ID A0A2P8AMS0_9ACTN Unreviewed; 314 AA.
AC A0A2P8AMS0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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_2 {ECO:0000313|EMBL:PSK61780.1};
GN Synonyms=fabH {ECO:0000256|HAMAP-Rule:MF_01815};
GN ORFNames=B0E53_06317 {ECO:0000313|EMBL:PSK61780.1};
OS Micromonospora sp. MH33.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1945509 {ECO:0000313|EMBL:PSK61780.1, ECO:0000313|Proteomes:UP000240342};
RN [1] {ECO:0000313|EMBL:PSK61780.1, ECO:0000313|Proteomes:UP000240342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH33 {ECO:0000313|EMBL:PSK61780.1,
RC ECO:0000313|Proteomes:UP000240342};
RA Thatcher L.F., Myers C.A., O'Sullivan C.A., Roper M.;
RT "Draft genome sequences of Micromonospora sp. MH33 and MH99.";
RL Submitted (FEB-2017) 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|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}.
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:PSK61780.1}.
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DR EMBL; MUYZ01000361; PSK61780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8AMS0; -.
DR OrthoDB; 9815506at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000240342; 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:PSK61780.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000240342};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01815}.
FT DOMAIN 106..183
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08545"
FT DOMAIN 224..312
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08541"
FT REGION 241..245
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 240
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT ACT_SITE 270
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
SQ SEQUENCE 314 AA; 32366 MW; A737A89FD4A19FAF CRC64;
MAGSRIVAMG HYQPSRVITN DDLAQMVDTN DEWIRDRVGI VTRRIAGDET VADMATAAAG
KALANSGLTA ADIDLVVVAT CTSVDRSPNV ACRVAAKLGI SAPGAYDINT ACSGFAYALG
TVDHAIQAGA ARNAIVIGAE KLSDFTDWTD RSTCIIFADG AGAAVVTAAA EGEPAGVGPV
VWGSVPEKSD AVRIEGWRPY IAQEGQAVFR WATTALAPLA LQACEKAGVD PSELAAFVPH
QANGRIIDGI AKRLNIPNAI IAKDIVESGN TSAASVPLAL SKLVERREVP AGAPVLLFGF
GGGLTYAGQV VRCP
//
