Reviewed,
UniProtKB/Swiss-Prot Q9Z3R3 (ACSA1_RHIME)
Last modified
November 3, 2009.
Version 57.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Acetoacetyl-coenzyme A synthetase EC=6.2.1.16 Alternative name(s): Acetoacetate--CoA ligase 1 Acyl-activating enzyme 1 | ||||||
| Gene names |
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| Organism | Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 382 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium |
Protein attributes
| Sequence length | 650 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Involved in poly-3-hydroxybutyrate degradation. Activates acetoacetate to acetoacetyl-CoA. HAMAP MF_01123 |
| Catalytic activity | ATP + acetoacetate + CoA = AMP + diphosphate + acetoacetyl-CoA. HAMAP MF_01123 |
| Post-translational modification | Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| PTM | Acetylation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | lipid metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate-CoA ligase activityInferred from electronic annotation. Source: HAMAP acetoacetate-CoA ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 650 | 650 | Acetoacetyl-coenzyme A synthetase HAMAP MF_01123 | PRO_0000208381 | |||||
Sites | |||||||||
| Active site | 521 | 1 | By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 612 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 144 | 1 | A → S in AAC64548. Ref.1 | ||||||
| Sequence conflict | 337 | 1 | G → C in AAC64548. Ref.1 | ||||||
| Sequence conflict | 358 | 1 | V → L in AAC64548. Ref.1 | ||||||
| Sequence conflict | 387 | 1 | L → V in AAC64548. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Requirement for the enzymes acetoacetyl coenzyme A synthetase and poly-3-hydroxybutyrate (PHB) synthase for growth of Sinorhizobium meliloti on PHB cycle intermediates." Cai G.-Q., Driscoll B.T., Charles T.C. J. Bacteriol. 182:2113-2118(2000) [PubMed: 10735852] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SU47 / 1021. |
| [2] | "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. Galibert F.Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021. |
Cross-references
Sequence databases | |
|---|---|
| AF080217 Genomic DNA. Translation: AAC64548.1. AL591688 Genomic DNA. Translation: CAC45291.1. | |
| RefSeq | NP_384825.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1232358. |
| GenomeReviews | Gene locus R00719 in contig AL591688_GR. |
| KEGG | sme:SMc00774. |
| NMPDR | fig|266834.1.peg.2013. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9Z3R3. |
| OMA | WAHGDYA. |
Enzyme and pathway databases | |
| BioCyc | SMEL266834:SMC00774-MON. |
Family and domain databases | |
| HAMAP | MF_01123. Divergent sequence. [Tree] |
| InterPro | IPR005914. Acac_CoA_synth. IPR000873. AMP-dep_Synth/Lig. [Graphical view] |
| Pfam | PF00501. AMP-binding. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01217. ac_ac_CoA_syn. 1 hit. |
| PROSITE | PS00455. AMP_BINDING. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACSA1_RHIME | ||||||||
| Accession | Primary (citable) accession number: Q9Z3R3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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