Skip Header

Contribute Send feedback
Read comments (?) or add your own

A7MPJ7 (ACSA_CROS8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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

EC=6.2.1.1
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene names
Name:acs
Ordered Locus Names:ESA_00122
OrganismCronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) [Complete proteome] [HAMAP]
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

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)
   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 652652Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000065290

Sites

Active site5171 By similarity

Amino acid modifications

Modified residue6091N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7MPJ7 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: E13500326E51D759

FASTA65271,752
        10         20         30         40         50         60 
MSQIHKHPIP AAIAERCLIT PEQYDAKYQQ SVHDPDAFWG EQGKILDWIT PYQTVKNTSF 

        70         80         90        100        110        120 
APGNVSIKWY EDGTLNLAAN CLDRHLSERG DQTAIIWEGD DATQSKHISY RELHRDVCRF 

       130        140        150        160        170        180 
ANTLTSLGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSSA 

       190        200        210        220        230        240 
RLVITADEGV RAGRAIPLKK NVDDALKNPG VTSVEHVVVF KRTGGNIEWH EGRDLWWSEL 

       250        260        270        280        290        300 
VKKASAHHQP VEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFL YAFDYHPGDI 

       310        320        330        340        350        360 
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPSAN RMAQVVDKHK VNILYTAPTA 

       370        380        390        400        410        420 
IRALMAEGDK AIDGTDRSSL RILGSVGEPI NPEAWEWYWK KIGNEKCPVI DTWWQTETGG 

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

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

       550        560        570        580        590        600 
KIAEAAVVGI PHSIKGQAIY AYVTLNHGEE PSAELYSEVR NWVRKEIGPL ATPDVLHWTD 

       610        620        630        640        650 
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQSIAM PS 

« Hide

References

[1]"Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species."
Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J.
PLoS ONE 5:E9556-E9556(2010) [PubMed: 20221447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-894.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000783 Genomic DNA. Translation: ABU75427.1.
RefSeqYP_001436263.1. NC_009778.1.

3D structure databases

ProteinModelPortalA7MPJ7.
SMRA7MPJ7. Positions 5-647.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7MPJ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5549082.
GenomeReviewsGene locus ESA_00122 in contig CP000783_GR.
KEGGesa:ESA_00122.
PATRIC20392563. VBICroSak107175_0109.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHBG547964.
OMALIQWAGG.
ProtClustDBPRK00174.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
[Tree]
InterProIPR011904. Ac_CoA_lig.
IPR024597. Acyl-CoA_synth_DUF3448.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
KOK01895.
PANTHERPTHR24095:SF42. PTHR24095:SF42. 1 hit.
PfamPF00501. AMP-binding. 1 hit.
PF11930. DUF3448. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACSA_CROS8
AccessionPrimary (citable) accession number: A7MPJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 2, 2007
Last modified: January 25, 2012
This is version 29 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