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ECOLI:ACSA
Contents
Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
Gene Name(s) | acs (ECO:0000255 with HAMAP-Rule:MF_01123) (synonyms: yfaC) | |
Protein Name(s) | Acetyl-coenzyme A synthetase (ECO:0000255 with HAMAP-Rule:MF_01123)
AcCoA synthetase (ECO:0000255 with HAMAP-Rule:MF_01123) Acs (ECO:0000255 with HAMAP-Rule:MF_01123) Acetate--CoA ligase (ECO:0000255 with HAMAP-Rule:MF_01123) Acyl-activating enzyme (ECO:0000255 with HAMAP-Rule:MF_01123) | |
External Links | ||
UniProt | P27550 | |
EMBL | U00006 U00096 AP009048 M87509 | |
PIR | D65215 | |
RefSeq | NP_418493.1 YP_492212.1 | |
ProteinModelPortal | P27550 | |
SMR | P27550 | |
IntAct | P27550 | |
STRING | 511145.b4069 | |
PaxDb | P27550 | |
PRIDE | P27550 | |
EnsemblBacteria | AAC77039 BAE78071 | |
GeneID | 12933681 948572 | |
KEGG | ecj:Y75_p3956 eco:b4069 | |
PATRIC | 32123687 | |
EchoBASE | EB1417 | |
EcoGene | EG11448 | |
eggNOG | COG0365 | |
HOGENOM | HOG000229981 | |
InParanoid | P27550 | |
KO | K01895 | |
OMA | SHRCLTI | |
OrthoDB | EOG68WR2H | |
PhylomeDB | P27550 | |
BioCyc | EcoCyc:ACS-MONOMER ECOL316407:JW4030-MONOMER MetaCyc:ACS-MONOMER | |
PRO | PR:P27550 | |
Proteomes | UP000000318 UP000000625 | |
Genevestigator | P27550 | |
GO | GO:0003987 GO:0016208 GO:0005524 GO:0046872 GO:0050218 GO:0033558 GO:0045733 GO:0019427 GO:0006935 GO:0018394 GO:0034421 GO:0006476 | |
HAMAP | MF_01123 | |
InterPro | IPR011904 IPR025110 IPR020845 IPR000873 | |
Pfam | PF00501 PF13193 | |
TIGRFAMs | TIGR02188 | |
PROSITE | PS00455 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0003987 |
acetate-CoA ligase activity |
ECO:0000314 |
F |
Figure 9. Also, Table 3 shows that Acs deficient strains were not able to activate acetate as well as the wild-type strain. |
complete | |||||
GO:0018394 |
peptidyl-lysine acetylation |
ECO:0000314 |
P |
Figure 3. Purified Acs was incubated with ATP, Mg2+, and acetate. Western blotting with anti-acetyl-lysine antibody showed lysine acetylation of Acs. |
complete | |||||
GO:0034421 |
post-translational protein acetylation |
ECO:0000314 |
P |
Figure 3. Purified Acs was incubated with Mg2+, ATP, and acetate. Acs showed acetylation. |
complete | |||||
GO:0033558 |
protein deacetylase activity |
ECO:0000314 |
F |
Figure 5b. Acs can catalyze deacetylation of CheY. |
complete | |||||
involved_in |
GO:0034421 |
post-translational protein acetylation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0033558 |
protein deacetylase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0018394 |
peptidyl-lysine acetylation |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0003987 |
acetate-CoA ligase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0045733 |
acetate catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0050218 |
propionate-CoA ligase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0045733 |
acetate catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0003987 |
acetate-CoA ligase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006476 |
protein deacetylation |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0033558 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003987 |
acetate-CoA ligase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016208 |
AMP binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0019427 |
acetyl-CoA biosynthetic process from acetate |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0003987 |
acetate-CoA ligase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0019427 |
acetyl-CoA biosynthetic process from acetate |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000100676 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0003987 |
acetate-CoA ligase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000100676 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006935 |
chemotaxis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000100676 |
P |
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:0005524 |
ATP binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0000166 |
nucleotide binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016874 |
ligase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
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 Kumari, S et al. (1995) Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli. J. Bacteriol. 177 2878-86 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 2.4 Barak, R et al. (2004) Acetylation of the chemotaxis response regulator CheY by acetyl-CoA synthetase purified from Escherichia coli. J. Mol. Biol. 342 383-401 PubMed GONUTS page
- ↑ 3.0 3.1 Barak, R et al. (2006) The chemotaxis response regulator CheY can catalyze its own acetylation. J. Mol. Biol. 359 251-65 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page