Reviewed,
UniProtKB/Swiss-Prot P46707 (THIL_MYCLE)
Last modified
November 3, 2009.
Version 56.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Probable acetyl-CoA acetyltransferase EC=2.3.1.9 Alternative name(s): Acetoacetyl-CoA thiolase | ||||||
| Gene names |
| ||||||
| Organism | Mycobacterium leprae [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1769 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 393 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 2 acetyl-CoA = CoA + acetoacetyl-CoA. |
| Sequence similarities | Belongs to the thiolase family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | acetyl-CoA C-acetyltransferase activity Inferred 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 – 393 | 393 | Probable acetyl-CoA acetyltransferase | PRO_0000206457 | |||||
Sites | |||||||||
| Active site | 88 | 1 | Acyl-thioester intermediate By similarity | ||||||
| Active site | 349 | 1 | Proton acceptor By similarity | ||||||
| Active site | 379 | 1 | Proton acceptor By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Smith D.R., Robison K. Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. Barrell B.G.Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN. |
Cross-references
Sequence databases | |
|---|---|
| U00014 Genomic DNA. Translation: AAA50881.1. AL583921 Genomic DNA. Translation: CAC31539.1. | |
| PIR | S72804. |
| RefSeq | NP_301848.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1PXT based on UniProtKB P27796. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 910257. |
| GenomeReviews | Gene locus ML1158 in contig AL450380_GR. |
| KEGG | mle:ML1158. |
| NMPDR | fig|272631.1.peg.720. |
Organism-specific databases | |
| Leproma | ML1158. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P46707. |
| OMA | DANTHDG. |
Enzyme and pathway databases | |
| BioCyc | MLEP272631:ML1158-MON. |
| BRENDA | 2.3.1.9. 808. |
Family and domain databases | |
| InterPro | IPR002155. Thiolase. IPR016038. Thiolase-like_subgr. [Graphical view] |
| Gene3D | G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit. |
| 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. |
| 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_MYCLE | ||||||||
| Accession | Primary (citable) accession number: P46707 | ||||||||
| 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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