O25686 (ACSA_HELPY) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 79.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
| ||||||
| Organism | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 85962 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › ![]() |
Protein attributes
| Sequence length | 662 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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. |
| Post-translational modification | Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123 |
| Miscellaneous | There is no ortholog for acsA in strain J99. HAMAP-Rule MF_01123 |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Ligase |
| PTM | Acetylation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | acetyl-CoA biosynthetic process from acetate Inferred from electronic annotation. Source: InterPro |
| Molecular_function | AMP binding Inferred from electronic annotation. Source: InterPro ATP bindingInferred from electronic annotation. Source: UniProtKB-KW acetate-CoA ligase activityInferred from electronic annotation. Source: HAMAP metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 662 | 662 | Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123 | PRO_0000208365 | |||||
Regions | |||||||||
| Region | 417 – 422 | 6 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 527 | 1 | By similarity | ||||||
| Metal binding | 549 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 552 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Binding site | 317 | 1 | Coenzyme A By similarity | ||||||
| Binding site | 393 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 510 | 1 | Substrate By similarity | ||||||
| Binding site | 525 | 1 | Substrate By similarity | ||||||
| Binding site | 533 | 1 | Coenzyme A By similarity | ||||||
| Binding site | 536 | 1 | Substrate By similarity | ||||||
| Binding site | 598 | 1 | Coenzyme A | ||||||
Amino acid modifications | |||||||||
| Modified residue | 623 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. Venter J.C.Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE000511 Genomic DNA. Translation: AAD08090.1. |
| PIR | E64650. |
| RefSeq | NP_207835.1. NC_000915.1. YP_006934961.1. NC_018939.1. |
3D structure databases | |
| ProteinModelPortal | O25686. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-3168N. |
| MINT | MINT-164557. |
| STRING | 85962.HP1045. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAD08090; AAD08090; HP_1045. |
| GeneID | 13870238. 899580. |
| KEGG | heo:C694_05405. hpy:HP1045. |
| PATRIC | 20593427. VBIHelPyl33062_1094. |
Phylogenomic databases | |
| eggNOG | COG0365. |
| KO | K01895. |
| OMA | AISKHEM. |
| ProtClustDB | PRK00174. |
Family and domain databases | |
| HAMAP | MF_01123. Ac_CoA_synth. |
| InterPro | IPR011904. Ac_CoA_lig. IPR024597. Acyl-CoA_synth_DUF3448. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR025110. DUF4009. [Graphical view] |
| Pfam | PF00501. AMP-binding. 1 hit. PF11930. DUF3448. 1 hit. PF13193. DUF4009. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02188. Ac_CoA_lig_AcsA. 1 hit. |
| PROSITE | PS00455. AMP_BINDING. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACSA_HELPY | ||||||||
| Accession | Primary (citable) accession number: O25686 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Helicobacter pylori Helicobacter pylori (strain 26695): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
