P0A3V5 · CAH_PSESP

  • Protein
    Cyanuric acid amidohydrolase
  • Gene
    trzD
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

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

Activity regulation

Inhibited by barbituric acid.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
58 μMcyanuric acid
50 μMcyanuric acid
kcat is 14.2 sec-1 with cyanuric acid as substrate (PubMed:22730121).
kcat is 15000 min-1 with cyanuric acid as substrate (PubMed:10427042).

pH Dependence

Optimum pH is 8-8.5.

Temperature Dependence

Optimum temperature is 45-50 degrees Celsius.

Pathway

Xenobiotic degradation; atrazine degradation; biuret from cyanurate: step 1/1.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site51substrate
Binding site82-83substrate
Active site163
Binding site195substrate
Active site233Nucleophile
Binding site233-234substrate
Binding site303Mg2+ (UniProtKB | ChEBI); structural
Site326Important for substrate specificity
Binding site330substrate
Binding site349-350substrate
Binding site352Mg2+ (UniProtKB | ChEBI); structural
Binding site355Mg2+ (UniProtKB | ChEBI); structural
Binding site356Mg2+ (UniProtKB | ChEBI); structural
Binding site357Mg2+ (UniProtKB | ChEBI); structural
Binding site360Mg2+ (UniProtKB | ChEBI); structural

GO annotations

AspectTerm
Molecular Functioncyanuric acid amidohydrolase activity
Molecular Functionmetal ion binding
Biological Processatrazine catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cyanuric acid amidohydrolase
  • EC number
  • Short names
    CAH

Gene names

    • Name
      trzD

Organism names

  • Taxonomic identifier
  • Strain
    • strain A / NRRLB 12227
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    P0A3V5
  • Secondary accessions
    • O87589

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000656491-370Cyanuric acid amidohydrolase

Interaction

Subunit

Homotetramer.

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-103RU A
Region113-250RU B
Region256-370RU C

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 status
    Complete
  • Length
    370
  • Mass (Da)
    39,420
  • Last updated
    2005-03-15 v1
  • Checksum
    E02B447694802035
MQAQVFRVPMSNPADVSGVAKLIDEGVIRAEEVVCVLGKTEGNGCVNDFTRGYTTLAFKVYFSEKLGVSRQEVGERIAFIMSGGTEGVMAPHCTIFTVQKTDNKQKTAAEGKRLAVQQIFTREFLPEEIGRMPQVTETADAVRRAMREAGIADASDVHFVQVKCPLLTAGRMHDAVERGHTVATEDTYESMGYSRGASALGIALALGEVEKANLSDEVITADYSLYSSVASTSAGIELMNNEIIVMGNSRAWGGDLVIGHAEMKDAIDGAAVRQALRDVGCCENDLPTVDELGRVVNVFAKAEASPDGEVRNRRHTMLDDSDINSTRHARAVVNAVIASIVGDPMVYVSGGSEHQGPAGGGPVAVIARTA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF086815
EMBL· GenBank· DDBJ
AAC61577.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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