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Reviewed, UniProtKB/Swiss-Prot Q8ZKF6 (ACSA_SALTY)

Last modified February 9, 2010. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Acetyl-coenzyme A synthetase
    EC=6.2.1.1
Alternative name(s):
    Acetate--CoA ligase
    Acyl-activating enzyme
Gene names
Name: acs
Ordered Locus Names: STM4275
OrganismSalmonella typhimurium [Complete proteome] [HAMAP]
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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Protein attributes

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

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General annotation (Comments)

Function

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. HAMAP MF_01123

Catalytic activity

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

Subunit structure

Monomer. HAMAP MF_01123

Post-translational modification

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

Sequence similarities

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

Mass spectrometry

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

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Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionAMP binding

Inferred from electronic annotation. Source: InterPro

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetate-CoA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 652652Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_0000208386

Sites

Active site5171 HAMAP MF_01123

Amino acid modifications

Modified residue6091N6-acetyllysine Ref.2

Secondary structure

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

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q8ZKF6-1 [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

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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: 11677609] [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: 12493915] [Abstract]
Cited for: ACETYLATION AT LYS-609 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: 12627952] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) AND OF ACETYLATED PROTEIN (2.3 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

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

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[»]
ModBaseSearch...

Proteomic databases

PRIDEQ8ZKF6.

Genome annotation databases

GeneID1255801.
GenomeReviewsGene locus STM4275 in contig AE006468_GR.
KEGGstm:STM4275.
NMPDRfig|99287.1.peg.4113.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG547964.
OMAETASEHC.

Enzyme and pathway databases

BioCycSTYP99287:STM4275-MONOMER.
BRENDA6.2.1.1. 2.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
[Tree]
InterProIPR011904. Ac_CoA_lig_AcsA.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: February 9, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents