A0A1V2GIU4 · A0A1V2GIU4_ECOLX
- ProteinFatty acid oxidation complex subunit alpha
- GenefadB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids729 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
Catalytic activity
- (3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA
Pathway
Lipid metabolism; fatty acid beta-oxidation.
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 119 | Important for catalytic activity | ||||
Sequence: E | ||||||
Site | 139 | Important for catalytic activity | ||||
Sequence: E | ||||||
Binding site | 296 | substrate | ||||
Sequence: D | ||||||
Binding site | 324 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 343 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 400-402 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: VVE | ||||||
Binding site | 407 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 429 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 450 | For 3-hydroxyacyl-CoA dehydrogenase activity | ||||
Sequence: H | ||||||
Binding site | 453 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 500 | substrate | ||||
Sequence: N | ||||||
Binding site | 660 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | fatty acid beta-oxidation multienzyme complex | |
Molecular Function | 3-hydroxyacyl-CoA dehydrogenase activity | |
Molecular Function | 3-hydroxybutyryl-CoA epimerase activity | |
Molecular Function | delta(3)-delta(2)-enoyl-CoA isomerase 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/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
- EC number
- Recommended name3-hydroxyacyl-CoA dehydrogenase
- EC number
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A1V2GIU4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-189 | Enoyl-CoA hydratase/isomerase | ||||
Sequence: MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVK | ||||||
Region | 311-729 | 3-hydroxyacyl-CoA dehydrogenase | ||||
Sequence: ETPKRAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYSGFDRVDVVVEAVVENPKVKKAVLAETEQKVRPDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEEDAVVDDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEDIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGDLKTA | ||||||
Domain | 316-494 | 3-hydroxyacyl-CoA dehydrogenase NAD binding | ||||
Sequence: AAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYSGFDRVDVVVEAVVENPKVKKAVLAETEQKVRPDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDC | ||||||
Domain | 496-592 | 3-hydroxyacyl-CoA dehydrogenase C-terminal | ||||
Sequence: GFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRY | ||||||
Domain | 627-691 | 3-hydroxyacyl-CoA dehydrogenase C-terminal | ||||
Sequence: IIARMMIPMVNEVVRCLEEDIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQ | ||||||
Region | 708-729 | Disordered | ||||
Sequence: RHNEPYYPPVEPARPVGDLKTA |
Sequence similarities
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length729
- Mass (Da)79,708
- Last updated2017-06-07 v1
- Checksum8722B174C5C1FCC5