P54810 (THIL_PARDE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 57.
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-CoA acetyltransferase EC=2.3.1.9 Alternative name(s): Acetoacetyl-CoA thiolase | ||
| Gene names |
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| Organism | Paracoccus denitrificans | ||
| Taxonomic identifier | 266 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus |
Protein attributes
| Sequence length | 391 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | 2 acetyl-CoA = CoA + acetoacetyl-CoA. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the thiolase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | PHB biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Acyltransferase Transferase |
| Gene Ontology (GO) | |
| Biological process | poly-hydroxybutyrate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | acetyl-CoA C-acetyltransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Analysis of beta-ketothiolase and acetoacetyl-CoA reductase genes of a methylotrophic bacterium, Paracoccus denitrificans, and their expression in Escherichia coli." Yabutani T., Maehara A., Ueda S., Yamane T. FEMS Microbiol. Lett. 133:85-90(1995) [PubMed: 8566717] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D49362 Genomic DNA. Translation: BAA08357.1. |
3D structure databases | |
| ProteinModelPortal | P54810. |
| SMR | P54810. Positions 5-389. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR002155. Thiolase. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. IPR020615. Thiolase_acyl_enz_int_AS. IPR020610. Thiolase_AS. IPR020617. Thiolase_C. IPR020613. Thiolase_CS. IPR020616. Thiolase_N. [Graphical view] |
| Gene3D | G3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits. |
| PANTHER | PTHR18919. Thiolase. 1 hit. |
| Pfam | PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000429. Ac-CoA_Ac_transf. 1 hit. |
| SUPFAM | SSF53901. Thiolase-like. 2 hits. |
| TIGRFAMs | TIGR01930. AcCoA-C-Actrans. 1 hit. |
| PROSITE | PS00098. THIOLASE_1. 1 hit. PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | THIL_PARDE | ||||||||
| Accession | Primary (citable) accession number: P54810 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with