ID   FABH_STAAM              Reviewed;         313 AA.
AC   P68795; Q99VA7;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=SaFabH;
GN   Name=fabH; OrderedLocusNames=SAV0983;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   FUNCTION, HOMODIMERIZATION, AND SUBSTRATE SPECIFICITY.
RX   PubMed=11959561; DOI=10.1128/aac.46.5.1310-1318.2002;
RA   He X., Reynolds K.A.;
RT   "Purification, characterization, and identification of novel inhibitors of
RT   the beta-ketoacyl-acyl carrier protein synthase III (FabH) from
RT   Staphylococcus aureus.";
RL   Antimicrob. Agents Chemother. 46:1310-1318(2002).
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       butyryl- and isobutyryl-CoA. Its substrate specificity determines the
CC       biosynthesis of branched-chain of fatty acids.
CC       {ECO:0000269|PubMed:11959561}.
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 HR12 (5-chloro-4-phenyl-[1,2]-dithiol-
CC       3-one) and HR19 (4-phenyl-5-phenylimino-[1,2,4]dithiazolidin-3-one)
CC       antibiotics. Weakly inhibited by thiolactomycin.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC       {ECO:0000305}.
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DR   EMBL; BA000017; BAB57145.1; -; Genomic_DNA.
DR   RefSeq; WP_001100526.1; NC_002758.2.
DR   AlphaFoldDB; P68795; -.
DR   SMR; P68795; -.
DR   ChEMBL; CHEMBL3673; -.
DR   World-2DPAGE; 0002:P68795; -.
DR   PaxDb; P68795; -.
DR   EnsemblBacteria; BAB57145; BAB57145; SAV0983.
DR   KEGG; sav:SAV0983; -.
DR   HOGENOM; CLU_039592_3_1_9; -.
DR   OMA; WGSEGDK; -.
DR   PhylomeDB; P68795; -.
DR   BioCyc; SAUR158878:SAV_RS05325-MON; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002481; 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..313
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT                   /id="PRO_0000110469"
FT   REGION          239..243
FT                   /note="ACP-binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        238
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        268
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   313 AA;  33879 MW;  728D2DCCAB9B95F7 CRC64;
     MNVGIKGFGA YAPEKIIDNA YFEQFLDTSD EWISKMTGIK ERHWADDDQD TSDLAYEASV
     KAIADAGIQP EDIDMIIVAT ATGDMPFPTV ANMLQERLGT GKVASMDQLA ACSGFMYSMI
     TAKQYVQSGD YHNILVVGAD KLSKITDLTD RSTAVLFGDG AGAVIIGEVS EGRGIISYEM
     GSDGTGGKHL YLDKDTGKLK MNGREVFKFA VRIMGDASTR VVEKANLTSD DIDLFIPHQA
     NIRIMESARE RLGISKDKMS VSVNKYGNTS AASIPLSIDQ ELKNGKLKDD DTIVLVGFGG
     GLTWGAMTIK WGK