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SALTY:ACKA
Contents
| 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 |
ECO:0000314 |
F |
Table 1 shows kinetic properties of the kinase activity that purified StAckA has on acetate. |
complete | |||||
| GO:0047900 |
formate kinase activity |
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 | |||||
| GO:0008980 |
propionate kinase activity |
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 | |||||
| GO:0008776 |
acetate kinase activity |
ECO:0000315 |
F |
This study provides necessary information by inactivating genes and seeing the effects |
complete | |||||
|
enables |
GO:0047900 |
formate kinase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008980 |
propionate kinase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008776 |
acetate kinase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006082 |
organic acid metabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016301 |
kinase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0016310 |
phosphorylation |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016774 |
phosphotransferase activity, carboxyl group as acceptor |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008776 |
acetate kinase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000287 |
magnesium ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000037499 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0016310 |
phosphorylation |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000037499 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000037499 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008776 |
acetate kinase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000037499 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0016310 |
phosphorylation |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000166 |
nucleotide binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0005524 |
ATP binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016740 |
transferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016301 |
kinase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006085 |
acetyl-CoA biosynthetic process |
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.
- ↑ 1.0 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
- ↑ 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