SitesBLAST
Comparing 206645 3-oxoacyl-(acyl-carrier-protein) reductase to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
53% identity, 94% coverage: 15:258/259 of query aligns to 2:245/246 of 3osuA
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
53% identity, 93% coverage: 17:258/259 of query aligns to 1:238/239 of 3sj7A
- active site: G12 (= G28), S138 (= S154), Q148 (= Q164), Y151 (= Y167), K155 (= K171)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G24), S10 (= S26), R11 (= R27), I13 (= I29), N31 (≠ T47), Y32 (= Y48), A33 (≠ V49), G34 (≠ S50), S35 (≠ K51), A58 (≠ L74), N59 (≠ D75), V60 (= V76), N86 (= N102), A87 (= A103), T109 (≠ V125), S138 (= S154), Y151 (= Y167), K155 (= K171), P181 (= P197), G182 (= G198)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
52% identity, 92% coverage: 20:257/259 of query aligns to 8:245/247 of 4jroC
- active site: G16 (= G28), S142 (= S154), Q152 (= Q164), Y155 (= Y167), K159 (= K171)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G24), S14 (= S26), R15 (= R27), G16 (= G28), I17 (= I29), N35 (≠ T47), Y36 (= Y48), N37 (≠ V49), G38 (≠ S50), S39 (≠ K51), N63 (≠ D75), V64 (= V76), N90 (= N102), A91 (= A103), I93 (= I105), I113 (≠ V125), S142 (= S154), Y155 (= Y167), K159 (= K171), P185 (= P197), I188 (= I200), T190 (= T202)
1edoA The x-ray structure of beta-keto acyl carrier protein reductase from brassica napus complexed with NADP+ (see paper)
50% identity, 93% coverage: 17:257/259 of query aligns to 1:242/244 of 1edoA
- active site: G12 (= G28), S138 (= S154), Y151 (= Y167), K155 (= K171)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G24), S10 (= S26), R11 (= R27), I13 (= I29), N31 (≠ T47), Y32 (= Y48), A33 (≠ V49), R34 (≠ S50), S35 (≠ K51), D59 (= D75), V60 (= V76), N86 (= N102), A87 (= A103), S138 (= S154), Y151 (= Y167), K155 (= K171), P181 (= P197), G182 (= G198), I184 (= I200), S186 (≠ T202), M188 (= M204)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
51% identity, 93% coverage: 20:259/259 of query aligns to 8:243/244 of 6t77A
- active site: G16 (= G28), S138 (= S154), Y151 (= Y167)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G24), S14 (= S26), R15 (= R27), T37 (≠ V49), L58 (= L74), N59 (≠ D75), V60 (= V76), A87 (= A103), G88 (= G104), I89 (= I105)
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
51% identity, 93% coverage: 20:259/259 of query aligns to 7:242/243 of 1q7bA
- active site: G15 (= G28), E101 (≠ D118), S137 (= S154), Q147 (= Q164), Y150 (= Y167), K154 (= K171)
- binding calcium ion: E232 (≠ Q249), T233 (≠ V250)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G24), S13 (= S26), R14 (= R27), T36 (≠ V49), N58 (≠ D75), V59 (= V76), N85 (= N102), A86 (= A103), G87 (= G104), I88 (= I105), S137 (= S154), Y150 (= Y167), K154 (= K171), P180 (= P197), G181 (= G198), I183 (= I200)
P0AEK2 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Escherichia coli (strain K12) (see 2 papers)
51% identity, 93% coverage: 20:259/259 of query aligns to 8:243/244 of P0AEK2
- GASR 12:15 (≠ GGSR 24:27) binding
- T37 (≠ V49) binding
- NV 59:60 (≠ DV 75:76) binding
- N86 (= N102) binding
- Y151 (= Y167) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YCAAK 167:171) binding
- A154 (= A170) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K171) mutation to A: Defect in the affinity for NADPH.
- I184 (= I200) binding
- E233 (≠ Q249) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
P73574 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
53% identity, 95% coverage: 13:257/259 of query aligns to 1:244/247 of P73574
- A14 (≠ G25) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ A162) mutation to F: 2.7-fold increase in activity on acetoacetyl-CoA.; mutation to V: 5.7-fold increase in activity on acetoacetyl-CoA.
- K160 (= K171) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (= F199) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ P209) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
P0A2C9 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
51% identity, 95% coverage: 13:258/259 of query aligns to 1:242/244 of P0A2C9
- M125 (= M141) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A239) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S240) mutation to F: Distorts the local conformation and prevent stacking around Phe-221. The S224F mutation would additionally disrupt the hydrogen bond formed between Ser-224 and Glu-226.
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
50% identity, 93% coverage: 20:259/259 of query aligns to 7:242/243 of 1q7cA
- active site: G15 (= G28), S137 (= S154), Q147 (= Q164), F150 (≠ Y167), K154 (= K171)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G24), S13 (= S26), R14 (= R27), A35 (≠ Y48), T36 (≠ V49), L57 (= L74), N58 (≠ D75), V59 (= V76), G87 (= G104), I88 (= I105)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
51% identity, 92% coverage: 21:258/259 of query aligns to 8:241/243 of 7emgB
4dmmB 3-oxoacyl-[acyl-carrier-protein] reductase from synechococcus elongatus pcc 7942 in complex with NADP
56% identity, 92% coverage: 20:257/259 of query aligns to 8:237/240 of 4dmmB
- active site: G16 (= G28), S142 (= S154), Q152 (= Q164), Y155 (= Y167), K159 (= K171)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G24), S14 (= S26), R15 (= R27), G16 (= G28), I17 (= I29), A37 (≠ V49), S38 (= S50), S39 (≠ K51), A62 (≠ L74), D63 (= D75), V64 (= V76), N90 (= N102), A91 (= A103), L113 (≠ V125), I140 (= I152), S142 (= S154), Y155 (= Y167), K159 (= K171), P185 (= P197), G186 (= G198), I188 (= I200), T190 (= T202), M192 (= M204)
3op4A Crystal structure of putative 3-ketoacyl-(acyl-carrier-protein) reductase from vibrio cholerae o1 biovar eltor str. N16961 in complex with NADP+ (see paper)
51% identity, 93% coverage: 20:259/259 of query aligns to 11:246/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G24), S17 (= S26), R18 (= R27), I20 (= I29), T40 (≠ V49), N62 (≠ D75), V63 (= V76), N89 (= N102), A90 (= A103), I92 (= I105), V139 (≠ I152), S141 (= S154), Y154 (= Y167), K158 (= K171), P184 (= P197), G185 (= G198), I187 (= I200), T189 (= T202), M191 (= M204)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
50% identity, 93% coverage: 20:259/259 of query aligns to 11:242/243 of 4i08A
- active site: G19 (= G28), N113 (= N126), S141 (= S154), Q151 (= Q164), Y154 (= Y167), K158 (= K171)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G24), S17 (= S26), R18 (= R27), I20 (= I29), T40 (≠ V49), N62 (≠ D75), V63 (= V76), N89 (= N102), A90 (= A103), G140 (≠ T153), S141 (= S154), Y154 (= Y167), K158 (= K171), P184 (= P197), G185 (= G198), T189 (= T202)
8jfgA Crystal structure of 3-oxoacyl-acp reductase fabg in complex with NADP+ and 3-keto-octanoyl-acp from helicobacter pylori (see paper)
45% identity, 93% coverage: 18:258/259 of query aligns to 7:247/248 of 8jfgA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G24), K16 (≠ R27), I18 (= I29), R38 (≠ V49), A65 (≠ V76), N91 (= N102), A92 (= A103), G93 (= G104), A142 (≠ T153), S143 (= S154), Y156 (= Y167), K160 (= K171), P186 (= P197), I189 (= I200), T191 (= T202), M193 (= M204), N194 (≠ T205)
- binding ~{S}-[2-[3-[[(2~{S})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] 3-oxidanylideneoctanethioate: D97 (= D108), S143 (= S154), I145 (≠ V156), M151 (≠ A162), G152 (= G163), Q153 (= Q164), Y156 (= Y167), G187 (= G198), F188 (= F199), Y205 (= Y216)
4ag3A Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with NADPH at 1.8a resolution (see paper)
49% identity, 95% coverage: 13:259/259 of query aligns to 8:253/254 of 4ag3A
- active site: G23 (= G28), S148 (= S154), Y161 (= Y167), K165 (= K171)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G24), S21 (= S26), R22 (= R27), G23 (= G28), I24 (= I29), T44 (≠ V49), L68 (= L74), D69 (= D75), V70 (= V76), N96 (= N102), A97 (= A103), I146 (= I152), S148 (= S154), Y161 (= Y167), K165 (= K171), P191 (= P197), G192 (= G198), F193 (= F199), I194 (= I200), T196 (= T202), M198 (= M204), T199 (= T205)
4iinA Crystal structure of a putative 3-oxoacyl-[acyl-carrier protein]reductase from helicobacter pylori 26695 complexed with NAD+
44% identity, 92% coverage: 21:258/259 of query aligns to 10:235/236 of 4iinA
- active site: G17 (= G28), S143 (= S154), Y156 (= Y167), K160 (= K171)
- binding nicotinamide-adenine-dinucleotide: G13 (= G24), G17 (= G28), I18 (= I29), N36 (≠ T47), R38 (≠ V49), A65 (≠ V76), N91 (= N102), A92 (= A103), G93 (= G104), V141 (≠ I152), S143 (= S154), Y156 (= Y167), K160 (= K171), P186 (= P197)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
44% identity, 95% coverage: 13:257/259 of query aligns to 4:245/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G24), R18 (= R27), G19 (= G28), I20 (= I29), D39 (≠ S50), R40 (≠ K51), C63 (≠ L74), I65 (≠ V76), N91 (= N102), G93 (= G104), I94 (= I105), V114 (= V125), Y155 (= Y167), K159 (= K171), I188 (= I200), T190 (= T202), T193 (= T205)
6wprA Crystal structure of a putative 3-oxoacyl-acp reductase (fabg) with NADP(h) from acinetobacter baumannii (see paper)
46% identity, 95% coverage: 13:259/259 of query aligns to 1:243/244 of 6wprA
- active site: G16 (= G28), S138 (= S154), Y151 (= Y167)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G24), S14 (= S26), R15 (= R27), T37 (≠ V49), L58 (= L74), D59 (= D75), V60 (= V76), N86 (= N102), A87 (= A103), G88 (= G104), I89 (= I105), I136 (= I152), Y151 (= Y167), K155 (= K171), P181 (= P197)
6t62A Crystal structure of acinetobacter baumannii fabg in complex with NADPH at 1.8 a resolution (see paper)
46% identity, 95% coverage: 13:259/259 of query aligns to 1:243/244 of 6t62A
- active site: G16 (= G28), S138 (= S154), Y151 (= Y167)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G24), S14 (= S26), R15 (= R27), A36 (≠ Y48), T37 (≠ V49), L58 (= L74), D59 (= D75), V60 (= V76), N86 (= N102), A87 (= A103), G88 (= G104), I89 (= I105), I136 (= I152), S137 (≠ T153), S138 (= S154), Y151 (= Y167), K155 (= K171), P181 (= P197), G182 (= G198), I184 (= I200), M188 (= M204)
Query Sequence
>206645 3-oxoacyl-(acyl-carrier-protein) reductase
MPFVKPQNARFVMSELTPTAIVTGGSRGIGKAVAETLARAGLQVFLTYVSKPDEAEAVAA
GIRDAGGSATAFRLDVSDAAAVAAFFQSEIKDKVRLDVLVNNAGITKDGLIMRMKDEDFE
RVLDVNLCGAFTCLREASKLMTRQRLGRIINITSVVGQMGNAGQANYCAAKAGLIGLTKS
AAKELAARNVTVNAVAPGFIETDMTAGLPEEVRKAYVEAIPLRRLGSAQDIADAVAFLAS
ERASYITGQVLAVNGGMYC
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory