C0M6X6 (ACKA_STRE4) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetate kinase
EC=2.7.2.1

Alternative name(s):
Acetokinase

Gene names

Name:	ackA
Ordered Locus Names:	SEQ_0118

Organism

Streptococcus equi subsp. equi (strain 4047) [Complete proteome] [HAMAP]

Taxonomic identifier

553482 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus dysgalactiae group › Streptococcus equi › Streptococcus equi subsp. equi

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction By similarity. HAMAP-Rule MF_00020
Catalytic activity	ATP + acetate = ADP + acetyl phosphate. HAMAP-Rule MF_00020
Cofactor	Mg2+. Can also accept Mn2+ By similarity.
Pathway	Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2. HAMAP-Rule MF_00020
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the acetokinase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway organic acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate kinase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 399	399	Acetate kinase HAMAP-Rule MF_00020		PRO_1000116809
Regions
	Nucleotide binding	206 – 210	5	ATP By similarity
	Nucleotide binding	283 – 285	3	ATP By similarity
	Nucleotide binding	331 – 335	5	ATP By similarity
Sites
	Active site	146	1	Proton donor/acceptor By similarity
	Metal binding	8	1	Magnesium By similarity
	Metal binding	383	1	Magnesium By similarity
	Binding site	15	1	ATP By similarity
	Binding site	89	1	Substrate By similarity
	Site	178	1	Transition state stabilizer By similarity
	Site	239	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	C0M6X6 [UniParc]. Last modified May 5, 2009. Version 1. Checksum: 3B381D6811DCF126	FASTA	399	43,597
	10 20 30 40 50 60 MSKTIAINAG SSSLKWQLYQ MPEEKVLAQG IIERIGLTDS ISTVKYDGKK EEHILDIPDH 70 80 90 100 110 120 TEAVKRLLND LIHFGIIGTY DEITGVGHRI VAGGEYFKES VVVDDKVVEQ VEELAALAPL 130 140 150 160 170 180 HNPGAAAGIR AFRKILPDIT SVCVFDTSFH TTMQKHTYLY PIPQKYYTDY KVRKYGAHGT 190 200 210 220 230 240 SHKYVAEEAA KMLGRPLDEL KLITAHVGNG VSITANYHGQ SVDTSMGFTP LAGPMMGTRS 250 260 270 280 290 300 GDIDPAIIPY LIAQDPELKD AADVVNMLNK QSGLGGVSGI SSDMRDIEAG LQANNPDAVL 310 320 330 340 350 360 AYNIFIDRIK KFIGQYFAVL NGADALVFTA GMGENAPLMR QDVVNGLSWF GMEIDPEKNV 370 380 390 FGYRGDISTA ASKVKVLVIS TDEELCIARD VERLKQTIS

References

[1]

"Genomic evidence for the evolution of Streptococcus equi: host restriction, increased virulence, and genetic exchange with human pathogens." Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A. , Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J., Waller A.S. PLoS Pathog. 5:E1000346-E1000346(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 4047.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FM204883 Genomic DNA. Translation: CAW92072.1.
RefSeq	YP_002745538.1. NC_012471.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	553482.SEQ_0118.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAW92072; CAW92072; SEQ_0118.
GeneID	7695550.
KEGG	seu:SEQ_0118.
PATRIC	19644975. VBIStrEqu13040_0115.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0282.
HOGENOM	HOG000288398.
KO	K00925.
OMA	HGGEKFN.
ProtClustDB	PRK00180.
Enzyme and pathway databases
BioCyc	SEQU553482:GJOY-150-MONOMER.
UniPathway	UPA00340; UER00458.
Family and domain databases
HAMAP	MF_00020. Acetate_kinase.
InterPro	IPR004372. Ac/Proprionate_kinase. IPR000890. Aliphatic_acid_kin_short-chain. IPR023865. Aliphatic_acid_kinase_CS. [Graphical view]
PANTHER	PTHR21060. PTHR21060. 1 hit.
Pfam	PF00871. Acetate_kinase. 1 hit. [Graphical view]
PIRSF	PIRSF000722. Acetate_prop_kin. 1 hit.
PRINTS	PR00471. ACETATEKNASE.
TIGRFAMs	TIGR00016. ackA. 1 hit.
PROSITE	PS01075. ACETATE_KINASE_1. 1 hit. PS01076. ACETATE_KINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACKA_STRE4

Accession

Primary (citable) accession number: C0M6X6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	May 5, 2009
Last modified:	May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program