ID R7ZTP7_9BACT Unreviewed; 332 AA.
AC R7ZTP7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 ORFNames=ADIS_2046 {ECO:0000313|EMBL:EON77516.1};
OS Lunatimonas lonarensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae.
OX NCBI_TaxID=1232681 {ECO:0000313|EMBL:EON77516.1, ECO:0000313|Proteomes:UP000013909};
RN [1] {ECO:0000313|EMBL:EON77516.1, ECO:0000313|Proteomes:UP000013909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK24 {ECO:0000313|EMBL:EON77516.1,
RC ECO:0000313|Proteomes:UP000013909};
RA Singh A.;
RT "A novel strain isolated from Lonar lake, Maharashtra, India.";
RL Submitted (FEB-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EON77516.1}.
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DR EMBL; AQHR01000054; EON77516.1; -; Genomic_DNA.
DR RefSeq; WP_010854184.1; NZ_AQHR01000054.1.
DR AlphaFoldDB; R7ZTP7; -.
DR STRING; 1232681.ADIS_2046; -.
DR PATRIC; fig|1288963.3.peg.2037; -.
DR OrthoDB; 9815506at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000013909; Unassembled WGS sequence.
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 ECO:0000313|EMBL:EON77516.1};
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:UP000013909};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01815}.
FT DOMAIN 108..189
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08545"
FT DOMAIN 243..332
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08541"
FT REGION 260..264
FT /note="ACP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 114
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 259
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 289
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
SQ SEQUENCE 332 AA; 36037 MW; 91E4FCBAF4AD40C5 CRC64;
MIKSKIIASG HYLPERVVTN DDLSKVMNTN HEWIVERTGI EKRRWFVPGK DTVTSMSLEA
SKMAISNAGI PVKEIDFIIF ATITPDYFIP GNGVLLQREL GLQGIGALDI RNACSGFVYA
LSIADQYIKS GMYKTILVVG AEIQSSALDK SDEGRSSAVI FADGAGAVIL QANESDDSGI
LSSHLHADGD FAEELYVKDP GSSREVRISQ EMIDAGGFNL YMNGNAVFKH AVVRFHEVIL
EALAANKMDV SQLNMLIPHQ ANLRISQYIQ QKLGLADSQV YNNIMDYGNT TAATIPIAIS
EAMAAGLIKR GDLVCLAAFG SGFAWGSALI RW
//