SitesBLAST
Comparing Dsui_0676 FitnessBrowser__PS:Dsui_0676 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)
A0A140FAN3 11-beta-hydroxysteroid dehydrogenase; 17-beta-hydroxysteroid dehydrogenase; Steroleosin; EC 1.1.1.146; EC 1.1.1.62 from Pinus massoniana (Chinese red pine) (see paper)
28% identity, 93% coverage: 6:245/257 of query aligns to 50:310/356 of A0A140FAN3
Sites not aligning to the query:
- 206:356 mutation Missing: Loss of binding to plant derived cholesterol, cholest-5-en-3beta-ol.
3p19A Improved NADPH-dependent blue fluorescent protein (see paper)
34% identity, 71% coverage: 6:188/257 of query aligns to 5:182/239 of 3p19A
- active site: S132 (= S138), Y145 (= Y151), K149 (= K155)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G10), S11 (= S12), S12 (= S13), G13 (= G14), I14 (= I15), A33 (= A34), R34 (= R35), R35 (= R36), D53 (= D57), V54 (= V58), N80 (= N84), A81 (= A85), G82 (= G86), I130 (= I136), S132 (= S138), Y145 (= Y151), K149 (= K155), P175 (= P181), A177 (≠ Y183), V178 (≠ I184), T180 (= T186), E181 (≠ P187), L182 (≠ M188)
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)
33% identity, 78% coverage: 7:207/257 of query aligns to 12:211/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G10), S17 (= S12), R18 (≠ S13), I20 (= I15), T40 (≠ A34), N62 (≠ D57), V63 (= V58), N89 (= N84), A90 (= A85), I92 (≠ V87), V139 (≠ I136), S141 (= S138), Y154 (= Y151), K158 (= K155), P184 (= P181), G185 (= G182), I187 (= I184), T189 (= T186), M191 (= M188)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
34% identity, 72% coverage: 6:189/257 of query aligns to 7:188/243 of 7emgB
1w4zA Structure of actinorhodin polyketide (actiii) reductase (see paper)
34% identity, 72% coverage: 7:190/257 of query aligns to 8:194/259 of 1w4zA
- active site: G15 (= G14), N112 (= N109), S142 (= S138), Y155 (= Y151), K159 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G10), T13 (≠ S12), S14 (= S13), G15 (= G14), I16 (= I15), R36 (= R35), G37 (≠ R36), D61 (= D57), V62 (= V58), N88 (= N84), G90 (= G86), S142 (= S138), Y155 (= Y151), K159 (= K155), P185 (= P181), G186 (= G182), V188 (≠ I184), T190 (= T186)
Sites not aligning to the query:
2rh4A Actinorhodin ketoreductase, actkr, with NADPH and inhibitor emodin (see paper)
34% identity, 72% coverage: 7:190/257 of query aligns to 6:192/257 of 2rh4A
- active site: G13 (= G14), N110 (= N109), S140 (= S138), Y153 (= Y151), K157 (= K155)
- binding 3-methyl-1,6,8-trihydroxyanthraquinone: T141 (≠ V139), Q145 (≠ R143), V147 (≠ L145), Y153 (= Y151), F185 (≠ Y183)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G10), T11 (≠ S12), S12 (= S13), G13 (= G14), I14 (= I15), A33 (= A34), R34 (= R35), G35 (≠ R36), C58 (≠ L56), D59 (= D57), V60 (= V58), N86 (= N84), G88 (= G86), S140 (= S138), Y153 (= Y151), K157 (= K155), P183 (= P181), G184 (= G182), V186 (≠ I184), T188 (= T186), M190 (= M188)
Sites not aligning to the query:
2rh4B Actinorhodin ketoreductase, actkr, with NADPH and inhibitor emodin (see paper)
34% identity, 72% coverage: 7:190/257 of query aligns to 17:203/268 of 2rh4B
- active site: G24 (= G14), N121 (= N109), S151 (= S138), Y164 (= Y151), K168 (= K155)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G20 (= G10), T22 (≠ S12), S23 (= S13), I25 (= I15), A44 (= A34), R45 (= R35), G46 (≠ R36), C69 (≠ L56), D70 (= D57), V71 (= V58), N97 (= N84), S151 (= S138), Y164 (= Y151), K168 (= K155), G195 (= G182), V197 (≠ I184), T199 (= T186), M201 (= M188)
Sites not aligning to the query:
1xr3A Actinorhodin polyketide ketoreductase with NADP and the inhibitor isoniazid bound (see paper)
34% identity, 72% coverage: 7:190/257 of query aligns to 5:191/256 of 1xr3A
- active site: G12 (= G14), N109 (= N109), S139 (= S138), Y152 (= Y151), K156 (= K155)
- binding 4-(diazenylcarbonyl)pyridine: T140 (≠ V139), G141 (≠ A140), V146 (≠ L145)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G10), T10 (≠ S12), S11 (= S13), G12 (= G14), I13 (= I15), A32 (= A34), R33 (= R35), G34 (≠ R36), C57 (≠ L56), D58 (= D57), V59 (= V58), N85 (= N84), A86 (= A85), G87 (= G86), S139 (= S138), Y152 (= Y151), K156 (= K155), G183 (= G182), V185 (≠ I184), T187 (= T186), P188 (= P187)
Sites not aligning to the query:
P16544 Putative ketoacyl reductase; EC 1.3.1.- from Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) (see 2 papers)
34% identity, 72% coverage: 7:190/257 of query aligns to 10:196/261 of P16544
- 11:39 (vs. 8:36, 41% identical) binding
- D63 (= D57) binding
- K161 (= K155) binding
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
34% identity, 71% coverage: 7:189/257 of query aligns to 12:192/243 of 4i08A
- active site: G19 (= G14), N113 (= N109), S141 (= S138), Q151 (≠ A148), Y154 (= Y151), K158 (= K155)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G10), S17 (= S12), R18 (≠ S13), I20 (= I15), T40 (≠ A34), N62 (≠ D57), V63 (= V58), N89 (= N84), A90 (= A85), G140 (≠ A137), S141 (= S138), Y154 (= Y151), K158 (= K155), P184 (= P181), G185 (= G182), T189 (= T186)
P73826 Acetoacetyl-CoA reductase; EC 1.1.1.36 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
35% identity, 72% coverage: 6:189/257 of query aligns to 11:185/240 of P73826
- S134 (= S138) mutation to A: 12% enzymatic activity.
- Y147 (= Y151) mutation to A: No enzymatic activity.
- K151 (= K155) mutation to A: 5% enzymatic activity.
6ci9D Rmm microcompartment-associated aminopropanol dehydrogenase NADP + aminoacetone holo-structure (see paper)
34% identity, 70% coverage: 7:186/257 of query aligns to 13:194/259 of 6ci9D
- active site: G20 (= G14), S145 (= S138), Y159 (= Y151)
- binding 1-aminopropan-2-one: F97 (vs. gap), S145 (= S138), T147 (≠ A140), W156 (≠ A148), Y159 (= Y151), G190 (= G182)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G16 (= G10), S18 (= S12), G20 (= G14), I21 (= I15), G40 (≠ A34), R41 (= R35), N42 (≠ R36), D66 (= D57), V67 (= V58), N93 (= N84), G95 (= G86), T143 (≠ I136), S145 (= S138), Y159 (= Y151), K163 (= K155), P189 (= P181), N191 (≠ Y183), I192 (= I184), T194 (= T186)
Sites not aligning to the query:
A0A1U8QWA2 Glycine betaine reductase ATRR; Nonribosomal peptide synthetase-like protein ATRR; EC 1.2.1.-; EC 1.1.1.- from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see paper)
34% identity, 72% coverage: 8:192/257 of query aligns to 1034:1219/1270 of A0A1U8QWA2
- G1036 (= G10) mutation to A: Compromises binding of the cosubstrate NADPH to aldehyde reductase domain R2. Decreases the aldehyde reductase activity by 4,000-fold; when associated with F-1178.
- Y1178 (= Y151) mutation to F: Does not substantially affect carboxylic acid reductase activity but results to a 150-fold loss of aldehyde reductase activity and the accumulation of glycine betaine aldehyde intermediate. Further decreases the aldehyde reductase activity by 4,000-fold; when associated with F-1178.
Sites not aligning to the query:
- 14:418 Adenylation (A) domain
- 643:937 Carboxylic acid reductase domain R1
- 812 Y→F: Abolishes overall carboxylic acid reductase activity but does nor affect aldehyde reductase activity.
- 1026:1256 Aldehyde reductase domain R2
4iiuA Crystal structure of a putative 3-oxoacyl-[acyl-carrier protein]reductase from escherichia coli strain cft073 complexed with NADP+ at 2.1 a resolution
32% identity, 79% coverage: 3:206/257 of query aligns to 2:217/243 of 4iiuA
- active site: G13 (= G14), S140 (= S138), Y153 (= Y151), K157 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G9 (= G10), S11 (= S12), K12 (≠ S13), G13 (= G14), I14 (= I15), H32 (≠ A33), H34 (≠ R35), D36 (vs. gap), D60 (= D57), V61 (= V58), N87 (= N84), A88 (= A85), G89 (= G86), I90 (≠ V87), S140 (= S138), Y153 (= Y151), K157 (= K155), P183 (= P181), G184 (= G182), I186 (= I184), T188 (= T186), M190 (= M188), I191 (vs. gap)
5jlaD Crystal structure of ribose-5-phosphate isomerase from brucella melitensis 16m
37% identity, 70% coverage: 8:187/257 of query aligns to 12:187/259 of 5jlaD
- active site: G18 (= G14), S139 (= S138), L148 (≠ A148), Y151 (= Y151), K155 (= K155)
- binding nicotinamide-adenine-dinucleotide: G14 (= G10), S17 (= S13), G18 (= G14), I19 (= I15), D38 (≠ A34), R39 (= R35), L58 (= L56), D59 (= D57), V60 (= V58), C86 (≠ N84), A87 (= A85), I137 (= I136), S139 (= S138), Y151 (= Y151), K155 (= K155), P181 (= P181), G182 (= G182), F183 (≠ Y183), T184 (≠ I184), T186 (= T186)
Sites not aligning to the query:
6ixjA The crystal structure of sulfoacetaldehyde reductase from klebsiella oxytoca (see paper)
33% identity, 72% coverage: 6:191/257 of query aligns to 4:191/251 of 6ixjA
- binding 2-hydroxyethylsulfonic acid: S138 (= S138), Y145 (≠ L145), Y151 (= Y151)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G10), T10 (≠ S12), S11 (= S13), G12 (= G14), F13 (≠ I15), R33 (= R35), R34 (= R36), D57 (= D57), V58 (= V58), N84 (= N84), A85 (= A85), G86 (= G86), T108 (= T108), I136 (= I136), S138 (= S138), Y151 (= Y151), K155 (= K155), P181 (= P181), G182 (= G182), A184 (≠ I184), T186 (= T186), E187 (≠ P187), F188 (≠ M188)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
32% identity, 73% coverage: 7:193/257 of query aligns to 11:194/244 of 4nbuB
- active site: G18 (= G14), N111 (= N109), S139 (= S138), Q149 (≠ A148), Y152 (= Y151), K156 (= K155)
- binding acetoacetyl-coenzyme a: D93 (≠ G90), K98 (≠ E94), S139 (= S138), N146 (≠ L145), V147 (≠ P146), Q149 (≠ A148), Y152 (= Y151), F184 (≠ Y183), M189 (= M188)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G10), N17 (≠ S13), G18 (= G14), I19 (= I15), D38 (≠ A34), F39 (≠ R35), V59 (≠ L56), D60 (= D57), V61 (= V58), N87 (= N84), A88 (= A85), G89 (= G86), I90 (≠ V87), T137 (≠ I136), S139 (= S138), Y152 (= Y151), K156 (= K155), P182 (= P181), F184 (≠ Y183), T185 (≠ I184), T187 (= T186), M189 (= M188)
Sites not aligning to the query:
5mlnB The crystal structure of alcohol dehydrogenase 10 from candida magnoliae
32% identity, 72% coverage: 7:190/257 of query aligns to 5:193/238 of 5mlnB
- active site: G12 (= G14), S141 (= S138), Y154 (= Y151)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G8 (= G10), S10 (= S12), R11 (≠ S13), G12 (= G14), I13 (= I15), S32 (≠ A34), R33 (= R35), S34 (≠ R36), L61 (≠ V58), N86 (= N84), A87 (= A85), G88 (= G86), I139 (= I136), S141 (= S138), Y154 (= Y151), K158 (= K155), P184 (= P181), G185 (= G182), Y186 (= Y183), T187 (≠ I184), T189 (= T186), M191 (= M188), T192 (= T189)
3o4rA Crystal structure of human dehydrogenase/reductase (sdr family) member 4 (dhrs4)
29% identity, 74% coverage: 1:189/257 of query aligns to 6:196/254 of 3o4rA
- active site: G19 (= G14), S145 (= S138), F155 (≠ A148), Y158 (= Y151), K162 (= K155)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G10), T17 (≠ S12), D18 (≠ S13), G19 (= G14), I20 (= I15), S39 (≠ A34), R40 (= R35), K41 (≠ R36), N44 (≠ A39), H65 (≠ Y54), V66 (≠ A55), N92 (= N84), A94 (≠ G86), S145 (= S138), Y158 (= Y151), K162 (= K155), P188 (= P181), G189 (= G182), L190 (≠ Y183), I191 (= I184), T193 (= T186), F195 (≠ M188), S196 (≠ T189)
Sites not aligning to the query:
Q9BTZ2 Dehydrogenase/reductase SDR family member 4; NADPH-dependent carbonyl reductase; CR; NADPH-dependent retinol dehydrogenase/reductase; NRDR; humNRDR; Peroxisomal short-chain alcohol dehydrogenase; PSCD; SCAD-SRL; Short chain dehydrogenase/reductase family 25C member 2; Protein SDR25C2; Short-chain dehydrogenase/reductase family member 4; EC 1.1.1.184 from Homo sapiens (Human) (see 2 papers)
29% identity, 74% coverage: 1:189/257 of query aligns to 30:220/278 of Q9BTZ2
- S176 (≠ L145) Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin; mutation to F: Decreased reduction activity for benzil, isatin and retinal and increased activity for 5beta-Pregnane-3,20-dione and 5beta-Dihydrotestosterone. No change of stereoselectivity in 3-ketosteroids reduction and no change in 3beta-hydroxysteroid oxidation. Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with L-179. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with L-179. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with L-179. Loss of cold catalytic inactivation; when associated with L-179 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with L-179 and N-195.
- F179 (≠ A148) Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin; mutation to L: Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with F-176. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with F-176. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176. Loss of cold catalytic inactivation; when associated with F-176 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and N-195.
- T195 (≠ S164) mutation to N: Loss of cold catalytic inactivation. Loss of cold catalytic inactivation; when associated with F-176 and L-179. Switch in stereoselective activity from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176 and L-179. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and L-179.
Query Sequence
>Dsui_0676 FitnessBrowser__PS:Dsui_0676
MASLKVFITGASSGIGAALARHYAEQGATLGLAARRQQALTDLLADLPGHHAAYALDVSD
APALAAAAADFTARHGAPDIVIANAGVSVGTLSECPEDLAAFRKVMDTNVYGMAATFVPF
IGPMAAAGGDRRLVGIASVAGIRGLPGAEAYSASKAAAIAYLESLRLEMAPKGIKVVTIA
PGYIETPMTAINPYPMPFLLPAAEAARRFARAVAKGTSYTVIPWQMGVVAKVLRLLPNWL
YDRLFTQAPRKPRGLLD
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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