FABF_ECOLI
ID FABF_ECOLI Reviewed; 413 AA.
AC P0AAI5; P39435;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2 {ECO:0000305};
DE EC=2.3.1.179 {ECO:0000269|PubMed:9013860, ECO:0000305|PubMed:6988423};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase II {ECO:0000305};
DE AltName: Full=Beta-ketoacyl-ACP synthase II {ECO:0000303|PubMed:6988423};
DE Short=KAS II {ECO:0000303|PubMed:7768872};
GN Name=fabF {ECO:0000303|PubMed:6988423};
GN Synonyms=fabJ {ECO:0000303|PubMed:7972002};
GN OrderedLocusNames=b1095, JW1081;
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 2-32.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7972002; DOI=10.1073/pnas.91.23.11027;
RA Siggaard-Andersen M., Wissenbach M., Chuck J.-A., Svendsen I., Olsen J.G.,
RA von Wettstein-Knowles P.V.;
RT "The fabJ-encoded beta-ketoacyl-[acyl carrier protein] synthase IV from
RT Escherichia coli is sensitive to cerulenin and specific for short-chain
RT substrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11027-11031(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTITY OF FABF AND FABJ.
RC STRAIN=K12 / UB1005;
RX PubMed=7768872; DOI=10.1128/jb.177.12.3593-3595.1995;
RA Magnuson K., Carey M.R., Cronan J.E. Jr.;
RT "The putative fabJ gene of Escherichia coli fatty acid synthesis is the
RT fabF gene.";
RL J. Bacteriol. 177:3593-3595(1995).
RN [3]
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 [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 IDENTIFICATION OF FABF AS KASII.
RX PubMed=3549687; DOI=10.1128/jb.169.4.1469-1473.1987;
RA Jackowski S., Rock C.O.;
RT "Altered molecular form of acyl carrier protein associated with beta-
RT ketoacyl-acyl carrier protein synthase II (fabF) mutants.";
RL J. Bacteriol. 169:1469-1473(1987).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=6988423; DOI=10.1016/s0021-9258(19)85692-2;
RA Garwin J.L., Klages A.L., Cronan J.E. Jr.;
RT "Beta-ketoacyl-acyl carrier protein synthase II of Escherichia coli.
RT Evidence for function in the thermal regulation of fatty acid synthesis.";
RL J. Biol. Chem. 255:3263-3265(1980).
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ARG-207.
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 [10] {ECO:0007744|PDB:1KAS}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-413, SUBUNIT, AND ACTIVE SITE.
RX PubMed=9482715; DOI=10.1093/emboj/17.5.1183;
RA Huang W., Jia J., Edwards P., Dehesh K., Schneider G., Lindqvist Y.;
RT "Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from
RT E.coli reveals the molecular architecture of condensing enzymes.";
RL EMBO J. 17:1183-1191(1998).
RN [11] {ECO:0007744|PDB:1B3N}
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 2-413 IN COMPLEX WITH CERULENIN,
RP AND ACTIVE SITE.
RX PubMed=10037680; DOI=10.1074/jbc.274.10.6031;
RA Moche M., Schneider G., Edwards P., Dehesh K., Lindqvist Y.;
RT "Structure of the complex between the antibiotic cerulenin and its target,
RT beta-ketoacyl-acyl carrier protein synthase.";
RL J. Biol. Chem. 274:6031-6034(1999).
RN [12] {ECO:0007744|PDB:2GFV, ECO:0007744|PDB:2GFW, ECO:0007744|PDB:2GFX, ECO:0007744|PDB:2GFY}
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 2-413 OF WILD-TYPE AND MUTANTS IN
RP COMPLEXES WITH DODECANOIC ACID AND PLATENSIMYCIN, AND MUTAGENESIS OF
RP CYS-164.
RX PubMed=16710421; DOI=10.1038/nature04784;
RA Wang J., Soisson S.M., Young K., Shoop W., Kodali S., Galgoci A.,
RA Painter R., Parthasarathy G., Tang Y.S., Cummings R., Ha S., Dorso K.,
RA Motyl M., Jayasuriya H., Ondeyka J., Herath K., Zhang C., Hernandez L.,
RA Allocco J., Basilio A., Tormo J.R., Genilloud O., Vicente F., Pelaez F.,
RA Colwell L., Lee S.H., Michael B., Felcetto T., Gill C., Silver L.L.,
RA Hermes J.D., Bartizal K., Barrett J., Schmatz D., Becker J.W., Cully D.,
RA Singh S.B.;
RT "Platensimycin is a selective FabF inhibitor with potent antibiotic
RT properties.";
RL Nature 441:358-361(2006).
RN [13] {ECO:0007744|PDB:3G0Y, ECO:0007744|PDB:3G11}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-413 IN COMPLEXES WITH
RP DIHYDROPLATENSIMYCIN AND DIHYDROPHENYL PLATENSIMYCIN.
RX PubMed=19233644; DOI=10.1016/j.bmcl.2009.02.006;
RA Shen H.C., Ding F.X., Singh S.B., Parthasarathy G., Soisson S.M., Ha S.N.,
RA Chen X., Kodali S., Wang J., Dorso K., Tata J.R., Hammond M.L., Maccoss M.,
RA Colletti S.L.;
RT "Synthesis and biological evaluation of platensimycin analogs.";
RL Bioorg. Med. Chem. Lett. 19:1623-1627(2009).
RN [14] {ECO:0007744|PDB:3HNZ, ECO:0007744|PDB:3HO2, ECO:0007744|PDB:3HO9, ECO:0007744|PDB:3I8P}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-413 OF MUTANT ALA-164 IN
RP COMPLEXES WITH PLATENSIMYCIN AND PLATENCIN.
RX PubMed=19581087; DOI=10.1016/j.bmcl.2009.06.061;
RA Singh S.B., Ondeyka J.G., Herath K.B., Zhang C., Jayasuriya H., Zink D.L.,
RA Parthasarathy G., Becker J.W., Wang J., Soisson S.M.;
RT "Isolation, enzyme-bound structure and antibacterial activity of platencin
RT A1 from Streptomyces platensis.";
RL Bioorg. Med. Chem. Lett. 19:4756-4759(2009).
CC -!- FUNCTION: Involved in the type II fatty acid elongation cycle
CC (PubMed:9013860, PubMed:6988423). Catalyzes the elongation of a wide
CC range of acyl-ACP by the addition of two carbons from malonyl-ACP to an
CC acyl acceptor (PubMed:9013860, PubMed:22017312). Can efficiently
CC catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP)
CC to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in
CC the thermal regulation of fatty acid composition (PubMed:9013860,
CC PubMed:6988423). Can use acyl chains from C-6 to C-16 (PubMed:9013860,
CC PubMed:22017312). Is able to catalyze the condensation reaction when
CC CoA is the carrier for both substrates (PubMed:22017312).
CC {ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:6988423,
CC 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 Evidence={ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:9013860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC Evidence={ECO:0000269|PubMed:22017312, ECO:0000269|PubMed:9013860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(11Z)-
CC octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:55040,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:10800,
CC Rhea:RHEA-COMP:14074, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:83989,
CC ChEBI:CHEBI:138538; EC=2.3.1.179;
CC Evidence={ECO:0000269|PubMed:9013860, ECO:0000305|PubMed:6988423};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55041;
CC Evidence={ECO:0000269|PubMed:9013860, ECO:0000305|PubMed:6988423};
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:9013860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901;
CC Evidence={ECO:0000269|PubMed:9013860};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.2 uM for malonyl-[ACP] (in the presence of dodecanoyl-[ACP])
CC {ECO:0000269|PubMed:22017312};
CC KM=510 uM for malonyl-CoA (in the presence of dodecanoyl-CoA)
CC {ECO:0000269|PubMed:22017312};
CC KM=53.7 uM for dodecanoyl-CoA (in the presence of malonyl-CoA)
CC {ECO:0000269|PubMed:22017312};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:6988423}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9013860,
CC ECO:0000269|PubMed:9482715}.
CC -!- INTERACTION:
CC P0AAI5; P0A6Y8: dnaK; NbExp=3; IntAct=EBI-542783, EBI-542092;
CC -!- MISCELLANEOUS: Identified as a drug target (PubMed:10037680,
CC PubMed:16710421, PubMed:19233644, PubMed:19581087). Inhibited by
CC platensimycin and platencin, which are antibiotic produced by various
CC strains of Streptomyces platensis, and by several
CC platensimycin/platencin analogs (PubMed:16710421, PubMed:19233644,
CC PubMed:19581087). Also inhibited by the fungal mycotoxin cerulenin that
CC binds in a hydrophobic pocket formed at the dimer interface
CC (PubMed:10037680). {ECO:0000269|PubMed:10037680,
CC ECO:0000269|PubMed:16710421, ECO:0000269|PubMed:19233644,
CC ECO:0000269|PubMed:19581087}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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DR EMBL; Z34979; CAA84431.1; -; Genomic_DNA.
DR EMBL; U20767; AAA83255.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74179.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35903.1; -; Genomic_DNA.
DR PIR; I41060; I41060.
DR RefSeq; NP_415613.1; NC_000913.3.
DR RefSeq; WP_000044679.1; NZ_STEB01000016.1.
DR PDB; 1B3N; X-ray; 2.65 A; A=2-413.
DR PDB; 1KAS; X-ray; 2.40 A; A=2-413.
DR PDB; 2GFV; X-ray; 2.29 A; A=2-413.
DR PDB; 2GFW; X-ray; 2.40 A; A=2-413.
DR PDB; 2GFX; X-ray; 2.59 A; A=2-413.
DR PDB; 2GFY; X-ray; 2.85 A; A=2-413.
DR PDB; 3G0Y; X-ray; 2.60 A; A=2-413.
DR PDB; 3G11; X-ray; 2.00 A; A=2-413.
DR PDB; 3HNZ; X-ray; 2.75 A; A=2-413.
DR PDB; 3HO2; X-ray; 2.00 A; A=2-413.
DR PDB; 3HO9; X-ray; 1.90 A; A=2-413.
DR PDB; 3I8P; X-ray; 1.90 A; A=2-413.
DR PDB; 6OKG; X-ray; 2.30 A; A=1-413.
DR PDB; 6OLT; X-ray; 2.35 A; A=1-413.
DR PDB; 7L4E; X-ray; 2.00 A; A=1-413.
DR PDB; 7L4L; X-ray; 2.65 A; A/B=1-413.
DR PDBsum; 1B3N; -.
DR PDBsum; 1KAS; -.
DR PDBsum; 2GFV; -.
DR PDBsum; 2GFW; -.
DR PDBsum; 2GFX; -.
DR PDBsum; 2GFY; -.
DR PDBsum; 3G0Y; -.
DR PDBsum; 3G11; -.
DR PDBsum; 3HNZ; -.
DR PDBsum; 3HO2; -.
DR PDBsum; 3HO9; -.
DR PDBsum; 3I8P; -.
DR PDBsum; 6OKG; -.
DR PDBsum; 6OLT; -.
DR PDBsum; 7L4E; -.
DR PDBsum; 7L4L; -.
DR AlphaFoldDB; P0AAI5; -.
DR SMR; P0AAI5; -.
DR BioGRID; 4260072; 208.
DR DIP; DIP-29377N; -.
DR IntAct; P0AAI5; 6.
DR STRING; 511145.b1095; -.
DR DrugBank; DB08366; 3-({3-[(1S,4aS,6S,7S,9S,9aR)-1,6-dimethyl-2-oxodecahydro-6,9-epoxy-4a,7-methanobenzo[7]annulen-1-yl]propanoyl}amino)-2,4-dihydroxybenzoic acid.
DR DrugBank; DB01034; Cerulenin.
DR DrugBank; DB03017; Lauric acid.
DR DrugBank; DB08407; Platensimycin.
DR SwissLipids; SLP:000001811; -.
DR jPOST; P0AAI5; -.
DR PaxDb; P0AAI5; -.
DR PRIDE; P0AAI5; -.
DR EnsemblBacteria; AAC74179; AAC74179; b1095.
DR EnsemblBacteria; BAA35903; BAA35903; BAA35903.
DR GeneID; 67414288; -.
DR GeneID; 946665; -.
DR KEGG; ecj:JW1081; -.
DR KEGG; eco:b1095; -.
DR PATRIC; fig|1411691.4.peg.1173; -.
DR EchoBASE; EB2490; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_6; -.
DR InParanoid; P0AAI5; -.
DR OMA; QIGHCLG; -.
DR PhylomeDB; P0AAI5; -.
DR BioCyc; EcoCyc:3-OXOACYL-ACP-SYNTHII-MON; -.
DR BioCyc; MetaCyc:3-OXOACYL-ACP-SYNTHII-MON; -.
DR BRENDA; 2.3.1.179; 2026.
DR SABIO-RK; P0AAI5; -.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; P0AAI5; -.
DR PRO; PR:P0AAI5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IDA:EcoCyc.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IDA:EcoCyc.
DR GO; GO:1903966; P:monounsaturated fatty acid biosynthetic process; IMP:EcoCyc.
DR GO; GO:0009409; P:response to cold; IMP:EcoCyc.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-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 PIRSF; PIRSF000447; KAS_II; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR03150; fabF; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7972002"
FT CHAIN 2..413
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT /id="PRO_0000180314"
FT ACT_SITE 164
FT /evidence="ECO:0000269|PubMed:10037680,
FT ECO:0000305|PubMed:9482715"
FT BINDING 271
FT /ligand="platencin"
FT /ligand_id="ChEBI:CHEBI:178056"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:19581087,
FT ECO:0007744|PDB:3HO2, ECO:0007744|PDB:3HO9"
FT BINDING 271
FT /ligand="platensimycin"
FT /ligand_id="ChEBI:CHEBI:178082"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:16710421,
FT ECO:0000269|PubMed:19233644, ECO:0000269|PubMed:19581087,
FT ECO:0007744|PDB:2GFX, ECO:0007744|PDB:3G0Y,
FT ECO:0007744|PDB:3G11, ECO:0007744|PDB:3HNZ,
FT ECO:0007744|PDB:3I8P"
FT BINDING 304
FT /ligand="platensimycin"
FT /ligand_id="ChEBI:CHEBI:178082"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:16710421,
FT ECO:0000269|PubMed:19233644, ECO:0007744|PDB:2GFX,
FT ECO:0007744|PDB:3G0Y, ECO:0007744|PDB:3G11"
FT BINDING 308..310
FT /ligand="platencin"
FT /ligand_id="ChEBI:CHEBI:178056"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:19581087,
FT ECO:0007744|PDB:3HO2, ECO:0007744|PDB:3HO9"
FT BINDING 308..310
FT /ligand="platensimycin"
FT /ligand_id="ChEBI:CHEBI:178082"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:16710421,
FT ECO:0000269|PubMed:19233644, ECO:0000269|PubMed:19581087,
FT ECO:0007744|PDB:2GFX, ECO:0007744|PDB:3G0Y,
FT ECO:0007744|PDB:3G11, ECO:0007744|PDB:3HNZ,
FT ECO:0007744|PDB:3I8P"
FT BINDING 341
FT /ligand="platencin"
FT /ligand_id="ChEBI:CHEBI:178056"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:19581087,
FT ECO:0007744|PDB:3HO2, ECO:0007744|PDB:3HO9"
FT BINDING 341
FT /ligand="platensimycin"
FT /ligand_id="ChEBI:CHEBI:178082"
FT /ligand_note="inhibitor"
FT /evidence="ECO:0000269|PubMed:16710421,
FT ECO:0000269|PubMed:19233644, ECO:0007744|PDB:2GFX,
FT ECO:0007744|PDB:3G0Y, ECO:0007744|PDB:3G11"
FT MUTAGEN 164
FT /note="C->Q: 50-fold increase in apparent binding of
FT platensimycin."
FT /evidence="ECO:0000269|PubMed:16710421"
FT MUTAGEN 207
FT /note="R->G: Impairs the binding of CoA. 10-fold increase
FT in catalytic efficiency with dodecanoyl-CoA and malonyl-
FT CoA."
FT /evidence="ECO:0000269|PubMed:22017312"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3HO9"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:3HO9"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2GFV"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 309..323
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 324..328
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:3HO9"
FT HELIX 346..360
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 393..400
FT /evidence="ECO:0007829|PDB:3HO9"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:3HO9"
FT STRAND 404..411
FT /evidence="ECO:0007829|PDB:3HO9"
SQ SEQUENCE 413 AA; 43046 MW; 5F60DB1F986B2EE5 CRC64;
MSKRRVVVTG LGMLSPVGNT VESTWKALLA GQSGISLIDH FDTSAYATKF AGLVKDFNCE
DIISRKEQRK MDAFIQYGIV AGVQAMQDSG LEITEENATR IGAAIGSGIG GLGLIEENHT
SLMNGGPRKI SPFFVPSTIV NMVAGHLTIM YGLRGPSISI ATACTSGVHN IGHAARIIAY
GDADVMVAGG AEKASTPLGV GGFGAARALS TRNDNPQAAS RPWDKERDGF VLGDGAGMLV
LEEYEHAKKR GAKIYAELVG FGMSSDAYHM TSPPENGAGA ALAMANALRD AGIEASQIGY
VNAHGTSTPA GDKAEAQAVK TIFGEAASRV LVSSTKSMTG HLLGAAGAVE SIYSILALRD
QAVPPTINLD NPDEGCDLDF VPHEARQVSG MEYTLCNSFG FGGTNGSLIF KKI
