ID   FABH2_BACCR             Reviewed;         327 AA.
AC   Q81F42;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Beta-ketoacyl-[acyl-carrier-protein] synthase III 2 {ECO:0000255|HAMAP-Rule:MF_01815};
DE            Short=Beta-ketoacyl-ACP synthase III 2 {ECO:0000255|HAMAP-Rule:MF_01815};
DE            Short=KAS III 2 {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 3 2 {ECO:0000255|HAMAP-Rule:MF_01815};
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III 2 {ECO:0000255|HAMAP-Rule:MF_01815};
GN   Name=fabH2 {ECO:0000255|HAMAP-Rule:MF_01815};
GN   OrderedLocusNames=BC_1760;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC   9373 / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP08736.1; -; Genomic_DNA.
DR   RefSeq; NP_831535.1; NC_004722.1.
DR   RefSeq; WP_000555762.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81F42; -.
DR   SMR; Q81F42; -.
DR   STRING; 226900.BC_1760; -.
DR   KEGG; bce:BC1760; -.
DR   PATRIC; fig|226900.8.peg.1749; -.
DR   HOGENOM; CLU_039592_3_1_9; -.
DR   OrthoDB; 9815506at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001417; 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   GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR   CDD; cd00830; KAS_III; 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   PANTHER; PTHR34069; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 3; 1.
DR   PANTHER; PTHR34069:SF2; BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE III; 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..327
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III 2"
FT                   /id="PRO_0000110396"
FT   REGION          252..256
FT                   /note="ACP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT   ACT_SITE        114
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   327 AA;  36247 MW;  8C03B6E178732409 CRC64;
     MHSKSRITAI GTYVPDQILS NNDLEKMVHT NDEWIVQRTG MRERRIASEE EYSSNLAIKA
     IENLCTTYKK NLEDVDCIIV ATTTADYVFP SVACQIQQYF NIPHTLAFDL NATCAGFTYG
     LHVGNSLITS ESHEKVLVVA TETLSKVTDY TDRTTCILFG DGAGAILLER DENTPSFIAA
     HMGTNGDGGI HLYRTNLSTT MNGTPLQTNE KIVQNGREVY KWATRTVPKG IKNLLHTVNM
     QVDDIDWFIP HSANLRMIES ICEKSQIPIQ KTLTSVEYMG NTSSVTIPLA LNLAIKEGKL
     NNGDTLLLYG FGGGLTHLGL IVEWNLI
//