CATH Classification

Domain Context

CATH Clusters

Superfamily Metal-dependent hydrolases
Functional Family CAD protein isoform X2

Enzyme Information

6.3.5.5
Carbamoyl-phosphate synthase (glutamine-hydrolyzing).
based on mapping to UniProt P27708
2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.
-!- The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. -!- The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. -!- The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. -!- The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. -!- The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. -!- The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. -!- Cf. EC 6.3.4.16. -!- Formerly EC 2.7.2.9.
2.1.3.2
Aspartate carbamoyltransferase.
based on mapping to UniProt P27708
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.
3.5.2.3
Dihydroorotase.
based on mapping to UniProt P27708
(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate.

UniProtKB Entries (1)

P27708
PYR1_HUMAN
Homo sapiens
CAD protein

PDB Structure

PDB 5YNZ
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structures of monometallic dihydropyrimidinase and the human dihydroorotase domain K1556A mutant reveal no lysine carbamylation within the active site
Cheng, J.H., Huang, Y.H., Lin, J.J., Huang, C.Y.
Biochem. Biophys. Res. Commun.
CATH-Gene3D is a Global Biodata Core Resource Learn more...