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 02-SEP-2026, entry version 156. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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:6988423, PubMed:9013860). 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:22017312, PubMed:9013860). 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:6988423, CC PubMed:9013860). Can use acyl chains from C-6 to C-16 (PubMed:22017312, CC PubMed:9013860). Is able to catalyze the condensation reaction when CoA CC 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] + malonyl-[ACP] + H(+) = a 3-oxoacyl-[ACP] CC + holo-[ACP] + CO2; 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] + malonyl-[ACP] + H(+) = 3-oxo-(11Z)- CC octadecenoyl-[ACP] + holo-[ACP] + CO2; 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=hexanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxooctanoyl-[ACP] + CC holo-[ACP] + CO2; 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=octanoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxodecanoyl-[ACP] + CC holo-[ACP] + CO2; 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] + malonyl-[ACP] + H(+) = 3-oxododecanoyl-[ACP] CC + holo-[ACP] + CO2; 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] + malonyl-[ACP] + H(+) = 3-oxotetradecanoyl- CC [ACP] + holo-[ACP] + CO2; 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=tetradecanoyl-[ACP] + malonyl-[ACP] + H(+) = 3- CC oxohexadecanoyl-[ACP] + holo-[ACP] + CO2; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_CP009789.1. 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 PDB; 9LPL; X-ray; 2.70 A; A/B=2-413. DR AlphaFoldDB; P0AAI5; -. DR MDposit; P0AAI5; -. DR MDRepo; P0AAI5; -. DR SMR; P0AAI5; -. DR BioGRID; 4260072; 212. DR DIP; DIP-29377N; -. DR FunCoup; P0AAI5; 848. 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; 511145-b1095; -. DR EnsemblBacteria; AAC74179; AAC74179; b1095. DR GeneID; 86945966; -. DR GeneID; 946665; -. DR KEGG; ecj:JW1081; -. DR KEGG; eco:b1095; -. DR KEGG; ecoc:C3026_06620; -. 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 OrthoDB; 9808669at2; -. DR PhylomeDB; P0AAI5; -. DR BioCyc; EcoCyc:3-OXOACYL-ACP-SYNTHII-MONOMER; -. DR BioCyc; MetaCyc:3-OXOACYL-ACP-SYNTHII-MONOMER; -. DR BRENDA; 2.3.1.179; 2026. DR SABIO-RK; P0AAI5; -. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; P0AAI5; -. DR PRO; PR:P0AAI5; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P0AAI5; -. 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:0042803; F:protein homodimerization activity; IDA:EcoCyc. 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 FunFam; 3.40.47.10:FF:000009; 3-oxoacyl-[acyl-carrier-protein] synthase 2; 1. DR Gene3D; 3.40.47.10; -; 1. DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-2. DR InterPro; IPR000794; Beta-ketoacyl_synthase. DR InterPro; IPR014031; KAS_C. DR InterPro; IPR014030; KAS_N. DR InterPro; IPR018201; Ketoacyl_synth_AS. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR016039; Thiolase-like. DR NCBIfam; TIGR03150; fabF; 1. DR NCBIfam; NF004970; PRK06333.1; 1. DR NCBIfam; NF005589; PRK07314.1; 1. DR NCBIfam; NF006434; PRK08722.1; 1. DR PANTHER; PTHR11712:SF336; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 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; Thiolase-like; 2. DR PROSITE; PS00606; KS3_1; 1. DR PROSITE; PS52004; KS3_2; 1. 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 PDBsum; 9LPL; -. 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 DOMAIN 3..412 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 164 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348, FT ECO:0000269|PubMed:10037680, ECO:0000305|PubMed:9482715" FT ACT_SITE 304 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 341 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" 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 FT malonyl-CoA." FT /evidence="ECO:0000269|PubMed:22017312" FT HELIX 3..5 FT /evidence="ECO:0007829|PDB:6OLT" 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 HELIX 53..55 FT /evidence="ECO:0007829|PDB:3HO2" 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:3G11" 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 //