A0A926P6B4 · A0A926P6B4_9HYPH
- ProteinCyanuric acid amidohydrolase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids369 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret.
Catalytic activity
- cyanurate + H2O = 1-carboxybiuret + H+
Activity regulation
Inhibited by barbituric acid.
Pathway
Xenobiotic degradation; atrazine degradation; biuret from cyanurate: step 1/1.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 56 | substrate | ||||
Sequence: R | ||||||
Binding site | 84-85 | substrate | ||||
Sequence: SG | ||||||
Active site | 161 | |||||
Sequence: K | ||||||
Binding site | 192 | substrate | ||||
Sequence: R | ||||||
Active site | 230 | Nucleophile | ||||
Sequence: S | ||||||
Binding site | 230-231 | substrate | ||||
Sequence: SA | ||||||
Binding site | 300 | Mg2+ (UniProtKB | ChEBI); structural | ||||
Sequence: E | ||||||
Site | 323 | Important for substrate specificity | ||||
Sequence: T | ||||||
Binding site | 327 | substrate | ||||
Sequence: R | ||||||
Binding site | 346-347 | substrate | ||||
Sequence: SG | ||||||
Binding site | 349 | Mg2+ (UniProtKB | ChEBI); structural | ||||
Sequence: A | ||||||
Binding site | 352 | Mg2+ (UniProtKB | ChEBI); structural | ||||
Sequence: Q | ||||||
Binding site | 353 | Mg2+ (UniProtKB | ChEBI); structural | ||||
Sequence: G | ||||||
Binding site | 354 | Mg2+ (UniProtKB | ChEBI); structural | ||||
Sequence: P | ||||||
Binding site | 357 | Mg2+ (UniProtKB | ChEBI); structural | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | cyanuric acid amidohydrolase activity | |
Molecular Function | metal ion binding | |
Biological Process | atrazine catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCyanuric acid amidohydrolase
- EC number
- Short namesCAH
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Stappiaceae > Roseibium
Accessions
- Primary accessionA0A926P6B4
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-103 | RU A | ||||
Sequence: MDPLLREARVHRLPMSSPDDTSAIETLVEQGKIDPKAVVAVLGKTEGNGCVNDFTRGYAVQSLRFLFGRYMEPADLDRICMVMSGGTEGALSPHWIVLEALPA | ||||||
Region | 253-369 | RU C | ||||
Sequence: LTIGHALMRDALDIDPIRETLSNLGISAPGQFPEETRERVTAVLVKAEASKSGHARGFRHTMLDDSDISSTRHARGFVAGVLAGLIGQTELFVSGGAEHQGPDGGGPCAVIGRRSDP | ||||||
Region | 348-369 | Disordered | ||||
Sequence: GAEHQGPDGGGPCAVIGRRSDP |
Domain
The monomer structure is formed from three repeating units (RUs) that share the same structure as one another. The monomer, the active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads. It is possible that any or all of the three active-site serines may act as nucleophile (albeit only one can do so per catalytic cycle).
Sequence similarities
Belongs to the cyclic amide hydrolase (CyAH) family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length369
- Mass (Da)38,694
- Last updated2023-02-22 v1
- ChecksumD9C0191B997CAB93