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 22-JAN-2014, entry version 86. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 1; DE EC=2.3.1.41; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase I; DE AltName: Full=Beta-ketoacyl-ACP synthase I; DE Short=KAS I; GN Name=fabB; Synonyms=fabC; OrderedLocusNames=b2323, JW2320; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 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; RA Kauppinen S., Siggaard-Andersen M., von Wettstein-Knowles P.; RT "Beta-ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence RT of the fabB gene and identification of the cerulenin binding RT 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., RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., RA Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli- RT K12 genome corresponding to 50.0-68.8 min on the linkage map and RT analysis of 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., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(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 RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP FUNCTION IN UNSATURATED FATTY ACID SYNTHESIS. RX PubMed=3076377; RA Siggaard-Andersen M.; RT "Role of Escherichia coli beta-ketoacyl-ACP synthase I in unsaturated RT fatty acid synthesis."; RL Carlsberg Res. Commun. 53:371-379(1988). RN [7] 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., RA Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=10571059; DOI=10.1016/S0014-5793(99)01303-4; RA Olsen J.G., Kadziola A., von Wettstein-Knowles P., RA Siggaard-Andersen M., 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: Catalyzes the condensation reaction of fatty acid CC synthesis by the addition to an acyl acceptor of two carbons from CC malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 CC and C-18 fatty acids. CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl- CC carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + CC [acyl-carrier-protein]. CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family. 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; YP_490565.1; NC_007779.1. 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; 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 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; 2VB7; -. DR PDBsum; 2VB8; -. DR PDBsum; 2VB9; -. DR PDBsum; 2VBA; -. DR ProteinModelPortal; P0A953; -. DR SMR; P0A953; 1-406. DR DIP; DIP-29379N; -. DR IntAct; P0A953; 9. DR MINT; MINT-1235843; -. DR STRING; 511145.b2323; -. DR BindingDB; P0A953; -. DR ChEMBL; CHEMBL4913; -. DR DrugBank; DB01034; Cerulenin. DR PaxDb; P0A953; -. DR PRIDE; P0A953; -. DR EnsemblBacteria; AAC75383; AAC75383; b2323. DR EnsemblBacteria; BAA16180; BAA16180; BAA16180. DR GeneID; 12931799; -. DR GeneID; 946799; -. DR KEGG; ecj:Y75_p2289; -. DR KEGG; eco:b2323; -. DR PATRIC; 32120019; VBIEscCol129921_2419. DR EchoBASE; EB0270; -. DR EcoGene; EG10274; fabB. DR eggNOG; COG0304; -. DR HOGENOM; HOG000060165; -. DR KO; K00647; -. DR OMA; IGNNTQE; -. DR OrthoDB; EOG6DG2SR; -. DR ProtClustDB; PRK07967; -. DR BioCyc; EcoCyc:FABB-MONOMER; -. DR BioCyc; ECOL316407:JW2320-MONOMER; -. DR BioCyc; MetaCyc:FABB-MONOMER; -. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; P0A953; -. DR PRO; PR:P0A953; -. DR Genevestigator; P0A953; -. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. 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 Gene3D; 3.40.47.10; -; 2. DR InterPro; IPR018201; Ketoacyl_synth_AS. DR InterPro; IPR014031; Ketoacyl_synth_C. DR InterPro; IPR014030; Ketoacyl_synth_N. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR016038; Thiolase-like_subgr. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 1. DR SUPFAM; SSF53901; SSF53901; 2. DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Complete proteome; Cytoplasm; KW Direct protein sequencing; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1 406 3-oxoacyl-[acyl-carrier-protein] synthase FT 1. FT /FTId=PRO_0000180311. FT ACT_SITE 163 163 FT VARIANT 4 4 A -> T (in strain: MA-1 / fabB3). FT VARIANT 140 140 S -> F (in strain: K1060 / fabB5). FT VARIANT 299 299 G -> S (in strain: MA-1 / fabB3). FT VARIANT 329 329 A -> V (in strain: M5 / fabB15). FT STRAND 4 13 FT STRAND 16 18 FT HELIX 19 28 FT STRAND 33 35 FT HELIX 37 41 FT STRAND 48 50 FT TURN 57 59 FT HELIX 62 65 FT HELIX 70 86 FT HELIX 90 93 FT STRAND 99 104 FT STRAND 106 108 FT HELIX 110 120 FT TURN 123 125 FT HELIX 126 129 FT HELIX 133 137 FT HELIX 141 147 FT TURN 148 151 FT STRAND 156 160 FT HELIX 162 164 FT HELIX 165 178 FT STRAND 183 191 FT HELIX 195 203 FT TURN 210 213 FT HELIX 215 217 FT STRAND 234 242 FT HELIX 243 248 FT STRAND 255 264 FT STRAND 269 271 FT HELIX 275 285 FT STRAND 294 296 FT HELIX 303 317 FT HELIX 318 320 FT STRAND 323 325 FT HELIX 328 331 FT HELIX 335 337 FT HELIX 338 352 FT STRAND 362 364 FT HELIX 366 368 FT STRAND 371 373 FT STRAND 384 391 FT TURN 392 394 FT STRAND 395 402 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 //