| ACT | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystal structure ofE. coli aspartokinase iii in complex with aspartate and adp (r-state) | |||||||||
| Identifiers | |||||||||
| Symbol | ACT | ||||||||
| Pfam | PF01842 | ||||||||
| Pfam clan | CL0070 | ||||||||
| InterPro | IPR002912 | ||||||||
| SCOP2 | 1psd /SCOPe /SUPFAM | ||||||||
| CDD | cd02116 | ||||||||
| |||||||||
In molecular biology, theACT domain is aprotein domain that is found in a variety of proteins involved in metabolism. ACTdomains are linked to a wide range ofmetabolicenzymes that are regulated byamino acidconcentration. The ACT domain is named after three of the proteins that contain it:aspartate kinase,chorismate mutase andTyrA. The archetypical ACT domain is the C-terminal regulatory domain of3-phosphoglyceratedehydrogenase (3PGDH), whichfolds with aferredoxin-like topology. A pair of ACTdomains form an eight-strandedantiparallel sheet with twomolecules ofallosteric inhibitorserine bound in the interface.Biochemical exploration of a few otherproteins containing ACT domains supports the suggestions that these domains contain the archetypical ACTstructure.[1]
The ACT domain was discovered by Aravind and Koonin usingiterative sequence searches.[2]