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Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis.

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation2 Publications

Cofactori

Mg2+UniRule annotation1 Publication

Kineticsi

  1. KM=0.15 mM for ATP (at pH 8.5 and 37 degrees Celsius)1 Publication
  2. KM=0.2 mM for CoA (at pH 8.5 and 37 degrees Celsius)1 Publication
  3. KM=0.2 mM for acetate (at pH 8.5 and 37 degrees Celsius)1 Publication
  1. Vmax=100 nmol/min/mg enzyme (at pH 8.5 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 8.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei311 – 3111Coenzyme AUniRule annotation
Binding sitei335 – 3351Coenzyme AUniRule annotation
Binding sitei500 – 5001ATPUniRule annotation
Binding sitei515 – 5151ATPUniRule annotation
Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation
Binding sitei526 – 5261ATPUniRule annotation
Metal bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei584 – 5841Coenzyme AUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi387 – 3893ATPUniRule annotation
Nucleotide bindingi411 – 4166ATPUniRule annotation

GO - Molecular functioni

  • acetate-CoA ligase activity Source: CACAO
  • AMP binding Source: InterPro
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • propionate-CoA ligase activity Source: EcoCyc
  • protein deacetylase activity Source: CACAO

GO - Biological processi

  • acetate catabolic process Source: EcoCyc
  • acetyl-CoA biosynthetic process from acetate Source: UniProtKB-HAMAP
  • chemotaxis Source: UniProtKB-HAMAP
  • peptidyl-lysine acetylation Source: CACAO
  • post-translational protein acetylation Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ACS-MONOMER.
ECOL316407:JW4030-MONOMER.
MetaCyc:ACS-MONOMER.
SABIO-RKP27550.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
Short name:
AcCoA synthetaseUniRule annotation
Short name:
AcsUniRule annotation
Alternative name(s):
Acetate--CoA ligaseUniRule annotation
Acyl-activating enzymeUniRule annotation
Gene namesi
Name:acsUniRule annotation
Synonyms:yfaC
Ordered Locus Names:b4069, JW4030
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11448. acs.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene grow as well as wild-type cells at high concentrations (>25 mM) of acetate as the sole carbon source, but grow poorly on lower concentrations (<10 mM).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 652652Acetyl-coenzyme A synthetasePRO_0000208362Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei609 – 6091N6-acetyllysineUniRule annotation1 Publication

Post-translational modificationi

Autoacetylated. Deacetylation by CobB activates the enzyme.

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP27550.
PaxDbiP27550.
PRIDEiP27550.

Expressioni

Inductioni

By CRP and FNR, in response to rising cAMP levels, falling oxygen partial pressure and changes in carbon flux. May also be induced by acetate.1 Publication

Interactioni

Subunit structurei

Forms a 1:1 complex with CobB/NAD-dependent deacetylase.

Protein-protein interaction databases

BioGridi4262675. 10 interactions.
IntActiP27550. 7 interactions.
STRINGi511145.b4069.

Structurei

3D structure databases

ProteinModelPortaliP27550.
SMRiP27550. Positions 5-647.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 1944Coenzyme A bindingUniRule annotation

Sequence similaritiesi

Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
InParanoidiP27550.
KOiK01895.
OMAiPMDSEDM.
OrthoDBiEOG68WR2H.
PhylomeDBiP27550.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27550-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQIHKHTIP ANIADRCLIN PQQYEAMYQQ SINVPDTFWG EQGKILDWIK
60 70 80 90 100
PYQKVKNTSF APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD
110 120 130 140 150
DASQSKHISY KELHRDVCRF ANTLLELGIK KGDVVAIYMP MVPEAAVAML
160 170 180 190 200
ACARIGAVHS VIFGGFSPEA VAGRIIDSNS RLVITSDEGV RAGRSIPLKK
210 220 230 240 250
NVDDALKNPN VTSVEHVVVL KRTGGKIDWQ EGRDLWWHDL VEQASDQHQA
260 270 280 290 300
EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAALTFK YVFDYHPGDI
310 320 330 340 350
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMAQVVDKHQ
360 370 380 390 400
VNILYTAPTA IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK
410 420 430 440 450
KIGNEKCPVV DTWWQTETGG FMITPLPGAT ELKAGSATRP FFGVQPALVD
460 470 480 490 500
NEGNPLEGAT EGSLVITDSW PGQARTLFGD HERFEQTYFS TFKNMYFSGD
510 520 530 540 550
GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP KIAEAAVVGI
560 570 580 590 600
PHNIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD
610 620 630 640 650
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM

PS
Length:652
Mass (Da):72,094
Last modified:October 1, 1993 - v2
Checksum:iF464062B6E82C099
GO

Sequence cautioni

The sequence AAA24715.1 differs from that shown. Reason: Frameshift at position 323. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA. Translation: AAC43163.1.
U00096 Genomic DNA. Translation: AAC77039.1.
AP009048 Genomic DNA. Translation: BAE78071.1.
M87509 Genomic DNA. Translation: AAA24715.1. Frameshift.
PIRiD65215.
RefSeqiNP_418493.1. NC_000913.3.
WP_000078239.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77039; AAC77039; b4069.
BAE78071; BAE78071; BAE78071.
GeneIDi948572.
KEGGiecj:JW4030.
eco:b4069.
PATRICi32123687. VBIEscCol129921_4192.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00006 Genomic DNA. Translation: AAC43163.1.
U00096 Genomic DNA. Translation: AAC77039.1.
AP009048 Genomic DNA. Translation: BAE78071.1.
M87509 Genomic DNA. Translation: AAA24715.1. Frameshift.
PIRiD65215.
RefSeqiNP_418493.1. NC_000913.3.
WP_000078239.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP27550.
SMRiP27550. Positions 5-647.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262675. 10 interactions.
IntActiP27550. 7 interactions.
STRINGi511145.b4069.

Proteomic databases

EPDiP27550.
PaxDbiP27550.
PRIDEiP27550.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77039; AAC77039; b4069.
BAE78071; BAE78071; BAE78071.
GeneIDi948572.
KEGGiecj:JW4030.
eco:b4069.
PATRICi32123687. VBIEscCol129921_4192.

Organism-specific databases

EchoBASEiEB1417.
EcoGeneiEG11448. acs.

Phylogenomic databases

eggNOGiENOG4108IQF. Bacteria.
COG0365. LUCA.
HOGENOMiHOG000229981.
InParanoidiP27550.
KOiK01895.
OMAiPMDSEDM.
OrthoDBiEOG68WR2H.
PhylomeDBiP27550.

Enzyme and pathway databases

BioCyciEcoCyc:ACS-MONOMER.
ECOL316407:JW4030-MONOMER.
MetaCyc:ACS-MONOMER.
SABIO-RKP27550.

Miscellaneous databases

PROiP27550.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR032387. ACAS_N.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF16177. ACAS_N. 1 hit.
PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "Isolation and characterization of Escherichia coli mutants affected in aerobic respiration: the cloning and nucleotide sequence of ubiG. Identification of an S-adenosylmethionine-binding motif in protein, RNA, and small-molecule methyltransferases."
    Wu G., Williams H.D., Zamanian M., Gibson F., Poole R.K.
    J. Gen. Microbiol. 138:2101-2112(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 299-652.
    Strain: K12.
  5. "The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli."
    Brown T.D., Jones-Mortimer M.C., Kornberg H.L.
    J. Gen. Microbiol. 102:327-336(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
  6. "Cloning, characterization, and functional expression of acs, the gene which encodes acetyl coenzyme A synthetase in Escherichia coli."
    Kumari S., Tishel R., Eisenbach M., Wolfe A.J.
    J. Bacteriol. 177:2878-2886(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
  7. Cited for: INDUCTION.
    Strain: K12.
  8. "Acetyladenylate or its derivative acetylates the chemotaxis protein CheY in vitro and increases its activity at the flagellar switch."
    Barak R., Welch M., Yanovsky A., Oosawa K., Eisenbach M.
    Biochemistry 31:10099-10107(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION OF CHEY.
  9. "Both acetate kinase and acetyl coenzyme A synthetase are involved in acetate-stimulated change in the direction of flagellar rotation in Escherichia coli."
    Barak R., Abouhamad W.N., Eisenbach M.
    J. Bacteriol. 180:985-988(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CHEMOTAXIS.
  10. "Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis."
    Barak R., Eisenbach M.
    Mol. Microbiol. 40:731-743(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CHEMOTAXIS.
  11. "Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli."
    Zhao K., Chai X., Marmorstein R.
    J. Mol. Biol. 337:731-741(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COBB, DEACETYLATION.
  12. "Acetylation of the chemotaxis response regulator CheY by acetyl-CoA synthetase purified from Escherichia coli."
    Barak R., Prasad K., Shainskaya A., Wolfe A.J., Eisenbach M.
    J. Mol. Biol. 342:383-401(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOACETYLATION AT LYS-609.
  13. "CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY."
    Li R., Gu J., Chen Y.Y., Xiao C.L., Wang L.W., Zhang Z.P., Bi L.J., Wei H.P., Wang X.D., Deng J.Y., Zhang X.E.
    Mol. Microbiol. 76:1162-1174(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEACETYLATION.

Entry informationi

Entry nameiACSA_ECOLI
AccessioniPrimary (citable) accession number: P27550
Secondary accession number(s): Q2M6N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 1, 1993
Last modified: July 6, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.