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A4TS06 (ACSA_YERPP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:YPDSF_3718
OrganismYersinia pestis (strain Pestoides F) [Complete proteome] [HAMAP]
Taxonomic identifier386656 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia ›

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_01123

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-Rule MF_01123

Catalytic activity

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

Cofactor

Magnesium By similarity.

Post-translational modification

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 652652Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
PRO_1000065336

Regions

Region191 – 1944Coenzyme A By similarity
Region411 – 4166Substrate binding By similarity

Sites

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

Amino acid modifications

Modified residue6091N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4TS06 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 933CF5A79F7E4D63

FASTA65272,072
        10         20         30         40         50         60 
MSQIHKHPIP AAIAEHALIT PEKYQHYYQQ SVQNPDEFWG EQGKIIDWIK PYKTVKNTSF 

        70         80         90        100        110        120 
DPGHVSIRWF EDGTLNLAAN CLDRHLAERG DQTAIIWEGD DPNQSKTVTY KQLHHDVCQF 

       130        140        150        160        170        180 
ANVLKSLGVK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPDA VAGRIIDSHS 

       190        200        210        220        230        240 
KLVITADEGI RAGRAIPLKK NVDEALKNPA ITSIKNVVVF QRTGNASYWE DGRDVWWHDL 

       250        260        270        280        290        300 
IKEASADCPP EEMNAEDPLF ILYTSGSTGK PKGVVHTTGG YLVYAALTFK YVFDYHPGDI 

       310        320        330        340        350        360 
YWCTADVGWV TGHSYLLYGP LACGAITLMF EGVPNYPGVN RLSQVVDKHK VNILYTAPTA 

       370        380        390        400        410        420 
IRALMAEGDK AIEGTKRDSL RIMGSVGEPI NPEAWEWYYN KIGNSKCPIV DTWWQTETGG 

       430        440        450        460        470        480 
FMITPLPGAT ELKAGSATRP FFGVQPALVD NLGNPQEGVA EGNLVITDSW PGQARTLFGD 

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

       550        560        570        580        590        600 
KIAEAAVVGV PHNIKGQAIY AYITLNHGEE PTPELYTEVR NWVRKEIGPL ATPDILHWTD 

       610        620        630        640        650 
SLPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPSVVEK LLEEKQSMQT PS

« Hide

References

[1]"Complete sequence of chromosome of Yersinia pestis Pestoides F."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pestoides F.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000668 Genomic DNA. Translation: ABP42068.1.
RefSeqYP_001165041.1. NC_009381.1.

3D structure databases

ProteinModelPortalA4TS06.
SMRA4TS06. Positions 5-647.
ModBaseSearch...

Protein-protein interaction databases

STRING386656.YPDSF_3718.

Proteomic databases

PRIDEA4TS06.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP42068; ABP42068; YPDSF_3718.
GeneID5063053.
KEGGypp:YPDSF_3718.
PATRIC18617513. VBIYerPes122972_4612.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAAISKHEM.
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...

Entry information

Entry nameACSA_YERPP
AccessionPrimary (citable) accession number: A4TS06
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 15, 2007
Last modified: May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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