Reviewed,
UniProtKB/Swiss-Prot A6TGM3 (FADA_KLEP7)
Last modified
November 3, 2009.
Version 20.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 3-ketoacyl-CoA thiolase EC=2.3.1.16 Alternative name(s): Fatty acid oxidation complex subunit beta Beta-ketothiolase Acetyl-CoA acyltransferase | ||||||
| Gene names |
| ||||||
| Organism | Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 272620 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella |
Protein attributes
| Sequence length | 387 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed By similarity. |
| Catalytic activity | Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. HAMAP MF_01620 |
| Pathway | |
| Subunit structure | Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the thiolase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid metabolism Lipid degradation Lipid metabolism |
| Cellular component | Cytoplasm |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | fatty acid metabolic process Inferred from electronic annotation. Source: HAMAP lipid catabolic processInferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | acetyl-CoA C-acyltransferase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 387 | 387 | 3-ketoacyl-CoA thiolase HAMAP MF_01620 | PRO_0000323547 | |||||
Sites | |||||||||
| Active site | 91 | 1 | Acyl-thioester intermediate By similarity | ||||||
| Active site | 343 | 1 | Proton acceptor By similarity | ||||||
| Active site | 373 | 1 | Proton acceptor By similarity | ||||||
Sequences
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References
| [1] | McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K. Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000647 Genomic DNA. Translation: ABR79707.1. | |
| RefSeq | YP_001337974.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A6TGM3. |
Genome annotation databases | |
| GeneID | 5338715. |
| GenomeReviews | Gene locus KPN78578_42830 in contig CP000647_GR. |
| KEGG | kpn:KPN_04339. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | AIDDIYW. |
Family and domain databases | |
| HAMAP | MF_01620. [Tree] |
| InterPro | IPR012805. FadA. IPR002155. Thiolase. IPR016038. Thiolase-like_subgr. [Graphical view] |
| Gene3D | G3DSA:3.40.47.10. Thiolase-like_subgr. 2 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. |
| TIGRFAMs | TIGR01930. AcCoA-C-Actrans. 1 hit. TIGR02445. fadA. 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 | FADA_KLEP7 | ||||||||
| Accession | Primary (citable) accession number: A6TGM3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


