A0KEL1 (FADB_AERHH) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 42.
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: Fatty acid oxidation complex subunit alpha | ||||
| Gene names |
| ||||
| Organism | Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 380703 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas |
Protein attributes
| Sequence length | 715 AA. |
| Sequence status | Complete. |
| 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 By similarity. HAMAP MF_01621 |
| 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 |
| 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: EC 3-hydroxybutyryl-CoA epimerase activityInferred from electronic annotation. Source: EC coenzyme bindingInferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activityInferred from electronic annotation. Source: EC enoyl-CoA hydratase activityInferred from electronic annotation. Source: EC nucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 715 | 715 | Fatty acid oxidation complex subunit alpha HAMAP MF_01621 | PRO_1000069557 | |||||
Regions | |||||||||
| Nucleotide binding | 401 – 403 | 3 | NAD By similarity | ||||||
| Nucleotide binding | 428 – 430 | 3 | NAD By similarity | ||||||
| Region | 1 – 189 | 189 | Enoyl-CoA hydratase/isomerase By similarity | ||||||
| Region | 311 – 715 | 405 | 3-hydroxyacyl-CoA dehydrogenase By similarity | ||||||
Sites | |||||||||
| Binding site | 296 | 1 | Substrate By similarity | ||||||
| Binding site | 325 | 1 | NAD; via amide nitrogen By similarity | ||||||
| Binding site | 344 | 1 | NAD By similarity | ||||||
| Binding site | 408 | 1 | NAD By similarity | ||||||
| Binding site | 454 | 1 | NAD By similarity | ||||||
| Binding site | 501 | 1 | Substrate By similarity | ||||||
| Binding site | 661 | 1 | Substrate By similarity | ||||||
| Site | 119 | 1 | Important for catalytic activity By similarity | ||||||
| Site | 139 | 1 | Important for catalytic activity By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades." Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F. J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 7966 / NCIB 9240. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000462 Genomic DNA. Translation: ABK38031.1. |
| RefSeq | YP_854676.1. NC_008570.1. |
3D structure databases | |
| ProteinModelPortal | A0KEL1. |
| SMR | A0KEL1. Positions 1-715. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A0KEL1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4490320. |
| GenomeReviews | Gene locus AHA_0139 in contig CP000462_GR. |
| KEGG | aha:AHA_0139. |
| PATRIC | 20777742. VBIAerHyd135212_0132. |
| TIGR | AHA_0139. |
Phylogenomic databases | |
| eggNOG | COG1250. |
| HOGENOM | HBG691737. |
| OMA | FGEQKAF. |
| PhylomeDB | A0KEL1. |
| ProtClustDB | PRK11730. |
Enzyme and pathway databases | |
| BioCyc | AHYD196024:AHA_0139-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01621. FadB. [Tree] |
| InterPro | IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR008927. 6-PGluconate_DH_C-like. IPR001753. Crotonase_core. IPR013328. DH_multihelical. 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. 2 hits. |
| KO | K01825. |
| Pfam | PF00725. 3HCDH. 2 hits. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view] |
| SUPFAM | SSF48179. 6DGDH_C_like. 2 hits. |
| TIGRFAMs | TIGR02437. FadB. 1 hit. |
| PROSITE | PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FADB_AERHH | ||||||||
| Accession | Primary (citable) accession number: A0KEL1 | ||||||||
| Entry history |
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| 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