Q97LU2 · FABV_CLOAB
- ProteinTrans-2-enoyl-CoA reductase [NADH]
- GenefabV
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids398 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the fatty acid synthesis (FAS II). Catalyzes the reduction of the carbon-carbon double bond of crotonyl-CoA to yield butyryl-CoA.
Miscellaneous
Possesses high activity for the reduction reaction, but no activity for the reverse oxidation reaction.
Catalytic activity
- a 2,3-saturated acyl-CoA + NAD+ = a (2E)-enoyl-CoA + NADH + H+
Biotechnology
Used in the biosynthesis of medium-chain volatile alcohols as biofuels engineered by microorganisms. The switch from the native flavin-dependent enoyl-CoA reductase used in the production of n-butanol, a key second-generation biofuel, to a flavin-independent trans-enoyl-CoA reductase from C.acetobutylicum leads to an order of magnitude increase in product yield in engineered E.coli.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
105.4 μM | NAD | 6.2 | 25 |
kcat is 28.2 sec-1 for reductase activity (at pH 6.2 and 25 degrees Celsius).
Pathway
Lipid metabolism; fatty acid biosynthesis.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 47-52 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 74-75 | NAD+ (UniProtKB | ChEBI) | |||
Site | 75 | Plays an important role in discriminating NADH against NADPH | |||
Binding site | 111-112 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 139-140 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 225 | substrate | |||
Active site | 235 | Proton donor | |||
Binding site | 244 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 274-276 | NAD+ (UniProtKB | ChEBI) | |||
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 nameTrans-2-enoyl-CoA reductase [NADH]
- EC number
- Short namesTER
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionQ97LU2
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 11 | Slight decrease of catalytic efficiency and 3-fold increase of the affinity for NADH compared to wild-type. | |||
Mutagenesis | 75 | Able to use both NADH and NADPH as cofactor. | |||
Mutagenesis | 225 | 12-fold decrease of catalytic efficiency and slight decrease of the affinity for NADH compared to wild-type. | |||
Mutagenesis | 235 | Loss of reductase activity. | |||
Mutagenesis | 244 | Loss of reductase activity. | |||
Mutagenesis | 245 | Slight decrease of catalytic efficiency and affinity for NADH compared to wild-type. | |||
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000220040 | 1-398 | Trans-2-enoyl-CoA reductase [NADH] | ||
Interaction
Structure
Sequence
- Sequence statusComplete
- Length398
- Mass (Da)45,650
- Last updated2001-10-01 v1
- Checksum59324A21CA466DFC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE001437 EMBL· GenBank· DDBJ | AAK78442.1 EMBL· GenBank· DDBJ | Genomic DNA |