Reviewed,
UniProtKB/Swiss-Prot Q8X8I2 (FADB_ECO57)
Last modified
June 16, 2009.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Fatty acid oxidation complex subunit alpha Including the following 2 domains: 1- Recommended name: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase EC=4.2.1.17 EC=5.3.3.8 EC=5.1.2.3 2- Recommended name: 3-hydroxyacyl-CoA dehydrogenase EC=1.1.1.35 | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83334 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 729 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities. Involved in the aerobic and anaerobic degradation of long-chain fatty acids By similarity. |
| Catalytic activity | (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. HAMAP MF_01621 (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. HAMAP MF_01621 (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP MF_01621 (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. HAMAP MF_01621 |
| Pathway | |
| Subunit structure | Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity. |
| Sequence similarities | In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid metabolism Lipid degradation Lipid metabolism |
| Ligand | NAD |
| Molecular function | Isomerase Lyase Oxidoreductase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | fatty acid catabolic process Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | fatty acid beta-oxidation multienzyme complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | 3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: HAMAP 3-hydroxybutyryl-CoA epimerase activityInferred from electronic annotation. Source: HAMAP coenzyme bindingInferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activityInferred from electronic annotation. Source: HAMAP enoyl-CoA hydratase activityInferred 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 – 729 | 729 | Fatty acid oxidation complex subunit alpha HAMAP MF_01621 | PRO_0000109269 | ||||
Regions | ||||||||
| Region | 1 – 189 | 189 | Enoyl-CoA hydratase/isomerase By similarity | |||||
| Region | 311 – 729 | 419 | 3-hydroxyacyl-CoA dehydrogenase By similarity | |||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG59040.1. BA000007 Genomic DNA. Translation: BAB38197.1. | |
| PIR | D86072. F91225. |
| RefSeq | NP_290476.1. NP_312801.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 3HDH based on UniProtKB P00348. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 915128. 960314. |
| GenomeReviews | Gene locus Z5367 in contig AE005174_GR. Gene locus ECs4774 in contig BA000007_GR. |
| KEGG | ece:Z5367. ecs:ECs4774. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8X8I2. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS4774-MON. |
Family and domain databases | |
| HAMAP | MF_01621. [Tree] |
| InterPro | IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR001753. Crotonase_core. IPR013328. DH_multihelical. IPR018376. Enoyl-CoA_hyd/isom_CS. IPR012799. FadB. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit. |
| Pfam | PF00725. 3HCDH. 2 hits. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02437. FadB. 1 hit. |
| PROSITE | PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FADB_ECO57 | ||||||||
| Accession | Primary (citable) accession number: Q8X8I2 | ||||||||
| 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


