FABH_HAEIN
ID FABH_HAEIN Reviewed; 316 AA.
AC P43711;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
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=HI_0157;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP INHIBITION BY ANTIBIOTICS.
RX PubMed=11375394; DOI=10.1074/jbc.m101769200;
RA Khandekar S.S., Gentry D.R., Van Aller G.S., Warren P., Xiang H.,
RA Silverman C., Doyle M.L., Chambers P.A., Konstantinidis A.K., Brandt M.,
RA Daines R.A., Lonsdale J.T.;
RT "Identification, substrate specificity, and inhibition of the Streptococcus
RT pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH).";
RL J. Biol. Chem. 276:30024-30030(2001).
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: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:0000255|HAMAP-
CC Rule:MF_01815}.
CC -!- MISCELLANEOUS: Inhibited by the SB418011 antibiotic. Not inhibited by
CC cerulenin, and weakly inhibited by thiolactomycin.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC {ECO:0000255|HAMAP-Rule:MF_01815}.
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DR EMBL; L42023; AAC21826.1; -; Genomic_DNA.
DR PIR; F64051; F64051.
DR RefSeq; NP_438327.1; NC_000907.1.
DR RefSeq; WP_005691510.1; NC_000907.1.
DR PDB; 3IL3; X-ray; 2.70 A; A=1-316.
DR PDBsum; 3IL3; -.
DR AlphaFoldDB; P43711; -.
DR SMR; P43711; -.
DR STRING; 71421.HI_0157; -.
DR BindingDB; P43711; -.
DR ChEMBL; CHEMBL3822; -.
DR EnsemblBacteria; AAC21826; AAC21826; HI_0157.
DR KEGG; hin:HI_0157; -.
DR PATRIC; fig|71421.8.peg.162; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_3_1_6; -.
DR OMA; WGSEGDK; -.
DR PhylomeDB; P43711; -.
DR BioCyc; HINF71421:G1GJ1-169-MON; -.
DR BRENDA; 2.3.1.180; 2529.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; P43711; -.
DR Proteomes; UP000000579; 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..316
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_0000110432"
FT REGION 244..248
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 112
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 273
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:3IL3"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:3IL3"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3IL3"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3IL3"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:3IL3"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:3IL3"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3IL3"
FT TURN 151..156
FT /evidence="ECO:0007829|PDB:3IL3"
FT STRAND 159..171
FT /evidence="ECO:0007829|PDB:3IL3"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:3IL3"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 208..228
FT /evidence="ECO:0007829|PDB:3IL3"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3IL3"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:3IL3"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:3IL3"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:3IL3"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:3IL3"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:3IL3"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:3IL3"
SQ SEQUENCE 316 AA; 34280 MW; 2D00ADD61DCB6A66 CRC64;
MNSRILSTGS YLPSHIRTNA DLEKMVDTSD EWIVTRSGIR ERRIAAEDET VATMGFEAAK
NAIEAAQINP QDIELIIVAT TSHSHAYPSA ACQVQGLLNI DDAISFDLAA ACTGFVYALS
VADQFIRAGK VKKALVIGSD LNSRKLDETD RSTVVLFGDG AGAVILEASE QEGIISTHLH
ASADKNNALV LAQPERGIEK SGYIEMQGNE TFKLAVRELS NVVEETLLAN NLDKKDLDWL
VPHQANLRII TATAKKLEMD MSQVVVTLDK YANNSAATVP VALDEAIRDG RIQRGQLLLL
EAFGGGWTWG SALVRF
