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InterPro: IPR002912 Amino acid-binding ACT

Protein matches Help

UniProtKB

Matches:

13897 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR002912 ACT_bd

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01842	ACT	13897
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001341 Aspartate kinase domain
IPR004643 Iron-sulphur-dependent L-serine dehydratase beta subunit
IPR004789 Acetolactate synthase, small subunit
IPR004810 Formyltetrahydrofolate deformylase
IPR004811 RelA/SpoT protein
IPR005260 Aspartate kinase, monofunctional class
IPR005789 Threonine dehydratase II
IPR005961 Phenylalanine-4-hydroxylase, tetrameric form
IPR005963 Tryptophan 5-monooxygenase
IPR006236 D-3-phosphoglycerate dehydrogenase
IPR008242 Bifunctional P-protein, chorismate mutase/prephenate dehydratase
IPR008310 Ligand-binding-predicted, ACT
IPR010043 Protein-PII uridylyltransferase
IPR011147 Bifunctional aspartokinase/homoserine dehydrogenase I
IPR014424 Uncharacterised ligand-binding protein UCP004897, ACT domain-containing, AF1020 type
IPR015832 Uncharacterised conserved protein UCP006363, ACT domain-containing, AF1403 type
IPR016204 Homoserine dehydrogenase
IPR016619 Uncharacterised conserved protein UCP014439, ACT
IPR016784 Uncharacterised conserved protein UCP021288, ACT
IPR016867 Glycine cleavage repressor GcvR
IPR019773 Tyrosine 3-monooxygenase-like

Contains

IPR018528 Prephenate dehydratase, conserved site

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0016597 amino acid binding

InterPro annotation

Entry Details in BioMart

Abstract

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 [1].

Structural links Help

PDB - click here

SCOP: d.58.18.1 , d.58.18.10 , d.58.18.11 , d.58.18.12 , d.58.18.3 , d.58.18.5 , d.58.18.6 , d.58.18.7

CATH: 1.10.800.10 , 3.30.70.260

Database links Help

PANDIT: PF01842

Blocks: IPB002912

Pfam Clan: CL0070.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002912

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00439 Phenylalanine-4-hydroxylase

P10869 Aspartokinase

P16331 Phenylalanine-4-hydroxylase

P17276 Protein henna

P90925 Probable phenylalanine-4-hydroxylase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001341	Aspartate kinase domain
IPR002912	Amino acid-binding ACT
IPR018042	Aspartate kinase, conserved site
IPR019773	Tyrosine 3-monooxygenase-like
IPR005961	Phenylalanine-4-hydroxylase, tetrameric form
IPR019774	Aromatic amino acid hydroxylase, C-terminal
IPR001273	Aromatic amino acid hydroxylase
IPR018301	Aromatic amino acid hydroxylase, iron/copper binding site
IPR001048	Aspartate/glutamate/uridylate kinase
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Chipman DM, Shaanan B. The ACT domain family. Curr. Opin. Struct. Biol. 11 694-700 2001 [PubMed: 11751050] http://dx.doi.org/10.1016/S0959-440X(01)00272-X

Additional Reading Open in usermanual
	Kaplun A, Vyazmensky M, Zherdev Y, Belenky I, Slutzker A, Mendel S, Barak Z, Chipman DM, Shaanan B. Structure of the regulatory subunit of acetohydroxyacid synthase isozyme III from Escherichia coli. J. Mol. Biol. 357 2006 951-63 [PubMed: 16458324] http://dx.doi.org/10.1016/j.jmb.2005.12.077
	Petkowski JJ, Chruszcz M, Zimmerman MD, Zheng H, Skarina T, Onopriyenko O, Cymborowski MT, Koclega KD, Savchenko A, Edwards A, Minor W. Crystal structures of TM0549 and NE1324--two orthologs of E. coli AHAS isozyme III small regulatory subunit. Protein Sci. 16 2007 1360-7 [PubMed: 17586771] http://dx.doi.org/10.1110/ps.072793807
	Dey S, Hu Z, Xu XL, Sacchettini JC, Grant GA. The effect of hinge mutations on effector binding and domain rotation in Escherichia coli D-3-phosphoglycerate dehydrogenase. J. Biol. Chem. 282 2007 18418-26 [PubMed: 17459882] http://dx.doi.org/10.1074/jbc.M701174200
	Tan K, Li H, Zhang R, Gu M, Clancy ST, Joachimiak A. Structures of open (R) and close (T) states of prephenate dehydratase (PDT)--implication of allosteric regulation by L-phenylalanine. J. Struct. Biol. 162 2008 94-107 [PubMed: 18171624] http://dx.doi.org/10.1016/j.jsb.2007.11.009
	Mas-Droux C, Curien G, Robert-Genthon M, Laurencin M, Ferrer JL, Dumas R. A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase. Plant Cell 18 2006 1681-92 [PubMed: 16731588] http://dx.doi.org/10.1105/tpc.105.040451
	Schuller DJ, Grant GA, Banaszak LJ. The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Nat. Struct. Biol. 2 1995 69-76 [PubMed: 7719856] http://dx.doi.org/10.1038/nsb0195-69
	Aravind L, Koonin EV. Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. J. Mol. Biol. 287 1999 1023-40 [PubMed: 10222208] http://dx.doi.org/10.1006/jmbi.1999.2653

InterPro 23.1