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A1RIK1 (ACSA_SHESW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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

Short name=AcCoA synthetase
Short name=Acs
EC=6.2.1.1
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene names
Name:acsA
Ordered Locus Names:Sputw3181_1659
OrganismShewanella sp. (strain W3-18-1) [Complete proteome] [HAMAP]
Taxonomic identifier351745 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length650 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. 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

Catalytic activity

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

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01123

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 – 650650Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
PRO_1000065325

Regions

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
A1RIK1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 3E623F228961B003

FASTA65072,374
        10         20         30         40         50         60 
MSSQSLYKVS GNIAANALVN NEQYKTMYQE SIVNPEGFWR EHGKRIDWIK PYTKIKKTSF 

        70         80         90        100        110        120 
DDHNLSINWF YDGTLNASAN CLDRHLAEHS DRVAIIWEGD NASEQRKITY GELHADVCKF 

       130        140        150        160        170        180 
ANALRSQGVR RGDIVTIYMP MVPEAAVAML ACARIGAVHS VVFGGFSPDS IASRVIDGKS 

       190        200        210        220        230        240 
KVVITSDEGM RGGRAIPLKR NIDDALNHPD VTSVEKVIVL KRTGGKIDWV EGRDVWWHSL 

       250        260        270        280        290        300 
LETASEHCQP EEMGAEDPLF LLYTSGSTGN PKGVLHTTGG YMVYASMTHE YVFDYKAGEV 

       310        320        330        340        350        360 
YWCTADVGWI TGHSYMVYGP LANGATVLIH EGVPNHPSPA RLGEMIDRHK VNILYTAPTL 

       370        380        390        400        410        420 
IRALMAEGKQ HFDQFDGSTL RIMGSVGEPI NPEAWRWYHE VIGHEHCPIV DTWWQTETGG 

       430        440        450        460        470        480 
ILITPLPGAT DTKPGSATRP FFGVQPALVD NMGNILEGEN EGNLVLLDSW PGQMRTVYGD 

       490        500        510        520        530        540 
HERFVLTYFK TFRGMYFTGD GARRDEDGYY WITGRVDDVI NVSGHRLGTA EVESALVSHE 

       550        560        570        580        590        600 
LVAEAAVVGY PHDIKGQGIY AYVTLTRGTE ESEELRQELR QWVRKEIGAL ATPDLIQWAS 

       610        620        630        640        650 
GLPKTRSGKI MRRFLRKIAA NEVTNLGDAS TLADPAVIET LIETRLNRTE 

« Hide

References

[1]"Complete sequence of Shewanella sp. W3-18-1."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: W3-18-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000503 Genomic DNA. Translation: ABM24496.1.
RefSeqYP_963050.1. NC_008750.1.

3D structure databases

ProteinModelPortalA1RIK1.
SMRA1RIK1. Positions 7-645.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351745.Sputw3181_1659.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM24496; ABM24496; Sputw3181_1659.
GeneID4661723.
KEGGshw:Sputw3181_1659.
PATRIC23596931. VBISheSp103602_1727.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAWVMGRVD.
OrthoDBEOG68WR2H.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycSSP351745:GCOY-1721-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 nameACSA_SHESW
AccessionPrimary (citable) accession number: A1RIK1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 49 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