D0CAD5 · D0CAD5_ACIB2
- ProteinEnoyl-[acyl-carrier-protein] reductase [NADH]
- GenefabI
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids288 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
Catalytic activity
- a 2,3-saturated acyl-[ACP] + NAD+ = a (2E)-enoyl-[ACP] + NADH + H+
Pathway
Lipid metabolism; fatty acid biosynthesis.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 36 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 36 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 36 | NAD+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 42 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 42-43 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SI | ||||||
Binding site | 43 | NAD+ 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: I | ||||||
Binding site | 43 | NAD+ 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: I | ||||||
Binding site | 44 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 44 | NAD+ 2 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 87 | NAD+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 87 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 87-88 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DV | ||||||
Binding site | 88 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 88 | NAD+ 2 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 115 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 115 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 116 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 116 | NAD+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 118 | substrate | ||||
Sequence: A | ||||||
Active site | 170 | Proton acceptor | ||||
Sequence: Y | ||||||
Active site | 180 | Proton acceptor | ||||
Sequence: Y | ||||||
Binding site | 187 | NAD+ 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: K | ||||||
Binding site | 187 | NAD+ 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: K | ||||||
Binding site | 187 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 216 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 216 | NAD+ 2 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 216-220 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: IRTLA | ||||||
Binding site | 218 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 218 | NAD+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 220 | NAD+ 2 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 220 | NAD+ 1 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Site | 225 | Involved in acyl-ACP binding | ||||
Sequence: K | ||||||
Site | 228 | Involved in acyl-ACP binding | ||||
Sequence: R | ||||||
Site | 229 | Involved in acyl-ACP binding | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | enoyl-[acyl-carrier-protein] reductase (NADH) activity | |
Molecular Function | nucleotide binding | |
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
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Acinetobacter > Acinetobacter calcoaceticus/baumannii complex
Accessions
- Primary accessionD0CAD5
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length288
- Mass (Da)31,031
- Last updated2009-11-24 v1
- Checksum475939970624830C
Keywords
- Technical term