CATH Classification

Domain Context

CATH Clusters

Superfamily Quinolinate phosphoribosyl transferase, N-terminal domain
Functional Family

Enzyme Information

6.3.4.21
Nicotinate phosphoribosyltransferase.
based on mapping to UniProt Q9HJ28
Nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H(2)O = beta- nicotinate D-ribonucleotide + diphosphate + ADP + phosphate.
-!- The enzyme, which is involved in pyridine nucleotide recycling, can form beta-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) in the absence of ATP. -!- However, when ATP is available the enzyme is phosphorylated resulting in a much lower K(m) for nicotinate. -!- The phospho-enzyme is hydrolyzed during the transferase reaction, regenerating the low affinity form. -!- The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100. -!- Formerly EC 2.4.2.11.

UniProtKB Entries (1)

Q9HJ28
PNCB_THEAC
Thermoplasma acidophilum DSM 1728
Putative nicotinate phosphoribosyltransferase

PDB Structure

PDB 1YTE
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum.
Shin, D.H., Oganesyan, N., Jancarik, J., Yokota, H., Kim, R., Kim, S.H.
J.Biol.Chem.
CATH-Gene3D is a Global Biodata Core Resource Learn more...