FABI_ECOLI
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 03-AUG-2022, entry version 144.
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; Proteobacteria; 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}.
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DR EMBL; M97219; AAA17755.1; -; Unassigned_DNA.
DR EMBL; X78733; CAA55381.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74370.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14841.1; -; 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 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 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 SWISS-2DPAGE; P0AEK4; -.
DR jPOST; P0AEK4; -.
DR PaxDb; P0AEK4; -.
DR PRIDE; P0AEK4; -.
DR EnsemblBacteria; AAC74370; AAC74370; b1288.
DR EnsemblBacteria; BAA14841; BAA14841; BAA14841.
DR GeneID; 67417387; -.
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 PhylomeDB; P0AEK4; -.
DR BioCyc; EcoCyc:ENOYL-ACP-REDUCT-NADH-MON; -.
DR BioCyc; MetaCyc:ENOYL-ACP-REDUCT-NADH-MON; -.
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; IPI:UniProtKB.
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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd05372; ENR_SDR; 1.
DR InterPro; IPR014358; Enoyl-ACP_Rdtase_NADH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43159; PTHR43159; 1.
DR PIRSF; PIRSF000094; Enoyl-ACP_rdct; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
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 DD-
FT 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 DD-
FT CoA substrate. Has a larger impact on substrate 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:1QSG"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1QSG"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1DFI"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:1QSG"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:1QSG"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1QSG"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:1QSG"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1QSG"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:1QSG"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:1QSG"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1QSG"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:4JX8"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1QSG"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:1QSG"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:1QSG"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1QSG"
FT STRAND 135..145
FT /evidence="ECO:0007829|PDB:1QSG"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1QSG"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:1QSG"
FT HELIX 158..177
FT /evidence="ECO:0007829|PDB:1QSG"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:1QSG"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:1QSG"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1QSG"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1MFP"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:1QSG"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:1QSG"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:1QSG"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1QSG"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1QSG"
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
