SitesBLAST
Comparing AZOBR_RS04635 FitnessBrowser__azobra:AZOBR_RS04635 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)
D4A1J4 Dehydrogenase/reductase SDR family member 6; (R)-beta-hydroxybutyrate dehydrogenase; 3-hydroxybutyrate dehydrogenase type 2; 4-oxo-L-proline reductase; Oxidoreductase UCPA; Short chain dehydrogenase/reductase family 15C member 1; EC 1.1.1.-; EC 1.1.1.30; EC 1.1.1.104 from Rattus norvegicus (Rat) (see paper)
50% identity, 99% coverage: 3:247/247 of query aligns to 2:245/245 of D4A1J4
- Y147 (= Y149) mutation to F: Loss of function.
Q8JZV9 Dehydrogenase/reductase SDR family member 6; (R)-beta-hydroxybutyrate dehydrogenase; 3-hydroxybutyrate dehydrogenase type 2; 4-oxo-L-proline reductase; Oxidoreductase UCPA; Short chain dehydrogenase/reductase family 15C member 1; EC 1.1.1.-; EC 1.1.1.30; EC 1.1.1.104 from Mus musculus (Mouse) (see paper)
51% identity, 99% coverage: 3:247/247 of query aligns to 2:245/245 of Q8JZV9
- Y147 (= Y149) active site, Proton acceptor; mutation to F: Loss of function.
Q9BUT1 Dehydrogenase/reductase SDR family member 6; (R)-beta-hydroxybutyrate dehydrogenase; 3-hydroxybutyrate dehydrogenase type 2; 4-oxo-L-proline reductase; Oxidoreductase UCPA; Short chain dehydrogenase/reductase family 15C member 1; EC 1.1.1.-; EC 1.1.1.30; EC 1.1.1.104 from Homo sapiens (Human) (see 4 papers)
52% identity, 99% coverage: 3:247/247 of query aligns to 2:245/245 of Q9BUT1
2ag5A Crystal structure of human dhrs6 (see paper)
52% identity, 99% coverage: 3:247/247 of query aligns to 2:245/246 of 2ag5A
- active site: S133 (= S135), Y147 (= Y149), K151 (= K153), R192 (≠ S194)
- binding nicotinamide-adenine-dinucleotide: Q16 (= Q17), G17 (= G18), I18 (≠ M19), D37 (≠ S38), I38 (≠ R39), D58 (= D60), V59 (= V61), V81 (≠ N83), G83 (= G85), L104 (≠ Q106), Y147 (= Y149), K151 (= K153), P177 (= P179), V180 (≠ T182), T182 (≠ S184), S184 (= S186)
- binding sulfate ion: R144 (= R146), R188 (= R190), F202 (= F204), R205 (= R207)
5jc8D Crystal structure of a putative short-chain dehydrogenase/reductase from burkholderia xenovorans
40% identity, 99% coverage: 3:246/247 of query aligns to 2:258/262 of 5jc8D
2dtxA Structure of thermoplasma acidophilum aldohexose dehydrogenase (aldt) in complex with d-mannose (see paper)
38% identity, 98% coverage: 5:247/247 of query aligns to 5:247/255 of 2dtxA
2dteA Structure of thermoplasma acidophilum aldohexose dehydrogenase (aldt) in complex with nadh (see paper)
38% identity, 98% coverage: 5:247/247 of query aligns to 5:247/255 of 2dteA
- active site: G18 (= G18), S132 (= S135), Y145 (= Y149), S148 (= S152), K149 (= K153)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G14), S16 (≠ G16), M17 (≠ Q17), G18 (= G18), I19 (≠ M19), S38 (= S38), I39 (≠ M44), C52 (≠ L59), D53 (= D60), V54 (= V61), N80 (= N83), A81 (= A84), I130 (≠ V133), S132 (= S135), Y145 (= Y149), K149 (= K153), P174 (= P179), A175 (≠ G180), T176 (= T181), I177 (≠ T182), T179 (≠ S184), P180 (= P185), L181 (≠ S186), V182 (≠ L187)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
36% identity, 98% coverage: 5:247/247 of query aligns to 6:242/243 of 4i08A
- active site: G19 (= G18), N113 (= N107), S141 (= S135), Q151 (≠ R146), Y154 (= Y149), K158 (= K153)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G14), S17 (≠ G16), R18 (≠ Q17), I20 (≠ M19), T40 (≠ R39), N62 (≠ D60), V63 (= V61), N89 (= N83), A90 (= A84), G140 (≠ A134), S141 (= S135), Y154 (= Y149), K158 (= K153), P184 (= P179), G185 (= G180), T189 (≠ S184)
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)
37% identity, 98% coverage: 5:247/247 of query aligns to 6:246/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G14), S17 (≠ G16), R18 (≠ Q17), I20 (≠ M19), T40 (≠ R39), N62 (≠ D60), V63 (= V61), N89 (= N83), A90 (= A84), I92 (≠ W86), V139 (= V133), S141 (= S135), Y154 (= Y149), K158 (= K153), P184 (= P179), G185 (= G180), I187 (≠ L187), T189 (≠ E189), M191 (≠ I191)
5b4tA Crystal structure of d-3-hydroxybutyrate dehydrogenase from alcaligenes faecalis complexed with NAD+ and a substrate d-3- hydroxybutyrate (see paper)
37% identity, 98% coverage: 5:246/247 of query aligns to 2:258/260 of 5b4tA
- active site: G15 (= G18), N114 (= N107), S142 (= S135), Y155 (= Y149), K159 (= K153), I200 (≠ S194)
- binding (3R)-3-hydroxybutanoic acid: Q94 (≠ V87), S142 (= S135), H144 (≠ S138), K152 (≠ R146), Y155 (= Y149), W187 (≠ T181), Q196 (≠ R190)
- binding nicotinamide-adenine-dinucleotide: G11 (= G14), T13 (≠ G16), G15 (= G18), I16 (≠ M19), F36 (≠ L41), D63 (= D60), L64 (≠ V61), N90 (= N83), G92 (= G85), L113 (≠ Q106), I140 (≠ V133), Y155 (= Y149), K159 (= K153), P185 (= P179), G186 (= G180), W187 (≠ T181), V188 (≠ T182), T190 (≠ S184), L192 (≠ S186), V193 (≠ L187)
3w8dA Crystal structure of d-3-hydroxybutyrate dehydrogenase from alcaligenes faecalis complexed with NAD+ and an inhibitor methylmalonate
37% identity, 98% coverage: 5:246/247 of query aligns to 2:258/260 of 3w8dA
- active site: G15 (= G18), N114 (= N107), S142 (= S135), Y155 (= Y149), K159 (= K153), I200 (≠ S194)
- binding methylmalonic acid: Q94 (≠ V87), S142 (= S135), H144 (≠ S138), K152 (≠ R146), Y155 (= Y149), W187 (≠ T181), Q196 (≠ R190), W257 (≠ Q245)
- binding nicotinamide-adenine-dinucleotide: G11 (= G14), T13 (≠ G16), S14 (≠ Q17), G15 (= G18), I16 (≠ M19), F36 (≠ L41), A62 (vs. gap), D63 (= D60), L64 (≠ V61), N90 (= N83), A91 (= A84), G92 (= G85), L113 (≠ Q106), S142 (= S135), Y155 (= Y149), K159 (= K153), P185 (= P179), G186 (= G180), W187 (≠ T181), V188 (≠ T182), T190 (≠ S184), L192 (≠ S186), V193 (≠ L187)
3vdrA Crystal structure of d-3-hydroxybutyrate dehydrogenase, prepared in the presence of the substrate d-3-hydroxybutyrate and NAD(+) (see paper)
37% identity, 98% coverage: 5:246/247 of query aligns to 2:258/260 of 3vdrA
- active site: G15 (= G18), N114 (= N107), S142 (= S135), Y155 (= Y149), K159 (= K153), I200 (≠ S194)
- binding (3R)-3-hydroxybutanoic acid: Q94 (≠ V87), H144 (≠ S138), K152 (≠ R146), Y155 (= Y149), W187 (≠ T181), Q196 (≠ R190), W257 (≠ Q245)
- binding acetoacetic acid: Q94 (≠ V87), H144 (≠ S138), K152 (≠ R146), Y155 (= Y149), W187 (≠ T181), Q196 (≠ R190), W257 (≠ Q245)
- binding nicotinamide-adenine-dinucleotide: G11 (= G14), T13 (≠ G16), I16 (≠ M19), F36 (≠ L41), D63 (= D60), L64 (≠ V61), N90 (= N83), A91 (= A84), G92 (= G85), L113 (≠ Q106), K159 (= K153), G186 (= G180), V188 (≠ T182), T190 (≠ S184), L192 (≠ S186), V193 (≠ L187)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G11 (= G14), T13 (≠ G16), I16 (≠ M19), F36 (≠ L41), D63 (= D60), L64 (≠ V61), N90 (= N83), A91 (= A84), G92 (= G85), L113 (≠ Q106), S142 (= S135), Y155 (= Y149), K159 (= K153), G186 (= G180), V188 (≠ T182), T190 (≠ S184), L192 (≠ S186), V193 (≠ L187)
3vdqA Crystal structure of alcaligenes faecalis d-3-hydroxybutyrate dehydrogenase in complex with NAD(+) and acetate (see paper)
37% identity, 98% coverage: 5:246/247 of query aligns to 2:258/260 of 3vdqA
- active site: G15 (= G18), N114 (= N107), S142 (= S135), Y155 (= Y149), K159 (= K153), I200 (≠ S194)
- binding acetate ion: Q94 (≠ V87), H144 (≠ S138), K152 (≠ R146), W187 (≠ T181), L192 (≠ S186), Q196 (≠ R190)
- binding nicotinamide-adenine-dinucleotide: G11 (= G14), S14 (≠ Q17), I16 (≠ M19), F36 (≠ L41), D63 (= D60), L64 (≠ V61), N90 (= N83), A91 (= A84), G92 (= G85), L113 (≠ Q106), I140 (≠ V133), S142 (= S135), Y155 (= Y149), K159 (= K153), P185 (= P179), G186 (= G180), W187 (≠ T181), V188 (≠ T182), T190 (≠ S184), L192 (≠ S186), V193 (≠ L187)
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
34% identity, 98% coverage: 5:247/247 of query aligns to 2:242/243 of 1q7bA
- active site: G15 (= G18), E101 (≠ D99), S137 (= S135), Q147 (≠ R146), Y150 (= Y149), K154 (= K153)
- binding calcium ion: E232 (≠ S237), T233 (≠ L238)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G14), S13 (≠ G16), R14 (≠ Q17), T36 (≠ R39), N58 (≠ D60), V59 (= V61), N85 (= N83), A86 (= A84), G87 (= G85), I88 (≠ W86), S137 (= S135), Y150 (= Y149), K154 (= K153), P180 (= P179), G181 (= G180), I183 (≠ T182)
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)
34% identity, 98% coverage: 5:247/247 of query aligns to 3:243/244 of P0AEK2
- GASR 12:15 (≠ GAGQ 14:17) binding
- T37 (≠ R39) binding
- NV 59:60 (≠ DV 60:61) binding
- N86 (= N83) binding
- Y151 (= Y149) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YGTSK 149:153) binding
- A154 (≠ S152) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K153) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ T182) binding
- E233 (≠ S237) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
39% identity, 96% coverage: 10:246/247 of query aligns to 5:248/250 of 2cfcA
- active site: G13 (= G18), S142 (= S135), Y155 (= Y149), K159 (= K153)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ V143), R152 (= R146), Y155 (= Y149), W195 (≠ E189), R196 (= R190)
- binding nicotinamide-adenine-dinucleotide: G9 (= G14), S12 (≠ Q17), G13 (= G18), N14 (≠ M19), D33 (≠ S38), L34 (≠ R39), A59 (≠ L59), D60 (= D60), V61 (= V61), N87 (= N83), A88 (= A84), G89 (= G85), I140 (≠ V133), P185 (= P179), G186 (= G180), M187 (≠ T181), I188 (≠ T182), T190 (≠ S184), P191 (= P185), M192 (≠ S186), T193 (≠ L187)
Q56840 2-(R)-hydroxypropyl-CoM dehydrogenase; R-HPCDH; 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase; Aliphatic epoxide carboxylation component III; Epoxide carboxylase component III; RHPCDH1; EC 1.1.1.268 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 4 papers)
39% identity, 96% coverage: 10:246/247 of query aligns to 5:248/250 of Q56840
- SGN 12:14 (≠ QGM 17:19) binding
- D33 (≠ S38) binding
- DV 60:61 (= DV 60:61) binding
- N87 (= N83) binding
- S142 (= S135) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (= R146) binding ; mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- Y155 (= Y149) mutation Y->E,F: Loss of activity.
- K159 (= K153) mutation to A: Loss of activity.
- R179 (= R173) mutation to A: Loss of activity.
- IETPM 188:192 (≠ THSPS 182:186) binding
- WR 195:196 (≠ ER 189:190) binding
- R196 (= R190) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- R203 (= R201) mutation to A: Slight decrease in catalytic efficiency.
- R209 (= R207) mutation to A: Does not affect catalytic efficiency.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4nbuB Crystal structure of fabg from bacillus sp (see paper)
35% identity, 98% coverage: 4:244/247 of query aligns to 4:241/244 of 4nbuB
- active site: G18 (= G18), N111 (= N107), S139 (= S135), Q149 (≠ R146), Y152 (= Y149), K156 (= K153)
- binding acetoacetyl-coenzyme a: D93 (≠ N89), K98 (≠ D94), S139 (= S135), N146 (≠ G142), V147 (= V143), Q149 (≠ R146), Y152 (= Y149), F184 (≠ T181), M189 (≠ S186), K200 (≠ Q203)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G14), N17 (≠ Q17), G18 (= G18), I19 (≠ M19), D38 (≠ S38), F39 (≠ R39), V59 (≠ L59), D60 (= D60), V61 (= V61), N87 (= N83), A88 (= A84), G89 (= G85), I90 (≠ W86), T137 (≠ V133), S139 (= S135), Y152 (= Y149), K156 (= K153), P182 (= P179), F184 (≠ T181), T185 (= T182), T187 (≠ S184), M189 (≠ S186)
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, 98% coverage: 5:247/247 of query aligns to 3:243/244 of P0A2C9
- M125 (= M122) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (= A227) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (= S228) 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.
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
34% identity, 98% coverage: 5:247/247 of query aligns to 3:243/244 of 6t77A
- active site: G16 (= G18), S138 (= S135), Y151 (= Y149)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G14), S14 (≠ G16), R15 (≠ Q17), T37 (≠ R39), L58 (= L59), N59 (≠ D60), V60 (= V61), A87 (= A84), G88 (= G85), I89 (≠ W86)
Query Sequence
>AZOBR_RS04635 FitnessBrowser__azobra:AZOBR_RS04635
MTGRLDGKRALVTGAGQGMGRAIALAFAREGASVVAASRTLSKMEDLPRIDSKITPVALD
VTDPAAVRRVVAEAGPLDILVNNAGWVHNGTILDCSDEDWARSLDQNVTSMFHTIRAALP
GMIERRQGSIVNVASVASSLTGVANRTAYGTSKAAVIGLTKAVARDFIGAGVRCNALCPG
TTHSPSLEERIQSSADPEGMRAQFIARQPMGRLGTVEEMAAAAVYLASDESGFMTGSLLV
ADGGQTL
Or try a new SitesBLAST search
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