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 02-SEP-2026, entry version 155. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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:19679654, CC PubMed:22017312, PubMed:8910376, PubMed:9013860). Can also use CC unsaturated fatty acids (PubMed:19679654, PubMed:3076377, CC PubMed:8910376). 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:19679654, PubMed:22017312, PubMed:8910376, PubMed:9013860). 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] + 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 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] + malonyl-[ACP] + H(+) = 3-oxo-(5Z)- CC dodecenoyl-[ACP] + holo-[ACP] + CO2; 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=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:8910376}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901; CC Evidence={ECO:0000269|PubMed:8910376}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(7Z)-tetradecenoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxo-(9Z)- CC hexadecenoyl-[ACP] + holo-[ACP] + CO2; 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 CC dodecanoyl-[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}. 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; 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_CP009789.1. 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 PDB; 7SQI; X-ray; 1.70 A; A/B=1-405. DR PDB; 7SZ9; X-ray; 2.20 A; A/B=2-405. DR PDB; 8SMS; X-ray; 1.93 A; A/B=2-405. DR PDB; 9MLW; X-ray; 2.21 A; A/B=2-406. DR AlphaFoldDB; P0A953; -. DR MDposit; P0A953; -. DR MDRepo; P0A953; -. DR SMR; P0A953; -. DR BioGRID; 4260793; 232. DR DIP; DIP-29379N; -. DR FunCoup; P0A953; 257. 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; 511145-b2323; -. DR EnsemblBacteria; AAC75383; AAC75383; b2323. DR GeneID; 67176107; -. DR GeneID; 75202594; -. DR GeneID; 946799; -. DR KEGG; ecj:JW2320; -. DR KEGG; eco:b2323; -. DR KEGG; ecoc:C3026_12945; -. 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; WMAGASE; -. DR OrthoDB; 9808669at2; -. DR PhylomeDB; P0A953; -. DR BioCyc; EcoCyc:FABB-MONOMER; -. DR BioCyc; MetaCyc:FABB-MONOMER; -. DR BRENDA; 2.3.1.41; 2026. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; P0A953; -. DR PRO; PR:P0A953; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P0A953; -. 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 FunFam; 3.40.47.10:FF:000005; 3-oxoacyl-[acyl-carrier-protein] synthase I; 1. DR FunFam; 3.40.47.10:FF:000006; 3-oxoacyl-[acyl-carrier-protein] synthase I; 1. DR Gene3D; 3.40.47.10; -; 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; NF005935; PRK07967.1; 1. DR PANTHER; PTHR11712:SF306; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 1; 1. DR PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 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; 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 PDBsum; 7SQI; -. DR PDBsum; 7SZ9; -. DR PDBsum; 8SMS; -. DR PDBsum; 9MLW; -. 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 DOMAIN 1..403 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 163 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348, FT ECO:0000305|PubMed:10571059" FT ACT_SITE 298 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 333 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" 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:1EK4" 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 HELIX 251..253 FT /evidence="ECO:0007829|PDB:2BUH" 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" FT HELIX 403..405 FT /evidence="ECO:0007829|PDB:2VB7" 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 //