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InterPro: IPR004372 Acetate kinase

Protein matches Help

UniProtKB

Matches:

1964 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

IPR004372 AckA

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF000722	Acetate_prop_kin	1804
PANTHER	PTHR21060:SF11	AckA	1720
TIGRFAMs	TIGR00016	ackA	1847
Signatures in BioMart

InterPro Relationships Help

Parent

IPR000890 Acetate/butyrate kinase

GO Term annotation Help

Process

GO:0006082 organic acid metabolic process

Function

GO:0016301 kinase activity
GO:0016774 phosphotransferase activity, carboxyl group as acceptor

InterPro annotation

Entry Details in BioMart

Abstract

Acetate kinase is involved in the activation of acetate to acetyl CoA and in the secretion of acetate. It catalyzes the reaction ATP + acetate = ADP + acetyl phosphate.

Structural links Help

PDB - click here

SCOP: c.55.1.2

Database links Help

Enzyme: EC:2.7.2.1

CluSTr: ALLvsALL:40880:85.2

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004372

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

B0CB11 Acetate kinase

O06961 Propionate kinase

P38502 Acetate kinase

P73162 Acetate kinase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004372	Acetate kinase
IPR000890	Acetate/butyrate kinase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Simanshu DK, Savithri HS, Murthy MR. Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily. J. Mol. Biol. 352 2005 876-92 [PubMed: 16139298] http://dx.doi.org/10.1016/j.jmb.2005.07.069
	Gorrell A, Lawrence SH, Ferry JG. Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila. J. Biol. Chem. 280 2005 10731-42 [PubMed: 15647264] http://dx.doi.org/10.1074/jbc.M412118200
	Hesslinger C, Fairhurst SA, Sawers G. Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate. Mol. Microbiol. 27 1998 477-92 [PubMed: 9484901] http://dx.doi.org/10.1046/j.1365-2958.1998.00696.x
	Simanshu DK, Murthy MR. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 2005 52-5 [PubMed: 16508089]
	Buss KA, Cooper DR, Ingram-Smith C, Ferry JG, Sanders DA, Hasson MS. Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases. J. Bacteriol. 183 2001 680-6 [PubMed: 11133963] http://dx.doi.org/10.1128/JB.183.2.680-686.2001
	Simanshu DK, Savithri HS, Murthy MR. Crystal structures of Salmonella typhimurium propionate kinase and its complex with Ap4A: evidence for a novel Ap4A synthetic activity. Proteins 70 2008 1379-88 [PubMed: 17894350] http://dx.doi.org/10.1002/prot.21626

InterPro 23.1