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Q8KBY0 (ACSA_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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
Synonyms:acs
Ordered Locus Names:CT1652
OrganismChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP]
Taxonomic identifier194439 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length659 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 – 659659Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123
PRO_0000208360

Regions

Region423 – 4286Substrate binding By similarity

Sites

Active site5291 By similarity
Metal binding5491Magnesium; via carbonyl oxygen By similarity
Metal binding5511Magnesium; via carbonyl oxygen By similarity
Metal binding5541Magnesium; via carbonyl oxygen By similarity
Binding site3231Coenzyme A By similarity
Binding site3471Coenzyme A By similarity
Binding site3991Substrate; via amide nitrogen By similarity
Binding site5121Substrate By similarity
Binding site5271Substrate By similarity
Binding site5351Coenzyme A By similarity
Binding site5381Substrate By similarity
Binding site5961Coenzyme A

Amino acid modifications

Modified residue6211N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8KBY0 [UniParc].

Last modified September 26, 2003. Version 2.
Checksum: 2BB84C9AB13EA034

FASTA65973,576
        10         20         30         40         50         60 
MATEQTKGQS SESISSVLSE RRKFPPPEAF SSQSHISSME QYEKLYADAA ADPDKYWGDL 

        70         80         90        100        110        120 
AEQFHWFKKW DSVLEWNAPY AKWFNGGTTN IAYNCLDVHV GSWRKNKAAI IWEGEEGNER 

       130        140        150        160        170        180 
ILTYGELHRQ VSKFANVLKI AGIKPGDKVA IYMGMVPELV IAVLACARVG AVHNVIFAGF 

       190        200        210        220        230        240 
AAHAITERVN DSRAKIVICA DGTRRRGSTI NLKNIVDEAI INTPSVKNVI VLKVTGEEIH 

       250        260        270        280        290        300 
MHDGMDHWWH DLMGLAVDEC EPAQVDSEHP LFLLYTSGST GKPKGILHTT AGYMVHAASS 

       310        320        330        340        350        360 
FKYVFDIKDE DIYFCTADIG WITGHTYIIY GPLLNGATVF MYEGAPNYPQ WDRFWDIINR 

       370        380        390        400        410        420 
HKITILYTAP TAIRAFIRAG NEWVTKHDLS SLRLLGTVGE PINPEAWMWY HKYVGQEKCP 

       430        440        450        460        470        480 
IVDTWWQTET GGIMISPMPG ATPTKPGTAT RPLPGIMVDV VRKDGTPCNA NEGGYLVVKR 

       490        500        510        520        530        540 
PWPSMLRTIY GDNERYEKTY WSEFPGMYFT GDGARKDDDG YIWIMGRVDD VVNVSGHRLG 

       550        560        570        580        590        600 
TSEVESALVS HEAVAEAAVV SRPDEIKGNA LVAFVTLKDG YEGDAKLRDS LGKHVAKEIG 

       610        620        630        640        650 
AIAKPDEIRW AKGLPKTRSG KIMRRLLREL ATSNEIKGDV TTLEDLGVIE NLREQEDEG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006470 Genomic DNA. Translation: AAM72877.1.
RefSeqNP_662535.2. NC_002932.3.

3D structure databases

ProteinModelPortalQ8KBY0.
SMRQ8KBY0. Positions 23-656.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING194439.CT1652.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM72877; AAM72877; CT1652.
GeneID1006138.
KEGGcte:CT1652.
PATRIC21401177. VBIChlTep116050_1493.

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAGGCEAVT.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycCTEP194439:GHN0-1691-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_CHLTE
AccessionPrimary (citable) accession number: Q8KBY0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: May 14, 2014
This is version 70 of the entry and version 2 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