FABH_STRPN
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 03-AUG-2022, entry version 97.
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}.
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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 AlphaFoldDB; P0A3C5; -.
DR SMR; P0A3C5; -.
DR STRING; 170187.SP_0417; -.
DR EnsemblBacteria; AAK74580; AAK74580; SP_0417.
DR GeneID; 60233360; -.
DR GeneID; 66805607; -.
DR KEGG; spn:SP_0417; -.
DR eggNOG; COG0332; Bacteria.
DR OMA; WGSEGDK; -.
DR PhylomeDB; P0A3C5; -.
DR BioCyc; SPNE170187:G1FZB-432-MON; -.
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; -; 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; 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
