The domain within your query sequence starts at position 17 and ends at position 82; the E-value for the ACT domain shown below is 6.9e-9.

VTLIFSLENEVGGLIKVLKIFQENHVSLLHIESRKSKQRNSEFEIFVDCDISREQLNDIF
PLLKSH

ACT

ACT
PFAM accession number:PF01842
Interpro abstract (IPR002912):

The ACT domain is found in a variety of contexts and is proposed to be a conserved regulatory binding fold. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. The archetypical ACT domain is the C-terminal regulatory domain of 3-phosphoglycerate dehydrogenase (3PGDH), which folds with a ferredoxin-like topology. A pair of ACT domains form an eight-stranded antiparallel sheet with two molecules of allosteric inhibitor serine bound in the interface. Biochemical exploration of a few other proteins containing ACT domains supports the suggestions that these domains contain the archetypical ACT structure [(PUBMED:11751050)].

Most of the proteins in which it is found are involved in amino acid and purine metabolism:

  • aspartokinases
  • chorismate mutases
  • prephenate dehydrogenases (TyrA)
  • prephenate dehydratases
  • homoserine dehydrogenases
  • malate dehydrogenases
  • phosphoglycerate dehydrogenases
  • phenylalanine and tryptophan-4-monooxygenases
  • phosphoribosylformylglycinamidine synthase (PurQ)
  • uridylyl transferase and removing enzyme (GlnD)
  • GTP pyrophosphokinase/phosphohydrolase (SpoT/RelA)
  • tyrosine and phenol metabolism operon regulators (TyrR)
  • several uncharacterised proteins from archaea, bacteria and plants that contain from one to four copies of this domain [(PUBMED:12481063)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ACT