Reviewed,
UniProtKB/Swiss-Prot Q48GW3 (FADB_PSE14)
Last modified
November 25, 2008.
Version 29.
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 | Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 264730 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 721 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 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 + H(2)O. 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 – 721 | 721 | Fatty acid oxidation complex subunit alpha HAMAP MF_01621 | PRO_0000109280 | ||||
Regions | ||||||||
| Region | 1 – 190 | 190 | Enoyl-CoA hydratase/isomerase By similarity | |||||
| Region | 312 – 721 | 410 | 3-hydroxyacyl-CoA dehydrogenase By similarity | |||||
Sequences
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References
| [1] | "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition." Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., Creasy T., Davidsen T.M., Haft D.H. Buell R.J. Bacteriol. 187:6488-6498(2005) [PubMed: 16159782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000058 Genomic DNA. Translation: AAZ34330.1. | |
| RefSeq | YP_275370.1. |
3D structure databases | |
| SMR | Q48GW3. Positions 1-715. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3556880. |
| GenomeReviews | Gene locus PSPPH_3210 in contig CP000058_GR. |
| KEGG | psp:PSPPH_3210. |
| NMPDR | fig|264730.3.peg.3186. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q48GW3. |
Family and domain databases | |
| HAMAP | MF_01621. [Tree] |
| InterPro | IPR006180. 3-OHacyl-CoA_DHase_CS. IPR006176. 3-OHacyl-CoA_DHase_NAD-bd. IPR006108. 3HC_DHase_C. IPR001753. Crotonase_core. IPR013328. DHase_multihelical. IPR012799. FadB. IPR016040. NAD(P)-bd. [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. 1 hit. 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. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FADB_PSE14 | ||||||||
| Accession | Primary (citable) accession number: Q48GW3 | ||||||||
| 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 |

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