Q8Z3C6 · FADB_SALTI
- ProteinFatty acid oxidation complex subunit alpha
- GenefadB
- StatusUniProtKB reviewed (Swiss-Prot)
- 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
- a (3S)-3-hydroxyacyl-CoA + NAD+ = a 3-oxoacyl-CoA + H+ + NADH
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 > Salmonella
Accessions
- Primary accessionQ8Z3C6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000109286 | 1-729 | Fatty acid oxidation complex subunit alpha | |||
Sequence: MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGQALEVLEKQHDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTLAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRLPRMLGADSALEIIAAGKDVGAEHALKIGLVDGVVKQEKLIEGAIAVLRQAITGDLDWRAKRQPKLEPLKLSKIEAAMSFTIAKGMVAQTAGKHYPAPMTAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDIETPKQAAVLGAGIMGGGIAYQSAWKGVPVIMKDINDKSLNLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDVVVEAVVENPKVKKAVLAETEQKVRPETVLASNTSTIPIGELASALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNNCPGFFVNRVLFPYFAGFSQLLRDGADFRKVDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKEYRDAIDALFDASRFGQKNGLGFWRYKEDSKGKPKKEEDAAVDDLLASVSQTKRDFSDDEIIARMMIPMINEVVRCLEEGIIASPAEADMALVYGLGFPPFHGGAFRWLDTQGSAKYLDMAQQYQHLGPLYEVPEGLRDKTRHNEPYYPPVEPARPVGSLKTA |
Interaction
Subunit
Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-189 | Enoyl-CoA hydratase/isomerase | ||||
Sequence: MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGQALEVLEKQHDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTLAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRLPRMLGADSALEIIAAGKDVGAEHALKIGLVDGVVK | ||||||
Region | 311-729 | 3-hydroxyacyl-CoA dehydrogenase | ||||
Sequence: ETPKQAAVLGAGIMGGGIAYQSAWKGVPVIMKDINDKSLNLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDVVVEAVVENPKVKKAVLAETEQKVRPETVLASNTSTIPIGELASALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNNCPGFFVNRVLFPYFAGFSQLLRDGADFRKVDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKEYRDAIDALFDASRFGQKNGLGFWRYKEDSKGKPKKEEDAAVDDLLASVSQTKRDFSDDEIIARMMIPMINEVVRCLEEGIIASPAEADMALVYGLGFPPFHGGAFRWLDTQGSAKYLDMAQQYQHLGPLYEVPEGLRDKTRHNEPYYPPVEPARPVGSLKTA | ||||||
Region | 707-729 | Disordered | ||||
Sequence: TRHNEPYYPPVEPARPVGSLKTA |
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length729
- Mass (Da)79,642
- Last updated2002-03-01 v1
- ChecksumC34C68ECFF35713C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL513382 EMBL· GenBank· DDBJ | CAD07910.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014613 EMBL· GenBank· DDBJ | AAO70843.1 EMBL· GenBank· DDBJ | Genomic DNA |