ID FABI_ECOLI Reviewed; 262 AA. AC P0AEK4; P29132; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 152. DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] FabI; DE Short=ENR; DE EC=1.3.1.9; DE AltName: Full=NADH-dependent enoyl-ACP reductase; GN Name=fabI; Synonyms=envM; OrderedLocusNames=b1288, JW1281; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31, AND RP MUTAGENESIS OF GLY-93. RX PubMed=1364817; DOI=10.1099/00221287-138-10-2093; RA Bergler H., Hoegenauer G., Turnowsky F.; RT "Sequences of the envM gene and of two mutated alleles in Escherichia RT coli."; RL J. Gen. Microbiol. 138:2093-2100(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8075395; DOI=10.1007/bf00028873; RA Kater M.M., Koningstein G.M., Nijkamp H.J.J., Stuitje A.R.; RT "The use of a hybrid genetic system to study the functional relationship RT between prokaryotic and plant multi-enzyme fatty acid synthetase RT complexes."; RL Plant Mol. Biol. 25:771-790(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., RA Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN ENOYL-ACP REDUCTASE, CATALYTIC RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION. RX PubMed=8119879; DOI=10.1016/s0021-9258(17)37485-9; RA Bergler H., Wallner P., Ebeling A., Leitinger B., Fuchsbichler S., RA Aschauer H., Kollenz G., Hoegenauer G., Turnowsky F.; RT "Protein EnvM is the NADH-dependent enoyl-ACP reductase (FabI) of RT Escherichia coli."; RL J. Biol. Chem. 269:5493-5496(1994). RN [7] RP PROTEIN SEQUENCE OF 2-13. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [8] RP PROTEIN SEQUENCE OF 2-12. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.; RL Submitted (FEB-1996) to UniProtKB. RN [9] RP FUNCTION IN FATTY ACID BIOSYNTHESIS, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=7592873; DOI=10.1074/jbc.270.44.26538; RA Heath R.J., Rock C.O.; RT "Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in RT completing cycles of fatty acid elongation in Escherichia coli."; RL J. Biol. Chem. 270:26538-26542(1995). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=8910376; DOI=10.1074/jbc.271.44.27795; RA Heath R.J., Rock C.O.; RT "Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein RT dehydratases in Escherichia coli fatty acid biosynthesis."; RL J. Biol. Chem. 271:27795-27801(1996). RN [11] RP ACTIVITY REGULATION, AND MUTAGENESIS OF GLY-93; MET-159 AND PHE-203. RX PubMed=9707111; DOI=10.1038/28970; RA McMurry L.M., Oethinger M., Levy S.B.; RT "Triclosan targets lipid synthesis."; RL Nature 394:531-532(1998). RN [12] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=10629181; DOI=10.1128/jb.182.2.365-370.2000; RA Choi K.-H., Heath R.J., Rock C.O.; RT "Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining RT factor in branched-chain fatty acid biosynthesis."; RL J. Bacteriol. 182:365-370(2000). RN [13] RP CATALYTIC ACTIVITY. RX PubMed=11007778; DOI=10.1074/jbc.m005611200; RA Heath R.J., Su N., Murphy C.K., Rock C.O.; RT "The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus RT subtilis."; RL J. Biol. Chem. 275:40128-40133(2000). RN [14] RP ACTIVITY REGULATION. RX PubMed=19959361; DOI=10.1016/j.bmcl.2009.11.042; RA Yao J., Zhang Q., Min J., He J., Yu Z.; RT "Novel enoyl-ACP reductase (FabI) potential inhibitors of Escherichia coli RT from Chinese medicine monomers."; RL Bioorg. Med. Chem. Lett. 20:56-59(2010). RN [15] RP FUNCTION IN BIOTIN BIOSYNTHESIS, AND PATHWAY. RX PubMed=20693992; DOI=10.1038/nchembio.420; RA Lin S., Hanson R.E., Cronan J.E.; RT "Biotin synthesis begins by hijacking the fatty acid synthetic pathway."; RL Nat. Chem. Biol. 6:682-688(2010). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, RP ACTIVITY REGULATION, AND SUBUNIT. RX PubMed=8953047; DOI=10.1126/science.274.5295.2107; RA Baldock C., Rafferty J.B., Sedelnikova S.E., Baker P.J., Stuitje A.R., RA Slabas A.R., Hawkes T.R., Rice D.W.; RT "A mechanism of drug action revealed by structural studies of enoyl RT reductase."; RL Science 274:2107-2110(1996). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, RP ACTIVITY REGULATION, AND SUBUNIT. RX PubMed=10493822; DOI=10.1021/bi9907779; RA Ward W.H., Holdgate G.A., Rowsell S., McLean E.G., Pauptit R.A., RA Clayton E., Nichols W.W., Colls J.G., Minshull C.A., Jude D.A., Mistry A., RA Timms D., Camble R., Hales N.J., Britton C.J., Taylor I.W.; RT "Kinetic and structural characteristics of the inhibition of enoyl (acyl RT carrier protein) reductase by triclosan."; RL Biochemistry 38:12514-12525(1999). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, RP ACTIVITY REGULATION, AND SUBUNIT. RX PubMed=10398587; DOI=10.1006/jmbi.1999.2907; RA Stewart M.J., Parikh S., Xiao G., Tonge P.J., Kisker C.; RT "Structural basis and mechanism of enoyl reductase inhibition by RT triclosan."; RL J. Mol. Biol. 290:859-865(1999). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR. RX PubMed=10201369; DOI=10.1038/18803; RA Levy C.W., Roujeinikova A., Sedelnikova S., Baker P.J., Stuitje A.R., RA Slabas A.R., Rice D.W., Rafferty J.B.; RT "Molecular basis of triclosan activity."; RL Nature 398:383-384(1999). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR. RX PubMed=10595560; DOI=10.1110/ps.8.11.2529; RA Qiu X., Janson C.A., Court R.I., Smyth M.G., Payne D.J., Abdel-Meguid S.S.; RT "Molecular basis for triclosan activity involves a flipping loop in the RT active site."; RL Protein Sci. 8:2529-2532(1999). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, RP AND ACTIVITY REGULATION. RX PubMed=11514139; DOI=10.1016/s0960-894x(01)00404-8; RA Heerding D.A., Chan G., DeWolf W.E., Fosberry A.P., Janson C.A., RA Jaworski D.D., McManus E., Miller W.H., Moore T.D., Payne D.J., Qiu X., RA Rittenhouse S.F., Slater-Radosti C., Smith W., Takata D.T., Vaidya K.S., RA Yuan C.C., Huffman W.F.; RT "1,4-Disubstituted imidazoles are potential antibacterial agents RT functioning as inhibitors of enoyl acyl carrier protein reductase (FabI)."; RL Bioorg. Med. Chem. Lett. 11:2061-2065(2001). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, RP AND ACTIVITY REGULATION. RX PubMed=12109908; DOI=10.1021/jm020050+; RA Miller W.H., Seefeld M.A., Newlander K.A., Uzinskas I.N., Burgess W.J., RA Heerding D.A., Yuan C.C., Head M.S., Payne D.J., Rittenhouse S.F., RA Moore T.D., Pearson S.C., Berry V., DeWolf W.E. Jr., Keller P.M., RA Polizzi B.J., Qiu X., Janson C.A., Huffman W.F.; RT "Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP RT reductase (FabI)."; RL J. Med. Chem. 45:3246-3256(2002). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, RP AND ACTIVITY REGULATION. RX PubMed=12699381; DOI=10.1021/jm0204035; RA Seefeld M.A., Miller W.H., Newlander K.A., Burgess W.J., DeWolf W.E. Jr., RA Elkins P.A., Head M.S., Jakas D.R., Janson C.A., Keller P.M., Manley P.J., RA Moore T.D., Payne D.J., Pearson S., Polizzi B.J., Qiu X., Rittenhouse S.F., RA Uzinskas I.N., Wallis N.G., Huffman W.F.; RT "Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases RT FabI and FabK."; RL J. Med. Chem. 46:1627-1635(2003). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), MUTAGENESIS OF TYR-146; TYR-156; RP LYS-201; ARG-204 AND LYS-205, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=17012233; DOI=10.1074/jbc.m608758200; RA Rafi S., Novichenok P., Kolappan S., Zhang X., Stratton C.F., Rawat R., RA Kisker C., Simmerling C., Tonge P.J.; RT "Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase RT from Escherichia coli."; RL J. Biol. Chem. 281:39285-39293(2006). CC -!- FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an CC enoyl moiety that is covalently linked to an acyl carrier protein CC (ACP). Involved in the elongation cycle of fatty acid which are used in CC the lipid metabolism and in the biotin biosynthesis. CC {ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:20693992, CC ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8119879, CC ECO:0000269|PubMed:8910376}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA- CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9; CC Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:11007778, CC ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8119879, CC ECO:0000269|PubMed:8910376}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10242; CC Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:11007778, CC ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8119879, CC ECO:0000269|PubMed:8910376}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-butenoyl-[ACP] + H(+) + NADH = butanoyl-[ACP] + NAD(+); CC Xref=Rhea:RHEA:54868, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:78453, ChEBI:CHEBI:78454; CC Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:11007778, CC ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8119879, CC ECO:0000269|PubMed:8910376}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54869; CC Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:11007778, CC ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8119879, CC ECO:0000269|PubMed:8910376}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-decenoyl-[ACP] + H(+) + NADH = decanoyl-[ACP] + NAD(+); CC Xref=Rhea:RHEA:54936, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:78467, ChEBI:CHEBI:78468; CC Evidence={ECO:0000269|PubMed:8910376}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54937; CC Evidence={ECO:0000269|PubMed:8910376}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-hexadecenoyl-[ACP] + H(+) + NADH = hexadecanoyl-[ACP] + CC NAD(+); Xref=Rhea:RHEA:54900, Rhea:RHEA-COMP:9651, Rhea:RHEA- CC COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:78481, ChEBI:CHEBI:78483; CC Evidence={ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8910376}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54901; CC Evidence={ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8910376}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,9Z)-hexadecadienoyl-[ACP] + H(+) + NADH = (9Z)- CC hexadecenoyl-[ACP] + NAD(+); Xref=Rhea:RHEA:54904, Rhea:RHEA- CC COMP:10800, Rhea:RHEA-COMP:14036, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83989, CC ChEBI:CHEBI:138403; Evidence={ECO:0000269|PubMed:7592873, CC ECO:0000269|PubMed:8910376}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54905; CC Evidence={ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8910376}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-5-methylhexenoyl-[ACP] + H(+) + NADH = 5-methylhexanoyl- CC [ACP] + NAD(+); Xref=Rhea:RHEA:55124, Rhea:RHEA-COMP:14097, CC Rhea:RHEA-COMP:14098, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:138610, ChEBI:CHEBI:138611; CC Evidence={ECO:0000269|PubMed:10629181}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55125; CC Evidence={ECO:0000269|PubMed:10629181}; CC -!- ACTIVITY REGULATION: Inhibited by diazaborines, triclosan (5-chloro-2- CC 2,4-dichlorophenoxyphenol), 1,4-disubstituted imidazoles, 1,4- CC benzodiazepine derivatives, naphthyridinone derivatives, luteolin and CC curcumin (PubMed:10398587, PubMed:10493822, PubMed:11514139, CC PubMed:12109908, PubMed:12699381, PubMed:19959361, PubMed:8119879, CC PubMed:8953047, PubMed:9707111). The antibiotic diazaborine interferes CC with the activity by binding to the protein and NAD (PubMed:8119879). CC {ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, CC ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, CC ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:19959361, CC ECO:0000269|PubMed:8119879, ECO:0000269|PubMed:8953047, CC ECO:0000269|PubMed:9707111}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.3 uM for trans-2-dodecenoyl-ACP (DD-ACP)(at 25 degrees Celsius CC and pH 8) {ECO:0000269|PubMed:17012233}; CC KM=22 uM for crotonyl-ACP (at 30 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:8119879}; CC KM=24 uM for trans-2-dodecenoyl-CoA (DD-CoA)(at 25 degrees Celsius CC and pH 8) {ECO:0000269|PubMed:17012233}; CC KM=2700 uM for crotonyl-CoA (at 30 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:8119879}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000269|PubMed:7592873}. CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis. CC {ECO:0000305|PubMed:20693992}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10201369, CC ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, CC ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, CC ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, CC ECO:0000269|PubMed:8953047}. CC -!- INTERACTION: CC P0AEK4; P0AF90: rraB; NbExp=2; IntAct=EBI-370029, EBI-544031; CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. FabI subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M97219; AAA17755.1; -; Unassigned_DNA. DR EMBL; X78733; CAA55381.1; -; Genomic_DNA. DR EMBL; U00096; AAC74370.1; -; Genomic_DNA. DR EMBL; AP009048; BAA14841.2; -; Genomic_DNA. DR PIR; S48029; S48029. DR RefSeq; NP_415804.1; NC_000913.3. DR RefSeq; WP_000506490.1; NZ_STEB01000005.1. DR PDB; 1C14; X-ray; 2.00 A; A/B=1-262. DR PDB; 1D8A; X-ray; 2.20 A; A/B=2-262. DR PDB; 1DFG; X-ray; 2.50 A; A/B=2-262. DR PDB; 1DFH; X-ray; 2.20 A; A/B=2-262. DR PDB; 1DFI; X-ray; 2.09 A; A/B/C/D=2-262. DR PDB; 1I2Z; X-ray; 2.80 A; A/B=1-262. DR PDB; 1I30; X-ray; 2.40 A; A/B=1-262. DR PDB; 1LX6; X-ray; 2.40 A; A/B=1-262. DR PDB; 1LXC; X-ray; 2.40 A; A/B=1-262. DR PDB; 1MFP; X-ray; 2.33 A; A/B=1-262. DR PDB; 1QG6; X-ray; 1.90 A; A/B/C/D=2-262. DR PDB; 1QSG; X-ray; 1.75 A; A/B/C/D/E/F/G/H=1-262. DR PDB; 2FHS; X-ray; 2.70 A; A/B=1-262. DR PDB; 3PJD; X-ray; 2.50 A; A/B=1-262. DR PDB; 3PJE; X-ray; 2.50 A; A/B=1-262. DR PDB; 3PJF; X-ray; 1.90 A; A/B=1-262. DR PDB; 4JQC; X-ray; 2.80 A; A/B=1-262. DR PDB; 4JX8; X-ray; 3.20 A; A/B=1-262. DR PDB; 5CFZ; X-ray; 1.97 A; A/B=1-262. DR PDB; 5CG1; X-ray; 2.07 A; A/B=1-262. DR PDB; 5CG2; X-ray; 2.11 A; A/B=1-262. DR PDB; 7UM8; X-ray; 1.70 A; A/B=1-262. DR PDB; 7UMW; X-ray; 1.54 A; A/B=1-262. DR PDBsum; 1C14; -. DR PDBsum; 1D8A; -. DR PDBsum; 1DFG; -. DR PDBsum; 1DFH; -. DR PDBsum; 1DFI; -. DR PDBsum; 1I2Z; -. DR PDBsum; 1I30; -. DR PDBsum; 1LX6; -. DR PDBsum; 1LXC; -. DR PDBsum; 1MFP; -. DR PDBsum; 1QG6; -. DR PDBsum; 1QSG; -. DR PDBsum; 2FHS; -. DR PDBsum; 3PJD; -. DR PDBsum; 3PJE; -. DR PDBsum; 3PJF; -. DR PDBsum; 4JQC; -. DR PDBsum; 4JX8; -. DR PDBsum; 5CFZ; -. DR PDBsum; 5CG1; -. DR PDBsum; 5CG2; -. DR PDBsum; 7UM8; -. DR PDBsum; 7UMW; -. DR AlphaFoldDB; P0AEK4; -. DR SMR; P0AEK4; -. DR BioGRID; 4260135; 290. DR DIP; DIP-31867N; -. DR IntAct; P0AEK4; 12. DR STRING; 511145.b1288; -. DR BindingDB; P0AEK4; -. DR ChEMBL; CHEMBL1857; -. DR ChEMBL; CHEMBL2364678; -. DR DrugBank; DB04030; 1,3,4,9-Tetrahydro-2-(Hydroxybenzoyl)-9-[(4-Hydroxyphenyl)Methyl]-6-Methoxy-2h-Pyrido[3,4-B]Indole. DR DrugBank; DB08265; 2-(TOLUENE-4-SULFONYL)-2H-BENZO[D][1,2,3]DIAZABORININ-1-OL. DR DrugBank; DB01865; 3-(6-Aminopyridin-3-Yl)-N-Methyl-N-[(1-Methyl-1h-Indol-2-Yl)Methyl]Acrylamide. DR DrugBank; DB03534; 3-[(Acetyl-Methyl-Amino)-Methyl]-4-Amino-N-Methyl-N-(1-Methyl-1h-Indol-2-Ylmethyl)-Benzamide. DR DrugBank; DB03030; 4-(2-Thienyl)-1-(4-Methylbenzyl)-1h-Imidazole. DR DrugBank; DB08605; 6-METHYL-2(PROPANE-1-SULFONYL)-2H-THIENO[3,2-D][1,2,3]DIAZABORININ-1-OL. DR DrugBank; DB02379; Beta-D-Glucose. DR DrugBank; DB01691; Indole Naphthyridinone. DR DrugBank; DB08604; Triclosan. DR DrugCentral; P0AEK4; -. DR SwissLipids; SLP:000001775; -. DR jPOST; P0AEK4; -. DR PaxDb; 511145-b1288; -. DR EnsemblBacteria; AAC74370; AAC74370; b1288. DR GeneID; 83576489; -. DR GeneID; 945870; -. DR KEGG; ecj:JW1281; -. DR KEGG; eco:b1288; -. DR PATRIC; fig|1411691.4.peg.991; -. DR EchoBASE; EB1490; -. DR eggNOG; COG0623; Bacteria. DR InParanoid; P0AEK4; -. DR OMA; GILDMIH; -. DR OrthoDB; 9803628at2; -. DR PhylomeDB; P0AEK4; -. DR BioCyc; EcoCyc:ENOYL-ACP-REDUCT-NADH-MONOMER; -. DR BioCyc; MetaCyc:ENOYL-ACP-REDUCT-NADH-MONOMER; -. DR BRENDA; 1.3.1.9; 2026. DR SABIO-RK; P0AEK4; -. DR UniPathway; UPA00078; -. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; P0AEK4; -. DR PRO; PR:P0AEK4; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:1902494; C:catalytic complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc. DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IDA:UniProtKB. DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IDA:EcoCyc. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. DR GO; GO:0070404; F:NADH binding; IDA:UniProtKB. DR GO; GO:0009102; P:biotin biosynthetic process; IMP:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; IDA:UniProtKB. DR GO; GO:0008610; P:lipid biosynthetic process; IDA:EcoCyc. DR GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR CDD; cd05372; ENR_SDR; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR43159; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1. DR PANTHER; PTHR43159:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH] FABI; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1. DR PRINTS; PR00081; GDHRDH. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SWISS-2DPAGE; P0AEK4; -. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic resistance; Direct protein sequencing; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; NAD; Oxidoreductase; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1364817, FT ECO:0000269|PubMed:9298646, ECO:0000269|Ref.8" FT CHAIN 2..262 FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH] FabI" FT /id="PRO_0000054899" FT ACT_SITE 146 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 156 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10201369, FT ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, FT ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, FT ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, FT ECO:0000269|PubMed:8953047" FT BINDING 19..20 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10201369, FT ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, FT ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, FT ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, FT ECO:0000269|PubMed:8953047" FT BINDING 40 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10201369, FT ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, FT ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, FT ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, FT ECO:0000269|PubMed:8953047" FT BINDING 64..65 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10201369, FT ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, FT ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, FT ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, FT ECO:0000269|PubMed:8953047" FT BINDING 92 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10201369, FT ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, FT ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, FT ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, FT ECO:0000269|PubMed:8953047" FT BINDING 95 FT /ligand="substrate" FT BINDING 163 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10201369, FT ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, FT ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, FT ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, FT ECO:0000269|PubMed:8953047" FT BINDING 192..196 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:10201369, FT ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, FT ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, FT ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, FT ECO:0000269|PubMed:8953047" FT SITE 201 FT /note="Involved in acyl-ACP binding" FT SITE 204 FT /note="Involved in acyl-ACP binding" FT SITE 205 FT /note="Involved in acyl-ACP binding" FT MUTAGEN 93 FT /note="G->S: Diazaborine resistance." FT /evidence="ECO:0000269|PubMed:1364817, FT ECO:0000269|PubMed:9707111" FT MUTAGEN 93 FT /note="G->V: Triclosan resistance." FT /evidence="ECO:0000269|PubMed:1364817, FT ECO:0000269|PubMed:9707111" FT MUTAGEN 146 FT /note="Y->F: Large impact on catalysis, with kcat and FT kcat/Km for DD-ACP decreasing by around 50-fold compared FT with wild-type." FT /evidence="ECO:0000269|PubMed:17012233" FT MUTAGEN 156 FT /note="Y->F: No effect on substrate reduction." FT /evidence="ECO:0000269|PubMed:17012233" FT MUTAGEN 159 FT /note="M->T: Triclosan resistance." FT /evidence="ECO:0000269|PubMed:9707111" FT MUTAGEN 201 FT /note="K->A: No effect on substrate reduction." FT /evidence="ECO:0000269|PubMed:17012233" FT MUTAGEN 201 FT /note="K->E: Little activity toward DD-CoA and DD-ACP." FT /evidence="ECO:0000269|PubMed:17012233" FT MUTAGEN 203 FT /note="F->L: Triclosan resistance." FT /evidence="ECO:0000269|PubMed:9707111" FT MUTAGEN 204 FT /note="R->A: No effect on substrate reduction." FT /evidence="ECO:0000269|PubMed:17012233" FT MUTAGEN 204 FT /note="R->E: Causes a further reduction in kcat/Km for FT reduction of DD-ACP without affecting kcat/Km for the FT DD-CoA substrate." FT /evidence="ECO:0000269|PubMed:17012233" FT MUTAGEN 205 FT /note="K->A: No effect on substrate reduction." FT /evidence="ECO:0000269|PubMed:17012233" FT MUTAGEN 205 FT /note="K->E: Causes a further reduction in kcat/Km for FT reduction of DD-ACP without affecting kcat/Km for the FT DD-CoA substrate. Has a larger impact on substrate FT reduction." FT /evidence="ECO:0000269|PubMed:17012233" FT MUTAGEN 241 FT /note="S->F: Produces temperature-sensitive phenotype." FT TURN 3..6 FT /evidence="ECO:0007829|PDB:7UMW" FT STRAND 8..11 FT /evidence="ECO:0007829|PDB:7UMW" FT STRAND 16..19 FT /evidence="ECO:0007829|PDB:1DFI" FT HELIX 20..30 FT /evidence="ECO:0007829|PDB:7UMW" FT STRAND 34..41 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 42..54 FT /evidence="ECO:0007829|PDB:7UMW" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 68..79 FT /evidence="ECO:0007829|PDB:7UMW" FT STRAND 83..90 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 97..100 FT /evidence="ECO:0007829|PDB:7UMW" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:4JX8" FT HELIX 104..107 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 110..120 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 122..131 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:7UMW" FT STRAND 135..145 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:7UMW" FT TURN 154..157 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 158..177 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:7UMW" FT STRAND 182..189 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:7UMW" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:1MFP" FT HELIX 203..213 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 222..232 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:7UMW" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:7UMW" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:7UMW" SQ SEQUENCE 262 AA; 27864 MW; 436A89AF349D1866 CRC64; MGFLSGKRIL VTGVASKLSI AYGIAQAMHR EGAELAFTYQ NDKLKGRVEE FAAQLGSDIV LQCDVAEDAS IDTMFAELGK VWPKFDGFVH SIGFAPGDQL DGDYVNAVTR EGFKIAHDIS SYSFVAMAKA CRSMLNPGSA LLTLSYLGAE RAIPNYNVMG LAKASLEANV RYMANAMGPE GVRVNAISAG PIRTLAASGI KDFRKMLAHC EAVTPIRRTV TIEDVGNSAA FLCSDLSAGI SGEVVHVDGG FSIAAMNELE LK //