FABH_STRGA
ID FABH_STRGA Reviewed; 333 AA.
AC Q54206;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3;
DE EC=2.3.1.180;
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III;
DE AltName: Full=Beta-ketoacyl-ACP synthase III;
DE Short=KAS III;
DE AltName: Full=SgFabH;
GN Name=fabH;
OS Streptomyces glaucescens.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1907;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 40716 / ETH 22794 / Tue 49;
RX PubMed=7626609; DOI=10.1021/bi00029a015;
RA Summers R.G., Ali A., Shen B., Wessel W.A., Hutchinson C.R.;
RT "Malonyl-coenzyme A:acyl carrier protein acyltransferase of Streptomyces
RT glaucescens: a possible link between fatty acid and polyketide
RT biosynthesis.";
RL Biochemistry 34:9389-9402(1995).
RN [2]
RP FUNCTION, HOMODIMERIZATION, AND SUBSTRATE SPECIFICITY.
RX PubMed=9721286; DOI=10.1128/jb.180.17.4481-4486.1998;
RA Han L., Lobo S., Reynolds K.A.;
RT "Characterization of beta-ketoacyl-acyl carrier protein synthase III from
RT Streptomyces glaucescens and its role in initiation of fatty acid
RT biosynthesis.";
RL J. Bacteriol. 180:4481-4486(1998).
RN [3]
RP FUNCTION.
RX PubMed=12173933; DOI=10.1021/bi0258804;
RA Florova G., Kazanina G., Reynolds K.A.;
RT "Enzymes involved in fatty acid and polyketide biosynthesis in Streptomyces
RT glaucescens: role of FabH and FabD and their acyl carrier protein
RT specificity.";
RL Biochemistry 41:10462-10471(2002).
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. Has a broad substrate specificity for
CC butyryl-CoA > acetyl-CoA > isobutyryl-CoA. Can also prime acyl-CoA. Its
CC substrate specificity determines the biosynthesis of both branched-
CC chain and straight-chain of fatty acids. Not involved in tetracenomycin
CC C (TCM C) biosynthesis. {ECO:0000269|PubMed:12173933,
CC ECO:0000269|PubMed:9721286}.
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;
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The last Arg residue of the ACP-binding site is essential for
CC the weak association between ACP/AcpP and FabH. {ECO:0000250}.
CC -!- MISCELLANEOUS: Inhibited by thiolactomycin.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L43074; AAA99447.1; -; Genomic_DNA.
DR PIR; T11212; T11212.
DR RefSeq; WP_043500561.1; NZ_CP009438.1.
DR AlphaFoldDB; Q54206; -.
DR SMR; Q54206; -.
DR STRING; 1907.SGLAU_10970; -.
DR KEGG; ag:AAA99447; -.
DR eggNOG; COG0332; Bacteria.
DR OMA; WGSEGDK; -.
DR OrthoDB; 872193at2; -.
DR BRENDA; 2.3.1.300; 6020.
DR UniPathway; UPA00094; -.
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 Gene3D; 3.40.47.10; -; 2.
DR HAMAP; MF_01815; FabH; 1.
DR InterPro; IPR013751; ACP_syn_III.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR004655; FabH_synth.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08545; ACP_syn_III; 1.
DR Pfam; PF08541; ACP_syn_III_C; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR TIGRFAMs; TIGR00747; fabH; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Multifunctional enzyme; Transferase.
FT CHAIN 1..333
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_0000110488"
FT REGION 259..263
FT /note="ACP-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 122
FT /evidence="ECO:0000250"
FT ACT_SITE 258
FT /evidence="ECO:0000250"
FT ACT_SITE 289
FT /evidence="ECO:0000250"
SQ SEQUENCE 333 AA; 34777 MW; 2A26467E65A3EA10 CRC64;
MSKIKPAKGA PYARILGVGG YRPTRVVPNE VILETIDSSD EWIRSRSGIQ TRHWANDEET
VAAMSIEASG KAIADAGITA AQVGAVIVST VTHFKQTPAV ATEIADKLGT NKAAAFDISA
GCAGFGYGLT LAKGMIVEGS AEYVLVIGVE RLSDLTDLED RATAFLFGDG AGAVVVGPSN
EPAIGPTIWG SEGDKAETIK QTVPWTDYRE GGVERFPAIT QEGQAVFRWA VFEMAKVAQQ
ALDAAGVAAA DLDVFIPHQA NERIIDSMVK TLKLPESVTV ARDVRTTGNT SAASIPLAME
RLLATGEAKS GDTALVIGFG AGLVYAASVV TLP
