ID   FABH_ECO24              Reviewed;         317 AA.
AC   A7ZKJ4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000255|HAMAP-Rule:MF_01815};
DE            EC=2.3.1.180 {ECO:0000255|HAMAP-Rule:MF_01815};
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE   AltName: Full=Beta-ketoacyl-ACP synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE            Short=KAS III {ECO:0000255|HAMAP-Rule:MF_01815};
GN   Name=fabH {ECO:0000255|HAMAP-Rule:MF_01815};
GN   OrderedLocusNames=EcE24377A_1212;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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. Its substrate specificity determines
CC       the biosynthesis of branched-chain and/or straight-chain of fatty
CC       acids. {ECO:0000255|HAMAP-Rule:MF_01815}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01815};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_01815}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01815}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815}.
CC   -!- DOMAIN: The last Arg residue of the ACP-binding site is essential for
CC       the weak association between ACP/AcpP and FabH. {ECO:0000255|HAMAP-
CC       Rule:MF_01815}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC       {ECO:0000255|HAMAP-Rule:MF_01815}.
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DR   EMBL; CP000800; ABV19409.1; -; Genomic_DNA.
DR   RefSeq; WP_000288132.1; NC_009801.1.
DR   AlphaFoldDB; A7ZKJ4; -.
DR   SMR; A7ZKJ4; -.
DR   EnsemblBacteria; ABV19409; ABV19409; EcE24377A_1212.
DR   GeneID; 66670643; -.
DR   KEGG; ecw:EcE24377A_1212; -.
DR   HOGENOM; CLU_039592_4_1_6; -.
DR   OMA; WGSEGDK; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001122; 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..317
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT                   /id="PRO_1000070228"
FT   REGION          245..249
FT                   /note="ACP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ   SEQUENCE   317 AA;  33515 MW;  BF3192CFF36023D3 CRC64;
     MYTKIIGTGS YLPEQVRTNA DLEKMVDTSD EWIVTRTGIR ERHIAAPNET VSTMGFEAAT
     RAIEMAGIEK DQIGLIVVAT TSATHAFPSA ACQIQSMLGI KGCPAFDVAA ACAGFTYALS
     VADQYVKSGA VKYALVVGSD VLARTCDPTD RGTIIIFGDG AGAAVLAASE EPGIISTHLH
     ADGSYGELLT LPNADRVNPE NSIHLTMAGN EVFKVAVTEL AHIVDETLAA NNLDRSQLDW
     LVPHQANLRI ISATAKKLGM SMDNVVVTLD RHGNTSAASV PCALDEAVRD GRIKPGQLVL
     LEAFGGGFTW GSALVRF