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Reviewed, UniProtKB/Swiss-Prot A8AN29 (ACSA_CITK8)

Last modified February 9, 2010. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

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: CKO_03816
OrganismCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) [Complete proteome] [HAMAP]
Taxonomic identifier290338 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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

Post-translational modification

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

Sequence similarities

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

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete 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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 652652Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000065289

Sites

Active site5171 By similarity

Amino acid modifications

Modified residue6091N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8AN29-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 1D3F4F3CDF8CBE74

FASTA65272,106
        10         20         30         40         50         60 
MSQIHKHAIP ANIADRCLIN PEQYEAKYQQ SINEPDTFWG EQGKILDWIT PYKKVKNTSF 

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

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

       190        200        210        220        230        240 
RLVITADEGV RAGRGIPLKK NVDDALKNPN VNSVEHVVVL KRTGGKVDWH EGRDLWWSDV 

       250        260        270        280        290        300 
IEKSSADHQP EEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPDDI 

       310        320        330        340        350        360 
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMAQVVDKHQ VTILYTAPTA 

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

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

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

       550        560        570        580        590        600 
KIAEAAVVGI PHNIKGQAIY AYVTLNHGED PSPELYTEVR NWVRKEIGPL ATPDVLHWTD 

       610        620        630        640        650 
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM PS 

« Hide

References

[1]McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000822 Genomic DNA. Translation: ABV14892.1.
RefSeqYP_001455328.1.

3D structure databases

SMRA8AN29. Positions 5-647.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8AN29.

Genome annotation databases

GeneID5581318.
GenomeReviewsGene locus CKO_03816 in contig CP000822_GR.
KEGGcko:CKO_03816.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHBG547964.
OMAETASEHC.

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...

Entry information

Entry nameACSA_CITK8
AccessionPrimary (citable) accession number: A8AN29
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: February 9, 2010
This is version 18 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)

Relevant documents

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