FABB_ECOLI
ID FABB_ECOLI Reviewed; 406 AA.
AC P0A953; P14926; Q9R828; Q9R829; Q9R830;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 1 {ECO:0000305};
DE EC=2.3.1.41 {ECO:0000269|PubMed:19679654, ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:8910376, ECO:0000269|PubMed:9013860};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase I {ECO:0000305};
DE AltName: Full=Beta-ketoacyl-ACP synthase I {ECO:0000303|PubMed:3076376};
DE Short=KAS I;
GN Name=fabB {ECO:0000303|PubMed:3076376}; Synonyms=fabC;
GN OrderedLocusNames=b2323, JW2320;
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 PROTEIN SEQUENCE OF 1-19 AND
RP 158-168.
RC STRAIN=B;
RX PubMed=3076376; DOI=10.1007/bf02983311;
RA Kauppinen S., Siggaard-Andersen M., von Wettstein-Knowles P.;
RT "Beta-ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of
RT the fabB gene and identification of the cerulenin binding residue.";
RL Carlsberg Res. Commun. 53:357-370(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K1060 / fabB5, M5 / fabB15, and MA-1 / fabB3;
RA Siggaard-Andersen M., von Wettstein-Knowles P., Gotthardt-Olsen J.,
RA Bangera G., Chuck J.-A., Pontoppidan B.;
RT "Catalytic residues of beta-ketoacyl-ACP synthases.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 FUNCTION IN UNSATURATED FATTY ACID SYNTHESIS.
RX PubMed=3076377; DOI=10.1007/bf02983312;
RA Siggaard-Andersen M.;
RT "Role of Escherichia coli beta-ketoacyl-ACP synthase I in unsaturated fatty
RT acid synthesis.";
RL Carlsberg Res. Commun. 53:371-379(1988).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=9013860; DOI=10.1016/s0014-5793(96)01437-8;
RA Edwards P., Nelsen J.S., Metz J.G., Dehesh K.;
RT "Cloning of the fabF gene in an expression vector and in vitro
RT characterization of recombinant fabF and fabB encoded enzymes from
RT Escherichia coli.";
RL FEBS Lett. 402:62-66(1997).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP INDUCTION.
RX PubMed=11859088; DOI=10.1074/jbc.m201399200;
RA Zhang Y.-M., Marrakchi H., Rock C.O.;
RT "The FabR (YijC) transcription factor regulates unsaturated fatty acid
RT biosynthesis in Escherichia coli.";
RL J. Biol. Chem. 277:15558-15565(2002).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=19679654; DOI=10.1074/jbc.m109.023440;
RA Feng Y., Cronan J.E.;
RT "Escherichia coli unsaturated fatty acid synthesis: complex transcription
RT of the fabA gene and in vivo identification of the essential reaction
RT catalyzed by FabB.";
RL J. Biol. Chem. 284:29526-29535(2009).
RN [12]
RP INDUCTION.
RX PubMed=21276098; DOI=10.1111/j.1365-2958.2011.07564.x;
RA Feng Y., Cronan J.E.;
RT "Complex binding of the FabR repressor of bacterial unsaturated fatty acid
RT biosynthesis to its cognate promoters.";
RL Mol. Microbiol. 80:195-218(2011).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22017312; DOI=10.1021/bi201199x;
RA Borgaro J.G., Chang A., Machutta C.A., Zhang X., Tonge P.J.;
RT "Substrate recognition by beta-ketoacyl-ACP synthases.";
RL Biochemistry 50:10678-10686(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=10571059; DOI=10.1016/s0014-5793(99)01303-4;
RA Olsen J.G., Kadziola A., von Wettstein-Knowles P., Siggaard-Andersen M.,
RA Lindquist Y., Larsen S.;
RT "The X-ray crystal structure of beta-ketoacyl [acyl carrier-protein]
RT synthase I.";
RL FEBS Lett. 460:46-52(1999).
CC -!- FUNCTION: Involved in the type II fatty acid elongation cycle.
CC Catalyzes the elongation of a wide range of acyl-ACP by the addition of
CC two carbons from malonyl-ACP to an acyl acceptor (PubMed:9013860,
CC PubMed:8910376, PubMed:19679654, PubMed:22017312). Can also use
CC unsaturated fatty acids (PubMed:3076377, PubMed:8910376,
CC PubMed:19679654). Catalyzes a key reaction in unsaturated fatty acid
CC (UFA) synthesis, the elongation of the cis-3-decenoyl-ACP produced by
CC FabA (PubMed:19679654). Can use acyl chains from C-6 to C-14
CC (PubMed:9013860, PubMed:8910376, PubMed:19679654, PubMed:22017312). Has
CC an absolute requirement for an ACP substrate as the acyl donor, and no
CC activity is detected when both substrates are based on CoA
CC (PubMed:22017312). {ECO:0000269|PubMed:19679654,
CC ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:3076377,
CC ECO:0000269|PubMed:8910376, ECO:0000269|PubMed:9013860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41; Evidence={ECO:0000269|PubMed:19679654,
CC ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:8910376,
CC ECO:0000269|PubMed:9013860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC Evidence={ECO:0000269|PubMed:19679654, ECO:0000269|PubMed:22017312,
CC ECO:0000269|PubMed:8910376, ECO:0000269|PubMed:9013860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3Z)-decenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(5Z)-
CC dodecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:54940, Rhea:RHEA-
CC COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9927, Rhea:RHEA-
CC COMP:14042, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78798, ChEBI:CHEBI:138410;
CC Evidence={ECO:0000269|PubMed:19679654};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54941;
CC Evidence={ECO:0000269|PubMed:19679654};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] +
CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460;
CC Evidence={ECO:0000269|PubMed:9013860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837;
CC Evidence={ECO:0000269|PubMed:9013860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] +
CC CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464;
CC Evidence={ECO:0000269|PubMed:9013860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853;
CC Evidence={ECO:0000269|PubMed:9013860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469;
CC Evidence={ECO:0000269|PubMed:9013860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869;
CC Evidence={ECO:0000269|PubMed:9013860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-
CC [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473;
CC Evidence={ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:9013860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885;
CC Evidence={ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:9013860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-
CC oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649,
CC Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477,
CC ChEBI:CHEBI:78478; Evidence={ECO:0000269|PubMed:8910376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901;
CC Evidence={ECO:0000269|PubMed:8910376};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z)-tetradecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(9Z)-
CC hexadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:54924,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:14038,
CC Rhea:RHEA-COMP:14039, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:138405,
CC ChEBI:CHEBI:138406; Evidence={ECO:0000269|PubMed:8910376};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54925;
CC Evidence={ECO:0000269|PubMed:8910376};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.5 uM for malonyl-[ACP] (in the presence of dodecanoyl-[ACP])
CC {ECO:0000269|PubMed:22017312};
CC KM=3.2 uM for dodecanoyl-[ACP] (in the presence of malonyl-[ACP])
CC {ECO:0000269|PubMed:22017312};
CC KM=153 uM for malonyl-CoA (in the presence of dodecanoyl-[ACP])
CC {ECO:0000269|PubMed:22017312};
CC KM=58.6 uM for dodecanoyl-CoA (in the presence of malonyl-[ACP])
CC {ECO:0000269|PubMed:22017312};
CC Note=kcat is 6.6 min(-1) with malonyl-[ACP] as substrate in the
CC presence of dodecanoyl-[ACP]. kcat is 3.4 min(-1) with dodecanoyl-
CC [ACP] in the presence of malonyl-[ACP].
CC {ECO:0000269|PubMed:22017312};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000305|PubMed:19679654, ECO:0000305|PubMed:8910376}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10571059,
CC ECO:0000269|PubMed:9013860}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Mainly activated by FadR, but minor repression is also
CC conferred by FabR (PubMed:11859088, PubMed:21276098).
CC {ECO:0000269|PubMed:11859088, ECO:0000269|PubMed:21276098}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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DR EMBL; M24427; AAC67304.1; -; Genomic_DNA.
DR EMBL; AJ012161; CAA09932.1; -; Genomic_DNA.
DR EMBL; AJ012162; CAA09933.1; -; Genomic_DNA.
DR EMBL; AJ012163; CAA09934.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75383.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16180.1; -; Genomic_DNA.
DR PIR; A31284; SYECA1.
DR RefSeq; NP_416826.1; NC_000913.3.
DR RefSeq; WP_000817178.1; NZ_SSZK01000006.1.
DR PDB; 1DD8; X-ray; 2.30 A; A/B/C/D=1-406.
DR PDB; 1EK4; X-ray; 1.85 A; A/B/C/D=1-406.
DR PDB; 1F91; X-ray; 2.40 A; A/B/C/D=1-406.
DR PDB; 1FJ4; X-ray; 2.35 A; A/B/C/D=1-406.
DR PDB; 1FJ8; X-ray; 2.27 A; A/B/C/D=1-406.
DR PDB; 1G5X; X-ray; 2.45 A; A/B/C/D=1-406.
DR PDB; 1H4F; X-ray; 2.00 A; A/B/C/D=1-406.
DR PDB; 2AQ7; X-ray; 2.30 A; A/B/C/D=1-406.
DR PDB; 2AQB; X-ray; 2.19 A; A/B/C/D=1-406.
DR PDB; 2BUH; X-ray; 1.90 A; A/B/C/D=1-406.
DR PDB; 2BUI; X-ray; 2.40 A; A/B/C/D=1-406.
DR PDB; 2BYW; X-ray; 1.70 A; A/B/C/D=1-406.
DR PDB; 2BYX; X-ray; 2.00 A; A/B/C/D=1-406.
DR PDB; 2BYY; X-ray; 2.20 A; A/B/C/D=1-406.
DR PDB; 2BYZ; X-ray; 1.95 A; A/B/C/D=1-406.
DR PDB; 2BZ3; X-ray; 2.00 A; A/B/C/D=1-406.
DR PDB; 2BZ4; X-ray; 1.86 A; A/B/C/D=1-406.
DR PDB; 2CDH; X-ray; 4.20 A; A/B/C/D/E/F=1-406.
DR PDB; 2CF2; X-ray; 4.30 A; A/J=1-406.
DR PDB; 2VB7; X-ray; 1.60 A; A/B/C/D=1-406.
DR PDB; 2VB8; X-ray; 1.52 A; A/B/C/D=1-406.
DR PDB; 2VB9; X-ray; 1.50 A; A/B/C/D=1-406.
DR PDB; 2VBA; X-ray; 1.36 A; A/B/C/D=1-406.
DR PDB; 5KOF; X-ray; 2.40 A; A/B=1-406.
DR PDB; 6OKC; X-ray; 1.55 A; A/B=1-406.
DR PDB; 6OKF; X-ray; 2.50 A; A/B=1-406.
DR PDBsum; 1DD8; -.
DR PDBsum; 1EK4; -.
DR PDBsum; 1F91; -.
DR PDBsum; 1FJ4; -.
DR PDBsum; 1FJ8; -.
DR PDBsum; 1G5X; -.
DR PDBsum; 1H4F; -.
DR PDBsum; 2AQ7; -.
DR PDBsum; 2AQB; -.
DR PDBsum; 2BUH; -.
DR PDBsum; 2BUI; -.
DR PDBsum; 2BYW; -.
DR PDBsum; 2BYX; -.
DR PDBsum; 2BYY; -.
DR PDBsum; 2BYZ; -.
DR PDBsum; 2BZ3; -.
DR PDBsum; 2BZ4; -.
DR PDBsum; 2CDH; -.
DR PDBsum; 2CF2; -.
DR PDBsum; 2VB7; -.
DR PDBsum; 2VB8; -.
DR PDBsum; 2VB9; -.
DR PDBsum; 2VBA; -.
DR PDBsum; 5KOF; -.
DR PDBsum; 6OKC; -.
DR PDBsum; 6OKF; -.
DR AlphaFoldDB; P0A953; -.
DR SMR; P0A953; -.
DR BioGRID; 4260793; 224.
DR DIP; DIP-29379N; -.
DR IntAct; P0A953; 9.
DR STRING; 511145.b2323; -.
DR BindingDB; P0A953; -.
DR ChEMBL; CHEMBL4913; -.
DR DrugBank; DB08627; (5R)-4-HYDROXY-3,5-DIMETHYL-5-[(1E,3E)-2-METHYLPENTA-1,3-DIENYL]THIOPHEN-2(5H)-ONE.
DR DrugBank; DB08628; (5R)-5-[(1E)-BUTA-1,3-DIENYL]-4-HYDROXY-3,5-DIMETHYLTHIOPHEN-2(5H)-ONE.
DR DrugBank; DB08359; 2-PHENYLAMINO-4-METHYL-5-ACETYL THIAZOLE.
DR DrugBank; DB04302; 4-Hydroxy-3,5-Dimethyl-5-(2-Methyl-Buta-1,3-Dienyl)-5h-Thiophen-2-One.
DR DrugBank; DB03600; Capric acid.
DR DrugBank; DB04519; Caprylic acid.
DR DrugBank; DB01034; Cerulenin.
DR DrugBank; DB03017; Lauric acid.
DR SwissLipids; SLP:000001786; -.
DR jPOST; P0A953; -.
DR PaxDb; P0A953; -.
DR PRIDE; P0A953; -.
DR EnsemblBacteria; AAC75383; AAC75383; b2323.
DR EnsemblBacteria; BAA16180; BAA16180; BAA16180.
DR GeneID; 67416753; -.
DR GeneID; 946799; -.
DR KEGG; ecj:JW2320; -.
DR KEGG; eco:b2323; -.
DR PATRIC; fig|1411691.4.peg.4409; -.
DR EchoBASE; EB0270; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_6; -.
DR InParanoid; P0A953; -.
DR OMA; YAYLSMQ; -.
DR PhylomeDB; P0A953; -.
DR BioCyc; EcoCyc:FABB-MON; -.
DR BioCyc; MetaCyc:FABB-MON; -.
DR BRENDA; 2.3.1.41; 2026.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; P0A953; -.
DR PRO; PR:P0A953; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IDA:EcoCyc.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:EcoCyc.
DR GO; GO:1903966; P:monounsaturated fatty acid biosynthetic process; IMP:EcoCyc.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11712; PTHR11712; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..406
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 1"
FT /id="PRO_0000180311"
FT ACT_SITE 163
FT /evidence="ECO:0000305|PubMed:10571059"
FT VARIANT 4
FT /note="A -> T (in strain: MA-1 / fabB3)"
FT VARIANT 140
FT /note="S -> F (in strain: K1060 / fabB5)"
FT VARIANT 299
FT /note="G -> S (in strain: MA-1 / fabB3)"
FT VARIANT 329
FT /note="A -> V (in strain: M5 / fabB15)"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2VBA"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2AQ7"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2VB9"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:2VBA"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:2VBA"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:2VBA"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:2VB7"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 255..264
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2VB9"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 303..317
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:2BUH"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 338..352
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:2VBA"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:2VB9"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:2VBA"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:2VBA"
FT STRAND 395..402
FT /evidence="ECO:0007829|PDB:2VBA"
SQ SEQUENCE 406 AA; 42613 MW; 489D8BAD23E78113 CRC64;
MKRAVITGLG IVSSIGNNQQ EVLASLREGR SGITFSQELK DSGMRSHVWG NVKLDTTGLI
DRKVVRFMSD ASIYAFLSME QAIADAGLSP EAYQNNPRVG LIAGSGGGSP RFQVFGADAM
RGPRGLKAVG PYVVTKAMAS GVSACLATPF KIHGVNYSIS SACATSAHCI GNAVEQIQLG
KQDIVFAGGG EELCWEMACE FDAMGALSTK YNDTPEKASR TYDAHRDGFV IAGGGGMVVV
EELEHALARG AHIYAEIVGY GATSDGADMV APSGEGAVRC MKMAMHGVDT PIDYLNSHGT
STPVGDVKEL AAIREVFGDK SPAISATKAM TGHSLGAAGV QEAIYSLLML EHGFIAPSIN
IEELDEQAAG LNIVTETTDR ELTTVMSNSF GFGGTNATLV MRKLKD
