3-ketoacyl ACP synthase III, 3-ketoacyl acyl carrier protein synthase III, 3-ketoacyl carrier protein synthase III, 3-ketoacyl-(acyl carrier protein) synthase IIIA, 3-ketoacyl-(acyl carrier protein) synthase IIIB, 3-ketoacyl-ACP synthase III, 3-ketoacyl-acyl carrier protein synthase III, 3-ketoacyl-acyl-carrier protein synthase III, 3-oxoacyl-ACP synthase III, 3-oxoacyl-acyl carrier protein synthase III, 3-oxoacyl-[acyl-carrier-protein] synthase III, 3-oxoacyl:ACP synthase III, AbyA1, acetoacetyl-ACP synthase, acetyl-CoA:ACP transacylase, acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase, ACO synthase III, ACP synthase III, AknE2, AlnI, AsuC3, AsuC4, AviN, BenQ, beta-ketoacyl (acyl carrier protein) synthase III, beta-ketoacyl acyl carrier protein synthase III, beta-ketoacyl acyl-carrier protein synthase III, beta-ketoacyl-(ACP) synthase III, beta-ketoacyl-(acyl-carrier-protein) synthase III, beta-ketoacyl-ACP III, beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP synthase III, beta-ketoacyl-ACP synthase III-like protein, beta-ketoacyl-ACP-synthase III, beta-ketoacyl-acyl carrier protein (ACP) synthase III, beta-ketoacyl-acyl carrier protein synthase III, beta-ketoacyl-acyl carrier protein synthase-III, beta-ketoacyl-[acyl-carrier protein (ACP)] synthase III, beta-ketoacyl-[acyl-carrier-protein] synthase III, beta-ketoacyl:acyl carrier protein synthase III, beta-ketoacylacylcarrier protein synthase III, beta-ketobutyryl-ACP synthase, BomK, CalO4, CerJ, ChlB3, ChlB6, CorB, DarB, DpsC, ecFabH, ecKAS III, efFabH, EsmD1, EvrI, FabH, FabH1, FabH2, FabH3, FabHA, FabHB, fatty acid biosynthesis, enzyme H, fatty acid synthase type II condensing enzyme, FdmS, FrenI/FrnI, HedS, hiFabH, initiation ketosynthase, JcKAS III, KAS III, KAS III-like protein, KAS IIIA, KAS IIIB, KAS-III, KAS3a, KAS3b, KASIII, KijB, LstA, LstAB, LstB, mtFabH, MxnB, nmFabH, NphT7, NzsF, paFabH, PpyS, PqsBC, PqsD, PtmR, RedP, RevR, RkD, saFabH, SalQ/Orf12, short-chain condensing enzyme, spFabH, spyFabH, SsfN, TcsB, ThgI, TiaF, Tmn15, [acyl-carrier-protein] synthase III
the YpFabH monomer contains 10 alpha-helices and 14 beta-strands, the core motif of YpFabH contains a characteristic thiolase fold, monomer interaction analysis, dimer interface structure, and structure comparison with FabF, EC 2.3.1.179
three-dimensional structure analysis, the enzyme contains a large solvent-accessible channel in the dimer interface as well as two cis-peptides, cis-Pro88 and cis-Phe308, in two of the disordered loops, structural instability
three-dimensional structure analysis, the enzyme contains a large solvent-accessible channel in the dimer interface as well as two cis-peptides, cis-Pro88 and cis-Phe308, in two of the disordered loops, structural instability
structural details of the dimer interface region by means of computational modeling, including molecular dynamics simulations, detailed overview. Residues required for intersubunit stability are Phe87 and its complementary residues from the adjacent monomer, Thr190, Leu191, Pro192, Asn193. The active site is composed of a catalytic triad formed by residues, Cys112, His244, and Asn274. Residue Cys112 is involved in acetyl transfer, while His244 and Asn274 play an active role in decarboxylation. Residues His244 and Asn274 are present close to Cys112 in the long active site tunnel. Cysteine 112 lies on the bottom of the active-site tunnel, the entrance of which is flanked by residues Trp32 and Arg151