FABG_ECOLI
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 03-AUG-2022, entry version 137.
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; Proteobacteria; 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 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; P0AEK2; -.
DR PRIDE; P0AEK2; -.
DR EnsemblBacteria; AAC74177; AAC74177; b1093.
DR EnsemblBacteria; BAA35901; BAA35901; BAA35901.
DR GeneID; 66670641; -.
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; KMPERDY; -.
DR PhylomeDB; P0AEK2; -.
DR BioCyc; EcoCyc:3-OXOACYL-ACP-REDUCT-MON; -.
DR BioCyc; MetaCyc:3-OXOACYL-ACP-REDUCT-MON; -.
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 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 PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01830; 3oxo_ACP_reduc; 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
