ID   FABH_MYCUA              Reviewed;         335 AA.
AC   A0PLS8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   10-JUN-2026, entry version 102.
DE   RecName: Full=Mycobacterial beta-ketoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE            Short=Beta-ketoacyl-ACP synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE            Short=KAS III {ECO:0000255|HAMAP-Rule:MF_01815};
DE            EC=2.3.1.301 {ECO:0000255|HAMAP-Rule:MF_01815};
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000255|HAMAP-Rule:MF_01815};
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
GN   Name=fabH {ECO:0000255|HAMAP-Rule:MF_01815};
GN   OrderedLocusNames=MUL_0632;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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=malonyl-[ACP] + dodecanoyl-CoA + H(+) = 3-oxotetradecanoyl-
CC         [ACP] + CO2 + CoA; Xref=Rhea:RHEA:43640, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9645, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:78449,
CC         ChEBI:CHEBI:78473; EC=2.3.1.301; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01815};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43641;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01815};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_01815}.
CC   -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC       {ECO:0000255|HAMAP-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; CP000325; ABL03297.1; -; Genomic_DNA.
DR   RefSeq; WP_011738922.1; NC_008611.1.
DR   AlphaFoldDB; A0PLS8; -.
DR   SMR; A0PLS8; -.
DR   KEGG; mul:MUL_0632; -.
DR   eggNOG; COG0332; Bacteria.
DR   HOGENOM; CLU_039592_4_0_11; -.
DR   UniPathway; UPA00094; -.
DR   UniPathway; UPA00915; -.
DR   Proteomes; UP000000765; 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   CDD; cd00830; KAS_III; 1.
DR   FunFam; 3.40.47.10:FF:000076; 3-oxoacyl-[acyl-carrier-protein] synthase 3; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   HAMAP; MF_01815; FabH; 1.
DR   InterPro; IPR013747; ACP_syn_III_C.
DR   InterPro; IPR013751; ACP_syn_III_N.
DR   InterPro; IPR004655; FabH.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR00747; fabH; 1.
DR   NCBIfam; NF006829; PRK09352.1; 1.
DR   PANTHER; PTHR43091; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE; 1.
DR   PANTHER; PTHR43091:SF1; BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE III, CHLOROPLASTIC; 1.
DR   Pfam; PF08545; ACP_syn_III; 1.
DR   Pfam; PF08541; ACP_syn_III_C; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 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..335
FT                   /note="Mycobacterial beta-ketoacyl-[acyl-carrier-protein]
FT                   synthase III"
FT                   /id="PRO_1000056380"
FT   REGION          259..263
FT                   /note="ACP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT   ACT_SITE        122
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ   SEQUENCE   335 AA;  34807 MW;  EB9E449AE4C3DAEF CRC64;
     MTEIATTSGI SSVGLLSVGA YRPTRVVTND EICENIDSSD EWIYSRTGIK TRRFAAPEES
     AASMAIEASR EAIAKAALTG SDIDGVIVAT STHFLQTPAC APIVAAALGC QNVPAFDISA
     GCSGFGHALG IAADMIRGGS AATILVIGTE KLSPTVDMTD RSNCFIFVDG AASVLVGHSP
     IQGIGPTVWG SDGEQAAAIR QDIDWISHAE NPAGPRPFLR MEGTAVFRWA AFEMGKVGQQ
     AMDAAGVKPD EIDVFIPHQA NSRINELLTK NLQLRPDAVI ANDIEHTGNT SAASIPLAMA
     ELLATGAAKP GDLALLIGYG AGLSYAAQVV RMPNS
//