A7ZU50 (FADA_ECO24) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 35.
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: 3-ketoacyl-CoA thiolase EC=2.3.1.16 Alternative name(s): Acetyl-CoA acyltransferase Beta-ketothiolase Fatty acid oxidation complex subunit beta | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 331111 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 387 AA. |
| Sequence status | Complete. |
| 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. HAMAP MF_01620 |
| 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 HAMAP MF_01620. |
| 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: UniProtKB-KW lipid catabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | acetyl-CoA C-acyltransferase 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 – 387 | 387 | 3-ketoacyl-CoA thiolase HAMAP MF_01620 | PRO_0000323545 | |||||
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
| ||||||||||||||||||
References
| [1] | "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E24377A / ETEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000800 Genomic DNA. Translation: ABV20513.1. |
| RefSeq | YP_001465329.1. NC_009801.1. |
3D structure databases | |
| ProteinModelPortal | A7ZU50. |
| SMR | A7ZU50. Positions 1-387. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A7ZU50. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000020448; EBESCP00000019510; EBESCG00000019502. |
| GeneID | 5587876. |
| GenomeReviews | Gene locus EcE24377A_4364 in contig CP000800_GR. |
| KEGG | ecw:EcE24377A_4364. |
| NMPDR | fig|331111.3.peg.1991. |
| PATRIC | 18297994. VBIEscCol31211_4590. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0183. |
| GeneTree | EBGT00050000009707. |
| HOGENOM | HBG370930. |
| OMA | AIDDIYW. |
| ProtClustDB | PRK08947. |
Enzyme and pathway databases | |
| BioCyc | ECOL331111:ECE24377A_4364-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01620. FadA. [Tree] |
| InterPro | IPR012805. FadA. 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. |
| KO | K00632. |
| PANTHER | PTHR18919:SF35. PTHR18919:SF35. 1 hit. 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. 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_ECO24 | ||||||||
| Accession | Primary (citable) accession number: A7ZU50 | ||||||||
| Entry history |
| ||||||||
| 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