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Q9KV59 (ACSA_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:acsA
Ordered Locus Names:VC_0298
OrganismVibrio cholerae
Taxonomic identifier666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length649 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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.

Sequence caution

The sequence AAF93472.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete proteome
Reference 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 – 649649Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_0000208392

Sites

Active site5171 By similarity

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...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2614968.
GenomeReviewsGene locus VC_0298 in contig AE003852_GR.
KEGGvch:VC0298.
PATRIC20079643. VBIVibCho83274_0280.
TIGRVC_0298.

Phylogenomic databases

HOGENOMHBG547964.
OMATRGTEES.
PhylomeDBQ9KV59.
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_VIBCH
AccessionPrimary (citable) accession number: Q9KV59
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: January 25, 2012
This is version 59 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

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