ID   FABG_ECOLI              Reviewed;         244 AA.
AC   P0AEK2; P25716; P78221; Q47202;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase FabG;
DE            EC=1.1.1.100 {ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8631920, ECO:0000269|PubMed:8910376};
DE   AltName: Full=3-ketoacyl-acyl carrier protein reductase;
DE   AltName: Full=Beta-Ketoacyl-acyl carrier protein reductase;
DE   AltName: Full=Beta-ketoacyl-ACP reductase;
GN   Name=fabG; OrderedLocusNames=b1093, JW1079;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NOMENCLATURE.
RC   STRAIN=K12;
RX   PubMed=1556094; DOI=10.1016/s0021-9258(18)42616-6;
RA   Rawlings M., Cronan J.E. Jr.;
RT   "The gene encoding Escherichia coli acyl carrier protein lies within a
RT   cluster of fatty acid biosynthetic genes.";
RL   J. Biol. Chem. 267:5751-5754(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RC   STRAIN=K12;
RX   PubMed=1314802; DOI=10.1128/jb.174.9.2851-2857.1992;
RA   Verwoert I.I.G.S., Verbree E.C., van der Linden K.H., Nijkamp H.J.,
RA   Stuitje A.R.;
RT   "Cloning, nucleotide sequence, and expression of the Escherichia coli fabD
RT   gene, encoding malonyl coenzyme A-acyl carrier protein transacylase.";
RL   J. Bacteriol. 174:2851-2857(1992).
RN   [6]
RP   SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=4381013; DOI=10.1016/0005-2760(66)90001-4;
RA   Toomey R.E., Wakil S.J.;
RT   "Studies on the mechanism of fatty acid synthesis. XV. Preparation and
RT   general properties of beta-ketoacyl acyl carrier protein reductase from
RT   Escherichia coli.";
RL   Biochim. Biophys. Acta 116:189-197(1966).
RN   [7]
RP   FUNCTION, 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   [8]
RP   FUNCTION AS A BETA-KETOACYL-ACP REDUCTASE, AND CATALYTIC ACTIVITY.
RX   PubMed=8631920; DOI=10.1074/jbc.271.18.10996;
RA   Heath R.J., Rock C.O.;
RT   "Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by
RT   acyl-acyl carrier protein in Escherichia coli.";
RL   J. Biol. Chem. 271:10996-11000(1996).
RN   [9]
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   [10]
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   [11]
RP   FUNCTION IN FATTY ACID BIOSYNTHESIS AND AS A BETA-KETOACYL-ACP REDUCTASE,
RP   AND MUTAGENESIS OF ALA-154 AND GLU-233.
RX   PubMed=14996818; DOI=10.1128/jb.186.6.1869-1878.2004;
RA   Lai C.Y., Cronan J.E.;
RT   "Isolation and characterization of beta-ketoacyl-acyl carrier protein
RT   reductase (fabG) mutants of Escherichia coli and Salmonella enterica
RT   serovar Typhimurium.";
RL   J. Bacteriol. 186:1869-1878(2004).
RN   [12]
RP   ACTIVITY REGULATION.
RX   PubMed=18977209; DOI=10.1016/j.cbi.2008.09.030;
RA   Kristan K., Bratkovic T., Sova M., Gobec S., Prezelj A., Urleb U.;
RT   "Novel inhibitors of beta-ketoacyl-ACP reductase from Escherichia coli.";
RL   Chem. Biol. Interact. 178:310-316(2009).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND SUBUNIT.
RX   PubMed=11669613; DOI=10.1021/bi010737g;
RA   Price A.C., Zhang Y.-M., Rock C.O., White S.W.;
RT   "Structure of beta-ketoacyl-[acyl carrier-protein] reductase from
RT   Escherichia coli: negative cooperativity and its structural basis.";
RL   Biochemistry 40:12772-12781(2001).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH NADP, MUTAGENESIS OF
RP   TYR-151 AND LYS-155, REACTION MECHANISM, AND SUBUNIT.
RX   PubMed=15016358; DOI=10.1016/j.str.2004.02.008;
RA   Price A.C., Zhang Y.M., Rock C.O., White S.W.;
RT   "Cofactor-induced conformational rearrangements establish a catalytically
RT   competent active site and a proton relay conduit in FabG.";
RL   Structure 12:417-428(2004).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP
CC       substrates to beta-hydroxyacyl-ACP products, the first reductive step
CC       in the elongation cycle of fatty acid biosynthesis.
CC       {ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:14996818,
CC       ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8631920,
CC       ECO:0000269|PubMed:8910376}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC         + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC         COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC         Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873,
CC         ECO:0000269|PubMed:8631920, ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399;
CC         Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873,
CC         ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxobutanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxybutanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41804, Rhea:RHEA-COMP:9625,
CC         Rhea:RHEA-COMP:9626, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78450, ChEBI:CHEBI:78451;
CC         Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873,
CC         ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41805;
CC         Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:7592873,
CC         ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxopentanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxypentanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:55100, Rhea:RHEA-COMP:9939,
CC         Rhea:RHEA-COMP:14091, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78818, ChEBI:CHEBI:78983;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55101;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxohexanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41824, Rhea:RHEA-COMP:9629,
CC         Rhea:RHEA-COMP:9630, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78456, ChEBI:CHEBI:78457;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41825;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxoheptanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyheptanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:55104, Rhea:RHEA-COMP:9943,
CC         Rhea:RHEA-COMP:14092, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78824, ChEBI:CHEBI:78987;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55105;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxooctanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41840, Rhea:RHEA-COMP:9633,
CC         Rhea:RHEA-COMP:9634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78460, ChEBI:CHEBI:78461;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41841;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxononanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxynonanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:55108, Rhea:RHEA-COMP:9944,
CC         Rhea:RHEA-COMP:14093, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78826, ChEBI:CHEBI:78988;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55109;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxodecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydecanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41856, Rhea:RHEA-COMP:9637,
CC         Rhea:RHEA-COMP:9638, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78464, ChEBI:CHEBI:78466;
CC         Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41857;
CC         Evidence={ECO:0000269|PubMed:10629181, ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxohexadecanoyl-[ACP] + H(+) + NADPH = (3R)-
CC         hydroxyhexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41904, Rhea:RHEA-
CC         COMP:9649, Rhea:RHEA-COMP:9650, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78478, ChEBI:CHEBI:78480;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41905;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxo-(9Z)-hexadecenoyl-[ACP] + H(+) + NADPH = (3R)-hydroxy-
CC         (9Z)-hexadecenoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:54928, Rhea:RHEA-
CC         COMP:14038, Rhea:RHEA-COMP:14040, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:138406,
CC         ChEBI:CHEBI:138407; Evidence={ECO:0000269|PubMed:8910376};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54929;
CC         Evidence={ECO:0000269|PubMed:8910376};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-methyl-3-oxopentanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxy-4-
CC         methylpentanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:55112, Rhea:RHEA-
CC         COMP:9940, Rhea:RHEA-COMP:14094, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78820,
CC         ChEBI:CHEBI:78984; Evidence={ECO:0000269|PubMed:10629181};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55113;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-methyl-3-oxohexanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxy-5-
CC         methylhexanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:55116, Rhea:RHEA-
CC         COMP:9941, Rhea:RHEA-COMP:14095, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78822,
CC         ChEBI:CHEBI:78986; Evidence={ECO:0000269|PubMed:10629181};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55117;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-methyl-3-oxohexanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxy-4-
CC         methylhexanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:55120, Rhea:RHEA-
CC         COMP:9942, Rhea:RHEA-COMP:14096, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78823,
CC         ChEBI:CHEBI:78985; Evidence={ECO:0000269|PubMed:10629181};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55121;
CC         Evidence={ECO:0000269|PubMed:10629181};
CC   -!- ACTIVITY REGULATION: Inhibited by cinnamic acid derivatives.
CC       {ECO:0000269|PubMed:18977209}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is between 6.0 and 7.0. {ECO:0000269|PubMed:4381013};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000269|PubMed:14996818, ECO:0000269|PubMed:7592873}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11669613,
CC       ECO:0000269|PubMed:15016358}.
CC   -!- MISCELLANEOUS: Calcium ions stabilize the structure, and may inhibit
CC       FabG activity by obstructing access to the active site.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; M84991; AAA23739.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74177.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35901.1; -; Genomic_DNA.
DR   EMBL; M87040; AAA23743.1; -; Genomic_DNA.
DR   PIR; B64853; B42147.
DR   RefSeq; NP_415611.1; NC_000913.3.
DR   RefSeq; WP_001008535.1; NZ_STEB01000016.1.
DR   PDB; 1I01; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-244.
DR   PDB; 1Q7B; X-ray; 2.05 A; A/B/C/D=1-244.
DR   PDB; 1Q7C; X-ray; 2.50 A; A/B=1-244.
DR   PDBsum; 1I01; -.
DR   PDBsum; 1Q7B; -.
DR   PDBsum; 1Q7C; -.
DR   AlphaFoldDB; P0AEK2; -.
DR   SASBDB; P0AEK2; -.
DR   SMR; P0AEK2; -.
DR   BioGRID; 4260080; 228.
DR   DIP; DIP-31869N; -.
DR   IntAct; P0AEK2; 6.
DR   STRING; 511145.b1093; -.
DR   DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR   SwissLipids; SLP:000000853; -.
DR   jPOST; P0AEK2; -.
DR   PaxDb; 511145-b1093; -.
DR   EnsemblBacteria; AAC74177; AAC74177; b1093.
DR   GeneID; 75203679; -.
DR   GeneID; 945645; -.
DR   KEGG; ecj:JW1079; -.
DR   KEGG; eco:b1093; -.
DR   PATRIC; fig|1411691.4.peg.1175; -.
DR   EchoBASE; EB1294; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_3_6; -.
DR   InParanoid; P0AEK2; -.
DR   OMA; LFGVQCD; -.
DR   OrthoDB; 9804774at2; -.
DR   PhylomeDB; P0AEK2; -.
DR   BioCyc; EcoCyc:3-OXOACYL-ACP-REDUCT-MONOMER; -.
DR   BioCyc; MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMER; -.
DR   BRENDA; 1.1.1.100; 2026.
DR   UniPathway; UPA00094; -.
DR   EvolutionaryTrace; P0AEK2; -.
DR   PRO; PR:P0AEK2; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0009102; P:biotin biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IMP:EcoCyc.
DR   GO; GO:0030497; P:fatty acid elongation; IMP:UniProtKB.
DR   GO; GO:0008610; P:lipid biosynthetic process; IMP:EcoCyc.
DR   CDD; cd05333; BKR_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR011284; 3oxo_ACP_reduc.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   NCBIfam; TIGR01830; 3oxo_ACP_reduc; 1.
DR   PANTHER; PTHR42879; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE; 1.
DR   PANTHER; PTHR42879:SF2; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Metal-binding; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..244
FT                   /note="3-oxoacyl-[acyl-carrier-protein] reductase FabG"
FT                   /id="PRO_0000054672"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         12..15
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:15016358,
FT                   ECO:0007744|PDB:1Q7B, ECO:0007744|PDB:1Q7C"
FT   BINDING         37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:15016358,
FT                   ECO:0007744|PDB:1Q7B, ECO:0007744|PDB:1Q7C"
FT   BINDING         50
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   BINDING         53
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   BINDING         59..60
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:15016358,
FT                   ECO:0007744|PDB:1Q7B, ECO:0007744|PDB:1Q7C"
FT   BINDING         86
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:15016358,
FT                   ECO:0007744|PDB:1Q7B"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   BINDING         151..155
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:15016358,
FT                   ECO:0007744|PDB:1Q7B, ECO:0007744|PDB:1Q7C"
FT   BINDING         184
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:15016358"
FT   BINDING         233
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   BINDING         234
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   MUTAGEN         151
FT                   /note="Y->F: Defect in the affinity for NADPH."
FT                   /evidence="ECO:0000269|PubMed:15016358"
FT   MUTAGEN         154
FT                   /note="A->T: Decreases in the thermolability of the
FT                   reductase; when associated with K-233."
FT                   /evidence="ECO:0000269|PubMed:14996818"
FT   MUTAGEN         155
FT                   /note="K->A: Defect in the affinity for NADPH."
FT                   /evidence="ECO:0000269|PubMed:15016358"
FT   MUTAGEN         233
FT                   /note="E->K: Decreases in the thermolability of the
FT                   reductase; when associated with T-154."
FT                   /evidence="ECO:0000269|PubMed:14996818"
FT   CONFLICT        30
FT                   /note="A -> G (in Ref. 1; AAA23739)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="Q -> R (in Ref. 1; AAA23739)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..12
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           16..27
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   STRAND          31..38
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           39..49
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           63..76
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   STRAND          81..85
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           100..110
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           112..128
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   STRAND          131..136
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           139..143
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           149..169
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           170..172
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   STRAND          174..181
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           187..190
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           194..201
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           212..223
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   HELIX           225..227
FT                   /evidence="ECO:0007829|PDB:1Q7B"
FT   STRAND          234..238
FT                   /evidence="ECO:0007829|PDB:1Q7B"
SQ   SEQUENCE   244 AA;  25560 MW;  48EC1F2A7F7EEFD9 CRC64;
     MNFEGKIALV TGASRGIGRA IAETLAARGA KVIGTATSEN GAQAISDYLG ANGKGLMLNV
     TDPASIESVL EKIRAEFGEV DILVNNAGIT RDNLLMRMKD EEWNDIIETN LSSVFRLSKA
     VMRAMMKKRH GRIITIGSVV GTMGNGGQAN YAAAKAGLIG FSKSLAREVA SRGITVNVVA
     PGFIETDMTR ALSDDQRAGI LAQVPAGRLG GAQEIANAVA FLASDEAAYI TGETLHVNGG
     MYMV
//