P0A6A3 (ACKA_ECOLI) 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
Synonyms:	ack
Ordered Locus Names:	b2296, JW2293

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the activation of acetate to acetyl CoA and the secretion of acetate. During anaerobic growth of the organism, this enzyme is also involved in the synthesis of most of the ATP formed catabolically. HAMAP MF_00020
Catalytic activity	ATP + acetate = ADP + acetyl phosphate. HAMAP MF_00020 ATP + propanoate = ADP + propanoyl phosphate. HAMAP MF_00020
Pathway	Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2. HAMAP MF_00020
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP MF_00020.
Sequence similarities	Belongs to the acetokinase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	organic acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB membrane Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate kinase activity Inferred from direct assay Ref.1. Source: EcoliWiki zinc ion binding Inferred from direct assay. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 400

400

Acetate kinase HAMAP MF_00020

PRO_0000107557

Experimental info

Sequence conflict

221

1

R → G in BAA04501. Ref.2

Sequence conflict

240

1

M → I in BAA04501. Ref.2

Secondary structure

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400

Helix Strand Turn

Details...

Beta strand

5 – 11

7

Beta strand

16 – 22

7

Turn

23 – 26

4

Beta strand

27 – 36

10

Beta strand

39 – 41

3

Beta strand

43 – 48

6

Turn

49 – 51

3

Beta strand

52 – 57

6

Helix

63 – 75

13

Beta strand

76 – 79

4

Beta strand

87 – 93

7

Turn

96 – 98

3

Helix

107 – 119

13

Helix

129 – 137

9

Beta strand

142 – 151

10

Helix

152 – 156

5

Helix

159 – 162

4

Helix

168 – 174

7

Helix

183 – 197

15

Helix

201 – 203

3

Beta strand

205 – 221

17

Beta strand

224 – 229

6

Beta strand

236 – 238

3

Helix

250 – 259

10

Helix

263 – 272

10

Helix

275 – 280

6

Helix

286 – 294

9

Helix

297 – 321

25

Beta strand

327 – 331

5

Helix

332 – 337

6

Helix

339 – 346

8

Helix

350 – 352

3

Helix

358 – 363

6

Beta strand

380 – 382

3

Helix

387 – 399

13

Sequences

	Sequence		Length	Mass (Da)
	P0A6A3 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 709C855C514656C8	FASTA	400	43,290
	10 20 30 40 50 60 MSSKLVLVLN CGSSSLKFAI IDAVNGEEYL SGLAECFHLP EARIKWKMDG NKQEAALGAG 70 80 90 100 110 120 AAHSEALNFI VNTILAQKPE LSAQLTAIGH RIVHGGEKYT SSVVIDESVI QGIKDAASFA 130 140 150 160 170 180 PLHNPAHLIG IEEALKSFPQ LKDKNVAVFD TAFHQTMPEE SYLYALPYNL YKEHGIRRYG 190 200 210 220 230 240 AHGTSHFYVT QEAAKMLNKP VEELNIITCH LGNGGSVSAI RNGKCVDTSM GLTPLEGLVM 250 260 270 280 290 300 GTRSGDIDPA IIFHLHDTLG MSVDAINKLL TKESGLLGLT EVTSDCRYVE DNYATKEDAK 310 320 330 340 350 360 RAMDVYCHRL AKYIGAYTAL MDGRLDAVVF TGGIGENAAM VRELSLGKLG VLGFEVDHER 370 380 390 400 NLAARFGKSG FINKEGTRPA VVIPTNEELV IAQDASRLTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression, and nucleotide sequence of the Escherichia coli K-12 ackA gene." Matsuyama A., Yamamoto H., Nakano E. J. Bacteriol. 171:577-580(1989) [PubMed: 2536666] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[2]	"Identification and characterization of the ackA (acetate kinase A)-pta (phosphotransacetylase) operon and complementation analysis of acetate utilization by an ackA-pta deletion mutant of Escherichia coli." Kakuda H., Hosono K., Shiroishi K., Ichihara S. J. Biochem. 116:916-922(1994) [PubMed: 7883769] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / KH131.
[3]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M22956 Genomic DNA. Translation: AAA23406.1.
D17576 Genomic DNA. Translation: BAA04501.1.
U00096 Genomic DNA. Translation: AAC75356.1.
AP009048 Genomic DNA. Translation: BAA16135.1.

PIR

KIECAA. JT0498.

RefSeq

NP_416799.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LRG	model	-	A	1-400	[»]

ProteinModelPortal

P0A6A3.

SMR

P0A6A3. Positions 1-400.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6A3. 12 interactions.

2D gel databases

SWISS-2DPAGE

P0A6A3.

ECO2DBASE

G041.3. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003664; EBESCP00000003664; EBESCG00000002995.
EBESCT00000014455; EBESCP00000013746; EBESCG00000013516.

GeneID

946775.

GenomeReviews

Gene locus JW2293 in contig AP009048_GR.
Gene locus b2296 in contig U00096_GR.

KEGG

ecj:JW2293.
eco:b2296.

PATRIC

32119963. VBIEscCol129921_2391.

Organism-specific databases

EchoBASE

EB0026.

EcoGene

EG10027. ackA.

Phylogenomic databases

eggNOG

COG0282.

GeneTree

EBGT00050000009666.

HOGENOM

HBG285863.

OMA

IVFHLHD.

PhylomeDB

P0A6A3.

ProtClustDB

PRK00180.

Enzyme and pathway databases

BioCyc

EcoCyc:ACETATEKINA-MONOMER.
MetaCyc:ACETATEKINA-MONOMER.

Gene expression databases

Genevestigator

P0A6A3.

Family and domain databases

HAMAP

MF_00020. Acetate_kinase.
[Tree]

InterPro

IPR004372. Ac/Proprionate_kinase.
IPR000890. Aliphatic_acid_kin_short-chain.
IPR023865. Aliphatic_acid_kinase_CS.
[Graphical view]

KO

K00925.

PANTHER

PTHR21060. Acetate_kin. 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_ECOLI

Accession

Primary (citable) accession number: P0A6A3
Secondary accession number(s): P15046, P78188, Q59386

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program