SitesBLAST
Comparing Ga0059261_0812 FitnessBrowser__Korea:Ga0059261_0812 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)
3toxA Crystal structure of a short chain dehydrogenase in complex with NAD(p) from sinorhizobium meliloti 1021
59% identity, 99% coverage: 2:252/253 of query aligns to 1:254/254 of 3toxA
- active site: G16 (= G17), S142 (= S140), V153 (≠ M151), Y156 (= Y154), K160 (= K158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), S14 (= S15), S15 (= S16), G16 (= G17), I17 (= I18), A36 (= A37), R37 (= R38), N38 (≠ R39), V63 (= V61), N89 (= N87), A90 (= A88), G91 (= G89), T140 (≠ S138), S142 (= S140), Y156 (= Y154), K160 (= K158), P186 (≠ I184), G188 (= G186), T189 (= T187), T191 (= T189)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
36% identity, 98% coverage: 1:249/253 of query aligns to 2:253/255 of 5itvA
- active site: G18 (= G17), S141 (= S140), Y154 (= Y154), K158 (= K158)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), S17 (= S16), G18 (= G17), I19 (= I18), D38 (≠ A37), I39 (≠ R38), T61 (≠ G59), I63 (≠ V61), N89 (= N87), G91 (= G89), T139 (≠ S138), S141 (= S140), Y154 (= Y154), K158 (= K158), P184 (≠ I184), G185 (= G185), I186 (≠ G186), I187 (≠ T187)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
36% identity, 97% coverage: 4:249/253 of query aligns to 3:246/248 of 6ixmC
- active site: G16 (= G17), S142 (= S140), Y155 (= Y154), K159 (= K158)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), S15 (= S16), G16 (= G17), I17 (= I18), D36 (≠ A37), I37 (≠ R38), A61 (≠ G59), D62 (= D60), T63 (≠ V61), N89 (= N87), A90 (= A88), M140 (≠ S138), S142 (= S140), Y155 (= Y154), K159 (= K158), P185 (≠ I184), A186 (≠ G185), Y187 (≠ G186), I188 (≠ T187), L192 (≠ A191)
4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
39% identity, 96% coverage: 4:247/253 of query aligns to 3:244/248 of 4urfB
- active site: G16 (= G17), S142 (= S140), I152 (≠ M151), Y155 (= Y154), K159 (= K158)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (= L213), R211 (≠ K214), R212 (= R215)
- binding bicarbonate ion: I92 (≠ A90), G94 (= G92), R109 (≠ W107), R179 (= R178), S228 (= S231)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), G14 (≠ S15), N15 (≠ S16), G16 (= G17), I17 (= I18), D36 (≠ R45), I37 (≠ V46), D62 (= D60), T63 (≠ V61), N89 (= N87), A90 (= A88), G91 (= G89), I140 (≠ S138), Y155 (= Y154), K159 (= K158), P185 (vs. gap), A186 (vs. gap), I188 (= I184), T190 (≠ G186)
4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
39% identity, 96% coverage: 4:247/253 of query aligns to 3:244/248 of 4urfA
- active site: G16 (= G17), S142 (= S140), I152 (≠ M151), Y155 (= Y154), K159 (= K158)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (≠ A90), S93 (≠ V91), G94 (= G92), E95 (≠ V93), T97 (≠ G95), E101 (≠ G99), T103 (≠ A101), Q106 (≠ D104), R109 (≠ W107), S175 (≠ P174), G177 (≠ R176)
- binding magnesium ion: S237 (≠ G240), Y238 (≠ A241)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), G14 (≠ S15), N15 (≠ S16), G16 (= G17), I17 (= I18), D36 (≠ R45), I37 (≠ V46), W41 (≠ L50), D62 (= D60), T63 (≠ V61), N89 (= N87), A90 (= A88), G91 (= G89), I140 (≠ S138), Y155 (= Y154), K159 (= K158), P185 (vs. gap), I188 (= I184), T190 (≠ G186)
4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
39% identity, 96% coverage: 4:247/253 of query aligns to 3:244/248 of 4ureB
- active site: G16 (= G17), S142 (= S140), I152 (≠ M151), Y155 (= Y154), K159 (= K158)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (≠ S16), G16 (= G17), I17 (= I18), N89 (= N87), G91 (= G89), Y155 (= Y154), P185 (vs. gap), A186 (vs. gap)
2zatA Crystal structure of a mammalian reductase (see paper)
37% identity, 97% coverage: 4:248/253 of query aligns to 3:247/251 of 2zatA
- active site: G16 (= G17), S142 (= S140), L152 (≠ M151), Y155 (= Y154), K159 (= K158), K200 (≠ P201)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A12 (≠ G13), T14 (≠ S15), D15 (≠ S16), G16 (= G17), I17 (= I18), S36 (≠ A37), R37 (= R38), K38 (≠ R39), N41 (≠ E42), H62 (≠ D63), N89 (= N87), A91 (≠ G89), V140 (≠ S138), S142 (= S140), Y155 (= Y154), K159 (= K158), P185 (≠ I184), G186 (= G185), I188 (≠ T187), T190 (= T189), F192 (≠ A191), S193 (= S192)
Q8WNV7 Dehydrogenase/reductase SDR family member 4; NADPH-dependent carbonyl reductase; CR; PHCR; NADPH-dependent retinol dehydrogenase/reductase; NDRD; Peroxisomal carbonyl reductase; PerCR; Peroxisomal short-chain alcohol dehydrogenase; PSCD; Short chain dehydrogenase/reductase family 25C member 2; Protein SDR25C2; EC 1.1.1.184; EC 1.1.1.300 from Sus scrofa (Pig) (see 2 papers)
37% identity, 96% coverage: 4:247/253 of query aligns to 31:274/279 of Q8WNV7
- 37:61 (vs. 10:34, 48% identical) binding
- F177 (≠ I148) Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoin; mutation to S: Change in stereoselective activity by the reduction of 3-ketosteroids and benzil into 3beta-hydroxysteroid and R-benzoin, respectively; when associated with F-180.
- L180 (≠ M151) Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoin; mutation to F: Change in stereoselective activity by the reduction of 3-ketosteroids and benzil into 3beta-hydroxysteroid and R-benzoin, respectively; when associated with S-177.
- Y183 (= Y154) active site, Proton acceptor
- K187 (= K158) binding
- N196 (≠ T167) Important for the maintenance of the quaternary structure, the catalytic activity and cold stability
Sites not aligning to the query:
- 277:279 Peroxisomal targeting signal
6zyzA Structure of the borneol dehydrogenases of salvia rosmarinus with NAD+ (see paper)
37% identity, 99% coverage: 3:252/253 of query aligns to 2:250/259 of 6zyzA
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), S15 (= S16), G16 (= G17), I17 (= I18), D36 (≠ A37), I37 (≠ R38), Q38 (≠ R39), C58 (≠ G59), D59 (= D60), V60 (= V61), N86 (= N87), A87 (= A88), V90 (= V91), I110 (≠ T111), T137 (≠ S138), Y152 (= Y154), K156 (= K158), V185 (≠ T187)
- binding (2S)-1-[3-{[(2R)-2-hydroxypropyl]oxy}-2,2-bis({[(2R)-2-hydroxypropyl]oxy}methyl)propoxy]propan-2-ol: P93 (≠ S94), N94 (≠ G95), S95 (≠ P96), D98 (≠ G99)
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
35% identity, 98% coverage: 4:250/253 of query aligns to 5:253/254 of 4fn4A
- active site: G18 (= G17), S144 (= S140), Y157 (= Y154), K161 (= K158), S202 (≠ A199)
- binding nicotinamide-adenine-dinucleotide: G14 (= G13), S17 (= S16), G18 (= G17), I19 (= I18), E38 (≠ A37), L39 (≠ R38), R43 (≠ E42), A63 (≠ G59), D64 (= D60), V65 (= V61), N91 (= N87), G93 (= G89), I94 (≠ A90), T142 (≠ S138), S144 (= S140), Y157 (= Y154), K161 (= K158), P187 (≠ I184), V190 (≠ T187), T192 (= T189), N193 (≠ P190), I194 (≠ A191)
5itvD Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
36% identity, 98% coverage: 1:249/253 of query aligns to 2:225/227 of 5itvD
- active site: G18 (= G17), S141 (= S140), Y154 (= Y154), K158 (= K158)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), S17 (= S16), G18 (= G17), I19 (= I18), D38 (≠ A37), I39 (≠ R38), T61 (≠ G59), D62 (= D60), I63 (≠ V61), N89 (= N87), T139 (≠ S138), S141 (= S140), Y154 (= Y154), K158 (= K158), P184 (≠ I184), G185 (= G185), I187 (≠ T187)
3o4rA Crystal structure of human dehydrogenase/reductase (sdr family) member 4 (dhrs4)
36% identity, 96% coverage: 4:247/253 of query aligns to 6:249/254 of 3o4rA
- active site: G19 (= G17), S145 (= S140), F155 (≠ M151), Y158 (= Y154), K162 (= K158), K203 (≠ P201)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G13), T17 (≠ S15), D18 (≠ S16), G19 (= G17), I20 (= I18), S39 (≠ A37), R40 (= R38), K41 (≠ R39), N44 (≠ E42), H65 (≠ D63), V66 (≠ E64), N92 (= N87), A94 (≠ G89), S145 (= S140), Y158 (= Y154), K162 (= K158), P188 (≠ I184), G189 (= G185), L190 (≠ G186), I191 (≠ T187), T193 (= T189), F195 (≠ S193), S196 (≠ A194)
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)
36% identity, 98% coverage: 1:247/253 of query aligns to 24:273/278 of Q9BTZ2
- S176 (≠ I148) 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 (≠ M151) 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 (= T167) 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.
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
37% identity, 97% coverage: 4:249/253 of query aligns to 5:251/261 of 1g6kA
- active site: G18 (= G17), S145 (≠ F141), Y158 (= Y154), K162 (= K158)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ S16), G18 (= G17), L19 (≠ I18), R39 (= R38), D65 (= D60), V66 (= V61), N92 (= N87), A93 (= A88), G94 (= G89), M143 (≠ S139), S145 (≠ F141), Y158 (= Y154), P188 (≠ I184), G189 (= G185), I191 (≠ T187), T193 (= T189)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
37% identity, 97% coverage: 4:249/253 of query aligns to 5:251/261 of P40288
- 11:35 (vs. 10:34, 56% identical) binding
- E96 (≠ S94) mutation E->A,G,K: Heat stable.
- D108 (= D104) mutation to N: Heat stable.
- V112 (≠ T108) mutation to A: Heat stable.
- E133 (≠ A129) mutation to K: Heat stable.
- V183 (≠ A179) mutation to I: Heat stable.
- P194 (= P190) mutation to Q: Heat stable.
- E210 (= E208) mutation to K: Heat stable.
- Y217 (≠ R215) mutation to H: Heat stable.
Sites not aligning to the query:
- 252 Q→L: Heat stable.
- 253 Y→C: Heat stable.
- 258 A→G: Heat stable.
4nbuB Crystal structure of fabg from bacillus sp (see paper)
39% identity, 98% coverage: 1:247/253 of query aligns to 2:241/244 of 4nbuB
- active site: G18 (= G17), N111 (= N112), S139 (= S140), Q149 (≠ M151), Y152 (= Y154), K156 (= K158)
- binding acetoacetyl-coenzyme a: D93 (≠ S94), K98 (≠ G99), S139 (= S140), N146 (≠ G147), V147 (≠ I148), Q149 (≠ M151), Y152 (= Y154), F184 (≠ G186), M189 (≠ S192), K200 (≠ W206)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), N17 (≠ S16), G18 (= G17), I19 (= I18), D38 (≠ A37), F39 (≠ R38), V59 (≠ G59), D60 (= D60), V61 (= V61), N87 (= N87), A88 (= A88), G89 (= G89), I90 (≠ V91), T137 (≠ S138), S139 (= S140), Y152 (= Y154), K156 (= K158), P182 (≠ I184), F184 (≠ G186), T185 (= T187), T187 (= T189), M189 (≠ S192)
Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
39% identity, 98% coverage: 3:249/253 of query aligns to 10:264/267 of Q9LBG2
- 17:42 (vs. 10:35, 65% identical) binding
- E103 (≠ V91) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.
1iy8A Crystal structure of levodione reductase (see paper)
39% identity, 98% coverage: 3:249/253 of query aligns to 1:255/258 of 1iy8A
- active site: G15 (= G17), S143 (= S140), Q153 (≠ M151), Y156 (= Y154), K160 (= K158)
- binding nicotinamide-adenine-dinucleotide: G11 (= G13), S14 (= S16), G15 (= G17), L16 (≠ I18), D35 (vs. gap), V36 (vs. gap), A62 (≠ G59), D63 (= D60), V64 (= V61), N90 (= N87), G92 (= G89), I93 (≠ A90), T141 (≠ S138), S143 (= S140), Y156 (= Y154), K160 (= K158), P186 (≠ I184), G187 (= G185), T191 (= T189), P192 (= P190), M193 (vs. gap)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
39% identity, 98% coverage: 3:249/253 of query aligns to 7:251/258 of 4wecA
- active site: G21 (= G17), S143 (= S140), Q154 (≠ M151), Y157 (= Y154), K161 (= K158)
- binding nicotinamide-adenine-dinucleotide: G17 (= G13), A19 (≠ S15), S20 (= S16), G21 (= G17), I22 (= I18), D41 (≠ A37), I42 (≠ R38), V61 (≠ G59), D62 (= D60), V63 (= V61), N89 (= N87), T141 (≠ S138), Y157 (= Y154), K161 (= K158), P187 (≠ I184), P189 (≠ G186), V190 (≠ T187)
3pk0B Crystal structure of short-chain dehydrogenase/reductase sdr from mycobacterium smegmatis (see paper)
34% identity, 100% coverage: 1:253/253 of query aligns to 5:256/262 of 3pk0B
Query Sequence
>Ga0059261_0812 FitnessBrowser__Korea:Ga0059261_0812
MARLDGKVAIITGASSGIGEAAARRFAAEGAKLVLAARRPAELERVADELGGETAFLAGD
VRDEAYAEALVALAVERFGGLDIAFNNAGAVGVSGPLTGLAAEDWGWTIATNLTAAFYGA
KHQAAAMAARGGGSILFSSSFVGAANGIPGMGAYAAAKAGLLGLVRTLAVELGPQRVRAN
ALIIGGTDTPASSARQPDADPGVQAWMEQLHALKRLAEPEEIAEMALFLASDAASFVTGG
AIAVDGGASITKT
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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