A0A9Q7BIU0 · A0A9Q7BIU0_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.

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 site53substrate
Binding site77-78substrate
Active site153
Binding site185substrate
Active site223Nucleophile
Binding site223-224substrate
Binding site282Mg2+ (UniProtKB | ChEBI); structural
Site305Important for substrate specificity
Binding site309substrate
Binding site328-329substrate
Binding site331Mg2+ (UniProtKB | ChEBI); structural
Binding site334Mg2+ (UniProtKB | ChEBI); structural
Binding site335Mg2+ (UniProtKB | ChEBI); structural
Binding site336Mg2+ (UniProtKB | ChEBI); structural
Binding site339Mg2+ (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
      J5287_19520

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • K1/93
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Rhizobium

Accessions

  • Primary accession
    A0A9Q7BIU0

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-97RU A
Region246-352RU 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
    352
  • Mass (Da)
    36,540
  • Last updated
    2023-09-13 v1
  • Checksum
    96F0E8073F27A641
MSSRRAFVARIAADGPNDIAGVEALFDAALPPGDLVAILGKTEGNGCVNDFTRAFATTSFETLFAKHGISGASIVMSGGTEGALSPHWTVFGRQQVADEGTGALAIGVARTSVLPWQHLGRRQQVLSVAEAVRAAITDAGIDTLEDVHFVQIKCPLLTQRRVLEVEHAGGTTVTRDALKSMAYSRGASALGVAVALGELDPDTISDSDVCTRLDLFSGRASTSAGVELEDHEIIVLGMSPRWSGPLAIDHAIMGDAIDTAGVKEARDRLGDATLVAVLAKAEADPSGSVRGRRHTMLDDSDISSTRHARAFVGGVLAGLFGATDLYVSGGAEHQGPPGGGPVAVIVERQELT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP072147
EMBL· GenBank· DDBJ
QXZ86803.1
EMBL· GenBank· DDBJ
Genomic DNA

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