248287 EMBL· GenBank· DDBJ | CAB50304.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
HE613800 EMBL· GenBank· DDBJ | CCE70842.1 EMBL· GenBank· DDBJ | Genomic DNA |