ID FABH_STRPN Reviewed; 324 AA. AC P0A3C5; Q93NA1; Q9FBC7; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 09-JAN-2013, entry version 59. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3; DE EC=2.3.1.180; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III; DE AltName: Full=Beta-ketoacyl-ACP synthase III; DE Short=KAS III; DE AltName: Full=SpFabH; GN Name=fabH; OrderedLocusNames=SP_0417; OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=170187; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, HOMODIMERIZATION, AND RP SUBSTRATE SPECIFICITY. RC STRAIN=ATCC BAA-334 / TIGR4; RX MEDLINE=21380102; PubMed=11375394; DOI=10.1074/jbc.M101769200; RA Khandekar S.S., Gentry D.R., Van Aller G.S., Warren P., Xiang H., RA Silverman C., Doyle M.L., Chambers P.A., Konstantinidis A.K., RA Brandt M., Daines R.A., Lonsdale J.T.; RT "Identification, substrate specificity, and inhibition of the RT Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase RT III (FabH)."; RL J. Biol. Chem. 276:30024-30030(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-334 / TIGR4; RX MEDLINE=21357209; PubMed=11463916; DOI=10.1126/science.1061217; RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D., RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., RA Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., RA Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.; RT "Complete genome sequence of a virulent isolate of Streptococcus RT pneumoniae."; RL Science 293:498-506(2001). 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. Catalyzes the first condensation reaction which CC initiates fatty acid synthesis and may therefore play a role in CC governing the total rate of fatty acid production. Possesses both CC acetoacetyl-ACP synthase and acetyl transacylase activities. Has CC some substrate preference for acetyl-CoA. Its substrate CC specificity determines the biosynthesis of straight-chain of fatty CC acids. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + malonyl-[acyl-carrier-protein] = CC acetoacetyl-[acyl-carrier-protein] + CoA + CO(2). CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). CC -!- DOMAIN: The last Arg residue of the ACP-binding site is essential CC for the weak association between ACP/AcpP and FabH (By CC similarity). CC -!- MISCELLANEOUS: Inhibited by the SB418011 antibiotic. Not inhibited CC by cerulenin, and weakly inhibited by thiolactomycin. CC -!- SIMILARITY: Belongs to the FabH 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; AF384041; AAK91994.1; -; Genomic_DNA. DR EMBL; AE005672; AAK74580.1; -; Genomic_DNA. DR PIR; C95048; C95048. DR RefSeq; NP_344940.1; NC_003028.3. DR ProteinModelPortal; P0A3C5; -. DR EnsemblBacteria; EBSTRT00000027127; EBSTRP00000026219; EBSTRG00000027127. DR GeneID; 930353; -. DR GenomeReviews; AE005672_GR; SP_0417. DR KEGG; spn:SP_0417; -. DR PATRIC; 19705179; VBIStrPne105772_0435. DR eggNOG; COG0332; -. DR HOGENOM; HOG000246674; -. DR KO; K00648; -. DR OMA; IFKRAIA; -. DR ProtClustDB; PRK09352; -. DR BioCyc; SPNE170187:GHGN-476-MONOMER; -. DR BRENDA; 2.3.1.41; 5946. DR UniPathway; UPA00094; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro. DR GO; GO:0033818; F:beta-ketoacyl-acyl-carrier-protein synthase III activity; IEA:EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.47.10; Thiolase-like_subgr; 2. DR HAMAP; MF_01815; FabH; 1; -. DR InterPro; IPR013751; ACP_syn_III. DR InterPro; IPR013747; ACP_syn_III_C. DR InterPro; IPR004655; FabH_synth. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR016038; Thiolase-like_subgr. DR Pfam; PF08545; ACP_syn_III; 1. DR Pfam; PF08541; ACP_syn_III_C; 1. DR SUPFAM; SSF53901; Thiolase-like; 1. DR TIGRFAMs; TIGR00747; fabH; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; KW Lipid metabolism; Multifunctional enzyme; Transferase. FT CHAIN 1 324 3-oxoacyl-[acyl-carrier-protein] synthase FT 3. FT /FTId=PRO_0000110491. FT REGION 250 254 ACP-binding (By similarity). FT ACT_SITE 112 112 By similarity. FT ACT_SITE 249 249 By similarity. FT ACT_SITE 279 279 By similarity. FT CONFLICT 71 71 E -> K (in Ref. 1; AAK91994). SQ SEQUENCE 324 AA; 34904 MW; 53E529125B392C70 CRC64; MAFAKISQVA HYVPEQVVTN HDLAQIMDTN DEWISSRTGI RQRHISRTES TSDLATEVAK KLMAKAGITG EELDFIILAT ITPDSMMPST AARVQANIGA NKAFAFDLTA ACSGFVFALS TAEKFIASGR FQKGLVIGSE TLSKAVDWSD RSTAVLFGDG AGGVLLEASE QEHFLAESLN SDGSRSECLT YGHSGLHSPF SDQESADSFL KMDGRTVFDF AIRDVAKSIK QTIDESPIEV TDLDYLLLHQ ANDRILDKMA RKIGVDRAKL PANMMEYGNT SAASIPILLS ECVEQGLIPL DGSQTVLLSG FGGGLTWGTL ILTI //