SitesBLAST
Comparing WP_053939027.1 NCBI__GCF_001294205.1:WP_053939027.1 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)
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)
61% identity, 99% coverage: 3:244/244 of query aligns to 4:246/246 of P14697
- GGI 13:15 (= GGI 12:14) binding NADP(+)
- G35 (≠ Y33) binding NADP(+)
- R40 (= R38) binding NADP(+)
- Q47 (≠ D45) 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 (≠ CNV 58:60) binding NADP(+)
- NAGIT 88:92 (= NAGIT 86:90) binding NADP(+)
- D94 (= D92) mutation to A: About 6% of wild-type activity.
- K99 (= K97) mutation to A: Nearly loss of activity.
- Q147 (= Q145) mutation to A: About 30% of wild-type activity.
- F148 (= F146) mutation to A: About 30% of wild-type activity.
- Q150 (= Q148) mutation to A: About 20% of wild-type activity.
- T173 (≠ R171) 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 (= PGYI 181:184) binding NADP(+)
- Y185 (= Y183) mutation to A: Nearly loss of activity.
- R195 (≠ P193) mutation to A: Nearly loss of activity.
3vzsB Crystal structure of phab from ralstonia eutropha in complex with acetoacetyl-coa and NADP (see paper)
61% identity, 99% coverage: 3:244/244 of query aligns to 7:249/249 of 3vzsB
- active site: N115 (= N110), S143 (= S138), Y156 (= Y151), K160 (= K155)
- binding acetoacetyl-coenzyme a: D97 (= D92), Q150 (= Q145), F151 (= F146), Q153 (= Q148), Y156 (= Y151), G187 (= G182), Y188 (= Y183), R198 (≠ P193)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G9), I18 (= I14), G38 (≠ Y33), R43 (= R38), G63 (≠ C58), N64 (= N59), V65 (= V60), G93 (= G88), I94 (= I89), T95 (= T90), P186 (= P181), I189 (= I184), M193 (= M188), V194 (= V189)
4k6fB X-ray crystal structure of a putative acetoacetyl-coa reductase from burkholderia cenocepacia bound to the co-factor NADP
62% identity, 98% coverage: 3:242/244 of query aligns to 2:243/245 of 4k6fB
- active site: G12 (= G13), N102 (≠ D102), S138 (= S138), Y151 (= Y151), K155 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), Y32 (= Y33), S33 (= S34), N36 (≠ R35), V58 (≠ C58), D59 (≠ N59), V60 (= V60), A87 (= A87), G88 (= G88), I89 (= I89)
5vmlA Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b with bound NADP
60% identity, 99% coverage: 3:244/244 of query aligns to 3:245/245 of 5vmlA
- active site: G13 (= G13), N111 (= N110), S139 (= S138), Y152 (= Y151), K156 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G9), G12 (= G12), G13 (= G13), I14 (= I14), C33 (≠ T32), G34 (≠ Y33), R39 (= R38), G59 (≠ C58), N60 (= N59), V61 (= V60), N87 (= N86), G89 (= G88), I90 (= I89), S139 (= S138), Y152 (= Y151), K156 (= K155), P182 (= P181), G183 (= G182), I185 (= I184)
5vt6A Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b complexed with NADP
57% identity, 98% coverage: 3:242/244 of query aligns to 2:243/245 of 5vt6A
- active site: G12 (= G13), D102 (= D102), S138 (= S138), Y151 (= Y151), K155 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), G11 (= G12), G12 (= G13), L13 (≠ I14), H32 (≠ Y33), S33 (= S34), N36 (≠ T36), V58 (≠ C58), D59 (≠ N59), V60 (= V60), N86 (= N86), A87 (= A87), G88 (= G88), I89 (= I89), I136 (= I136), Y151 (= Y151), K155 (= K155), P181 (= P181), Y183 (= Y183), L184 (≠ I184), T186 (= T186)
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)
44% identity, 98% coverage: 3:242/244 of query aligns to 9:245/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G9), S17 (≠ M11), R18 (≠ G12), I20 (= I14), T40 (≠ Y33), N62 (= N59), V63 (= V60), N89 (= N86), A90 (= A87), I92 (= I89), V139 (≠ I136), S141 (= S138), Y154 (= Y151), K158 (= K155), P184 (= P181), G185 (= G182), I187 (= I184), T189 (= T186), M191 (= M188)
4ag3A Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with NADPH at 1.8a resolution (see paper)
43% identity, 98% coverage: 3:242/244 of query aligns to 13:252/254 of 4ag3A
- active site: G23 (= G13), S148 (= S138), Y161 (= Y151), K165 (= K155)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G9), S21 (≠ M11), R22 (≠ G12), G23 (= G13), I24 (= I14), T44 (≠ S34), L68 (≠ C58), D69 (≠ N59), V70 (= V60), N96 (= N86), A97 (= A87), I146 (= I136), S148 (= S138), Y161 (= Y151), K165 (= K155), P191 (= P181), G192 (= G182), F193 (≠ Y183), I194 (= I184), T196 (= T186), M198 (= M188), T199 (≠ V189)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
40% identity, 99% coverage: 1:242/244 of query aligns to 3:245/246 of 3osuA
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: 3:242/244 of query aligns to 6:242/244 of P0AEK2
- GASR 12:15 (≠ GGMG 9:12) binding NADP(+)
- T37 (≠ Y33) binding NADP(+)
- NV 59:60 (= NV 59:60) binding NADP(+)
- N86 (= N86) binding NADP(+)
- Y151 (= Y151) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YSAAK 151:155) binding NADP(+)
- A154 (= A154) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K155) mutation to A: Defect in the affinity for NADPH.
- I184 (= I184) binding NADP(+)
- E233 (≠ A233) 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: 3:242/244 of query aligns to 5:241/243 of 1q7bA
- active site: G15 (= G13), E101 (≠ D102), S137 (= S138), Q147 (= Q148), Y150 (= Y151), K154 (= K155)
- binding calcium ion: E232 (≠ A233), T233 (≠ N234)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G9), S13 (≠ M11), R14 (≠ G12), T36 (≠ Y33), N58 (= N59), V59 (= V60), N85 (= N86), A86 (= A87), G87 (= G88), I88 (= I89), S137 (= S138), Y150 (= Y151), K154 (= K155), P180 (= P181), G181 (= G182), I183 (= I184)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
44% identity, 98% coverage: 3:242/244 of query aligns to 9:241/243 of 4i08A
- active site: G19 (= G13), N113 (= N110), S141 (= S138), Q151 (= Q148), Y154 (= Y151), K158 (= K155)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G9), S17 (≠ M11), R18 (≠ G12), I20 (= I14), T40 (≠ Y33), N62 (= N59), V63 (= V60), N89 (= N86), A90 (= A87), G140 (≠ S137), S141 (= S138), Y154 (= Y151), K158 (= K155), P184 (= P181), G185 (= G182), T189 (= T186)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
42% identity, 98% coverage: 3:242/244 of query aligns to 6:242/244 of 6t77A
- active site: G16 (= G13), S138 (= S138), Y151 (= Y151)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G9), S14 (≠ M11), R15 (≠ G12), T37 (≠ Y33), L58 (≠ C58), N59 (= N59), V60 (= V60), A87 (= A87), G88 (= G88), I89 (= I89)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
42% identity, 98% coverage: 3:242/244 of query aligns to 5:241/243 of 1q7cA
- active site: G15 (= G13), S137 (= S138), Q147 (= Q148), F150 (≠ Y151), K154 (= K155)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G9), S13 (≠ M11), R14 (≠ G12), A35 (≠ T32), T36 (≠ Y33), L57 (≠ C58), N58 (= N59), V59 (= V60), G87 (= G88), I88 (= I89)
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)
42% identity, 98% coverage: 3:242/244 of query aligns to 6:242/244 of P0A2C9
- M125 (= M125) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A223) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S224) 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)
40% identity, 98% coverage: 3:242/244 of query aligns to 5:241/243 of 7emgB
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
39% identity, 99% coverage: 2:242/244 of query aligns to 1:238/239 of 3sj7A
- active site: G12 (= G13), S138 (= S138), Q148 (= Q148), Y151 (= Y151), K155 (= K155)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), S10 (≠ M11), R11 (≠ G12), I13 (= I14), N31 (≠ T32), Y32 (= Y33), A33 (≠ S34), G34 (≠ R35), S35 (≠ T36), A58 (≠ C58), N59 (= N59), V60 (= V60), N86 (= N86), A87 (= A87), T109 (= T109), S138 (= S138), Y151 (= Y151), K155 (= K155), P181 (= P181), G182 (= G182)
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
43% identity, 99% coverage: 3:243/244 of query aligns to 9:240/240 of P73826
- S134 (= S138) mutation to A: 12% enzymatic activity.
- Y147 (= Y151) mutation to A: No enzymatic activity.
- K151 (= K155) mutation to A: 5% enzymatic activity.
4bo4C Crystal structure of 3-oxoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with n-(2-methoxyphenyl)-3,4- dihydro-2h-quinoline-1-carboxamide at 2.7a resolution (see paper)
42% identity, 98% coverage: 3:242/244 of query aligns to 19:253/255 of 4bo4C