Q1AHB5 · Q1AHB5_PSEAI
- ProteinEnoyl-[acyl-carrier-protein] reductase [NADH]
- GenefabV
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids398 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP).
Catalytic activity
- a 2,3-saturated acyl-CoA + NAD+ = a (2E)-enoyl-CoA + H+ + NADH
Pathway
Lipid metabolism; fatty acid biosynthesis.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 48-53 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GSSTGY | ||||||
Binding site | 74-75 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FE | ||||||
Site | 75 | Plays an important role in discriminating NADH against NADPH | ||||
Sequence: E | ||||||
Binding site | 111-112 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DA | ||||||
Binding site | 139-140 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: LA | ||||||
Binding site | 225 | substrate | ||||
Sequence: Y | ||||||
Active site | 235 | Proton donor | ||||
Sequence: Y | ||||||
Binding site | 244 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 273-275 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: VVT |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | enoyl-[acyl-carrier-protein] reductase (NADH) activity | |
Molecular Function | NAD binding | |
Molecular Function | trans-2-enoyl-CoA reductase (NADH) activity | |
Biological Process | fatty acid biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEnoyl-[acyl-carrier-protein] reductase [NADH]
- EC number
- Short namesENR
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ1AHB5
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-80 | Trans-2-enoyl-CoA reductase-like NAD(P)H binding | ||||
Sequence: IIKPRVRGFICVTTHPAGCEANVKQQIDYVEAKGPVVNGPKKVLVIGSSTGYGLAARITAAFGSGADTLGVFFERPGSE | ||||||
Domain | 82-317 | Trans-2-enoyl-CoA reductase catalytic | ||||
Sequence: KPGTAGWYNSATFEKFAHEKGLYARSINGDAFSDEVKRLTIETIKRDLGKVDLVVYSLAAPRRTHPKSGEVFSSTLKPIGKSVSFRGLDTDKEVIKDVVLEAASDQEVADTVAVMGGEDWQMWIDALLEADVLADGAKTTAFTYLGEKITHDIYWNGSIGAAKKDLDQKVLGIRDKLAPLGGDARVSVLKAVVTQASSAIPMMPLYLSLLFKVMKEQGTHEGCIEQVDGLYRESLY | ||||||
Domain | 323-386 | Enoyl reductase FAD binding | ||||
Sequence: LDDEGRLRADYKELQPEVQSRVEELWDKVTNENLYELTDFAGYKSEFLNLFGFEVAGVDYEQDV |
Sequence similarities
Belongs to the TER reductase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length398
- Mass (Da)43,514
- Last updated2006-07-11 v1
- Checksum8A63D511AC824ACC