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A3MG40 (ACSA_BURM7) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 30. 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:BMA10247_A2054
OrganismBurkholderia mallei (strain NCTC 10247) [Complete proteome] [HAMAP]
Taxonomic identifier320389 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

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_1000065277

Sites

Active site5301 By similarity

Amino acid modifications

Modified residue6251N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A3MG40 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: B067B10A94777DF9

FASTA66072,282
        10         20         30         40         50         60 
MSAIESVLHE RRQFAPPAAV EKAAAISGMA AYRALAEEAE RDYEGFWARL ARETLEWRKP 

        70         80         90        100        110        120 
FGKVLDETNA PFYKWFEDGE LNASYNCLDR HVAAGLGERV AVIFEADDGT VTRVTYADLL 

       130        140        150        160        170        180 
ARVSRFANAL KKRGVGRGDR VVIYIPMSVE GIVAMQACAR IGATHSVVFG GFSSKSLHER 

       190        200        210        220        230        240 
IVDVGATALV TADEQMRGGK TLPLKSIADE ALAMGGCDAV KTVVVYRRTG GNVDWHAGRD 

       250        260        270        280        290        300 
VWMHEMVANE SDACEPEWVG AEHPLFILYT SGSTGKPKGV QHSTAGYLLW VAQTMKWTFD 

       310        320        330        340        350        360 
WKPDDVFWCT ADIGWVTGHS YITYGPLAVG ATQVVFEGVP TYPNAGRFWK MIGDHKVTVF 

       370        380        390        400        410        420 
YTAPTAIRSL IKAAEADDRV HPRSYDLSSL RIIGTVGEPI NPEAWIWYHK NVGQARCPIV 

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

       490        500        510        520        530        540 
PAMARTIWGD PERFKKSYFP EELGGRLYLA GDGTVRDKET GYFTIMGRID DVLNVSGHRL 

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

       610        620        630        640        650        660 
KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEAI TQDTSTLENP AILEQLAEVR

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 10247.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000547 Genomic DNA. Translation: ABO03882.1.
RefSeqYP_001079226.1. NC_009079.1.

3D structure databases

ProteinModelPortalA3MG40.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3MG40.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4890506.
GenomeReviewsGene locus BMA10247_A2054 in contig CP000547_GR.
KEGGbmn:BMA10247_A2054.
PATRIC19141709. VBIBurMal96640_1923.
TIGRBMA10247_A2054.

Phylogenomic databases

HOGENOMHBG547964.
OMATRGTEES.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycBMAL320389:BMA10247_A2054-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_BURM7
AccessionPrimary (citable) accession number: A3MG40
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 3, 2007
Last modified: December 14, 2011
This is version 30 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

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