A0A926P6B4 · A0A926P6B4_9HYPH

  • Protein
    Cyanuric acid amidohydrolase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

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.

TypeIDPosition(s)Description
Binding site56substrate
Binding site84-85substrate
Active site161
Binding site192substrate
Active site230Nucleophile
Binding site230-231substrate
Binding site300Mg2+ (UniProtKB | ChEBI); structural
Site323Important for substrate specificity
Binding site327substrate
Binding site346-347substrate
Binding site349Mg2+ (UniProtKB | ChEBI); structural
Binding site352Mg2+ (UniProtKB | ChEBI); structural
Binding site353Mg2+ (UniProtKB | ChEBI); structural
Binding site354Mg2+ (UniProtKB | ChEBI); structural
Binding site357Mg2+ (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

    • ORF names
      HK439_20375

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • PHM038
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Stappiaceae > Roseibium

Accessions

  • Primary accession
    A0A926P6B4

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-103RU A
Region253-369RU C
Region348-369Disordered

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
    369
  • Mass (Da)
    38,694
  • Last updated
    2023-02-22 v1
  • Checksum
    D9C0191B997CAB93
MDPLLREARVHRLPMSSPDDTSAIETLVEQGKIDPKAVVAVLGKTEGNGCVNDFTRGYAVQSLRFLFGRYMEPADLDRICMVMSGGTEGALSPHWIVLEALPATGVTQTPALALGVHVTEDFAPVEIGRMAQVTKVADGVRKAMVQAGISDPKDVHFVQIKCPLLTAERVRAAGGAHAVATADTLRSMGLSRGASALGVAVALGEIDETALSDTAIGDDLSLYSTRASCSAGVELMGCEILVMGMSDMWSGPLTIGHALMRDALDIDPIRETLSNLGISAPGQFPEETRERVTAVLVKAEASKSGHARGFRHTMLDDSDISSTRHARGFVAGVLAGLIGQTELFVSGGAEHQGPDGGGPCAVIGRRSDP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABFCZ010000024
EMBL· GenBank· DDBJ
MBD1548627.1
EMBL· GenBank· DDBJ
Genomic DNA

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Disclaimer

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