ID A0A1I5KP49_9PSEU Unreviewed; 331 AA.
AC A0A1I5KP49;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05421810_101231 {ECO:0000313|EMBL:SFO86466.1};
OS Amycolatopsis arida.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=587909 {ECO:0000313|EMBL:SFO86466.1, ECO:0000313|Proteomes:UP000198727};
RN [1] {ECO:0000313|Proteomes:UP000198727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5579 {ECO:0000313|Proteomes:UP000198727};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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; FOWW01000001; SFO86466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5KP49; -.
DR STRING; 587909.SAMN05421810_101231; -.
DR OrthoDB; 9815506at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000198727; 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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00830; KAS_III; 1.
DR Gene3D; 3.40.47.10; -; 2.
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 Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
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:UP000198727};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01815}.
FT DOMAIN 123..200
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08545"
FT DOMAIN 239..328
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08541"
FT REGION 254..258
FT /note="ACP-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 129
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 253
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 287
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
SQ SEQUENCE 331 AA; 34743 MW; C4B14D69AC025A5E CRC64;
MTTPSTPRPA LRLSRGPAAT RILGIGSTQP ERVVTNDDLA KTMDTTDQWI RDRVGIIERR
FADKDELLVD MAVTAGTRAL ADAGVEASEV DTVIVPNCTM PAPIPNAAAQ VADRIGVRAA
GAFDLNAACA GFCYGLGVAS DLIRAGSSGK VLVIGAEKLT DVVDPVDRAN AIIFADGAGA
AVVGPSDEPG IGPVAWGSAG ELVDTIYMRE QKYIYQEGQS VFRWATTQIA PIAMRAVEVA
GLRLSDVDVL VPHQANLRIV EAIAKRLRAK GAREDMVVAD DIKYSGNTSS ASIPMALDHM
RADGRVRSGD VVLMVGFGAG LSYAGQVVIC P
//
