S1PUS3 · S1PUS3_ECOLX
- ProteinFatty acid oxidation complex subunit alpha
- GenefadJ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids714 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities.
Catalytic activity
- (3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA
Pathway
Lipid metabolism; fatty acid beta-oxidation.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 118 | Important for catalytic activity | ||||
Sequence: E | ||||||
Site | 140 | Important for catalytic activity | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-hydroxyacyl-CoA dehydrogenase activity | |
Molecular Function | 3-hydroxybutyryl-CoA epimerase activity | |
Molecular Function | enoyl-CoA hydratase activity | |
Molecular Function | NAD+ binding | |
Biological Process | fatty acid beta-oxidation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFatty acid oxidation complex subunit alpha
Including 2 domains:
- Recommended nameEnoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase
- EC number
- Recommended name3-hydroxyacyl-CoA dehydrogenase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionS1PUS3
Proteomes
Subcellular Location
Interaction
Subunit
Heterotetramer of two alpha chains (FadJ) and two beta chains (FadI).
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-190 | Enoyl-CoA hydratase | ||||
Sequence: MEMASAFTLNVRLDNIAIITIDVPGEKMNTLKVEFASQVRAIIKQLRENKELRGVVFVSAKPDNFIAGADIKMIGNCKTAQEAEVLARQGQQLMAEIHALPIPVIAAIHGACLGGGLELALACHGRVCTDDPKTVLGLPEVQLGLLPGSGGTQRLPRLIGVSTALEMILTGKQLRAKQAVKLGLVDDVVP | ||||||
Region | 306-714 | 3-hydroxyacyl-CoA dehydrogenase | ||||
Sequence: APLNSVGILGGGLMGGGIAYVTACKAGLPVRIKDINPQGINHALKYSWDQLEGKVRRRHLKASERDKQLALISGTTDYCGFAHRDLIIEAVFENLELKQQMVAEVEQNCATHTIFASNTSSLPIGDIAAHAARPEQVIGLHFFSPVEKMPLVEIIPHASTSAQTIATTVKLAKKQGKTPIVVRDKAGFYVNRILAPYINEAIRMLTEGERIEHIDAALVKFGFPVGPIQLLDEVGIDTGTKIMPVLEAAYGERFSAPANVVSSILNDDRKGRKNGRGFYLYGQKGRKSKKQVDPAIYPLIGAQGQGRLSAPQVAERCVMLMLNEAVRCLDEQVIRSVRDGDIGAVFGIGFPPFLGGPFRYIDSLGAGEVVAIMQRLATQYGSRFTPCNRLVEMSERGESFWKTTATDLQ | ||||||
Domain | 311-489 | 3-hydroxyacyl-CoA dehydrogenase NAD binding | ||||
Sequence: VGILGGGLMGGGIAYVTACKAGLPVRIKDINPQGINHALKYSWDQLEGKVRRRHLKASERDKQLALISGTTDYCGFAHRDLIIEAVFENLELKQQMVAEVEQNCATHTIFASNTSSLPIGDIAAHAARPEQVIGLHFFSPVEKMPLVEIIPHASTSAQTIATTVKLAKKQGKTPIVVRD | ||||||
Domain | 492-586 | 3-hydroxyacyl-CoA dehydrogenase C-terminal | ||||
Sequence: GFYVNRILAPYINEAIRMLTEGERIEHIDAALVKFGFPVGPIQLLDEVGIDTGTKIMPVLEAAYGERFSAPANVVSSILNDDRKGRKNGRGFYLY | ||||||
Domain | 618-704 | 3-hydroxyacyl-CoA dehydrogenase C-terminal | ||||
Sequence: VAERCVMLMLNEAVRCLDEQVIRSVRDGDIGAVFGIGFPPFLGGPFRYIDSLGAGEVVAIMQRLATQYGSRFTPCNRLVEMSERGES |
Sequence similarities
In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length714
- Mass (Da)77,205
- Last updated2013-09-18 v1
- ChecksumA8A4938C612D9DC4
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ASUG01000038 EMBL· GenBank· DDBJ | EOW97004.1 EMBL· GenBank· DDBJ | Genomic DNA |