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P0A6A3 (ACKA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetate kinase

EC=2.7.2.1
Alternative name(s):
Acetokinase
Gene names
Name:ackA
Synonyms:ack
Ordered Locus Names:b2296, JW2293
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. During anaerobic growth of the organism, this enzyme is also involved in the synthesis of most of the ATP formed catabolically. 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.

Subcellular location

Cytoplasm HAMAP-Rule MF_00020.

Sequence similarities

Belongs to the acetokinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Acetate kinase HAMAP-Rule MF_00020
PRO_0000107557

Regions

Nucleotide binding210 – 2145ATP By similarity
Nucleotide binding285 – 2873ATP By similarity
Nucleotide binding333 – 3375ATP By similarity

Sites

Active site1501Proton donor/acceptor By similarity
Metal binding101Magnesium By similarity
Metal binding3871Magnesium By similarity
Binding site171ATP By similarity
Binding site911Substrate By similarity
Site1821Transition state stabilizer By similarity
Site2431Transition state stabilizer By similarity

Experimental info

Sequence conflict2211R → G in BAA04501. Ref.2
Sequence conflict2401M → I in BAA04501. Ref.2

Secondary structure

................................................................ 400
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6A3 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 709C855C514656C8

FASTA40043,290
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.

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.
PIRKIECAA. JT0498.
RefSeqNP_416799.1. NC_000913.2.
YP_490538.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LRGmodel-A1-400[»]
ProteinModelPortalP0A6A3.
SMRP0A6A3. Positions 1-400.
ModBaseSearch...

Protein-protein interaction databases

IntActP0A6A3. 12 interactions.
STRING511145.b2296.

2D gel databases

SWISS-2DPAGEP0A6A3.

Proteomic databases

PaxDbP0A6A3.
PRIDEP0A6A3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75356; AAC75356; b2296.
BAA16135; BAA16135; BAA16135.
GeneID12932696.
946775.
KEGGecj:Y75_p2262.
eco:b2296.
PATRIC32119963. VBIEscCol129921_2391.

Organism-specific databases

EchoBASEEB0026.
EcoGeneEG10027. ackA.

Phylogenomic databases

eggNOGCOG0282.
HOGENOMHOG000288398.
KOK00925.
OMAIDHERNL.
ProtClustDBPRK00180.

Enzyme and pathway databases

BioCycEcoCyc:ACETATEKINA-MONOMER.
ECOL316407:JW2293-MONOMER.
MetaCyc:ACETATEKINA-MONOMER.
SABIO-RKP0A6A3.
UniPathwayUPA00340; UER00458.

Gene expression databases

GenevestigatorP0A6A3.

Family and domain databases

HAMAPMF_00020. Acetate_kinase.
InterProIPR004372. Ac/Proprionate_kinase.
IPR000890. Aliphatic_acid_kin_short-chain.
IPR023865. Aliphatic_acid_kinase_CS.
[Graphical view]
PANTHERPTHR21060. PTHR21060. 1 hit.
PfamPF00871. Acetate_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF000722. Acetate_prop_kin. 1 hit.
PRINTSPR00471. ACETATEKNASE.
TIGRFAMsTIGR00016. ackA. 1 hit.
PROSITEPS01075. ACETATE_KINASE_1. 1 hit.
PS01076. ACETATE_KINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACKA_ECOLI
AccessionPrimary (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: May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families