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Q8ZKF6 (ACSA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase
Short name=AcCoA synthetase
Short name=Acs
EC=6.2.1.1
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene names
Name:acs
Ordered Locus Names:STM4275
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

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 By similarity. Ref.4

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123

Cofactor

Magnesium.

Subunit structure

Homodimer. Ref.3 Ref.4

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme. HAMAP-Rule MF_01123

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=77.1 µM for ATP (at pH 7.5 and at 37 degrees Celsius) Ref.4

KM=50 µM for CoA (at pH 7.5 and at 37 degrees Celsius)

KM=6047 µM for acetate (at pH 7.5 and at 37 degrees Celsius)

KM=9413 µM for propionate (at pH 7.5 and at 37 degrees Celsius)

KM=9450 µM for glycine (at pH 7.5 and at 37 degrees Celsius)

Mass spectrometry

Molecular mass is 733.4 Da from positions 607 - 612. Determined by MALDI. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 652652Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
PRO_0000208386

Regions

Region191 – 1944Coenzyme A HAMAP-Rule MF_01123
Region411 – 4166Substrate binding HAMAP-Rule MF_01123

Sites

Active site5171
Metal binding5371Magnesium; via carbonyl oxygen
Metal binding5391Magnesium; via carbonyl oxygen
Metal binding5421Magnesium; via carbonyl oxygen
Binding site3111Coenzyme A
Binding site3351Coenzyme A
Binding site3871Substrate; via amide nitrogen
Binding site5001Substrate
Binding site5151Substrate
Binding site5231Coenzyme A
Binding site5261Substrate
Binding site5841Coenzyme A

Amino acid modifications

Modified residue6091N6-acetyllysine Ref.2

Experimental info

Mutagenesis1941R → A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 3-fold reduction for CoA. Ref.4
Mutagenesis1941R → E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 2-fold reduction for CoA. Ref.4
Mutagenesis3571A → V: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 3-fold reduction for CoA. Ref.4
Mutagenesis5171D → G: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 10-fold reduction for CoA.
Mutagenesis5171D → P: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold reduction in the affinity for ATP and 4.5-fold reduction for CoA.
Mutagenesis5241G → L: No acetyl-coenzyme A synthetase activity. Ref.4
Mutagenesis5241G → S: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. Almost the same affinity as the wild-type for ATP, but 9-fold reduction in the affinity for CoA. Ref.4
Mutagenesis5261R → A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 4-fold reduction for CoA. Ref.4
Mutagenesis5841R → A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 7-fold reduction for CoA. Ref.4
Mutagenesis5841R → E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 8-fold reduction for CoA. Ref.4
Mutagenesis6091K → A: No acetyl-coenzyme A synthetase activity. Ref.4

Secondary structure

1 ............................................................................................................... 652
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8ZKF6 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 347209D1D3D349D8

FASTA65272,153
        10         20         30         40         50         60 
MSQTHKHAIP ANIADRCLIN PEQYETKYKQ SINDPDTFWG EQGKILDWIT PYQKVKNTSF 

        70         80         90        100        110        120 
APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD DTSQSKHISY RELHRDVCRF 

       130        140        150        160        170        180 
ANTLLDLGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSSS 

       190        200        210        220        230        240 
RLVITADEGV RAGRSIPLKK NVDDALKNPN VTSVEHVIVL KRTGSDIDWQ EGRDLWWRDL 

       250        260        270        280        290        300 
IEKASPEHQP EAMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPGDI 

       310        320        330        340        350        360 
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMCQVVDKHQ VNILYTAPTA 

       370        380        390        400        410        420 
IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK KIGKEKCPVV DTWWQTETGG 

       430        440        450        460        470        480 
FMITPLPGAI ELKAGSATRP FFGVQPALVD NEGHPQEGAT EGNLVITDSW PGQARTLFGD 

       490        500        510        520        530        540 
HERFEQTYFS TFKNMYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP 

       550        560        570        580        590        600 
KIAEAAVVGI PHAIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD 

       610        620        630        640        650 
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM PS

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine."
Starai V.J., Celic I., Cole R.N., Boeke J.D., Escalante-Semerena J.C.
Science 298:2390-2392(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-609, DEACETYLATION BY SIR2 HOMOLOG, MASS SPECTROMETRY.
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5'-propylphosphate and coenzyme A."
Gulick A.M., Starai V.J., Horswill A.R., Homick K.M., Escalante-Semerena J.C.
Biochemistry 42:2866-2873(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), SUBUNIT.
[4]"Biochemical and crystallographic analysis of substrate binding and conformational changes in acetyl-CoA synthetase."
Reger A.S., Carney J.M., Gulick A.M.
Biochemistry 46:6536-6546(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF WILD-TYPE AND MUTANTS IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS, FUNCTION, MUTAGENESIS OF ARG-194; ALA-357; GLY-524; ARG-526; ARG-584 AND LYS-609, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE006468 Genomic DNA. Translation: AAL23099.1.
RefSeqNP_463140.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PG3X-ray2.30A/B1-652[»]
1PG4X-ray1.75A/B1-652[»]
2P20X-ray2.22A/B1-652[»]
2P2BX-ray2.20A/B1-652[»]
2P2FX-ray2.58A/B1-652[»]
2P2JX-ray2.30A/B1-652[»]
2P2MX-ray2.11A/B1-652[»]
2P2QX-ray2.42A/B1-652[»]
ProteinModelPortalQ8ZKF6.
SMRQ8ZKF6. Positions 5-647.
ModBaseSearch...

Protein-protein interaction databases

STRING99287.STM4275.

Proteomic databases

PaxDbQ8ZKF6.
PRIDEQ8ZKF6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL23099; AAL23099; STM4275.
GeneID1255801.
KEGGstm:STM4275.
PATRIC32387457. VBISalEnt20916_4496.

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAPPIKRSC.
ProtClustDBPRK00174.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR024597. Acyl-CoA_synth_DUF3448.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR025110. DUF4009.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF11930. DUF3448. 1 hit.
PF13193. DUF4009. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8ZKF6.

Entry information

Entry nameACSA_SALTY
AccessionPrimary (citable) accession number: Q8ZKF6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: March 1, 2002
Last modified: May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents