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A9IYZ3 (ACSA_BART1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:BT_2482
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length647 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 – 647647Acetyl-coenzyme A synthetase HAMAP MF_01123
PRO_1000084998

Sites

Active site5171 By similarity

Amino acid modifications

Modified residue6091N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A9IYZ3 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 8408FB0F3D9ECAF6

FASTA64773,010
        10         20         30         40         50         60 
MTEKIYPISE EIKKNTLLDE ETYQKWYRES INDPESFWAK HGQCIEWFKP FTKVKNTSFN 

        70         80         90        100        110        120 
DGVSIQWYED GITNVAYNCI DRHLKTHGDQ IALIWEGDNP YHDKKITYNE LYEHVCRFAN 

       130        140        150        160        170        180 
LLKNHGVKKG DKVTIYLPMI PEAAYAMLAC ARIGAVHSVI FAGFSAEAIA GRIVDCESTF 

       190        200        210        220        230        240 
IITADHGLRG GKRINLKDNV DHAIEIAARQ NVRVDQVMVI RRTCGPIDWI EGRDFWYHEE 

       250        260        270        280        290        300 
ITHAKTNCPA EPMNAEDPLF ILYTSGSTGK PKGVLHSTGG YLVYAAITHK YVFDYHPGEI 

       310        320        330        340        350        360 
YWCTADIGWI TGHSYLVYGP LCNGATTLMF EGTPTFPDKG RFWEIVDKHK VNTLYTAPTA 

       370        380        390        400        410        420 
IRALMGAGNS FVEHSKRTSL RLLGTVGEPI NPEAWEWFYH TVGNDRCPIL DTWWQTETGG 

       430        440        450        460        470        480 
HMITPLPGAT PLKAGSATRP FFGVQLQIID EQGNILEGEA EGNLCIIDSW PGQMRTLYKD 

       490        500        510        520        530        540 
HERFIETYFS TYKGKYFTGD GCRRDSDGYY WITGRVDDIL NVSGHRLGTA EIESALVLHP 

       550        560        570        580        590        600 
AVSEAAVVGY PHPIKGQGVY SFVTLMEGTA PSEELQKDLI KHVRKEIGSI AILDKIQFAP 

       610        620        630        640 
QLPKTRSGKI MRRILRKIAE NNFDNLGDIS TLAEPQVVED LIANRQN 

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References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIP 105476 / IBS 506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260525 Genomic DNA. Translation: CAK02456.1.
RefSeqYP_001610451.1. NC_010161.1.

3D structure databases

ProteinModelPortalA9IYZ3.
SMRA9IYZ3. Positions 6-646.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9IYZ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5828978.
GenomeReviewsGene locus BT_2482 in contig AM260525_GR.
PATRIC20552810. VBIBarTri113218_2522.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG547964.
OMATRGTEES.
ProtClustDBPRK00174.

Enzyme and pathway databases

BioCycBTRI382640:BT_2482-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]
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_BART1
AccessionPrimary (citable) accession number: A9IYZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 31 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