Cyanate lyase C-terminal domain, Cyanate hydratase
SMART accession number:SM01116
Description: Cyanate lyase (also known as cyanase) EC: is responsible for the hydrolysis of cyanate, allowing organisms that possess the enzyme to overcome the toxicity of environmental cyanate. This enzyme is composed of two domains, an N-terminal helix-turn-helix and this structurally unique C-terminal domain ((PUBMED:10801492)).
Interpro abstract (IPR003712):

Some bacteria can overcome the toxicity of environmental cyanate by hydrolysis of cyanate. This reaction is catalyzed by cyanate lyase (also known as cyanase) [(PUBMED:3049588)]. Cyanate lyase is found in bacteria and plants and catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.

The cyanate lyase monomer is composed of two domains. The N-terminal domain shows structural similarity to the DNA-binding alpha-helix bundle motif. The C-terminal domain has an 'open fold' with no structural homology to other proteins. The dimer structure reveals the C-terminal domains to be intertwined, and the decamer is formed by a pentamer of these dimers. The active site of the enzyme is located between dimers and is comprised of residues from four adjacent subunits of the homodecamer [(PUBMED:10801492)].

GO process:cyanate metabolic process (GO:0009439)
Family alignment:
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There are 3452 Cyanate_lyase domains in 3452 proteins in SMART's nrdb database.

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