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 4C6Q
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure, Functional Characterization and Evolution of the Dihydroorotase Domain of Human Cad.
Grande-Garcia, A., Lallous, N., Diaz-Tejada, C., Ramon-Maiques, S.
Structure