ID   C0ZFP5_BREBN            Unreviewed;       338 AA.
AC   C0ZFP5;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   02-SEP-2026, entry version 87.
DE   RecName: Full=Beta-ketoacyl-[acyl-carrier-protein] synthase III {ECO:0000256|HAMAP-Rule:MF_01815};
DE            Short=Beta-ketoacyl-ACP synthase III {ECO:0000256|HAMAP-Rule:MF_01815};
DE            Short=KAS III {ECO:0000256|HAMAP-Rule:MF_01815};
DE            EC=2.3.1.180 {ECO:0000256|HAMAP-Rule:MF_01815};
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000256|HAMAP-Rule:MF_01815};
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000256|HAMAP-Rule:MF_01815};
GN   Name=fabHA {ECO:0000313|EMBL:BAH44604.1};
GN   Synonyms=fabH {ECO:0000256|HAMAP-Rule:MF_01815}, fabH1
GN   {ECO:0000313|EMBL:BAH44604.1};
GN   OrderedLocusNames=BBR47_36270 {ECO:0000313|EMBL:BAH44604.1};
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Paenibacillaceae;
OC   Brevibacillus.
OX   NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH44604.1, ECO:0000313|Proteomes:UP000001877};
RN   [1] {ECO:0000313|EMBL:BAH44604.1, ECO:0000313|Proteomes:UP000001877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599
RC   {ECO:0000313|Proteomes:UP000001877};
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01815}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-methylbutanoyl-CoA + malonyl-[ACP] + H(+) = (4S)-4-
CC         methyl-3-oxohexanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42276,
CC         Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:17148, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:78449,
CC         ChEBI:CHEBI:88166, ChEBI:CHEBI:167462; EC=2.3.1.300;
CC         Evidence={ECO:0000256|ARBA:ARBA00052407};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42277;
CC         Evidence={ECO:0000256|ARBA:ARBA00052407};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylpropanoyl-CoA + malonyl-[ACP] + H(+) = 4-methyl-3-
CC         oxopentanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42268, Rhea:RHEA-
CC         COMP:9623, Rhea:RHEA-COMP:9940, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57338, ChEBI:CHEBI:78449,
CC         ChEBI:CHEBI:78820; EC=2.3.1.300;
CC         Evidence={ECO:0000256|ARBA:ARBA00052467};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42269;
CC         Evidence={ECO:0000256|ARBA:ARBA00052467};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methylbutanoyl-CoA + malonyl-[ACP] + H(+) = 5-methyl-3-
CC         oxohexanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42272, Rhea:RHEA-
CC         COMP:9623, Rhea:RHEA-COMP:9941, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57345, ChEBI:CHEBI:78449,
CC         ChEBI:CHEBI:78822; EC=2.3.1.300;
CC         Evidence={ECO:0000256|ARBA:ARBA00052985};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42273;
CC         Evidence={ECO:0000256|ARBA:ARBA00052985};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=malonyl-[ACP] + acetyl-CoA + H(+) = 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:0000256|ARBA:ARBA00051096};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12081;
CC         Evidence={ECO:0000256|ARBA:ARBA00051096};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_01815}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01815}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_01815}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC       {ECO:0000256|ARBA:ARBA00008642, ECO:0000256|HAMAP-Rule:MF_01815}.
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; AP008955; BAH44604.1; -; Genomic_DNA.
DR   RefSeq; WP_015891898.1; NC_012491.1.
DR   AlphaFoldDB; C0ZFP5; -.
DR   STRING; 358681.BBR47_36270; -.
DR   KEGG; bbe:BBR47_36270; -.
DR   eggNOG; COG0332; Bacteria.
DR   HOGENOM; CLU_039592_3_1_9; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001877; 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:000004; 3-oxoacyl-[acyl-carrier-protein] synthase 3; 1.
DR   Gene3D; 3.40.47.10; -; 1.
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 {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_01815}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01815};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW   Rule:MF_01815};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW   Rule:MF_01815};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_01815};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_01815};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01815}; Reference proteome {ECO:0000313|Proteomes:UP000001877};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01815}.
FT   DOMAIN          110..188
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08545"
FT   DOMAIN          240..329
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08541"
FT   REGION          257..261
FT                   /note="ACP-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
SQ   SEQUENCE   338 AA;  35795 MW;  76B839466A711A68 CRC64;
     MSAKRSVGIL STGSYTPERV LTNFDLEKMV ETSDEWIVSR TGIRERRISS PEQASSDLAY
     EAAKAALEKA NISAEQLDMI IVATVTPDMS FPSTACLLQE KLGATRAAAM DLSAACTGFL
     YGITTATQFI QNGLYKKVLV VGVETLSKIT NYKDRNTCVL FGDGAGAAVI GEVTEGYGFQ
     SFELGADGSG GSLLCMPAGG SRTPASVESV EQGLHYLYMA GGEVFKFAVR VMNSATEAVL
     SKAGVSKDEI DLLVPHQANK RIIDSAVQRF GLSEDKVAIN LDRYGNMSSA SIPVALDEAV
     KAGRVKEGDN LILVGFGGGL TWGATLLKWC TTPAEGSK
//