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Comparing N515DRAFT_2873 N515DRAFT_2873 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)
4k6fB X-ray crystal structure of a putative acetoacetyl-coa reductase from burkholderia cenocepacia bound to the co-factor NADP
51% identity, 98% coverage: 3:245/247 of query aligns to 2:244/245 of 4k6fB
- active site: G12 (= G13), N102 (≠ H104), S138 (= S140), Y151 (= Y153), K155 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), Y32 (≠ D33), S33 (≠ L34), N36 (≠ R37), V58 (= V60), D59 (= D61), V60 (= V62), A87 (= A89), G88 (= G90), I89 (= I91)
5vt6A Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b complexed with NADP
51% identity, 99% coverage: 3:246/247 of query aligns to 2:245/245 of 5vt6A
- active site: G12 (= G13), D102 (≠ H104), S138 (= S140), Y151 (= Y153), K155 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), G11 (= G12), G12 (= G13), L13 (= L14), H32 (≠ L34), S33 (≠ P35), N36 (≠ A38), V58 (= V60), D59 (= D61), V60 (= V62), N86 (≠ A88), A87 (= A89), G88 (= G90), I89 (= I91), I136 (≠ L138), Y151 (= Y153), K155 (= K157), P181 (= P183), Y183 (= Y185), L184 (≠ C186), T186 (= T188)
5vmlA Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b with bound NADP
49% identity, 98% coverage: 3:245/247 of query aligns to 3:244/245 of 5vmlA
- active site: G13 (= G13), N111 (= N112), S139 (= S140), Y152 (= Y153), K156 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G9), G12 (= G12), G13 (= G13), I14 (≠ L14), C33 (≠ D33), G34 (≠ L34), R39 (≠ D39), G59 (≠ V60), N60 (≠ D61), V61 (= V62), N87 (≠ A88), G89 (= G90), I90 (= I91), S139 (= S140), Y152 (= Y153), K156 (= K157), P182 (= P183), G183 (= G184), I185 (≠ C186)
P14697 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) (see 2 papers)
47% identity, 98% coverage: 3:245/247 of query aligns to 4:245/246 of P14697
- GGI 13:15 (≠ GGL 12:14) binding
- G35 (≠ L34) binding
- R40 (≠ D39) binding
- Q47 (≠ A46) mutation to L: 2.4-fold increase in activity. 2-fold decrease in affinity for NADPH and 2.8-fold decrease in affinity for acetoacetyl-CoA.
- GNV 60:62 (≠ -DV 61:62) binding
- NAGIT 88:92 (≠ AAGIT 88:92) binding
- D94 (= D94) mutation to A: About 6% of wild-type activity.
- K99 (= K99) mutation to A: Nearly loss of activity.
- Q147 (= Q147) mutation to A: About 30% of wild-type activity.
- F148 (= F148) mutation to A: About 30% of wild-type activity.
- Q150 (= Q150) mutation to A: About 20% of wild-type activity.
- T173 (≠ R173) mutation to S: 3.5-fold increase in activity. 4-fold decrease in affinity for NADPH and 2.4-fold decrease in affinity for acetoacetyl-CoA.
- PGYI 183:186 (≠ PGYC 183:186) binding
- Y185 (= Y185) mutation to A: Nearly loss of activity.
- R195 (≠ P195) mutation to A: Nearly loss of activity.
3vzsB Crystal structure of phab from ralstonia eutropha in complex with acetoacetyl-coa and NADP (see paper)
47% identity, 98% coverage: 3:245/247 of query aligns to 7:248/249 of 3vzsB
- active site: N115 (= N112), S143 (= S140), Y156 (= Y153), K160 (= K157)
- binding acetoacetyl-coenzyme a: D97 (= D94), Q150 (= Q147), F151 (= F148), Q153 (= Q150), Y156 (= Y153), G187 (= G184), Y188 (= Y185), R198 (≠ P195)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G9), I18 (≠ L14), G38 (≠ L34), R43 (≠ D39), G63 (vs. gap), N64 (≠ D61), V65 (= V62), G93 (= G90), I94 (= I91), T95 (= T92), P186 (= P183), I189 (≠ C186), M193 (≠ L190), V194 (= V191)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
43% identity, 98% coverage: 3:245/247 of query aligns to 8:244/244 of 4nbuB
- active site: G18 (= G13), N111 (= N112), S139 (= S140), Q149 (= Q150), Y152 (= Y153), K156 (= K157)
- binding acetoacetyl-coenzyme a: D93 (= D94), K98 (= K99), S139 (= S140), N146 (≠ Q147), V147 (≠ F148), Q149 (= Q150), Y152 (= Y153), F184 (≠ Y185), M189 (≠ L190), K200 (≠ Q201)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G9), N17 (≠ G12), G18 (= G13), I19 (≠ L14), D38 (= D33), F39 (≠ L34), V59 (= V60), D60 (= D61), V61 (= V62), N87 (≠ A88), A88 (= A89), G89 (= G90), I90 (= I91), T137 (≠ L138), S139 (= S140), Y152 (= Y153), K156 (= K157), P182 (= P183), F184 (≠ Y185), T185 (≠ C186), T187 (= T188), M189 (≠ L190)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
43% identity, 98% coverage: 3:245/247 of query aligns to 6:243/244 of 6t77A
- active site: G16 (= G13), S138 (= S140), Y151 (= Y153)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G9), S14 (≠ I11), R15 (≠ G12), T37 (≠ D39), L58 (≠ V60), N59 (≠ D61), V60 (= V62), A87 (= A89), G88 (= G90), I89 (= I91)
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)
42% identity, 98% coverage: 3:245/247 of query aligns to 6:243/244 of P0AEK2
- GASR 12:15 (≠ GGIG 9:12) binding
- T37 (≠ R37) binding
- NV 59:60 (≠ DV 61:62) binding
- N86 (≠ A88) binding
- Y151 (= Y153) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (= YAAAK 153:157) binding
- A154 (= A156) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K157) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ C186) binding
- E233 (≠ A235) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
42% identity, 98% coverage: 3:245/247 of query aligns to 5:242/243 of 1q7bA
- active site: G15 (= G13), E101 (≠ H104), S137 (= S140), Q147 (= Q150), Y150 (= Y153), K154 (= K157)
- binding calcium ion: E232 (≠ A235), T233 (≠ N236)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G9), S13 (≠ I11), R14 (≠ G12), T36 (≠ R37), N58 (≠ D61), V59 (= V62), N85 (≠ A88), A86 (= A89), G87 (= G90), I88 (= I91), S137 (= S140), Y150 (= Y153), K154 (= K157), P180 (= P183), G181 (= G184), I183 (≠ C186)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
42% identity, 98% coverage: 3:245/247 of query aligns to 5:242/243 of 1q7cA
- active site: G15 (= G13), S137 (= S140), Q147 (= Q150), F150 (≠ Y153), K154 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G9), S13 (≠ I11), R14 (≠ G12), A35 (= A36), T36 (≠ R37), L57 (≠ V60), N58 (≠ D61), V59 (= V62), G87 (= G90), I88 (= I91)
4nbwA Crystal structure of fabg from plesiocystis pacifica (see paper)
44% identity, 97% coverage: 3:242/247 of query aligns to 2:248/253 of 4nbwA
- active site: G12 (= G13), S146 (= S140), Y159 (= Y153), K163 (= K157)
- binding nicotinamide-adenine-dinucleotide: G8 (= G9), N11 (≠ G12), G12 (= G13), I13 (≠ L14), D32 (= D33), L33 (= L34), V57 (= V60), D58 (= D61), V59 (= V62), N85 (≠ A88), A86 (= A89), G87 (= G90), S146 (= S140), Y159 (= Y153), K163 (= K157), I192 (≠ C186), T194 (= T188)
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)
42% identity, 98% coverage: 3:245/247 of query aligns to 9:246/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G9), S17 (≠ I11), R18 (≠ G12), I20 (≠ L14), T40 (≠ D39), N62 (≠ D61), V63 (= V62), N89 (≠ A88), A90 (= A89), I92 (= I91), V139 (≠ L138), S141 (= S140), Y154 (= Y153), K158 (= K157), P184 (= P183), G185 (= G184), I187 (≠ C186), T189 (= T188), M191 (≠ L190)
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)
41% identity, 98% coverage: 3:245/247 of query aligns to 6:243/244 of P0A2C9
- M125 (= M127) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A225) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (≠ A226) 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.
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
41% identity, 98% coverage: 3:245/247 of query aligns to 5:242/243 of 7emgB
4ag3A Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with NADPH at 1.8a resolution (see paper)
40% identity, 99% coverage: 3:246/247 of query aligns to 13:254/254 of 4ag3A
- active site: G23 (= G13), S148 (= S140), Y161 (= Y153), K165 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G9), S21 (≠ I11), R22 (≠ G12), G23 (= G13), I24 (≠ L14), T44 (≠ L34), L68 (≠ V60), D69 (= D61), V70 (= V62), N96 (≠ A88), A97 (= A89), I146 (≠ L138), S148 (= S140), Y161 (= Y153), K165 (= K157), P191 (= P183), G192 (= G184), F193 (≠ Y185), I194 (≠ C186), T196 (= T188), M198 (≠ L190), T199 (≠ V191)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
42% identity, 98% coverage: 3:245/247 of query aligns to 9:242/243 of 4i08A
- active site: G19 (= G13), N113 (= N112), S141 (= S140), Q151 (= Q150), Y154 (= Y153), K158 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G9), S17 (≠ I11), R18 (≠ G12), I20 (≠ L14), T40 (≠ D39), N62 (≠ D61), V63 (= V62), N89 (≠ A88), A90 (= A89), G140 (≠ S139), S141 (= S140), Y154 (= Y153), K158 (= K157), P184 (= P183), G185 (= G184), T189 (= T188)
4nbtA Crystal structure of fabg from acholeplasma laidlawii (see paper)
40% identity, 97% coverage: 3:242/247 of query aligns to 6:236/239 of 4nbtA
- active site: G16 (= G13), S132 (= S140), Y145 (= Y153), K149 (= K157)
- binding nicotinamide-adenine-dinucleotide: G12 (= G9), K15 (≠ G12), G16 (= G13), L17 (= L14), D36 (= D33), L37 (= L34), L52 (≠ V60), N53 (≠ D61), V54 (= V62), N80 (≠ A88), A81 (= A89), G82 (= G90), I130 (≠ L138), S132 (= S140), Y145 (= Y153), K149 (= K157), P177 (= P183), G178 (= G184), I180 (≠ C186), T182 (= T188)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
41% identity, 99% coverage: 1:245/247 of query aligns to 3:246/246 of 3osuA
6wprA Crystal structure of a putative 3-oxoacyl-acp reductase (fabg) with NADP(h) from acinetobacter baumannii (see paper)
38% identity, 99% coverage: 3:246/247 of query aligns to 6:244/244 of 6wprA
- active site: G16 (= G13), S138 (= S140), Y151 (= Y153)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G9), S14 (≠ I11), R15 (≠ G12), T37 (≠ D33), L58 (≠ V60), D59 (= D61), V60 (= V62), N86 (≠ A88), A87 (= A89), G88 (= G90), I89 (= I91), I136 (≠ L138), Y151 (= Y153), K155 (= K157), P181 (= P183)
6t62A Crystal structure of acinetobacter baumannii fabg in complex with NADPH at 1.8 a resolution (see paper)
38% identity, 99% coverage: 3:246/247 of query aligns to 6:244/244 of 6t62A
- active site: G16 (= G13), S138 (= S140), Y151 (= Y153)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G9), S14 (≠ I11), R15 (≠ G12), A36 (= A32), T37 (≠ D33), L58 (≠ V60), D59 (= D61), V60 (= V62), N86 (≠ A88), A87 (= A89), G88 (= G90), I89 (= I91), I136 (≠ L138), S137 (= S139), S138 (= S140), Y151 (= Y153), K155 (= K157), P181 (= P183), G182 (= G184), I184 (≠ C186), M188 (≠ L190)
Query Sequence
>N515DRAFT_2873 N515DRAFT_2873 3-oxoacyl-[acyl-carrier-protein] reductase
MTRIAIVTGGIGGLGTEICRQLALAGRQVIAADLPARADRVAAFQAELADLDGAVRFEPV
DVSDFASCSELIARVEAAHGRVDVLVNAAGITRDTTLRKMDPQHWQELMRVNLDGVFNMC
RHVVEGMSARGFGRIVNLSSVNGQTGQFGQTNYAAAKAGVHGFGMALARETARKGVTVNT
VSPGYCDTPLVARVPAEIRAQILEDIPVGRLGSPADIARAVCFLAADDAGYITGANLPVN
GGYFMSF
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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