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B5R939 (B5R939_SALG2) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
Short name=AcCoA synthetase HAMAP-Rule MF_01123
Short name=Acs HAMAP-Rule MF_01123
EC=6.2.1.1 HAMAP-Rule MF_01123
Alternative name(s):
Acetate--CoA ligase HAMAP-Rule MF_01123
Acyl-activating enzyme HAMAP-Rule MF_01123
Gene names
Name:acs HAMAP-Rule MF_01123
Ordered Locus Names:SG4119
OrganismSalmonella gallinarum (strain 287/91 / NCTC 13346) [Complete proteome] [HAMAP] EMBL CAR39886.1
Taxonomic identifier550538 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

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

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA 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. HAMAP-Rule MF_01123 SAAS SAAS020845

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. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

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

Sites

Active site5171 By similarity HAMAP-Rule MF_01123
Metal binding5371Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5391Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5421Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3111Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3351Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3871Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5001Substrate By similarity HAMAP-Rule MF_01123
Binding site5151Substrate By similarity HAMAP-Rule MF_01123
Binding site5231Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5261Substrate By similarity HAMAP-Rule MF_01123
Binding site5841Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6091N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
B5R939 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: 5544EBC7416BEEF5

FASTA65272,181
        10         20         30         40         50         60 
MSQTHKHAIP ANIADRCLIN PEQYETKYKQ SINDPDTFWG EQGKILDWIT PYQKVKNTSF 

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

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

       190        200        210        220        230        240 
RLVITADEGV RAGRSIPLKK NVDDALKNPN VTSVEHVIVL KRTDSDIDWQ 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

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References

[1]"Comparative genome analysis of Salmonella Enteritidis PT4 and Salmonella Gallinarum 287/91 provides insights into evolutionary and host adaptation pathways."
Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. expand/collapse author list , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Sanders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphrey T., Roberts M., Barrow P.A., Dougan G., Parkhill J.
Genome Res. 18:1624-1637(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 287/91 / NCTC 13346.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM933173 Genomic DNA. Translation: CAR39886.1.
RefSeqYP_002228846.1. NC_011274.1.

3D structure databases

ProteinModelPortalB5R939.
ModBaseSearch...

Protein-protein interaction databases

STRING550538.SG4119.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR39886; CAR39886; SG4119.
GeneID6926009.
KEGGseg:SG4119.
PATRIC18507047. VBISalEnt1629_4376.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAPPIKRSC.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycSENT550538:GJ93-4067-MONOMER.

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 nameB5R939_SALG2
AccessionPrimary (citable) accession number: B5R939
Entry history
Integrated into UniProtKB/TrEMBL: November 4, 2008
Last sequence update: November 4, 2008
Last modified: May 1, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info