ID   FABH_LIMRJ              Reviewed;         324 AA.
AC   B2G7L1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
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}; OrderedLocusNames=LAR_0927;
OS   Limosilactobacillus reuteri (strain JCM 1112) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 1112;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA   Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA   Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT   fermentum reveal a genomic island for reuterin and cobalamin production.";
RL   DNA Res. 15:151-161(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; AP007281; BAG25443.1; -; Genomic_DNA.
DR   RefSeq; WP_003667751.1; NC_010609.1.
DR   AlphaFoldDB; B2G7L1; -.
DR   SMR; B2G7L1; -.
DR   GeneID; 66471079; -.
DR   KEGG; lrf:LAR_0927; -.
DR   HOGENOM; CLU_039592_4_1_9; -.
DR   OMA; QFVFKNA; -.
DR   UniPathway; UPA00094; -.
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..324
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT                   /id="PRO_1000187875"
FT   REGION          252..256
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        251
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ   SEQUENCE   324 AA;  34911 MW;  0A64C2EF4D86B754 CRC64;
     MQNLRITSTA SYHPPLNITN QQLSTIMDTS DEWIKTRTGI HQRYISNIEN TSDLALNVGN
     QLLTNANLKT TELDLIIIAT MSPDAYTPST AAIVQGELGA KNAIAFDISA ACTGFIYAMN
     TAELMLKSSN WQNAMVIGAE VLSKLIDWKD RSTAVLFGDG AGGVLLQKTT TATPLILGRD
     LHTFGDLGDK IVAGKTTPKA GFPKQLTSLS PFAMAGRDVY RFATHEVPRS IASAVQQANL
     KLDDIDYFLL HQANERIINQ IAKRLGQPIT KFPMNISEYG NTGAASEPIL LTQAVAHELV
     KPGNIIAMSG FGGGLSTGTI ILNY