ID   FABHL_CAMJE             Reviewed;         353 AA.
AC   Q9PMZ6; Q0P8V4;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Putative 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;
GN   OrderedLocusNames=Cj1303;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- FUNCTION: May catalyze the condensation reaction of fatty acid
CC       synthesis by the addition to an acyl acceptor of two carbons from
CC       malonyl-ACP. {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:0000305}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Lacks the Asn-Xaa-Arg residues, which are typical of the ACP-
CC       binding site and are essential for the association between AcpP and
CC       FabH. {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; AL111168; CAL35417.1; -; Genomic_DNA.
DR   PIR; D81273; D81273.
DR   RefSeq; WP_002789842.1; NC_002163.1.
DR   RefSeq; YP_002344693.1; NC_002163.1.
DR   AlphaFoldDB; Q9PMZ6; -.
DR   SMR; Q9PMZ6; -.
DR   IntAct; Q9PMZ6; 39.
DR   STRING; 192222.Cj1303; -.
DR   PaxDb; Q9PMZ6; -.
DR   PRIDE; Q9PMZ6; -.
DR   EnsemblBacteria; CAL35417; CAL35417; Cj1303.
DR   GeneID; 905595; -.
DR   KEGG; cje:Cj1303; -.
DR   PATRIC; fig|192222.6.peg.1285; -.
DR   eggNOG; COG0332; Bacteria.
DR   HOGENOM; CLU_039592_1_0_7; -.
DR   OMA; SCVLQHR; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000799; 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-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR013751; ACP_syn_III.
DR   InterPro; IPR013747; ACP_syn_III_C.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF08545; ACP_syn_III; 1.
DR   Pfam; PF08541; ACP_syn_III_C; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
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..353
FT                   /note="Putative 3-oxoacyl-[acyl-carrier-protein] synthase
FT                   3"
FT                   /id="PRO_0000110520"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   353 AA;  39480 MW;  B865A6A8637A8E37 CRC64;
     MKTRFDKAKI SGICVSVPEH KICIDDELES VFSNDIKTLK RMKKVIGLNT RYICDENTCV
     SDLGKHAANT LLQGLNIDKN SLDALIVVTQ SPDFFMPSTA CYLHQLLNLS SKTVAFDLGQ
     ACAGYLYGLF VAHSLIQSGL GKILLICGDT LSKFIHPKNM NLAPIFGDGV SATLIEKTDF
     NEAFFELGSD GKYFDKLIIP KGAMRIPKAD IFNDDSLMQT EEFRQLENLY MDGANIFNMA
     LECEPKSFKE ILEFSKVDEK DIAFHLFHQS NAYLVDCIKE ELKLNDDKVP NFIMEKYANL
     SACSLPTLLC ELDTPKEFKA SLSAFGAGLS WGSAVLNFKD LYTKNILIYT KEK