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	PROSITE documentation PDOC51671 [for PROSITE entry PS51671]

ACT and ACT-like domain profiles

The ACT domain is a 90 amino acid long domain, which has been named after three of the allosterically regulated enzymes in which it is found: aspartate kinase, chorismate mutase and TyrA (prephenate dehydrogenase) [1]. The ACT domain is found in a variety of contexts and is proposed to be a structurally conserved regulatory domain involved in the binding of small ligands, such as amino acids. 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 uncharacterized proteins from archaea, bacteria and plants that contain from one to four copies of this domain [2].

The ACT domain forms a β-sheet with appressed helices (see <PDB:1PSD>) [1].

Threonine dehydratases (TDs) contain an ACT-like regulatory domain that possesses structural, rather than sequence, homology to the ACT domain [3].

The profile we developed cover the entire ACT and ACT-like domains.

Last update:

April 2013 / First entry.

PROSITE methods (with tools and information) covered by this documentation:

ACT, PS51671; ACT domain profile  (MATRIX)

• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 560
  • detected by PS51671: 544 (true positives)
  • undetected by PS51671: 16 (16 false negatives and 0 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS51671:
  NONE.
• Domain architecture view of Swiss-Prot proteins matching PS51671
  
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS51671
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS51671
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS51671
• View ligand binding statistics of PS51671
• Matching PDB structures: 1PHZ 1PSD 1SC6 1Y7P ... [ALL]

ACT_LIKE, PS51672; ACT-like domain profile  (MATRIX)

• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 33
  • detected by PS51672: 33 (true positives)
  • undetected by PS51672: 0 (false negative or 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS51672:
  NONE.
• Domain architecture view of Swiss-Prot proteins matching PS51672
  
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS51672
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS51672
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS51672
• View ligand binding statistics of PS51672
• Matching PDB structures: 1TDJ [ALL]

1	Authors	Aravind L., Koonin E.V.
	Title	Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches.
	Source	J. Mol. Biol. 287:1023-1040(1999).
	PubMed ID	10222208
	DOI	10.1006/jmbi.1999.2653

2	Authors	Hsieh M.-H., Goodman H.M.
	Title	Molecular characterization of a novel gene family encoding ACT domain repeat proteins in Arabidopsis.
	Source	Plant Physiol. 130:1797-1806(2002).
	PubMed ID	12481063
	DOI	10.1104/pp.007484

3	Authors	Chipman D.M., Shaanan B.
	Title	The ACT domain family.
	Source	Curr. Opin. Struct. Biol. 11:694-700(2001).
	PubMed ID	11751050

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