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A6WXV8 (ACSA_OCHA4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase

Short name=AcCoA synthetase
Short name=Acs
EC=6.2.1.1
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene names
Name:acsA
Ordered Locus Names:Oant_1092
OrganismOchrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168) [Complete proteome] [HAMAP]
Taxonomic identifier439375 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA By similarity. HAMAP-Rule MF_01123

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01123

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 651651Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
PRO_1000065300

Regions

Region411 – 4166Substrate binding By similarity

Sites

Active site5171 By similarity
Metal binding5371Magnesium; via carbonyl oxygen By similarity
Metal binding5391Magnesium; via carbonyl oxygen By similarity
Metal binding5421Magnesium; via carbonyl oxygen By similarity
Binding site3111Coenzyme A By similarity
Binding site3351Coenzyme A By similarity
Binding site3871Substrate; via amide nitrogen By similarity
Binding site5001Substrate By similarity
Binding site5151Substrate By similarity
Binding site5231Coenzyme A By similarity
Binding site5261Substrate By similarity
Binding site5861Coenzyme A

Amino acid modifications

Modified residue6111N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6WXV8 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 6B8B09BA21A762B7

FASTA65172,591
        10         20         30         40         50         60 
MSEKLYPVLA EAKRNTLIDN ATYLEWYQES VSDPDSFWAK HGRRIDWFKP FTKVKNTDFN 

        70         80         90        100        110        120 
GDVSIKWYED GVTNVSYNCI DRHLKSRGDQ VAIIWEGDNP YIDKKITYRE LHENVCRLAN 

       130        140        150        160        170        180 
VLKKHGVKKG DRVTIYLPMI PEAAYAMLAC ARIGAVHSVV FAGFSPEALA GRIVDCESTF 

       190        200        210        220        230        240 
VITADEGVRG GKPVPLKENT DTAIDIAAKQ YVMVNKVLTV RRTGGKVSWG PGRDLWYHQE 

       250        260        270        280        290        300 
VASVEPTCDP EPMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASMTHQ YVFDYHDGDI 

       310        320        330        340        350        360 
YWCTADVGWV TGHSYIVYGP LANGATTLMF EGVPNFPDQG RFWEVVDKHH VNIFYTAPTA 

       370        380        390        400        410        420 
IRALMGAGDE FVTRSSRSTL RLLGSVGEPI NPEAWEWYYN VVGDQRSPIV DTWWQTETGG 

       430        440        450        460        470        480 
ILITPLPGAT DLKPGSATRP FFGIKPELVD NEGAVIEGAV DGNLCIIDSW PGQMRTLYGD 

       490        500        510        520        530        540 
HKRFIEAYFS TYKGKYFTGD GCRRDEDGYY WITGRVDDVL NISGHRLGTA EIESALVSHH 

       550        560        570        580        590        600 
SVSEAAVVGY PHPIKGQGIY CYVTLMTGEA VQDEDALRKE LTQHVRKEIG PIATPDKIQF 

       610        620        630        640        650 
SPGLPKTRSG KIMRRILRKI AEDEFGALGD TSTLADPGVV DDLIENRQNK K 

« Hide

References

[1]"Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic pathogen and symbiont of several eukaryotic hosts."
Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M., Ugalde R.A., Garcia E., Tolmasky M.E.
J. Bacteriol. 193:4274-4275(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49188 / DSM 6882 / NCTC 12168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000758 Genomic DNA. Translation: ABS13812.1.
RefSeqYP_001369641.1. NC_009667.1.

3D structure databases

ProteinModelPortalA6WXV8.
SMRA6WXV8. Positions 17-648.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439375.Oant_1092.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS13812; ABS13812; Oant_1092.
GeneID5380140.
KEGGoan:Oant_1092.
PATRIC20467255. VBIOchAnt73124_1142.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAAWIWYRD.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycOANT439375:GJIT-1108-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACSA_OCHA4
AccessionPrimary (citable) accession number: A6WXV8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 47 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