ID   FABH_DEIGD              Reviewed;         346 AA.
AC   Q1J198;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=Dgeo_0433;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) 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: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; CP000359; ABF44736.1; -; Genomic_DNA.
DR   RefSeq; WP_011529579.1; NC_008025.1.
DR   AlphaFoldDB; Q1J198; -.
DR   SMR; Q1J198; -.
DR   STRING; 319795.Dgeo_0433; -.
DR   EnsemblBacteria; ABF44736; ABF44736; Dgeo_0433.
DR   KEGG; dge:Dgeo_0433; -.
DR   eggNOG; COG0332; Bacteria.
DR   HOGENOM; CLU_039592_3_1_0; -.
DR   OMA; WGSEGDK; -.
DR   OrthoDB; 872193at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002431; 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; -; 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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..346
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT                   /id="PRO_1000187862"
FT   REGION          257..261
FT                   /note="ACP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ   SEQUENCE   346 AA;  36203 MW;  79850BC0D014325F CRC64;
     MTTPSGSRPS IGITALGTYV PPRVVTNKDF EAHMDTSDEW IVSRTGIRER RFAAENEFTS
     DLGVRAVQDL LARDPDGLRD VDVVICATAT PDALFPSTAA LIAGQVGLSG AGAFDLSTAC
     SGFVYALSMA QGLILGGTAR RVLVVGAETL SRLVDQHDRS TAILFGDGAG AAVVGPVPQG
     HGFQEFVLGA DSAGGPSLYA RCMADRLPGG ILMGERVGMN GREVFKFAVR VLGDSGQQVL
     DKSGLTSADV DWVIPHQANI RIIEAANERF GVPMSKTVVN IDRYGNTSSA SLPLALREAV
     DDGRIQDGQQ LLLVAFGGGL SWGACTVKWW AGAPSLTAAQ QAEVTA