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3-oxoacyl-[acyl-carrier-protein] synthase 3 (EC 2.3.1.180) (3-oxoacyl-[acyl-carrier-protein] synthase III) (Beta-ketoacyl-ACP synthase III) (KAS III)

 FABH_STRLI              Reviewed;         339 AA.
Q9F6D4;
15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
15-MAR-2017, entry version 79.
RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000255|HAMAP-Rule:MF_01815};
EC=2.3.1.180 {ECO:0000255|HAMAP-Rule:MF_01815};
AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
AltName: Full=Beta-ketoacyl-ACP synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
Short=KAS III {ECO:0000255|HAMAP-Rule:MF_01815};
Name=fabH; Synonyms=zhuH;
Streptomyces lividans.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1916;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10931852; DOI=10.1074/jbc.M006766200;
Marti T., Hu Z., Pohl N.L., Shah A.N., Khosla C.;
"Cloning, nucleotide sequence, and heterologous expression of the
biosynthetic gene cluster for R1128, a non-steroidal estrogen receptor
antagonist. Insights into an unusual priming mechanism.";
J. Biol. Chem. 275:33443-33448(2000).
[2]
FUNCTION, AND SUBSTRATE SPECIFICITY.
PubMed=11732905; DOI=10.1021/bi0113723;
Meadows E.S., Khosla C.;
"In vitro reconstitution and analysis of the chain initiating enzymes
of the R1128 polyketide synthase.";
Biochemistry 40:14855-14861(2001).
[3]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
PubMed=12429097; DOI=10.1016/S0969-2126(02)00889-4;
Pan H., Tsai S.-C., Meadows E.S., Miercke L.J.W., Keatinge-Clay A.T.,
O'Connell J.D. III, Khosla C., Stroud R.M.;
"Crystal structure of the priming beta-ketosynthase from the R1128
polyketide biosynthetic pathway.";
Structure 10:1559-1568(2002).
-!- FUNCTION: Catalyzes the condensation reaction of fatty acid
synthesis by the addition to an acyl acceptor of two carbons from
malonyl-ACP. Catalyzes the first condensation reaction which
initiates fatty acid synthesis and may therefore play a role in
governing the total rate of fatty acid production. Possesses both
acetoacetyl-ACP synthase and acetyl transacylase activities. Has
some substrate preference for butyryl-CoA and can tolerate
branched substrates. Can also prime acyl-CoA. Its substrate
specificity determines the biosynthesis of branched-chain and/or
straight-chain of fatty acids. Involved in the biosynthesis of
R1128 polyketide. {ECO:0000269|PubMed:11732905}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + malonyl-[acyl-carrier-protein] =
acetoacetyl-[acyl-carrier-protein] + CoA + CO(2).
{ECO:0000255|HAMAP-Rule:MF_01815}.
-!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_01815}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01815,
ECO:0000269|PubMed:12429097}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815}.
-!- DOMAIN: The last Arg residue of the ACP-binding site is essential
for the weak association between ACP/AcpP and FabH.
{ECO:0000255|HAMAP-Rule:MF_01815}.
-!- SIMILARITY: Belongs to the FabH family. {ECO:0000255|HAMAP-
Rule:MF_01815, ECO:0000305}.
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EMBL; AF293442; AAG30195.1; -; Genomic_DNA.
PDB; 1MZJ; X-ray; 2.10 A; A/B=1-339.
PDBsum; 1MZJ; -.
ProteinModelPortal; Q9F6D4; -.
SMR; Q9F6D4; -.
DrugBank; DB01992; Coenzyme A.
UniPathway; UPA00094; -.
EvolutionaryTrace; Q9F6D4; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
GO; GO:0033818; F:beta-ketoacyl-acyl-carrier-protein synthase III activity; IEA:UniProtKB-EC.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.47.10; -; 2.
HAMAP; MF_01815; FabH; 1.
InterPro; IPR013751; ACP_syn_III.
InterPro; IPR013747; ACP_syn_III_C.
InterPro; IPR004655; FabH_synth.
InterPro; IPR016039; Thiolase-like.
Pfam; PF08545; ACP_syn_III; 1.
Pfam; PF08541; ACP_syn_III_C; 1.
SUPFAM; SSF53901; SSF53901; 1.
TIGRFAMs; TIGR00747; fabH; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Cytoplasm; Fatty acid biosynthesis;
Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
Multifunctional enzyme; Transferase.
CHAIN 1 339 3-oxoacyl-[acyl-carrier-protein] synthase
3.
/FTId=PRO_0000110489.
REGION 258 262 ACP-binding. {ECO:0000255|HAMAP-
Rule:MF_01815}.
ACT_SITE 121 121 {ECO:0000305|PubMed:12429097}.
ACT_SITE 257 257 {ECO:0000305|PubMed:12429097}.
ACT_SITE 288 288 {ECO:0000305|PubMed:12429097}.
STRAND 11 20 {ECO:0000244|PDB:1MZJ}.
STRAND 25 27 {ECO:0000244|PDB:1MZJ}.
HELIX 28 31 {ECO:0000244|PDB:1MZJ}.
TURN 32 34 {ECO:0000244|PDB:1MZJ}.
HELIX 39 46 {ECO:0000244|PDB:1MZJ}.
STRAND 49 52 {ECO:0000244|PDB:1MZJ}.
HELIX 60 75 {ECO:0000244|PDB:1MZJ}.
HELIX 79 81 {ECO:0000244|PDB:1MZJ}.
STRAND 84 88 {ECO:0000244|PDB:1MZJ}.
HELIX 99 107 {ECO:0000244|PDB:1MZJ}.
STRAND 113 118 {ECO:0000244|PDB:1MZJ}.
HELIX 120 122 {ECO:0000244|PDB:1MZJ}.
HELIX 123 137 {ECO:0000244|PDB:1MZJ}.
STRAND 143 150 {ECO:0000244|PDB:1MZJ}.
HELIX 151 154 {ECO:0000244|PDB:1MZJ}.
TURN 160 165 {ECO:0000244|PDB:1MZJ}.
STRAND 168 180 {ECO:0000244|PDB:1MZJ}.
STRAND 187 190 {ECO:0000244|PDB:1MZJ}.
HELIX 192 197 {ECO:0000244|PDB:1MZJ}.
STRAND 198 201 {ECO:0000244|PDB:1MZJ}.
HELIX 204 207 {ECO:0000244|PDB:1MZJ}.
STRAND 211 213 {ECO:0000244|PDB:1MZJ}.
STRAND 218 220 {ECO:0000244|PDB:1MZJ}.
HELIX 222 242 {ECO:0000244|PDB:1MZJ}.
TURN 243 245 {ECO:0000244|PDB:1MZJ}.
HELIX 248 250 {ECO:0000244|PDB:1MZJ}.
STRAND 252 256 {ECO:0000244|PDB:1MZJ}.
HELIX 261 271 {ECO:0000244|PDB:1MZJ}.
STRAND 277 279 {ECO:0000244|PDB:1MZJ}.
HELIX 283 286 {ECO:0000244|PDB:1MZJ}.
HELIX 292 304 {ECO:0000244|PDB:1MZJ}.
STRAND 305 307 {ECO:0000244|PDB:1MZJ}.
STRAND 312 319 {ECO:0000244|PDB:1MZJ}.
TURN 320 322 {ECO:0000244|PDB:1MZJ}.
STRAND 323 330 {ECO:0000244|PDB:1MZJ}.
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


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