ID A0A0P7ZNL6_9GAMM Unreviewed; 319 AA.
AC A0A0P7ZNL6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ECO:0000313|EMBL:KPQ03895.1};
GN ORFNames=HLUCCO02_02760 {ECO:0000313|EMBL:KPQ03895.1};
OS Idiomarinaceae bacterium HL-53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae.
OX NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ03895.1, ECO:0000313|Proteomes:UP000053932};
RN [1] {ECO:0000313|EMBL:KPQ03895.1, ECO:0000313|Proteomes:UP000053932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-53 {ECO:0000313|EMBL:KPQ03895.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (AUG-2015) 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:KPQ03895.1}.
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DR EMBL; LIHO01000009; KPQ03895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7ZNL6; -.
DR STRING; 1298881.Ga0003345_1923; -.
DR PATRIC; fig|1298881.4.peg.523; -.
DR OrthoDB; 9815506at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000053932; 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; PTHR43091; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE; 1.
DR PANTHER; PTHR43091:SF1; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE III, CHLOROPLASTIC; 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:KPQ03895.1}; Cytoplasm {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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01815}.
FT DOMAIN 106..182
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08545"
FT DOMAIN 230..319
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08541"
FT REGION 247..251
FT /note="ACP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 112
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 246
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 276
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
SQ SEQUENCE 319 AA; 34227 MW; 50899BC881F6A219 CRC64;
MYSKIAGTGH YLPAQVLSNQ DLERRVDTSD QWIRERTGIR ERRIAEKHEN VVSMAVAAGK
DALESAKLDA AQLNMIIVAT TSADKAFPSA ACEVQAALGA KHAAAFDVAA ACAGFMFAMS
VADQYIKTGM ARHVLIVGSD VLSRLCNPDD RNTIVLFGDG AGAAVLSASA TQGVLSTHIY
CAGEYAELLG ADLPSRHPDP IEEQAWLYMK GSEVFKVAVQ KLSELVNTTL KQHEIAASEL
DWLVPHQANY RIIQATAKKL SMPMERVVMT LEQTGNTSAA SVPIALDCAI KDGRIQPGHL
LLLEAFGGGF AWGSALVKY
//