ID   FABH_STRR6              Reviewed;         324 AA.
AC   P0A3C6; Q93NA1; Q9FBC7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=spr0377;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10910344; DOI=10.1038/35018162;
RA   Heath R.J., Rock C.O.;
RT   "A triclosan-resistant bacterial enzyme.";
RL   Nature 406:145-146(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC       {ECO:0000305}.
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DR   EMBL; AF197933; AAF98271.1; -; Genomic_DNA.
DR   EMBL; AE007317; AAK99181.1; -; Genomic_DNA.
DR   PIR; A97919; A97919.
DR   RefSeq; NP_357971.1; NC_003098.1.
DR   RefSeq; WP_000852948.1; NC_003098.1.
DR   AlphaFoldDB; P0A3C6; -.
DR   SMR; P0A3C6; -.
DR   STRING; 171101.spr0377; -.
DR   EnsemblBacteria; AAK99181; AAK99181; spr0377.
DR   GeneID; 60233360; -.
DR   GeneID; 66805607; -.
DR   KEGG; spr:spr0377; -.
DR   PATRIC; fig|171101.6.peg.418; -.
DR   eggNOG; COG0332; Bacteria.
DR   HOGENOM; CLU_039592_4_1_9; -.
DR   OMA; WGSEGDK; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000586; 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; -; 1.
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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..324
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT                   /id="PRO_0000110492"
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"
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