[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=K12; PubMed=2536666 [NCBI, ExPASy, EBI, Israel, Japan] Matsuyama A., Yamamoto H., Nakano E.; "Cloning, expression, and nucleotide sequence of the Escherichia coli K-12 ackA gene."; J. Bacteriol. 171:577-580(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12 / KH131; PubMed=7883769 [NCBI, ExPASy, EBI, Israel, Japan] Kakuda H., Hosono K., Shiroishi K., Ichihara S.; "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."; J. Biochem. 116:916-922(1994).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/4.2.91; PubMed=9205837 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "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."; DNA Res. 4:91-113(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

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.
CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate.
CATALYTIC ACTIVITY: ATP + propanoate = ADP + propanoyl phosphate.
PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2 .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the acetokinase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M22956; AAA23406.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D17576; BAA04501.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75356.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA16135.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JT0498; KIECAA.

RefSeq

AP_002896.1; -.
NP_416799.1; -.

3D structure databases

PDB

1LRG; Model; -; A=1-400.

[ExPASy / RCSB / EBI]

PDBsum

1LRG; -.

ModBase

P0A6A3.

Enzyme and pathway databases

BioCyc

EcoCyc:ACETATEKINA-MON; -.
MetaCyc:ACETATEKINA-MON; -.

2D gel databases

SWISS-2DPAGE

P0A6A3; -.

ECO2DBASE

G041.3; 6TH EDITION.

Organism-specific databases

EchoBASE

EB0026; -.

EcoGene

EG10027; ackA.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0008776;	Molecular function: acetate kinase activity (inferred from electronic annotation from HAMAP).
GO:0006082;	Biological process: organic acid metabolic process (inferred from electronic annotation from InterPro).
GO:0016310;	Biological process: phosphorylation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00020; -; 1.
PBIL [Tree]

InterPro

IPR000890; Acetate_kin.
IPR004372; AckA.
Graphical view of domain structure.

PANTHER

PTHR21060; Acetate_kin; 1.
PTHR21060:SF11; AckA; 1.

Pfam

PF00871; Acetate_kinase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000722; Acetate_prop_kin; 1.

PRINTS

PR00471; ACETATEKNASE.

TIGRFAMs

TIGR00016; ackA; 1.

PROSITE

PS01075; ACETATE_KINASE_1; 1.
PS01076; ACETATE_KINASE_2; 1.

Genome annotation databases

GeneID

946775; -.

GenomeReviews

AP009048_GR; JW2293.
U00096_GR; b2296.

KEGG

ecj:JW2293; -.
eco:b2296; -.

Phylogenomic databases

HOGENOM

P0A6A3; -.

Genome annotation databases

CMR

P0A6A3; b2296.

Other

ProtoNet

P0A6A3.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 400`	`400`	`Acetate kinase.`	`PRO_0000107557`
`CONFLICT`	`221 221`		`R -> G (in Ref. 2; BAA04501).`
`CONFLICT`	`240 240`		`M -> I (in Ref. 2; BAA04501).`
`STRAND`	`5 11`	`7`
`STRAND`	`16 22`	`7`
`TURN`	`23 26`	`4`
`STRAND`	`27 36`	`10`
`STRAND`	`39 41`	`3`
`STRAND`	`43 48`	`6`
`TURN`	`49 51`	`3`
`STRAND`	`52 57`	`6`
`HELIX`	`63 75`	`13`
`STRAND`	`76 79`	`4`
`STRAND`	`87 93`	`7`
`TURN`	`96 98`	`3`
`HELIX`	`107 119`	`13`
`HELIX`	`129 137`	`9`
`STRAND`	`142 151`	`10`
`HELIX`	`152 156`	`5`
`HELIX`	`159 162`	`4`
`HELIX`	`168 174`	`7`
`HELIX`	`183 197`	`15`
`HELIX`	`201 203`	`3`
`STRAND`	`205 221`	`17`
`STRAND`	`224 229`	`6`
`STRAND`	`236 238`	`3`
`HELIX`	`250 259`	`10`
`HELIX`	`263 272`	`10`
`HELIX`	`275 280`	`6`
`HELIX`	`286 294`	`9`
`HELIX`	`297 321`	`25`
`STRAND`	`327 331`	`5`
`HELIX`	`332 337`	`6`
`HELIX`	`339 346`	`8`
`HELIX`	`350 352`	`3`
`HELIX`	`358 363`	`6`
`STRAND`	`380 382`	`3`
`HELIX`	`387 399`	`13`

Sequence information

Length: 400 AA [This is the length of the unprocessed precursor]

Molecular weight: 43290 Da [This is the MW of the unprocessed precursor]

CRC64: 709C855C514656C8 [This is a checksum on the sequence]

        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

P0A6A3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools