ID A0A1B1MKW8_STRLN Unreviewed; 340 AA.
AC A0A1B1MKW8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Beta-ketoacyl-[acyl-carrier-protein] synthase III {ECO:0000256|ARBA:ARBA00012333, 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|ARBA:ARBA00012333, 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=SLCG_6978 {ECO:0000313|EMBL:AXG58133.1}, SLINC_6990
GN {ECO:0000313|EMBL:ANS69214.1};
OS Streptomyces lincolnensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS69214.1, ECO:0000313|Proteomes:UP000092598};
RN [1] {ECO:0000313|EMBL:ANS69214.1, ECO:0000313|Proteomes:UP000092598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS69214.1,
RC ECO:0000313|Proteomes:UP000092598};
RA Meng S.C.;
RT "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT actinobacteria.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXG58133.1, ECO:0000313|Proteomes:UP000253884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC-G {ECO:0000313|EMBL:AXG58133.1,
RC ECO:0000313|Proteomes:UP000253884};
RX PubMed=29574602; DOI=10.1007/s10295-018-2029-1;
RA Xu Y., Tan G., Ke M., Li J., Tang Y., Meng S., Niu J., Wang Y., Liu R.,
RA Wu H., Bai L., Zhang L., Zhang B.;
RT "Enhanced lincomycin production by co-overexpression of metK1 and metK2 in
RT Streptomyces lincolnensis.";
RL J. Ind. Microbiol. Biotechnol. 45:345-355(2018).
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|ARBA:ARBA00043707};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12081;
CC Evidence={ECO:0000256|ARBA:ARBA00043707};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|HAMAP-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; CP016438; ANS69214.1; -; Genomic_DNA.
DR EMBL; CP022744; AXG58133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B1MKW8; -.
DR STRING; 1915.SLINC_6990; -.
DR KEGG; sls:SLINC_6990; -.
DR PATRIC; fig|1915.4.peg.7701; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000092598; Chromosome.
DR Proteomes; UP000253884; 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; 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 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:UP000092598};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01815}.
FT DOMAIN 132..204
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08545"
FT DOMAIN 250..338
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08541"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..271
FT /note="ACP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
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 340 AA; 35169 MW; 485FB0BCD205DD1D CRC64;
MPSYPRVTDQ TGGSRYLKSN EGDPPMTGSR IAAIGHYQPA RVLTNKDLAG MVDTSDEWIT
SRVGIRTRRI AGPDEPVDEL AGHAAAKALA AAGLTPGDID LVLVATSTAV DRSPNMAARV
AARLGIPSPA VMDLNVVCAG FTHALATADH TVRAGAATRA LVIGADKMSE VADWTDRTTC
VLVGDGAGAA VVEACGPGEE PGIGPVLWGS VPEMGNAVRI EGQPARFAQE GQSVYRWATT
QLPAFARKAC ERAGLTPADL AAVVLHQANL RIIEPLAEKI GAVNAVVARD VVESGNTSAA
SIPMAFSKLV ERGEISSGDP VLLFGFGGNL SYAGQVVRCP
//
