FABH_COXBR
ID FABH_COXBR Reviewed; 319 AA.
AC A9NBY3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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};
GN OrderedLocusNames=COXBURSA331_A0602;
OS Coxiella burnetii (strain RSA 331 / Henzerling II).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=360115;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 331 / Henzerling II;
RA Seshadri R., Samuel J.E.;
RT "Genome sequencing of phylogenetically and phenotypically diverse Coxiella
RT burnetii isolates.";
RL Submitted (NOV-2007) 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; CP000890; ABX78580.1; -; Genomic_DNA.
DR RefSeq; WP_012220235.1; NC_010117.1.
DR AlphaFoldDB; A9NBY3; -.
DR SMR; A9NBY3; -.
DR KEGG; cbs:COXBURSA331_A0602; -.
DR HOGENOM; CLU_039592_4_1_6; -.
DR OMA; WGSEGDK; -.
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..319
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_1000088309"
FT REGION 247..251
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 115
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 246
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 276
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ SEQUENCE 319 AA; 34687 MW; FF85294CDBC55793 CRC64;
MTYARIQGVG SYIPQQILSN ADLEKMVNTT DEWIMQRVGV RERHVIANSP DNTTTMAVDA
AKRAIEMAGI DPAVIDMIIV GTATAEYYFP STACLVQKHL NLREDIPAFD INAACAGFVY
ALSIADQYIR NEGAKHILVI GVDSLTKVVD WKDRSTCILF GDGAGAVILQ AHKEPGILNT
ILHANGDYSD LITAKSGVWE RESVPHLHMY GKEVFKLAVT KLGEIVDEII EKSGLKQSGI
DWLIPHQANL RIIEATAKRL GLPRERVILT IEQHGNTSAA SIPLALDAAV RAGKIKRGDT
LLLEAFGAGL AWGAALLKL
