ID L0DEL8_SINAD Unreviewed; 339 AA.
AC L0DEL8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Beta-ketoacyl-[acyl-carrier-protein] synthase III {ECO:0000256|HAMAP-Rule:MF_01815};
DE Short=Beta-ketoacyl-ACP synthase III {ECO:0000256|HAMAP-Rule:MF_01815};
DE Short=KAS III {ECO:0000256|HAMAP-Rule:MF_01815};
DE EC=2.3.1.180 {ECO:0000256|HAMAP-Rule:MF_01815};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000256|HAMAP-Rule:MF_01815};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000256|HAMAP-Rule:MF_01815};
GN Name=fabH {ECO:0000256|HAMAP-Rule:MF_01815};
GN OrderedLocusNames=Sinac_2979 {ECO:0000313|EMBL:AGA27263.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA27263.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA27263.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) 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:0000256|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:0000256|HAMAP-Rule:MF_01815};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC Rule:MF_01815}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01815}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01815}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC {ECO:0000256|ARBA:ARBA00008642, ECO:0000256|HAMAP-Rule:MF_01815}.
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DR EMBL; CP003364; AGA27263.1; -; Genomic_DNA.
DR RefSeq; WP_015246412.1; NZ_JH621478.1.
DR AlphaFoldDB; L0DEL8; -.
DR STRING; 886293.Sinac_2979; -.
DR KEGG; saci:Sinac_2979; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_3_1_0; -.
DR OrthoDB; 9815506at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000010798; 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 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 {ECO:0000256|HAMAP-Rule:MF_01815};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01815};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW Rule:MF_01815};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW Rule:MF_01815};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01815};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01815}; Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01815};
KW Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01815}.
FT DOMAIN 120..198
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08545"
FT DOMAIN 251..339
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08541"
FT REGION 267..271
FT /note="ACP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 126
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 266
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 296
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
SQ SEQUENCE 339 AA; 36350 MW; E19933C8B9C860B7 CRC64;
MSNGQLHVEP RTRSLTGIQI LGTGSYVPEN VVTNHDLRDS HGFDPEWIVN RTGIHERRFA
LPHQATSDLC TQAAIRCLKA AGCEPAEVDL LVVGTFTPDM CFPSTGNLVQ DRLKLNCPAF
DIQAACAGFI FALITAAQFV AAGTSKRALV IGGDCNSRVI NPGDQKSFPL FGDGAGAVLL
GPGSPEQGLV SYQLGSDGSG GDLLSRPACG SRIPPTVEAL QQGLHFLTMD GRAVFKWAVR
ILTDSTVEVM RKADCLVDDV RWFIPHQANV RIIHAASDVL GFHRDAVFKN LERYGNTSAG
SVPIALDELV QAGSIERGDL LLTSGFGAGL NWGTALWRW
//
