Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9KV59 (ACSA_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:VC_0298
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length649 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 caution

The sequence AAF93472.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 649649Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
PRO_0000208392

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
Q9KV59 [UniParc].

Last modified September 26, 2003. Version 2.
Checksum: A0C7282B14806B6E

FASTA64971,895
        10         20         30         40         50         60 
MSEAHIYPVK QNIKAHTHAD NDTYLAMYQQ SIKDPEGFWS EHGKIVDWIK PFTKVKHTSF 

        70         80         90        100        110        120 
DPGHIDIRWF EDGTLNVSAN CIDRHLATRG DQVAIIWEGD DPTQDKTLTY KQLHQEVCRF 

       130        140        150        160        170        180 
ANALKEQGVR KGDVVCIYMP MVPEAAVAML ACTRIGAVHT IVFGGFSPEA LAGRIIDSNA 

       190        200        210        220        230        240 
KLVITADEGV RGGRAVPLKK NVDEALCNPE VKNISKVMVL KRTGGNVAWH EHRDIWWHEA 

       250        260        270        280        290        300 
TAKASDNCPP EEMKAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYATMTFK YVFDYQPNEV 

       310        320        330        340        350        360 
FWCTADVGWI TGHSYLVYGP LANGAKTILF EGVPNYPTTA RMSEVVDKHK VNILYTAPTA 

       370        380        390        400        410        420 
IRALMAKGDE AIKGTSRDSL RIMGSVGEPI NPEAWEWYYR TIGNEKSPIV DTWWQTETGG 

       430        440        450        460        470        480 
ILITPLPGAT ALKPGSATRP FFGVQPALVD NMGEIVEGAT EGNLVLLDSW PGQMRTVYGD 

       490        500        510        520        530        540 
HDRFEQTYFS TFKGMYFTGD GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESALVAFN 

       550        560        570        580        590        600 
KIAEAAVVGV PHDIKGQAIY AYITLNDGVY PSAELHKEVK DWVRKEIGAI ATPDVLHWTD 

       610        620        630        640 
ALPKTRSGKI MRRILRKIAT GDTSNLGDTS TLADPSVVDR LIAEKAQLK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF93472.1. Different initiation.
PIRD82339.
RefSeqNP_229953.2. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KV59.
SMRQ9KV59. Positions 5-645.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC0298.

Protocols and materials databases

DNASU2614968.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF93472; AAF93472; VC_0298.
GeneID2614968.
KEGGvch:VC0298.
PATRIC20079643. VBIVibCho83274_0280.

Phylogenomic databases

eggNOGCOG0365.
KOK01895.
OMAAWIWYRD.
OrthoDBEOG68WR2H.

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_VIBCH
AccessionPrimary (citable) accession number: Q9KV59
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: May 14, 2014
This is version 76 of the entry and version 2 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