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Comparing AZOBR_RS25545 FitnessBrowser__azobra:AZOBR_RS25545 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
61% identity, 99% coverage: 2:244/246 of query aligns to 1:243/245 of 5vmlA
- active site: G13 (= G14), N111 (= N112), S139 (= S140), Y152 (= Y153), K156 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G10), G12 (= G13), G13 (= G14), I14 (≠ L15), C33 (= C34), G34 (≠ L35), R39 (≠ P40), G59 (= G60), N60 (≠ D61), V61 (= V62), N87 (= N88), G89 (= G90), I90 (= I91), S139 (= S140), Y152 (= Y153), K156 (= K157), P182 (= P183), G183 (= G184), I185 (= I186)
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: 1:244/246 of query aligns to 1:244/246 of P14697
- GGI 13:15 (≠ GGL 13:15) binding
- G35 (≠ L35) binding
- R40 (≠ P40) binding
- Q47 (= Q47) 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 (≠ GDV 60:62) binding
- NAGIT 88:92 (= NAGIT 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 (≠ A148) mutation to A: About 30% of wild-type activity.
- Q150 (= Q150) mutation to A: About 20% of wild-type activity.
- T173 (= T173) 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 183:186) binding
- Y185 (= Y185) mutation to A: Nearly loss of activity.
- R195 (= R195) mutation to A: Nearly loss of activity.
3vzsB Crystal structure of phab from ralstonia eutropha in complex with acetoacetyl-coa and NADP (see paper)
60% identity, 99% coverage: 2:244/246 of query aligns to 5:247/249 of 3vzsB
- active site: N115 (= N112), S143 (= S140), Y156 (= Y153), K160 (= K157)
- binding acetoacetyl-coenzyme a: D97 (= D94), Q150 (= Q147), F151 (≠ A148), Q153 (= Q150), Y156 (= Y153), G187 (= G184), Y188 (= Y185), R198 (= R195)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G10), I18 (≠ L15), G38 (≠ L35), R43 (≠ P40), G63 (= G60), N64 (≠ D61), V65 (= V62), G93 (= G90), I94 (= I91), T95 (= T92), P186 (= P183), I189 (= I186), M193 (= M190), V194 (= V191)
4k6fB X-ray crystal structure of a putative acetoacetyl-coa reductase from burkholderia cenocepacia bound to the co-factor NADP
54% identity, 99% coverage: 3:246/246 of query aligns to 1:245/245 of 4k6fB
- active site: G12 (= G14), N102 (≠ Q104), S138 (= S140), Y151 (= Y153), K155 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G10), Y32 (≠ C34), S33 (≠ L35), N36 (≠ F38), V58 (≠ G60), D59 (= D61), V60 (= V62), A87 (= A89), G88 (= G90), I89 (= I91)
5vt6A Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b complexed with NADP
49% identity, 98% coverage: 3:244/246 of query aligns to 1:243/245 of 5vt6A
- active site: G12 (= G14), D102 (≠ Q104), S138 (= S140), Y151 (= Y153), K155 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G10), G11 (= G13), G12 (= G14), L13 (= L15), H32 (≠ C34), S33 (≠ L35), N36 (≠ F38), V58 (≠ G60), D59 (= D61), V60 (= V62), N86 (= N88), A87 (= A89), G88 (= G90), I89 (= I91), I136 (= I138), Y151 (= Y153), K155 (= K157), P181 (= P183), Y183 (= Y185), L184 (≠ I186), T186 (= T188)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
44% identity, 98% coverage: 4:243/246 of query aligns to 5:244/246 of 3osuA
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
46% identity, 98% coverage: 4:243/246 of query aligns to 5:240/243 of 7emgB
6wprA Crystal structure of a putative 3-oxoacyl-acp reductase (fabg) with NADP(h) from acinetobacter baumannii (see paper)
44% identity, 98% coverage: 3:243/246 of query aligns to 5:241/244 of 6wprA
- active site: G16 (= G14), S138 (= S140), Y151 (= Y153)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G10), S14 (≠ M12), R15 (≠ G13), T37 (≠ N33), L58 (≠ F55), D59 (= D61), V60 (= V62), N86 (= N88), A87 (= A89), G88 (= G90), I89 (= I91), I136 (= I138), Y151 (= Y153), K155 (= K157), P181 (= P183)
6t62A Crystal structure of acinetobacter baumannii fabg in complex with NADPH at 1.8 a resolution (see paper)
44% identity, 98% coverage: 3:243/246 of query aligns to 5:241/244 of 6t62A
- active site: G16 (= G14), S138 (= S140), Y151 (= Y153)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G10), S14 (≠ M12), R15 (≠ G13), A36 (= A32), T37 (≠ N33), L58 (≠ F55), D59 (= D61), V60 (= V62), N86 (= N88), A87 (= A89), G88 (= G90), I89 (= I91), I136 (= I138), S137 (= S139), S138 (= S140), Y151 (= Y153), K155 (= K157), P181 (= P183), G182 (= G184), I184 (= I186), M188 (= M190)
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
43% identity, 98% coverage: 4:243/246 of query aligns to 2:237/239 of 3sj7A
- active site: G12 (= G14), S138 (= S140), Q148 (= Q150), Y151 (= Y153), K155 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G10), S10 (≠ M12), R11 (≠ G13), I13 (≠ L15), N31 (= N33), Y32 (≠ C34), A33 (≠ L35), G34 (≠ P36), S35 (≠ N37), A58 (≠ G60), N59 (≠ D61), V60 (= V62), N86 (= N88), A87 (= A89), T109 (= T111), S138 (= S140), Y151 (= Y153), K155 (= K157), P181 (= P183), G182 (= G184)
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)
46% identity, 98% coverage: 4:243/246 of query aligns to 9:244/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G10), S17 (≠ M12), R18 (≠ G13), I20 (≠ L15), T40 (≠ N33), N62 (≠ D61), V63 (= V62), N89 (= N88), A90 (= A89), I92 (= I91), V139 (≠ I138), S141 (= S140), Y154 (= Y153), K158 (= K157), P184 (= P183), G185 (= G184), I187 (= I186), T189 (= T188), M191 (= M190)
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
47% identity, 98% coverage: 4:243/246 of query aligns to 5:240/243 of 1q7bA
- active site: G15 (= G14), E101 (≠ Q104), S137 (= S140), Q147 (= Q150), Y150 (= Y153), K154 (= K157)
- binding calcium ion: E232 (≠ S235), T233 (= T236)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G10), S13 (≠ M12), R14 (≠ G13), T36 (≠ N33), N58 (≠ D61), V59 (= V62), N85 (= N88), A86 (= A89), G87 (= G90), I88 (= I91), S137 (= S140), Y150 (= Y153), K154 (= K157), P180 (= P183), G181 (= G184), I183 (= I186)
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)
47% identity, 98% coverage: 4:243/246 of query aligns to 6:241/244 of P0AEK2
- GASR 12:15 (≠ GAMG 10:13) binding
- T37 (≠ N33) binding
- NV 59:60 (≠ DV 61:62) binding
- N86 (= N88) binding
- Y151 (= Y153) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YSAAK 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 (= I186) binding
- E233 (≠ S235) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
45% identity, 98% coverage: 4:243/246 of query aligns to 6:241/244 of 6t77A
- active site: G16 (= G14), S138 (= S140), Y151 (= Y153)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G10), S14 (≠ M12), R15 (≠ G13), T37 (≠ N33), L58 (≠ F55), N59 (≠ D61), V60 (= V62), A87 (= A89), G88 (= G90), I89 (= I91)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
47% identity, 98% coverage: 4:243/246 of query aligns to 5:240/243 of 1q7cA
- active site: G15 (= G14), S137 (= S140), Q147 (= Q150), F150 (≠ Y153), K154 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G10), S13 (≠ M12), R14 (≠ G13), A35 (= A32), T36 (≠ N33), L57 (≠ V57), N58 (≠ D61), V59 (= V62), G87 (= G90), I88 (= I91)
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)
46% identity, 98% coverage: 4:243/246 of query aligns to 6:241/244 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 (= S226) 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.
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
46% identity, 98% coverage: 4:243/246 of query aligns to 9:240/243 of 4i08A
- active site: G19 (= G14), N113 (= N112), S141 (= S140), Q151 (= Q150), Y154 (= Y153), K158 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G10), S17 (≠ M12), R18 (≠ G13), I20 (≠ L15), T40 (≠ N33), N62 (≠ D61), V63 (= V62), N89 (= N88), A90 (= A89), G140 (≠ S139), S141 (= S140), Y154 (= Y153), K158 (= K157), P184 (= P183), G185 (= G184), T189 (= T188)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
44% identity, 99% coverage: 1:243/246 of query aligns to 5:242/244 of 4nbuB
- active site: G18 (= G14), N111 (= N112), S139 (= S140), Q149 (= Q150), Y152 (= Y153), K156 (= K157)
- binding acetoacetyl-coenzyme a: D93 (= D94), K98 (= K99), S139 (= S140), N146 (≠ Q147), V147 (≠ A148), Q149 (= Q150), Y152 (= Y153), F184 (≠ Y185), M189 (= M190), K200 (≠ A201)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G10), N17 (≠ G13), G18 (= G14), I19 (≠ L15), D38 (≠ N37), F39 (= F38), V59 (≠ A58), D60 (= D61), V61 (= V62), N87 (= N88), A88 (= A89), G89 (= G90), I90 (= I91), T137 (≠ I138), S139 (= S140), Y152 (= Y153), K156 (= K157), P182 (= P183), F184 (≠ Y185), T185 (≠ I186), T187 (= T188), M189 (= M190)
4ag3A Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with NADPH at 1.8a resolution (see paper)
45% identity, 98% coverage: 4:243/246 of query aligns to 13:251/254 of 4ag3A
- active site: G23 (= G14), S148 (= S140), Y161 (= Y153), K165 (= K157)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G19 (= G10), S21 (≠ M12), R22 (≠ G13), G23 (= G14), I24 (≠ L15), T44 (≠ N33), L68 (≠ V57), D69 (= D61), V70 (= V62), N96 (= N88), A97 (= A89), I146 (= I138), S148 (= S140), Y161 (= Y153), K165 (= K157), P191 (= P183), G192 (= G184), F193 (≠ Y185), I194 (= I186), T196 (= T188), M198 (= M190), T199 (≠ V191)
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
46% identity, 98% coverage: 1:241/246 of query aligns to 6:236/240 of P73826
- S134 (= S140) mutation to A: 12% enzymatic activity.
- Y147 (= Y153) mutation to A: No enzymatic activity.
- K151 (= K157) mutation to A: 5% enzymatic activity.
Query Sequence
>AZOBR_RS25545 FitnessBrowser__azobra:AZOBR_RS25545
MSQKIALVTGAMGGLGTAICQALAKDGYIVAANCLPNFEPAAAWLGQQEALGFKFYVAEG
DVSDFESCKAMVAKIEADLGPVDILVNNAGITRDKFFAKMEKAQWDAVIATNLSSLFNVT
QQVSAKMAERGWGRIINISSVNGVKGQAGQTNYSAAKAGVIGFTKALAAELATKGVTVNA
IAPGYIGTDMVMAIREDIRQAITDSVPMKRLGRPDEIGGAVSYLASEIAGYVTGSTLNIN
GGLNYQ
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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