Reviewed,
UniProtKB/Swiss-Prot P21177 (FADB_ECOLI)
Last modified
November 3, 2009.
Version 95.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
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 (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [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 | Evidence at protein level. |
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. Ref.7 |
| 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). HAMAP MF_01621 |
| Induction | Repressed by fadR in the absence of LCFAs (fatty acids of, at least, 12 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs which bind to fadR resulting in its release from the DNA and thus derepression of the transcription. HAMAP MF_01621 |
| 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_0000109268 | |||||
Regions | |||||||||
| Nucleotide binding | 400 – 402 | 3 | NAD By similarity | ||||||
| Nucleotide binding | 427 – 429 | 3 | NAD By similarity | ||||||
| Region | 1 – 189 | 189 | Enoyl-CoA hydratase/isomerase HAMAP MF_01621 | ||||||
| Region | 311 – 729 | 419 | 3-hydroxyacyl-CoA dehydrogenase HAMAP MF_01621 | ||||||
Sites | |||||||||
| Binding site | 296 | 1 | Substrate By similarity | ||||||
| Binding site | 324 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 343 | 1 | NAD By similarity | ||||||
| Binding site | 407 | 1 | NAD By similarity | ||||||
| Binding site | 453 | 1 | NAD By similarity | ||||||
| Binding site | 500 | 1 | Substrate By similarity | ||||||
| Binding site | 660 | 1 | Substrate By similarity | ||||||
| Site | 119 | 1 | Important for catalytic activity By similarity | ||||||
| Site | 139 | 1 | Important for catalytic activity By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 518 | 1 | A → R in AAA23750. Ref.1 | ||||||
| Sequence conflict | 664 | 1 | F → L Ref.2 | ||||||
| Sequence conflict | 666 | 1 | P → A Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes." Dirusso C.C. J. Bacteriol. 172:6459-6468(1990) [PubMed: 1699931] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Nucleotide sequence of the fadA and fadB genes from Escherichia coli." Nakahigashi K., Inokuchi H. Nucleic Acids Res. 18:4937-4937(1990) [PubMed: 2204034] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [3] | "Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli." Yang X.Y.H., Schulz H., Elzinga M., Yang S.Y. Biochemistry 30:6788-6795(1991) [PubMed: 1712230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [4] | "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R. Science 257:771-778(1992) [PubMed: 1379743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [5] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [6] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [7] | "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway." Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr. Mol. Microbiol. 47:793-805(2003) [PubMed: 12535077] [Abstract] Cited for: FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY. Strain: K12 / MG1655 / ATCC 47076. |
Cross-references
Sequence databases | |
|---|---|
| M59368 Genomic DNA. Translation: AAA23750.1. X52837 Genomic DNA. Translation: CAB40809.1. M74164 Genomic DNA. Translation: AAA62777.1. M87049 Genomic DNA. Translation: AAA67643.1. U00096 Genomic DNA. Translation: AAC76849.1. AP009048 Genomic DNA. Translation: BAE77457.1. | |
| PIR | A39592. |
| RefSeq | AP_003956.1. NP_418288.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 3HDH based on UniProtKB P00348. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P21177. |
2-D gel databases | |
| ECO2DBASE | G073.4. 6TH EDITION. G073.5. 6TH EDITION. |
Proteomic databases | |
| PRIDE | P21177. |
Genome annotation databases | |
| GeneID | 948336. |
| GenomeReviews | Gene locus JW3822 in contig AP009048_GR. Gene locus b3846 in contig U00096_GR. |
| KEGG | ecj:JW3822. eco:b3846. |
Organism-specific databases | |
| EchoBASE | EB0275. |
| EcoGene | EG10279. fadB. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P21177. |
| OMA | ANNGSYY. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:FADB-MON. MetaCyc:FADB-MON. |
Gene expression databases | |
| Genevestigator | P21177. |
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_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P21177 Secondary accession number(s): Q2M8E9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


