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SALTY:ACKA

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Species (Taxon ID) Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). (99287)
Gene Name(s) ackA (ECO:0000255 with HAMAP-Rule:MF_00020)
Protein Name(s) Acetate kinase (ECO:0000255 with HAMAP-Rule:MF_00020)

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

External Links
UniProt P63411
EMBL AE006468
RefSeq NP_461279.1
PDB 3SK3
3SLC
PDBsum 3SK3
3SLC
ProteinModelPortal P63411
STRING 99287.STM2337
PaxDb P63411
PRIDE P63411
EnsemblBacteria AAL21238
GeneID 1253859
KEGG stm:STM2337
PATRIC 32383289
eggNOG COG0282
HOGENOM HOG000288398
KO K00925
OMA IDMANEK
OrthoDB EOG69975F
PhylomeDB P63411
BioCyc SENT99287:GCTI-2352-MONOMER
UniPathway UPA00340
Proteomes UP000001014
GO GO:0005737
GO:0008776
GO:0005524
GO:0047900
GO:0000287
GO:0008980
GO:0006085
GO:0006082
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:0008776

acetate kinase activity

PMID:23031654[1]

ECO:0000314

F

Table 1 shows kinetic properties of the kinase activity that purified StAckA has on acetate.

complete
CACAO 5562

GO:0047900

formate kinase activity

PMID:23031654[1]

ECO:0000314

F

Table 1 shows kinetic properties of the kinase activity that purified StAckA has on formate. "It was observed that StAckA could catalyze phosphate transfer at significant rate from ATP to formate"

complete
CACAO 5563

GO:0008980

propionate kinase activity

PMID:23031654[1]

ECO:0000314

F

Table 1 shows that kinetic properties of purified StAckA kinase activity on propionate. "It was observed that StAckA could catalyze phosphate transfer at significant rate from ATP to ... propionate"

complete
CACAO 5564

GO:0008776

acetate kinase activity

PMID:25642214[2]

ECO:0000315

F

This study provides necessary information by inactivating genes and seeing the effects

complete
CACAO 10597

enables

GO:0047900

formate kinase activity

PMID:23031654[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008980

propionate kinase activity

PMID:23031654[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008776

acetate kinase activity

PMID:23031654[1]

ECO:0000314

direct assay evidence used in manual assertion

F

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: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

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

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: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

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: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

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: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

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: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

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. 1.0 1.1 1.2 1.3 1.4 1.5 Chittori, S et al. (2012) Structural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identification of a putative ligand binding pocket at the dimeric interface. BMC Struct. Biol. 12 24 PubMed GONUTS page
  2. Marx, P et al. (2014) Activity of the response regulator CiaR in mutants of Streptococcus pneumoniae R6 altered in acetyl phosphate production. Front Microbiol 5 772 PubMed GONUTS page