FABH_ENTFA
ID FABH_ENTFA Reviewed; 321 AA.
AC Q820T1;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000255|HAMAP-Rule:MF_01815};
DE EC=2.3.1.180 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III {ECO:0000255|HAMAP-Rule:MF_01815};
GN Name=fabH {ECO:0000255|HAMAP-Rule:MF_01815}; OrderedLocusNames=EF_2885;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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:0000255|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:0000255|HAMAP-Rule:MF_01815};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_01815}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01815}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01815}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC {ECO:0000255|HAMAP-Rule:MF_01815}.
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DR EMBL; AE016830; AAO82575.1; -; Genomic_DNA.
DR RefSeq; NP_816505.1; NC_004668.1.
DR RefSeq; WP_002365153.1; NZ_KE136528.1.
DR PDB; 3IL4; X-ray; 3.00 A; A/B/C/D=2-321.
DR PDB; 3IL5; X-ray; 2.60 A; A/B/C/D=1-321.
DR PDB; 3IL6; X-ray; 2.50 A; A=1-321.
DR PDBsum; 3IL4; -.
DR PDBsum; 3IL5; -.
DR PDBsum; 3IL6; -.
DR AlphaFoldDB; Q820T1; -.
DR SMR; Q820T1; -.
DR STRING; 226185.EF_2885; -.
DR BindingDB; Q820T1; -.
DR ChEMBL; CHEMBL5070; -.
DR DrugBank; DB07429; 2-({[4-bromo-3-(diethylsulfamoyl)phenyl]carbonyl}amino)benzoic acid.
DR EnsemblBacteria; AAO82575; AAO82575; EF_2885.
DR GeneID; 60894810; -.
DR KEGG; efa:EF2885; -.
DR PATRIC; fig|226185.45.peg.688; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_4_1_9; -.
DR OMA; WGSEGDK; -.
DR BRENDA; 2.3.1.180; 2095.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; Q820T1; -.
DR PRO; PR:Q820T1; -.
DR Proteomes; UP000001415; 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 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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1..321
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_0000110427"
FT REGION 247..251
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 113
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 246
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 276
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:3IL6"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:3IL6"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3IL6"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:3IL6"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:3IL6"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:3IL6"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:3IL6"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3IL6"
FT STRAND 161..172
FT /evidence="ECO:0007829|PDB:3IL6"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:3IL6"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3IL5"
FT HELIX 216..232
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:3IL6"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:3IL6"
FT HELIX 281..291
FT /evidence="ECO:0007829|PDB:3IL6"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:3IL6"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:3IL6"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:3IL6"
SQ SEQUENCE 321 AA; 35182 MW; 1306C774594D6D9D CRC64;
MKNYARISCT SRYVPENCVT NHQLSEMMDT SDEWIHSRTG ISERRIVTQE NTSDLCHQVA
KQLLEKSGKQ ASEIDFILVA TVTPDFNMPS VACQVQGAIG ATEAFAFDIS AACSGFVYAL
SMAEKLVLSG RYQTGLVIGG ETFSKMLDWT DRSTAVLFGD GAAGVLIEAA ETPHFLNEKL
QADGQRWAAL TSGYTINESP FYQGHKQASK TLQMEGRSIF DFAIKDVSQN ILSLVTDETV
DYLLLHQANV RIIDKIARKT KISREKFLTN MDKYGNTSAA SIPILLDEAV ENGTLILGSQ
QRVVLTGFGG GLTWGSLLLT L
