CATH Classification

Domain Context

CATH Clusters

Superfamily HUPs
Functional Family Phosphopantetheine adenylyltransferase

Enzyme Information

2.7.7.3
Pantetheine-phosphate adenylyltransferase.
based on mapping to UniProt P9WPA5
ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA.
-!- The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157.

UniProtKB Entries (1)

P9WPA5
COAD_MYCTU
Mycobacterium tuberculosis H37Rv
Phosphopantetheine adenylyltransferase

PDB Structure

PDB 1TFU
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase.
Morris, V.K., Izard, T.
Protein Sci.