FABH_STRLI
ID FABH_STRLI Reviewed; 339 AA.
AC Q9F6D4;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 88.
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; Synonyms=zhuH;
OS Streptomyces lividans.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1916;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10931852; DOI=10.1074/jbc.m006766200;
RA Marti T., Hu Z., Pohl N.L., Shah A.N., Khosla C.;
RT "Cloning, nucleotide sequence, and heterologous expression of the
RT biosynthetic gene cluster for R1128, a non-steroidal estrogen receptor
RT antagonist. Insights into an unusual priming mechanism.";
RL J. Biol. Chem. 275:33443-33448(2000).
RN [2]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=11732905; DOI=10.1021/bi0113723;
RA Meadows E.S., Khosla C.;
RT "In vitro reconstitution and analysis of the chain initiating enzymes of
RT the R1128 polyketide synthase.";
RL Biochemistry 40:14855-14861(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=12429097; DOI=10.1016/s0969-2126(02)00889-4;
RA Pan H., Tsai S.-C., Meadows E.S., Miercke L.J.W., Keatinge-Clay A.T.,
RA O'Connell J.D. III, Khosla C., Stroud R.M.;
RT "Crystal structure of the priming beta-ketosynthase from the R1128
RT polyketide biosynthetic pathway.";
RL Structure 10:1559-1568(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 some substrate preference for
CC butyryl-CoA and can tolerate branched substrates. Can also prime acyl-
CC CoA. Its substrate specificity determines the biosynthesis of branched-
CC chain and/or straight-chain of fatty acids. Involved in the
CC biosynthesis of R1128 polyketide. {ECO:0000269|PubMed:11732905}.
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 ECO:0000269|PubMed:12429097}.
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, ECO:0000305}.
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DR EMBL; AF293442; AAG30195.1; -; Genomic_DNA.
DR PDB; 1MZJ; X-ray; 2.10 A; A/B=1-339.
DR PDBsum; 1MZJ; -.
DR AlphaFoldDB; Q9F6D4; -.
DR SMR; Q9F6D4; -.
DR DrugBank; DB01992; Coenzyme A.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; Q9F6D4; -.
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; Transferase.
FT CHAIN 1..339
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_0000110489"
FT REGION 258..262
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 121
FT /evidence="ECO:0000305|PubMed:12429097"
FT ACT_SITE 257
FT /evidence="ECO:0000305|PubMed:12429097"
FT ACT_SITE 288
FT /evidence="ECO:0000305|PubMed:12429097"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:1MZJ"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 60..75
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 123..137
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:1MZJ"
FT TURN 160..165
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 168..180
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 222..242
FT /evidence="ECO:0007829|PDB:1MZJ"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:1MZJ"
FT HELIX 292..304
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:1MZJ"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:1MZJ"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:1MZJ"
SQ SEQUENCE 339 AA; 35392 MW; F0CA49FD80A7A26D CRC64;
MPGLRVPERR FSRVLGVGSY RPRREVSNKE VCTWIDSTEE WIETRTGIRS RRIAEPDETI
QVMGVAASRR ALEHAGVDPA EIDLVVVSTM TNFVHTPPLS VAIAHELGAD NAGGFDLSAA
CAGFCHALSI AADAVESGGS RHVLVVATER MTDVIDLADR SLSFLFGDGA GAAVVGPSDV
PGIGPVVRGI DGTGLGSLHM SSSWDQYVED PSVGRPALVM DGKRVFRWAV ADVVPAAREA
LEVAGLTVGD LVAFVPHQAN LRIIDVLVDR LGVPEHVVVS RDAEDTGNTS SASVALALDR
LVRSGAVPGG GPALMIGFGA GLSYAGQALL LPDPPSTPA
