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ECOLI:ACKA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ackA (ECO:0000255 with HAMAP-Rule:MF_00020) (synonyms: ack)
Protein Name(s) Acetate kinase (ECO:0000255 with HAMAP-Rule:MF_00020)

Acetokinase (ECO:0000255 with HAMAP-Rule:MF_00020)

External Links
UniProt P0A6A3
EMBL M22956
D17576
U00096
AP009048
PIR JT0498
RefSeq NP_416799.1
YP_490538.1
PDB 1LRG
PDBsum 1LRG
ProteinModelPortal P0A6A3
SMR P0A6A3
DIP DIP-9042N
IntAct P0A6A3
STRING 511145.b2296
SWISS-2DPAGE P0A6A3
PaxDb P0A6A3
PRIDE P0A6A3
EnsemblBacteria AAC75356
BAA16135
GeneID 12932696
946775
KEGG ecj:Y75_p2262
eco:b2296
PATRIC 32119963
EchoBASE EB0026
EcoGene EG10027
eggNOG COG0282
HOGENOM HOG000288398
InParanoid P0A6A3
KO K00925
OMA KIITCHI
OrthoDB EOG69975F
PhylomeDB P0A6A3
BioCyc EcoCyc:ACETATEKINA-MONOMER
ECOL316407:JW2293-MONOMER
MetaCyc:ACETATEKINA-MONOMER
SABIO-RK P0A6A3
UniPathway UPA00340
PRO PR:P0A6A3
Proteomes UP000000318
UP000000625
Genevestigator P0A6A3
GO GO:0005829
GO:0016020
GO:0008776
GO:0005524
GO:0000287
GO:0008270
GO:0019413
GO:0006083
GO:0006085
GO:0042710
GO:0019542
HAMAP MF_00020
InterPro IPR004372
IPR000890
IPR023865
PANTHER PTHR21060
Pfam PF00871
PIRSF PIRSF000722
PRINTS PR00471
TIGRFAMs TIGR00016
PROSITE PS01075
PS01076

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0003922

GMP synthase (glutamine-hydrolyzing) activity

PMID:1356964[1]

ECO:0000315

F

Table 2 shows that ackA had little effect on the wild type when considering the synthesis of glutamine synthetase.

complete

involved_in

GO:0044011

single-species biofilm formation on inanimate substrate

PMID:12753190[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006083

acetate metabolic process

PMID:21941[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:16858726[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0019542

propionate biosynthetic process

PMID:9484901[5]

ECO:0000316

genetic interaction evidence used in manual assertion

EcoliWiki:tdcD

P

Seeded From UniProt

complete

involved_in

GO:0019413

acetate biosynthetic process

PMID:9484901[5]

ECO:0000316

genetic interaction evidence used in manual assertion

EcoliWiki:tdcD

P

Seeded From UniProt

complete

enables

GO:0008776

acetate kinase activity

PMID:2536666[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:11985624[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006082

organic acid metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004372

P

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000890
InterPro:IPR004372
InterPro:IPR023865

F

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000890
InterPro:IPR023865

P

Seeded From UniProt

complete

enables

GO:0016774

phosphotransferase activity, carboxyl group as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000890
InterPro:IPR004372
InterPro:IPR023865

F

Seeded From UniProt

complete

enables

GO:0008776

acetate kinase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.7.2.1

F

Seeded From UniProt

complete

enables

GO:0008776

acetate kinase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000037499

F

Seeded From UniProt

complete

GO:0006083

acetate metabolic process

PMID:21941[3]

ECO:0000315

P

Fig 1: showed decreased acetate production in the mutant phenotype.

complete
CACAO 1990

GO:0044011

single-species biofilm formation on inanimate substrate

PMID:12753190[2]

ECO:0000315

P

Fig. 6: formation of microcolonies and pellicle

complete
CACAO 2003

involved_in

GO:0016310

phosphorylation

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000037499

P

Seeded From UniProt

complete

GO:0008776

acetate kinase activity

PMID:2536666[6]

ECO:0000315

F

Table 1

complete
CACAO 4501

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000037499

C

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000037499

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

involved_in

GO:0016310

phosphorylation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

P

Seeded From UniProt

complete

enables

GO:0016301

kinase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0418

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0006085

acetyl-CoA biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00340

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Feng, J et al. (1992) Role of phosphorylated metabolic intermediates in the regulation of glutamine synthetase synthesis in Escherichia coli. J. Bacteriol. 174 6061-70 PubMed GONUTS page
  2. 2.0 2.1 Wolfe, AJ et al. (2003) Evidence that acetyl phosphate functions as a global signal during biofilm development. Mol. Microbiol. 48 977-88 PubMed GONUTS page
  3. 3.0 3.1 Brown, TD et al. (1977) The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli. J. Gen. Microbiol. 102 327-36 PubMed GONUTS page
  4. 4.0 4.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  5. 5.0 5.1 Hesslinger, C et al. (1998) Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate. Mol. Microbiol. 27 477-92 PubMed GONUTS page
  6. 6.0 6.1 Matsuyama, A et al. (1989) Cloning, expression, and nucleotide sequence of the Escherichia coli K-12 ackA gene. J. Bacteriol. 171 577-80 PubMed GONUTS page
  7. Katayama, A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur. J. Biochem. 269 2403-13 PubMed GONUTS page
  8. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  9. Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page