SitesBLAST
Comparing HSERO_RS02925 FitnessBrowser__HerbieS:HSERO_RS02925 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)
6d9yB Crystal structure of a short chain dehydrogenase/reductase sdr from burkholderia phymatum with partially occupied NAD
45% identity, 97% coverage: 9:244/244 of query aligns to 6:251/251 of 6d9yB
- active site: G20 (= G23), S145 (= S138), Y158 (= Y151)
- binding nicotinamide-adenine-dinucleotide: G16 (= G19), R19 (≠ G22), G20 (= G23), D40 (= D43), L41 (≠ Q44), V64 (≠ I57), D65 (= D58), Q66 (≠ I59), A93 (= A86), S145 (= S138), Y158 (= Y151), K162 (= K155), P188 (= P181), A189 (= A182), A190 (= A183), A191 (≠ V184), T193 (= T186)
5h5xC Crystal structure of nadh bound carbonyl reductase from streptomyces coelicolor
40% identity, 92% coverage: 9:233/244 of query aligns to 10:246/257 of 5h5xC
- active site: G24 (= G23), S151 (= S138), Y164 (= Y151), K168 (= K155)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G20 (= G19), S23 (≠ G22), G24 (= G23), I25 (= I24), D44 (= D43), F45 (≠ Q44), L69 (≠ I57), D70 (= D58), N97 (= N85), A98 (= A86), Y164 (= Y151), K168 (= K155), P194 (= P181), G195 (≠ A182), I197 (≠ V184), T199 (= T186)
1zemA Crystal structure of NAD+-bound xylitol dehydrogenase (see paper)
33% identity, 95% coverage: 10:240/244 of query aligns to 3:260/260 of 1zemA
- active site: N16 (≠ G23), S142 (= S138), Y155 (= Y151), K159 (= K155), D212 (≠ M192)
- binding nicotinamide-adenine-dinucleotide: G12 (= G19), G15 (= G22), N16 (≠ G23), I17 (= I24), D36 (= D43), M37 (≠ Q44), D62 (= D58), V63 (≠ I59), N89 (= N85), A90 (= A86), G91 (= G87), T140 (≠ I136), S142 (= S138), Y155 (= Y151), K159 (= K155), P185 (= P181), M188 (vs. gap)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
33% identity, 94% coverage: 12:240/244 of query aligns to 7:241/244 of 4nbuB
- active site: G18 (= G23), N111 (= N110), S139 (= S138), Q149 (≠ A148), Y152 (= Y151), K156 (= K155)
- binding acetoacetyl-coenzyme a: D93 (≠ P91), K98 (≠ E97), S139 (= S138), N146 (≠ T145), V147 (≠ P146), Q149 (≠ A148), Y152 (= Y151), F184 (≠ A183), M189 (≠ L188), K200 (≠ T199)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G19), N17 (≠ G22), G18 (= G23), I19 (= I24), D38 (= D43), F39 (≠ Q44), V59 (≠ I57), D60 (= D58), V61 (≠ I59), N87 (= N85), A88 (= A86), G89 (= G87), I90 (≠ Y88), T137 (≠ I136), S139 (= S138), Y152 (= Y151), K156 (= K155), P182 (= P181), F184 (≠ A183), T185 (≠ V184), T187 (= T186), M189 (≠ L188)
5vmlA Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b with bound NADP
35% identity, 93% coverage: 14:240/244 of query aligns to 4:241/245 of 5vmlA
- active site: G13 (= G23), N111 (= N110), S139 (= S138), Y152 (= Y151), K156 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G19), G12 (= G22), G13 (= G23), I14 (= I24), C33 (vs. gap), G34 (vs. gap), R39 (vs. gap), G59 (≠ S56), N60 (≠ D58), V61 (≠ I59), N87 (= N85), G89 (= G87), I90 (≠ Y88), S139 (= S138), Y152 (= Y151), K156 (= K155), P182 (= P181), G183 (≠ A182), I185 (≠ V184)
5vt6A Crystal structure of acetoacetyl-coa reductase from burkholderia pseudomallei 1710b complexed with NADP
36% identity, 93% coverage: 14:240/244 of query aligns to 3:241/245 of 5vt6A
- active site: G12 (= G23), D102 (≠ E102), S138 (= S138), Y151 (= Y151), K155 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G19), G11 (= G22), G12 (= G23), L13 (≠ I24), H32 (vs. gap), S33 (vs. gap), N36 (vs. gap), V58 (≠ I57), D59 (= D58), V60 (≠ I59), N86 (= N85), A87 (= A86), G88 (= G87), I89 (≠ Y88), I136 (= I136), Y151 (= Y151), K155 (= K155), P181 (= P181), Y183 (≠ A183), L184 (≠ V184), T186 (= T186)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
34% identity, 93% coverage: 14:240/244 of query aligns to 7:244/248 of 6ixmC
- active site: G16 (= G23), S142 (= S138), Y155 (= Y151), K159 (= K155)
- binding nicotinamide-adenine-dinucleotide: G12 (= G19), S15 (≠ G22), G16 (= G23), I17 (= I24), D36 (= D43), I37 (≠ Q44), A61 (≠ I57), D62 (= D58), T63 (≠ I59), N89 (= N85), A90 (= A86), M140 (≠ I136), S142 (= S138), Y155 (= Y151), K159 (= K155), P185 (= P181), A186 (= A182), Y187 (≠ A183), I188 (≠ V184), L192 (= L188)
4k6fB X-ray crystal structure of a putative acetoacetyl-coa reductase from burkholderia cenocepacia bound to the co-factor NADP
35% identity, 93% coverage: 14:241/244 of query aligns to 3:242/245 of 4k6fB
- active site: G12 (= G23), N102 (≠ E102), S138 (= S138), Y151 (= Y151), K155 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G19), Y32 (vs. gap), S33 (vs. gap), N36 (vs. gap), V58 (≠ I57), D59 (= D58), V60 (≠ I59), A87 (= A86), G88 (= G87), I89 (≠ Y88)
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
33% identity, 95% coverage: 9:240/244 of query aligns to 1:239/243 of 1q7bA
- active site: G15 (= G23), E101 (= E102), S137 (= S138), Q147 (≠ A148), Y150 (= Y151), K154 (= K155)
- binding calcium ion: E232 (≠ A233), T233 (≠ V234)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G19), S13 (≠ H21), R14 (≠ G22), T36 (≠ V41), N58 (≠ D58), V59 (≠ I59), N85 (= N85), A86 (= A86), G87 (= G87), I88 (≠ Y88), S137 (= S138), Y150 (= Y151), K154 (= K155), P180 (= P181), G181 (≠ A182), I183 (≠ V184)
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)
33% identity, 95% coverage: 9:240/244 of query aligns to 2:240/244 of P0AEK2
- GASR 12:15 (≠ GGHG 19:22) binding
- T37 (≠ V41) binding
- NV 59:60 (≠ DI 58:59) binding
- N86 (= N85) binding
- Y151 (= Y151) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YSAAK 151:155) binding
- 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 (≠ V184) binding
- E233 (≠ A233) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
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)
34% identity, 93% coverage: 14:240/244 of query aligns to 5:242/246 of P14697
- GGI 13:15 (= GGI 22:24) binding
- G35 (vs. gap) binding
- R40 (vs. gap) binding
- Q47 (= Q44) 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 (≠ IDI 57:59) binding
- NAGIT 88:92 (≠ NAGYA 85:89) binding
- D94 (≠ P91) mutation to A: About 6% of wild-type activity.
- K99 (≠ E97) mutation to A: Nearly loss of activity.
- Q147 (≠ T145) mutation to A: About 30% of wild-type activity.
- F148 (≠ P146) mutation to A: About 30% of wild-type activity.
- Q150 (≠ A148) mutation to A: About 20% of wild-type activity.
- T173 (≠ E171) 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 (≠ PAAV 181:184) binding
- Y185 (≠ A183) mutation to A: Nearly loss of activity.
- R195 (≠ S193) mutation to A: Nearly loss of activity.
3vzsB Crystal structure of phab from ralstonia eutropha in complex with acetoacetyl-coa and NADP (see paper)
34% identity, 93% coverage: 14:240/244 of query aligns to 8:245/249 of 3vzsB
- active site: N115 (= N110), S143 (= S138), Y156 (= Y151), K160 (= K155)
- binding acetoacetyl-coenzyme a: D97 (≠ P91), Q150 (≠ T145), F151 (≠ P146), Q153 (≠ A148), Y156 (= Y151), G187 (≠ A182), Y188 (≠ A183), R198 (≠ S193)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G19), I18 (= I24), G38 (vs. gap), R43 (vs. gap), G63 (≠ I57), N64 (≠ D58), V65 (≠ I59), G93 (= G87), I94 (≠ Y88), T95 (≠ A89), P186 (= P181), I189 (≠ V184), M193 (≠ L188), V194 (≠ L189)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
33% identity, 95% coverage: 9:240/244 of query aligns to 1:239/243 of 1q7cA
- active site: G15 (= G23), S137 (= S138), Q147 (≠ A148), F150 (≠ Y151), K154 (= K155)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G19), S13 (≠ H21), R14 (≠ G22), A35 (vs. gap), T36 (≠ V41), L57 (≠ I57), N58 (≠ D58), V59 (≠ I59), G87 (= G87), I88 (≠ Y88)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
33% identity, 95% coverage: 10:240/244 of query aligns to 3:240/244 of 6t77A
- active site: G16 (= G23), S138 (= S138), Y151 (= Y151)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G19), S14 (≠ H21), R15 (≠ G22), T37 (≠ V41), L58 (≠ I57), N59 (≠ D58), V60 (≠ I59), A87 (= A86), G88 (= G87), I89 (≠ Y88)
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)
33% identity, 95% coverage: 10:240/244 of query aligns to 3:240/244 of P0A2C9
- M125 (= M125) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (≠ C223) 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.
4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 93% coverage: 15:240/244 of query aligns to 8:244/248 of 4urfB
- active site: G16 (= G23), S142 (= S138), I152 (≠ A148), Y155 (= Y151), K159 (= K155)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (≠ M206), R211 (≠ H207), R212 (= R208)
- binding bicarbonate ion: I92 (≠ Y88), G94 (= G90), R109 (= R105), R179 (≠ L175), S228 (= S224)
- binding nicotinamide-adenine-dinucleotide: G12 (= G19), G14 (≠ H21), N15 (≠ G22), G16 (= G23), I17 (= I24), D36 (= D43), I37 (vs. gap), D62 (= D47), T63 (≠ A48), N89 (= N85), A90 (= A86), G91 (= G87), I140 (= I136), Y155 (= Y151), K159 (= K155), P185 (= P181), A186 (= A182), I188 (≠ V184), T190 (= T186)
4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 93% coverage: 15:240/244 of query aligns to 8:244/248 of 4urfA
- active site: G16 (= G23), S142 (= S138), I152 (≠ A148), Y155 (= Y151), K159 (= K155)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (≠ Y88), S93 (≠ A89), G94 (= G90), E95 (≠ P91), T97 (≠ V93), E101 (= E97), T103 (≠ D99), Q106 (≠ E102), R109 (= R105), S175 (≠ E171), G177 (= G173)
- binding magnesium ion: S237 (≠ A233), Y238 (≠ V234)
- binding nicotinamide-adenine-dinucleotide: G12 (= G19), G14 (≠ H21), N15 (≠ G22), G16 (= G23), I17 (= I24), D36 (= D43), I37 (vs. gap), W41 (vs. gap), D62 (= D47), T63 (≠ A48), N89 (= N85), A90 (= A86), G91 (= G87), I140 (= I136), Y155 (= Y151), K159 (= K155), P185 (= P181), I188 (≠ V184), T190 (= T186)
4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 93% coverage: 15:240/244 of query aligns to 8:244/248 of 4ureB
- active site: G16 (= G23), S142 (= S138), I152 (≠ A148), Y155 (= Y151), K159 (= K155)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (≠ G22), G16 (= G23), I17 (= I24), N89 (= N85), G91 (= G87), Y155 (= Y151), P185 (= P181), A186 (= A182)
6zzsD Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and 3-oxovalerate (see paper)
34% identity, 93% coverage: 14:240/244 of query aligns to 9:257/261 of 6zzsD
- active site: G18 (= G23), S143 (= S138), Y156 (= Y151)
- binding nicotinamide-adenine-dinucleotide: G14 (= G19), S17 (≠ G22), I19 (= I24), D38 (= D43), M39 (≠ Q44), D64 (vs. gap), V65 (≠ I59), N91 (= N85), A92 (= A86), G93 (= G87), M141 (≠ I136), A142 (= A137), S143 (= S138), Y156 (= Y151), K160 (= K155), P186 (= P181), G187 (≠ A182), V189 (= V184), T191 (= T186), L193 (= L188)
- binding 3-oxidanylidenepentanoic acid: Q95 (≠ A89), S143 (= S138), N145 (≠ A140), K153 (≠ A148), Y156 (= Y151), Q197 (= Q191)
6zzqA Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and acetoacetate (see paper)
34% identity, 93% coverage: 14:240/244 of query aligns to 8:256/260 of 6zzqA
- active site: G17 (= G23), S142 (= S138), Y155 (= Y151)
- binding acetoacetic acid: Q94 (≠ A89), S142 (= S138), K152 (≠ A148), Y155 (= Y151), Q196 (= Q191)
- binding nicotinamide-adenine-dinucleotide: G13 (= G19), S16 (≠ G22), G17 (= G23), I18 (= I24), D37 (= D43), M38 (≠ Q44), D63 (vs. gap), V64 (≠ I59), N90 (= N85), A91 (= A86), G92 (= G87), M140 (≠ I136), A141 (= A137), S142 (= S138), Y155 (= Y151), K159 (= K155), Y187 (≠ A183), V188 (= V184), T190 (= T186)
Query Sequence
>HSERO_RS02925 FitnessBrowser__HerbieS:HSERO_RS02925
MTYSRASYDFGDCVAVVTGGHGGIGAAISARLAAGGAQVVVWDQHHDAASPYRQQSIDIT
DAPAVMQAAQELLADTGRIDFLINNAGYAGPTVPLDEYDVGEWHRIVQVNLLGVFHACRS
VTPAMRAARRGRIVNIASLAGKEGTPNASAYSAAKAGVLALTKSLGKELAESGVLVNAIA
PAAVKTALLGQMSPAHVQTMIAKSPMHRLGSVDEVADMCAWLCSGSCSFNTGAVFDLSGG
RATY
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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