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InterPro: IPR000890 Acetate/butyrate kinase

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UniProtKB

Matches:

2341 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR000890 Acetate/butyrate_kinase

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00871	Acetate_kinase	2326
PRINTS	PR00471	ACETATEKNASE	2286
PROSITE pattern	PS01075	ACETATE_KINASE_1	1979
PROSITE pattern	PS01076	ACETATE_KINASE_2	2044
PANTHER	PTHR21060	Acetate_kin	2321
Signatures in BioMart

InterPro Relationships Help

Children

IPR004372 Acetate kinase
IPR011245 Butyrate kinase

GO Term annotation Help

Process

GO:0008152 metabolic process
GO:0016310 phosphorylation

Function

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

Component

GO:0005622 intracellular

InterPro annotation

Entry Details in BioMart

Abstract

Acetate kinase, which is predominantly found in micro-organisms, facilitates the production of acetyl-CoA by phosphorylating acetate in the presence of ATP and a divalent cation [1, 2]. The enzyme is important in the process of glycolysis, enzyme levels being increased in the presence of excess glucose. The growth of a bacterial mutant lacking acetate kinase has been shown to be inhibited by glucose, suggesting that the enzyme is involved in excretion of excess carbohydrate [1]. A related enzyme, butyrate kinase, facilitates the formation of butyryl-CoA by phosphorylating butyrate in the presence of ATP to form butyryl phosphate [2].

Structural links Help

PDB - click here

SCOP: c.55.1.2

Database links Help

PDBe-motif: PS01075 , PS01076

Enzyme: EC:2.7.2.1

PROSITE doc: PDOC00826

PANDIT: PF00871

Blocks: IPB000890

Pfam Clan: CL0108.12

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000890

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 Open in usermanual
1.	Grundy FJ, Waters DA, Allen SH, Henkin TM. Regulation of the Bacillus subtilis acetate kinase gene by CcpA. J. Bacteriol. 175 7348-55 1993 [PubMed: 8226682] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=8226682&action=stream&blobtype=pdf
2.	Oultram JD, Burr ID, Elmore MJ, Minton NP. Cloning and sequence analysis of the genes encoding phosphotransbutyrylase and butyrate kinase from Clostridium acetobutylicum NCIMB 8052. Gene 131 107-12 1993 [PubMed: 8396545] http://dx.doi.org/10.1016/0378-1119(93)90677-U

Additional Reading Open in usermanual
	Diao J, Cooper DR, Sanders DA, Hasson MS. Crystallization of butyrate kinase 2 from Thermotoga maritima mediated by vapor diffusion of acetic acid. Acta Crystallogr. D Biol. Crystallogr. 59 2003 1100-2 [PubMed: 12777787] http://dx.doi.org/10.1107/S0907444903007832
	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
	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]
	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