FABH_YERPP
ID FABH_YERPP Reviewed; 316 AA.
AC A4TLS3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=YPDSF_1850;
OS Yersinia pestis (strain Pestoides F).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=386656;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pestoides F;
RG US DOE Joint Genome Institute;
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 Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Worsham P., Chu M., Bearden S., Garcia E.,
RA Richardson P.;
RT "Complete sequence of chromosome of Yersinia pestis Pestoides F.";
RL Submitted (FEB-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; CP000668; ABP40235.1; -; Genomic_DNA.
DR RefSeq; WP_011906295.1; NZ_CP009715.1.
DR AlphaFoldDB; A4TLS3; -.
DR SMR; A4TLS3; -.
DR KEGG; ypp:YPDSF_1850; -.
DR PATRIC; fig|386656.14.peg.3305; -.
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..316
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_1000056449"
FT REGION 244..248
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 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 273
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ SEQUENCE 316 AA; 33768 MW; 1BC70254F7EFA6C9 CRC64;
MYTKILGTGS YLPVQVRSNA DLEKMVDTSD EWIVTRTGIR ERRIAGLDET VATMGFQAAE
KTLEMAGIDK DDIGLIIVAT TSSSHAFPSS ACQVQRMLGI KDAASFDLAA ACAGFTYALS
VADQYVKSGA VKHAIVIGSD VLSRALDPED RGTIILFGDG AGAVVLGASE QPGIMSTHLH
ADGRYGELLA LPYPDRQQDQ PAYVTMAGNE VFKVAVTELA HIVDETLQAN NLDRTALDWL
VPHQANLRII SATAKKLGMG MDKVVITLDR HGNTSAASVP SAFDEAVRDG RIQRGQLVLL
EAFGGGFTWG SALVRF
