Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
Also known as: JW1281, b1288, envM, fabI
Function
Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis.
Classification
- Family (Pfam)
- PF13561 adh_short_C2
- InterPro
- Enoyl-ACP_Rdtase_NADH, NAD(P)-bd_dom_sf, SDR_fam
- Functional cluster
- RuBisCO & Carbon-Fixation Enzymes
Experimental structures · PDB · 23
- 1C14 X-ray 2.00A
- 1D8A X-ray 2.20A
- 1DFG X-ray 2.50A
- 1DFH X-ray 2.20A
- 1DFI X-ray 2.09A
- 1I2Z X-ray 2.80A
- 1I30 X-ray 2.40A
- 1LX6 X-ray 2.40A
- 1LXC X-ray 2.40A
- 1MFP X-ray 2.33A
- 1QG6 X-ray 1.90A
- 1QSG X-ray 1.75A
- … and 11 more
A predicted model is available from AlphaFold.
Gene Ontology · 12
- GO:1902494 catalytic complex
- GO:0005829 cytosol
- GO:0016020 membrane
- GO:0032991 protein-containing complex
- GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
- GO:0042802 identical protein binding
- GO:0070404 NADH binding
- GO:0009102 biotin biosynthetic process
- GO:0030497 fatty acid elongation
- GO:0008610 lipid biosynthetic process
- GO:0051289 protein homotetramerization
- GO:0046677 response to antibiotic
Drugs targeting this protein · 2
- HEXACHLOROPHENE inhibitor
- TRICLOSAN inhibitor
Related proteins · sequence + function similarity
- Enoyl-[acyl-carrier-protein] reductase [NADH] FabI 1.00
- Enoyl-[acyl-carrier-protein] reductase [NADH] FabI 1.00
- Enoyl-[acyl-carrier-protein] reductase [NADH] FabI 0.95
- Enoyl-[acyl-carrier-protein] reductase [NADH] 2 0.94
- Enoyl-[acyl-carrier-protein] reductase [NADH] 1 0.93
- Enoyl-[acyl-carrier-protein] reductase [NADH] FabI 0.93
- Enoyl-[acyl-carrier-protein] reductase [NADH] FabI 0.93
- Enoyl-[acyl-carrier-protein] reductase [NADH] FabI 0.90
- Enoyl-[acyl-carrier-protein] reductase [NADH] FabI 0.89
- Enoyl-[acyl-carrier-protein] reductase [NADH] FabI 0.86
- Enoyl-[acyl-carrier-protein] reductase [NADH] FabI 0.86
- Enoyl-[acyl-carrier-protein] reductase [NADH] 0.86
Co-cited proteins · studied together in the literature
- Uncharacterized protein YcjD 2 shared papers
- Enoyl-[acyl-carrier-protein] reductase [NADPH] FabI 3 shared papers
- Enoyl-[acyl-carrier-protein] reductase [NADH] FabI 2 shared papers
- Enoyl-[acyl-carrier-protein] reductase [NADH] FabI 1 shared papers
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase 3 shared papers
- 3-oxoacyl-[acyl-carrier-protein] reductase FabG 3 shared papers
- Beta-ketoacyl-[acyl-carrier-protein] synthase III 3 shared papers
- Enoyl-[acyl-carrier-protein] reductase [NADPH] FabL 1 shared papers
- 8-amino-7-oxononanoate synthase 1 shared papers
- Malonyl-[acyl-carrier protein] O-methyltransferase 1 shared papers
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ 2 shared papers
- Pimeloyl-[acyl-carrier protein] methyl ester esterase 1 shared papers
Literature · 23 cited papers
- Biotin synthesis begins by hijacking the fatty acid synthetic pathway. Nat. Chem. Biol. · 2010
- Novel enoyl-ACP reductase (FabI) potential inhibitors of Escherichia coli from Chinese medicine monomers. Bioorg. Med. Chem. Lett. · 2010
- Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli. J. Biol. Chem. · 2006
- Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol. Syst. Biol. · 2006
- Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK. J. Med. Chem. · 2003
- Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP reductase (FabI). J. Med. Chem. · 2002
- 1,4-Disubstituted imidazoles are potential antibacterial agents functioning as inhibitors of enoyl acyl carrier protein reductase (FabI). Bioorg. Med. Chem. Lett. · 2001
- The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis. J. Biol. Chem. · 2000
- Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis. J. Bacteriol. · 2000
- Molecular basis for triclosan activity involves a flipping loop in the active site. Protein Sci. · 1999
- Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan. Biochemistry · 1999
- Structural basis and mechanism of enoyl reductase inhibition by triclosan. J. Mol. Biol. · 1999
- … and 11 more in the literature graph
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