SitesBLAST
Comparing 3609684 FitnessBrowser__Dino:3609684 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)
5vmlA Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b with bound NADP
51% 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 (≠ K39), G59 (≠ W54), N60 (= N55), V61 (= V56), N87 (= N82), G89 (= G84), I90 (= I85), S139 (= S134), Y152 (= Y147), K156 (= K151), P182 (= P177), G183 (= G178), I185 (= I180)
4k6fB X-ray crystal structure of a putative acetoacetyl-coa reductase from burkholderia cenocepacia bound to the co-factor NADP
48% 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 (≠ N55), V60 (= V56), A87 (= A83), G88 (= G84), I89 (= I85)
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)
48% 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 (≠ K39) 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 (≠ -NV 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)
48% 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 (≠ K39), G63 (vs. gap), N64 (= N55), V65 (= V56), G93 (= G84), I94 (= I85), T95 (= T86), P186 (= P177), I189 (= I180), M193 (= M184), V194 (= V185)
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 (≠ D37), V58 (≠ W54), D59 (≠ N55), V60 (= V56), N86 (= N82), A87 (= A83), G88 (= G84), I89 (= I85), I136 (= I132), Y151 (= Y147), K155 (= K151), P181 (= P177), Y183 (= Y179), L184 (≠ I180), T186 (= T182)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
46% 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)
50% identity, 98% coverage: 3:237/240 of query aligns to 9:238/240 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)
46% 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 (= N55), 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)
44% identity, 100% coverage: 2:240/240 of query aligns to 4:243/243 of 7emgB
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
44% identity, 100% coverage: 2:240/240 of query aligns to 5:244/244 of 6t77A
- active site: G16 (= G13), S138 (= S134), Y151 (= Y147)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G9), S14 (= S11), R15 (= R12), T37 (≠ G35), L58 (≠ W54), N59 (= N55), V60 (= V56), A87 (= A83), G88 (= G84), I89 (= I85)
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)
44% identity, 100% coverage: 2:240/240 of query aligns to 5:244/244 of P0AEK2
- GASR 12:15 (≠ GGSR 9:12) binding
- T37 (≠ G35) binding
- NV 59:60 (= NV 55:56) 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)
44% identity, 100% coverage: 2:240/240 of query aligns to 4:243/243 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 (≠ G35), N58 (= N55), V59 (= V56), N85 (= N82), A86 (= A83), G87 (= G84), I88 (= I85), S137 (= S134), Y150 (= Y147), K154 (= K151), P180 (= P177), G181 (= G178), I183 (= I180)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
44% identity, 100% coverage: 2:240/240 of query aligns to 4:243/243 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 (= A34), T36 (≠ G35), L57 (≠ W54), N58 (= N55), V59 (= V56), G87 (= G84), I88 (= I85)
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)
45% identity, 97% coverage: 3:235/240 of query aligns to 24:249/255 of P71534
5ovkA Crystal structure maba bound to NADPH from m. Smegmatis (see paper)
45% identity, 97% coverage: 3:235/240 of query aligns to 11:236/242 of 5ovkA
5ovlA Crystal structure of maba bound to NADP+ from m. Smegmatis (see paper)
45% identity, 97% coverage: 3:235/240 of query aligns to 10:235/241 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 (≠ N55), V56 (= V56), N82 (= N82), A83 (= A83), I85 (= I85), T105 (= T105), I132 (= I132), S134 (= S134), Y147 (= Y147), K151 (= K151), P177 (= P177), G178 (= G178), I180 (= I180)
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)
44% identity, 100% coverage: 2:240/240 of query aligns to 5:244/244 of P0A2C9
- M125 (= M121) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A219) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S220) 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.
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, 100% coverage: 2:240/240 of query aligns to 8:247/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G9), S17 (= S11), R18 (= R12), I20 (= I14), T40 (≠ G35), N62 (= N55), 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)
42% identity, 97% coverage: 3:235/240 of query aligns to 16:241/247 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 (≠ NV 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)
43% identity, 97% coverage: 3:235/240 of query aligns to 8:233/239 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 (≠ N55), V54 (= V56), A81 (= A83), G82 (= G84)
Query Sequence
>3609684 FitnessBrowser__Dino:3609684
MGRVALVTGGSRGIGEAISKKLKADGYTVAATYAGNDEKAAAFTEATGIKTYKWNVADYE
SSKAGIAQVEADLGPIEVVVANAGITRDAPFHKMTPEQWHEVIDTNLTGVFNTIHPVWPG
MRERKFGRIIVISSINGQKGQFAQVNYAATKAGDLGIVKSLAQEGARAGITANAVCPGYI
ATEMVMAIPEKVRESIIAGIPVGRLGEPEEIARCVAFLASDDAGFISGSTISANGAQFFV
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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