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Reviewed, UniProtKB/Swiss-Prot B3R1X2 (ACSA_CUPTR)

Last modified November 3, 2009. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: RALTA_A2028
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 660660Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000137262

Sites

Active site5301 By similarity

Amino acid modifications

Modified residue6251N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B3R1X2-1 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: CDBE1FB125782102

FASTA66072,452
        10         20         30         40         50         60 
MSAIESVMQE HRVFNPPEAF ASQAAIPSMD AYRALCDEAE RDYEGFWARY ARELLHWNKP 

        70         80         90        100        110        120 
FTKVLDESNA PFYKWFEDGE LNASYNCLDR NLQNGNADKV AIVFEADDGT VTRVTYRELH 

       130        140        150        160        170        180 
AKVCRLANGL KTLGIRKGDR VVIYMPMSVE GVAAMQACAR LGATHSVVFG GFSAKSLQER 

       190        200        210        220        230        240 
LVDVGAVALI TADEQMRGGK ALPLKAIADD ALALGGCEAV KNVIVYRRTG GNVGWTEGRD 

       250        260        270        280        290        300 
RWLDDVCANQ PDTCEAEPVG AEHPLFVLYT SGSTGKPKGV QHSTGGYLLW ALMTMKWTFD 

       310        320        330        340        350        360 
IKPDDLFWCT ADIGWVTGHT YIAYGPLAAG ATQVVFEGVP TYPNAGRFWD MIARHKVSIF 

       370        380        390        400        410        420 
YTAPTAIRSL IKAAEADEKI HPKQYDLSSL RLLGTVGEPI NPEAWMWYYK NVGNENCPIV 

       430        440        450        460        470        480 
DTFWQTETGG HMITPLPGAT PLVPGSCTLP LPGIMAAIVD ETGHDVPNGS GGILVVKRPW 

       490        500        510        520        530        540 
PAMIRTIWGD PERFKKSYFP EELGGKLYLA GDGSIRDKDT GYFTIMGRID DVLNVSGHRM 

       550        560        570        580        590        600 
GTMEIESALV ANPLVAEAAV VGRPDDMTGE AICAFVVLKR SRPSGEEAAK LATELRNWVG 

       610        620        630        640        650        660 
KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEEI TQDTSTLENP AILEQLKQAQ 

« Hide

References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CU633749 Genomic DNA. Translation: CAQ69969.1.
RefSeqYP_002006032.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6453493.
GenomeReviewsGene locus RALTA_A2028 in contig CU633749_GR.
KEGGcti:RALTA_A2028.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMATGGYNLY.

Family and domain databases

HAMAPMF_01123.
[Tree]
InterProIPR011904. Ac_CoA_lig_AcsA.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACSA_CUPTR
AccessionPrimary (citable) accession number: B3R1X2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: November 3, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents