SitesBLAST
Comparing GFF328 PGA1_c03390 acetoacetyl-CoA reductase PhaB 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
47% identity, 99% coverage: 3:239/240 of query aligns to 2:244/245 of 4k6fB
- active site: G12 (= G13), N102 (≠ Q98), S138 (= S134), Y151 (= Y147), K155 (= K151)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), Y32 (= Y33), S33 (≠ A34), N36 (≠ D37), V58 (≠ W54), D59 (= D55), V60 (= V56), A87 (= A83), G88 (= G84), I89 (= I85)
5vt6A Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b complexed with NADP
47% identity, 97% coverage: 3:235/240 of query aligns to 2:240/245 of 5vt6A
- active site: G12 (= G13), D102 (≠ Q98), S138 (= S134), Y151 (= Y147), K155 (= K151)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), G11 (≠ R12), G12 (= G13), L13 (≠ I14), H32 (≠ Y33), S33 (≠ A34), N36 (= N36), V58 (≠ W54), D59 (= D55), V60 (= V56), N86 (= N82), A87 (= A83), G88 (= G84), I89 (= I85), I136 (= I132), Y151 (= Y147), K155 (= K151), P181 (= P177), Y183 (= Y179), L184 (≠ I180), T186 (= T182)
5vmlA Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b with bound NADP
48% identity, 97% coverage: 3:235/240 of query aligns to 3:240/245 of 5vmlA
- active site: G13 (= G13), N111 (= N106), S139 (= S134), Y152 (= Y147), K156 (= K151)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G9), G12 (≠ R12), G13 (= G13), I14 (= I14), C33 (≠ Y33), G34 (≠ A34), R39 (≠ A39), G59 (≠ W54), N60 (≠ D55), V61 (= V56), N87 (= N82), G89 (= G84), I90 (= I85), S139 (= S134), Y152 (= Y147), K156 (= K151), P182 (= P177), G183 (= G178), I185 (= I180)
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)
45% identity, 97% coverage: 3:235/240 of query aligns to 4:241/246 of P14697
- GGI 13:15 (≠ RGI 12:14) binding
- G35 (≠ A34) binding
- R40 (≠ A39) binding
- Q47 (≠ E46) 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 55:56) binding
- NAGIT 88:92 (= NAGIT 82:86) binding
- D94 (= D88) mutation to A: About 6% of wild-type activity.
- K99 (= K93) mutation to A: Nearly loss of activity.
- Q147 (= Q141) mutation to A: About 30% of wild-type activity.
- F148 (= F142) mutation to A: About 30% of wild-type activity.
- Q150 (= Q144) mutation to A: About 20% of wild-type activity.
- T173 (≠ R167) 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 177:180) binding
- Y185 (= Y179) mutation to A: Nearly loss of activity.
- R195 (≠ P189) mutation to A: Nearly loss of activity.
3vzsB Crystal structure of phab from ralstonia eutropha in complex with acetoacetyl-coa and NADP (see paper)
45% identity, 97% coverage: 3:235/240 of query aligns to 7:244/249 of 3vzsB
- active site: N115 (= N106), S143 (= S134), Y156 (= Y147), K160 (= K151)
- binding acetoacetyl-coenzyme a: D97 (= D88), Q150 (= Q141), F151 (= F142), Q153 (= Q144), Y156 (= Y147), G187 (= G178), Y188 (= Y179), R198 (≠ P189)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G9), I18 (= I14), G38 (≠ A34), R43 (≠ A39), G63 (vs. gap), N64 (≠ D55), V65 (= V56), G93 (= G84), I94 (= I85), T95 (= T86), P186 (= P177), I189 (= I180), M193 (= M184), V194 (= V185)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
43% identity, 100% coverage: 1:239/240 of query aligns to 3:246/246 of 3osuA
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
46% identity, 97% coverage: 6:237/240 of query aligns to 12:238/240 of P73826
- S134 (= S134) mutation to A: 12% enzymatic activity.
- Y147 (= Y147) mutation to A: No enzymatic activity.
- K151 (= K151) mutation to A: 5% enzymatic activity.
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
42% identity, 99% coverage: 3:239/240 of query aligns to 2:239/239 of 3sj7A
- active site: G12 (= G13), S138 (= S134), Q148 (= Q144), Y151 (= Y147), K155 (= K151)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), S10 (= S11), R11 (= R12), I13 (= I14), N31 (≠ T32), Y32 (= Y33), A33 (= A34), G34 (= G35), S35 (≠ N36), A58 (≠ W54), N59 (≠ D55), V60 (= V56), N86 (= N82), A87 (= A83), T109 (= T105), S138 (= S134), Y151 (= Y147), K155 (= K151), P181 (= P177), G182 (= G178)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
42% identity, 98% coverage: 6:240/240 of query aligns to 8:243/243 of 7emgB
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)
43% identity, 98% coverage: 5:240/240 of query aligns to 8:244/244 of P0AEK2
- GASR 12:15 (≠ GGSR 9:12) binding
- T37 (≠ A34) binding
- NV 59:60 (≠ YK 52:53) binding
- N86 (= N82) binding
- Y151 (= Y147) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YAATK 147:151) binding
- A154 (≠ T150) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K151) mutation to A: Defect in the affinity for NADPH.
- I184 (= I180) binding
- E233 (≠ S229) 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)
43% identity, 98% coverage: 5:240/240 of query aligns to 7:243/243 of 1q7bA
- active site: G15 (= G13), E101 (≠ Q98), S137 (= S134), Q147 (= Q144), Y150 (= Y147), K154 (= K151)
- binding calcium ion: E232 (≠ S229), T233 (= T230)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G9), S13 (= S11), R14 (= R12), T36 (≠ A34), N58 (≠ Y52), V59 (≠ K53), N85 (= N82), A86 (= A83), G87 (= G84), I88 (= I85), S137 (= S134), Y150 (= Y147), K154 (= K151), P180 (= P177), G181 (= G178), I183 (= I180)
5ovkA Crystal structure maba bound to NADPH from m. Smegmatis (see paper)
43% identity, 98% coverage: 1:235/240 of query aligns to 9:236/242 of 5ovkA
5ovlA Crystal structure of maba bound to NADP+ from m. Smegmatis (see paper)
43% identity, 98% coverage: 1:235/240 of query aligns to 8:235/241 of 5ovlA
- active site: G20 (= G13), S134 (= S134), Y147 (= Y147), L154 (≠ D154)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G16 (= G9), N18 (≠ S11), R19 (= R12), G20 (= G13), I21 (= I14), R41 (≠ A34), D55 (≠ Y52), V56 (≠ K53), N82 (= N82), A83 (= A83), I85 (= I85), T105 (= T105), I132 (= I132), S134 (= S134), Y147 (= Y147), K151 (= K151), P177 (= P177), G178 (= G178), I180 (= I180)
P71534 3-oxoacyl-[acyl-carrier-protein] reductase MabA; 3-ketoacyl-acyl carrier protein reductase; Acetoacetyl-CoA reductase; Beta-ketoacyl-ACP reductase; Beta-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100; EC 1.1.1.36 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
43% identity, 98% coverage: 1:235/240 of query aligns to 22:249/255 of P71534
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
43% identity, 98% coverage: 5:240/240 of query aligns to 7:243/243 of 1q7cA
- active site: G15 (= G13), S137 (= S134), Q147 (= Q144), F150 (≠ Y147), K154 (= K151)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G9), S13 (= S11), R14 (= R12), A35 (≠ Y33), T36 (≠ A34), L57 (≠ T51), N58 (≠ Y52), V59 (≠ K53), G87 (= G84), I88 (= I85)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
43% identity, 96% coverage: 5:235/240 of query aligns to 10:240/244 of 4nbuB
- active site: G18 (= G13), N111 (= N106), S139 (= S134), Q149 (= Q144), Y152 (= Y147), K156 (= K151)
- binding acetoacetyl-coenzyme a: D93 (= D88), K98 (= K93), S139 (= S134), N146 (≠ Q141), V147 (≠ F142), Q149 (= Q144), Y152 (= Y147), F184 (≠ Y179), M189 (= M184), K200 (≠ S195)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G9), N17 (≠ R12), G18 (= G13), I19 (= I14), D38 (≠ G35), F39 (≠ N36), V59 (≠ W54), D60 (= D55), V61 (= V56), N87 (= N82), A88 (= A83), G89 (= G84), I90 (= I85), T137 (≠ I132), S139 (= S134), Y152 (= Y147), K156 (= K151), P182 (= P177), F184 (≠ Y179), T185 (≠ I180), T187 (= T182), M189 (= M184)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
43% identity, 98% coverage: 5:240/240 of query aligns to 8:244/244 of 6t77A
- active site: G16 (= G13), S138 (= S134), Y151 (= Y147)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G9), S14 (= S11), R15 (= R12), T37 (= T32), L58 (≠ T51), N59 (≠ Y52), V60 (≠ K53), A87 (= A83), G88 (= G84), I89 (= I85)
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)
40% identity, 98% coverage: 5:240/240 of query aligns to 11:247/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G9), S17 (= S11), R18 (= R12), I20 (= I14), T40 (= T32), N62 (≠ D55), V63 (= V56), N89 (= N82), A90 (= A83), I92 (= I85), V139 (≠ I132), S141 (= S134), Y154 (= Y147), K158 (= K151), P184 (= P177), G185 (= G178), I187 (= I180), T189 (= T182), M191 (= M184)
P9WGT3 3-oxoacyl-[acyl-carrier-protein] reductase MabA; 3-ketoacyl reductase; 3-ketoacyl-acyl carrier protein reductase; Acetoacetyl-CoA reductase; Beta-ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; Mycolic acid biosynthesis A; EC 1.1.1.100; EC 1.1.1.36 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 7 papers)
41% identity, 98% coverage: 1:235/240 of query aligns to 14:241/247 of P9WGT3
- T21 (= T8) modified: Phosphothreonine; mutation to A: Slight decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-114 and A-191.
- RGI 25:27 (= RGI 12:14) binding
- R47 (≠ A34) binding
- C60 (≠ W54) mutation to V: Displays a lower activity than the wild-type and a slightly decreased affinity for the cofactor. Retains 84% of activity; when associated with L-144. Totally inactive; when associated with A-139 and L-144.
- DV 61:62 (= DV 55:56) binding
- G90 (= G84) binding
- T114 (= T108) modified: Phosphothreonine; mutation to A: Slight decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-21 and A-191.
- G139 (≠ S133) mutation to A: Complete protein inactivation and freezes the catalytic site into its closed form. Totally inactive; when associated with V-60 and L-144.
- S140 (= S134) mutation to A: Loss of activity. Can still bind NADPH.; mutation to T: Loss of activity. Impaired NADPH binding.
- S144 (≠ Q138) mutation to L: Stabilizes the catalytic loop in its open active form. Retains 84% of activity; when associated with V-60. Totally inactive; when associated with V-60 and A-139.
- Y185 (= Y179) mutation to L: 70% decrease in activity with acetoacetyl-CoA as substrate. Does not affect NADP binding.
- T191 (≠ V185) modified: Phosphothreonine; mutation to A: Retains 22% of wild-type reductase activity. Strong decrease in phosphorylation by PknB. Lack of phosphorylation by PknB; when associated with A-21 and A-114.; mutation to D: Phosphomimetic mutant that retains less than 10% of wild-type reductase activity. Impaired NADPH binding. Overproduction of the mutant leads to a significant inhibition of de novo biosynthesis of mycolic acids.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1uznA Maba from mycobacterium tuberculosis (see paper)
41% identity, 98% coverage: 1:235/240 of query aligns to 6:233/239 of 1uznA
- active site: G18 (= G13), S132 (= S134), Y145 (= Y147), K149 (= K151)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G14 (= G9), N16 (≠ S11), R17 (= R12), I19 (= I14), R39 (≠ A34), D53 (= D55), V54 (= V56), A81 (= A83), G82 (= G84)
Query Sequence
>GFF328 PGA1_c03390 acetoacetyl-CoA reductase PhaB
MARNALVTGGSRGIGAAISQALKAEGYTVAATYAGNDEAAAKFTNETGIKTYKWDVASYE
DSAAGIAKVEADIGPIDIVVANAGITRDAPFHKMTLEQWQQVIDTNLTGVFNTVHPIWPG
MRERKFGRVIVISSINGQKGQFAQVNYAATKAGDLGIVKSLAQEGARAGITANAICPGYI
ATEMVMAVPEKVRESIIGQIPAGRLGEPEEIARCVAFLASEDSGFINGSTISANGAQFFV
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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