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 26-FEB-2020, entry version 89. 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 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., Brandt M., RA Daines R.A., Lonsdale J.T.; RT "Identification, substrate specificity, and inhibition of the Streptococcus RT pneumoniae beta-ketoacyl-acyl carrier protein synthase 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 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., Hickey E.K., RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., RA 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 synthesis CC by the addition to an acyl acceptor of two carbons from malonyl-ACP. CC Catalyzes the first condensation reaction which initiates fatty acid CC synthesis and may therefore play a role in governing the total rate of CC fatty acid production. Possesses both acetoacetyl-ACP synthase and CC acetyl transacylase activities. Has some substrate preference for CC acetyl-CoA. Its substrate specificity determines the biosynthesis of CC straight-chain of fatty acids. {ECO:0000269|PubMed:11375394}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 CC + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA- CC COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; CC EC=2.3.1.180; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DOMAIN: The last Arg residue of the ACP-binding site is essential for CC the weak association between ACP/AcpP and FabH. {ECO:0000250}. CC -!- MISCELLANEOUS: Inhibited by the SB418011 antibiotic. Not inhibited by CC cerulenin, and weakly inhibited by thiolactomycin. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family. CC {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; AF384041; AAK91994.1; -; Genomic_DNA. DR EMBL; AE005672; AAK74580.1; -; Genomic_DNA. DR PIR; C95048; C95048. DR RefSeq; WP_000852948.1; NZ_AKVY01000001.1. DR SMR; P0A3C5; -. DR STRING; 170187.SP_0417; -. DR EnsemblBacteria; AAK74580; AAK74580; SP_0417. DR KEGG; spn:SP_0417; -. DR eggNOG; ENOG4105CCZ; Bacteria. DR eggNOG; COG0332; LUCA. DR KO; K00648; -. DR OMA; RTTCIIF; -. DR BioCyc; SPNE170187:G1FZB-432-MONOMER; -. DR BRENDA; 2.3.1.180; 1960. DR BRENDA; 2.3.1.41; 1960. DR UniPathway; UPA00094; -. DR Proteomes; UP000000585; Chromosome. 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:UniProtKB-UniRule. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.47.10; -; 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 Pfam; PF08545; ACP_syn_III; 1. DR Pfam; PF08541; ACP_syn_III_C; 1. DR SUPFAM; SSF53901; SSF53901; 1. DR TIGRFAMs; TIGR00747; fabH; 1. PE 3: Inferred from homology; KW Acyltransferase; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; Multifunctional enzyme; Transferase. FT CHAIN 1..324 FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3" FT /id="PRO_0000110491" FT REGION 250..254 FT /note="ACP-binding" FT /evidence="ECO:0000250" FT ACT_SITE 112 FT /evidence="ECO:0000250" FT ACT_SITE 249 FT /evidence="ECO:0000250" FT ACT_SITE 279 FT /evidence="ECO:0000250" FT CONFLICT 71 FT /note="E -> K (in Ref. 1; AAK91994)" FT /evidence="ECO:0000305" 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 //