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Q39EK2 (ACSA_BURS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:Bcep18194_A5520
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length660 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.

Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical termComplete 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 – 660660Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000065285

Sites

Active site5301 By similarity

Amino acid modifications

Modified residue6251N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q39EK2 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 11AA74649AC7871B

FASTA66072,195
        10         20         30         40         50         60 
MSAIESVLHE TRQFAPPAAL EQAATISGMP AYRALAAEAE NDYEGFWARL AREGLAWHKP 

        70         80         90        100        110        120 
FTKVLDESNA PFYKWFEDGE LNASYNCLDR HVEAGNGERV AVIFEADDGT VTRVTYADLL 

       130        140        150        160        170        180 
ARVSRFANAL KKRGIGKGDR VVIYIPMSIE GIVAMQACAR IGATHSVVFG GFSAKSLNER 

       190        200        210        220        230        240 
LVDVGATALI TADEQARGGK TLPLKSIADE AIALGGCEAV KSVIVYRRTG GKIDWHAERD 

       250        260        270        280        290        300 
LWMHELTAGE SDQCEPEWVG AEHPLFILYT SGSTGKPKGV QHSTGGYLLW AAQTMKWTFD 

       310        320        330        340        350        360 
WKPTDVFWCT ADIGWVTGHT YITYGPLACG GTQVVFEGVP TYPDAGRFWK MIGDHKVTVF 

       370        380        390        400        410        420 
YTAPTAIRSL IKAAEADDKV HPKSYDLSSL RIIGTVGEPI NPEAWMWYHK HVGQERCPIV 

       430        440        450        460        470        480 
DTWWQTETGG HMITPLPGAT PTVPGSCTLP LPGIMAAVVD ETGQDVPNGQ GGILVVKRPW 

       490        500        510        520        530        540 
PAMIRTIWGD PERFKKSYYP EELGGRLYLA GDGTVRDKDT GYFTIMGRID DVLNVSGHRL 

       550        560        570        580        590        600 
GTMEIESALV SHELVAEAAV VGRPDDTTGE AVVAFVVLKR SRPEGEEAAA LAKTLRDWVG 

       610        620        630        640        650        660 
KQIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEAI TQDTSTLENP AILDQLAEVR 

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References

[1]"Complete sequence of chromosome 1 of Burkholderia sp. 383."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 383.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000151 Genomic DNA. Translation: ABB09114.1.
RefSeqYP_369758.1. NC_007510.1.

3D structure databases

ProteinModelPortalQ39EK2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ39EK2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3750742.
GenomeReviewsGene locus Bcep18194_A5520 in contig CP000151_GR.
KEGGbur:Bcep18194_A5520.
NMPDRfig|269483.3.peg.6754.
PATRIC19288486. VBIBurSp120713_3632.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHBG547964.
OMATRGTEES.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycBSP36773:BCEP18194_A5520-MONOMER.

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_BURS3
AccessionPrimary (citable) accession number: Q39EK2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 40 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