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I2EEB1 (I2EEB1_CROSK) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 13. 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 EMBL AFJ98013.1
ORF Names:ES15_0440 EMBL AFJ98013.1
OrganismCronobacter sakazakii ES15 [Complete proteome] EMBL AFJ98013.1
Taxonomic identifier1138308 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

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
I2EEB1 [UniParc].

Last modified July 11, 2012. Version 1.
Checksum: D14199F1015FBDFD

FASTA65271,733
        10         20         30         40         50         60 
MSQIHKHPIP AAIAERCLIT PEQYDAKYQQ SVHDPDAFWG EQGKILDWIT PYQTVKNTSF 

        70         80         90        100        110        120 
APGNISIKWY 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 VTSVEHVVVL KRTGGNIEWH EGRDLWWSEL 

       250        260        270        280        290        300 
VEKASAHHQP 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 

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References

[1]"Complete Genome Sequence of the Opportunistic Food-Borne Pathogen Cronobacter sakazakii ES15."
Shin H., Lee J.H., Choi Y., Ryu S.
J. Bacteriol. 194:4438-4439(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ES15 EMBL AFJ98013.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003312 Genomic DNA. Translation: AFJ98013.1.
RefSeqYP_006341524.1. NC_017933.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFJ98013; AFJ98013; ES15_0440.
GeneID13032260.
KEGGcsk:ES15_0440.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01895.

Enzyme and pathway databases

BioCycCSAK1138308:GLC5-451-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameI2EEB1_CROSK
AccessionPrimary (citable) accession number: I2EEB1
Entry history
Integrated into UniProtKB/TrEMBL: July 11, 2012
Last sequence update: July 11, 2012
Last modified: February 19, 2014
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)