SitesBLAST
Comparing 7025539 FitnessBrowser__ANA3:7025539 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
64% identity, 98% coverage: 4:254/255 of query aligns to 3:254/254 of 3toxA
- active site: G16 (= G17), S142 (= S144), V153 (≠ T155), Y156 (= Y158), K160 (= K162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), S14 (= S15), S15 (= S16), G16 (= G17), I17 (= I18), A36 (= A37), R37 (= R38), N38 (≠ R39), V63 (= V64), N89 (= N90), A90 (≠ V91), G91 (= G92), T140 (= T142), S142 (= S144), Y156 (= Y158), K160 (= K162), P186 (= P188), G188 (= G190), T189 (= T191), T191 (= T193)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
41% identity, 97% coverage: 4:251/255 of query aligns to 5:251/261 of P40288
- 11:35 (vs. 10:34, 56% identical) binding
- E96 (= E96) mutation E->A,G,K: Heat stable.
- D108 (≠ E108) mutation to N: Heat stable.
- V112 (≠ T112) mutation to A: Heat stable.
- E133 (≠ K133) mutation to K: Heat stable.
- V183 (= V183) mutation to I: Heat stable.
- P194 (= P194) mutation to Q: Heat stable.
- E210 (≠ K210) mutation to K: Heat stable.
- Y217 (≠ R217) 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.
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
40% identity, 97% coverage: 4:251/255 of query aligns to 5:251/261 of 1g6kA
- active site: G18 (= G17), S145 (≠ F145), Y158 (= Y158), K162 (= K162)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ S16), G18 (= G17), L19 (≠ I18), R39 (= R38), D65 (= D63), V66 (= V64), N92 (= N90), A93 (≠ V91), G94 (= G92), M143 (≠ S143), S145 (≠ F145), Y158 (= Y158), P188 (= P188), G189 (= G189), I191 (≠ T191), T193 (= T193)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
39% identity, 97% coverage: 3:249/255 of query aligns to 2:244/248 of 6ixmC
- active site: G16 (= G17), S142 (= S144), Y155 (= Y158), K159 (= K162)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), S15 (= S16), G16 (= G17), I17 (= I18), D36 (≠ A37), I37 (≠ R38), A61 (≠ G62), D62 (= D63), T63 (≠ V64), N89 (= N90), A90 (≠ V91), M140 (≠ T142), S142 (= S144), Y155 (= Y158), K159 (= K162), P185 (= P188), A186 (≠ G189), Y187 (≠ G190), I188 (≠ T191), L192 (≠ M195)
4wecA Crystal structure of a short chain dehydrogenase from mycobacterium smegmatis
39% identity, 97% coverage: 4:251/255 of query aligns to 8:251/258 of 4wecA
- active site: G21 (= G17), S143 (= S144), Q154 (≠ T155), Y157 (= Y158), K161 (= K162)
- binding nicotinamide-adenine-dinucleotide: G17 (= G13), A19 (≠ S15), S20 (= S16), G21 (= G17), I22 (= I18), D41 (≠ A37), I42 (≠ R38), V61 (≠ G62), D62 (= D63), V63 (= V64), N89 (= N90), T141 (= T142), Y157 (= Y158), K161 (= K162), P187 (= P188), P189 (≠ G190), V190 (≠ T191)
7djsD Crystal structure of isopiperitenol dehydrogenase from pseudomonas aeruginosa complexed with NAD
43% identity, 98% coverage: 3:251/255 of query aligns to 2:249/251 of 7djsD
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), G16 (= G17), I17 (= I18), D36 (≠ A37), L37 (≠ R38), C61 (≠ G62), D62 (= D63), V63 (= V64), N89 (= N90), A90 (≠ V91), T140 (= T142), S142 (= S144), Y155 (= Y158), K159 (= K162), A186 (≠ G189), V187 (≠ G190)
3ay6B Crystal structure of bacillus megaterium glucose dehydrogenase 4 a258f mutant in complex with nadh and d-glucose (see paper)
38% identity, 97% coverage: 4:251/255 of query aligns to 11:257/267 of 3ay6B
- active site: G24 (= G17), S151 (≠ F145), Y164 (= Y158), K168 (= K162)
- binding beta-D-glucopyranose: E102 (= E96), S151 (≠ F145), H153 (≠ G147), W158 (≠ F152), Y164 (= Y158), N202 (≠ G196), K205 (≠ F199)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G20 (= G13), T23 (≠ S16), G24 (= G17), L25 (≠ I18), Y45 (≠ R38), D71 (= D63), V72 (= V64), N98 (= N90), A99 (≠ V91), G100 (= G92), V101 (≠ I93), M149 (≠ S143), S151 (≠ F145), Y164 (= Y158), K168 (= K162), P194 (= P188), G195 (= G189), M197 (≠ T191), T199 (= T193), P200 (= P194), I201 (≠ M195), N202 (≠ G196)
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
37% identity, 96% coverage: 4:249/255 of query aligns to 5:251/255 of 5itvA
- active site: G18 (= G17), S141 (= S144), Y154 (= Y158), K158 (= K162)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), S17 (= S16), G18 (= G17), I19 (= I18), D38 (≠ A37), I39 (≠ R38), T61 (≠ G62), I63 (≠ V64), N89 (= N90), G91 (= G92), T139 (= T142), S141 (= S144), Y154 (= Y158), K158 (= K162), P184 (= P188), G185 (= G189), I186 (≠ G190), I187 (≠ T191)
5jc8D Crystal structure of a putative short-chain dehydrogenase/reductase from burkholderia xenovorans
39% identity, 97% coverage: 4:251/255 of query aligns to 4:258/262 of 5jc8D
4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
36% identity, 97% coverage: 3:249/255 of query aligns to 2:244/248 of 4urfB
- active site: G16 (= G17), S142 (= S144), I152 (≠ T155), Y155 (= Y158), K159 (= K162)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (= L215), R211 (≠ K216), R212 (= R217)
- binding bicarbonate ion: I92 (= I93), G94 (= G95), R109 (≠ N111), R179 (= R182), S228 (= S233)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), G14 (≠ S15), N15 (≠ S16), G16 (= G17), I17 (= I18), D36 (≠ A37), I37 (≠ R38), D62 (= D63), T63 (≠ V64), N89 (= N90), A90 (≠ V91), G91 (= G92), I140 (≠ T142), Y155 (= Y158), K159 (= K162), P185 (= P188), A186 (≠ G189), I188 (≠ T191), T190 (= T193)
4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
36% identity, 97% coverage: 3:249/255 of query aligns to 2:244/248 of 4urfA
- active site: G16 (= G17), S142 (= S144), I152 (≠ T155), Y155 (= Y158), K159 (= K162)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (= I93), S93 (≠ N94), G94 (= G95), E95 (= E96), T97 (≠ G98), E101 (≠ D102), T103 (≠ S105), Q106 (≠ E108), R109 (≠ N111), S175 (≠ A178), G177 (= G180)
- binding magnesium ion: S237 (≠ I242), Y238 (≠ A243)
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), G14 (≠ S15), N15 (≠ S16), G16 (= G17), I17 (= I18), D36 (≠ A37), I37 (≠ R38), W41 (≠ I42), D62 (= D63), T63 (≠ V64), N89 (= N90), A90 (≠ V91), G91 (= G92), I140 (≠ T142), Y155 (= Y158), K159 (= K162), P185 (= P188), I188 (≠ T191), T190 (= T193)
4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
36% identity, 97% coverage: 3:249/255 of query aligns to 2:244/248 of 4ureB
- active site: G16 (= G17), S142 (= S144), I152 (≠ T155), Y155 (= Y158), K159 (= K162)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (≠ S16), G16 (= G17), I17 (= I18), N89 (= N90), G91 (= G92), Y155 (= Y158), P185 (= P188), A186 (≠ G189)
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
40% identity, 98% coverage: 4:252/255 of query aligns to 5:253/254 of 4fn4A
- active site: G18 (= G17), S144 (= S144), Y157 (= Y158), K161 (= K162), S202 (≠ P203)
- binding nicotinamide-adenine-dinucleotide: G14 (= G13), S17 (= S16), G18 (= G17), I19 (= I18), E38 (≠ A37), L39 (≠ R38), R43 (≠ I42), A63 (≠ G62), D64 (= D63), V65 (= V64), N91 (= N90), G93 (= G92), I94 (= I93), T142 (= T142), S144 (= S144), Y157 (= Y158), K161 (= K162), P187 (= P188), V190 (≠ T191), T192 (= T193), N193 (≠ P194), I194 (≠ M195)
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)
35% identity, 96% coverage: 4:249/255 of query aligns to 30:273/278 of Q9BTZ2
- S176 (≠ G151) 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 (≠ T155) 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 (≠ S171) 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.
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)
36% identity, 96% coverage: 4:249/255 of query aligns to 31:274/279 of Q8WNV7
- 37:61 (vs. 10:34, 44% identical) binding
- F177 (= F152) 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 (≠ T155) 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 (= Y158) active site, Proton acceptor
- K187 (= K162) binding
- N196 (≠ S171) 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
3o4rA Crystal structure of human dehydrogenase/reductase (sdr family) member 4 (dhrs4)
35% identity, 96% coverage: 4:249/255 of query aligns to 6:249/254 of 3o4rA
- active site: G19 (= G17), S145 (= S144), F155 (≠ T155), Y158 (= Y158), K162 (= K162), K203 (≠ P203)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G13), T17 (≠ S15), D18 (≠ S16), G19 (= G17), I20 (= I18), S39 (≠ A37), R40 (= R38), K41 (≠ R39), N44 (≠ L46), H65 (≠ D66), V66 (≠ E67), N92 (= N90), A94 (≠ G92), S145 (= S144), Y158 (= Y158), K162 (= K162), P188 (= P188), G189 (= G189), L190 (≠ G190), I191 (≠ T191), T193 (= T193), F195 (≠ M195), S196 (≠ G196)
2zatA Crystal structure of a mammalian reductase (see paper)
36% identity, 96% coverage: 4:249/255 of query aligns to 3:246/251 of 2zatA
- active site: G16 (= G17), S142 (= S144), L152 (≠ T155), Y155 (= Y158), K159 (= K162), K200 (≠ P203)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A12 (≠ G13), T14 (≠ S15), D15 (≠ S16), G16 (= G17), I17 (= I18), S36 (≠ A37), R37 (= R38), K38 (≠ R39), N41 (≠ L46), H62 (≠ D66), N89 (= N90), A91 (≠ G92), V140 (≠ T142), S142 (= S144), Y155 (= Y158), K159 (= K162), P185 (= P188), G186 (= G189), I188 (≠ T191), T190 (= T193), F192 (≠ M195), S193 (≠ G196)
6zyzA Structure of the borneol dehydrogenases of salvia rosmarinus with NAD+ (see paper)
40% identity, 98% coverage: 4:252/255 of query aligns to 3:248/259 of 6zyzA
- binding nicotinamide-adenine-dinucleotide: G12 (= G13), S15 (= S16), G16 (= G17), I17 (= I18), D36 (≠ A37), I37 (≠ R38), Q38 (≠ R39), C58 (≠ G62), D59 (= D63), V60 (= V64), N86 (= N90), A87 (≠ V91), V90 (vs. gap), I110 (≠ T115), T137 (= T142), Y152 (= Y158), K156 (= K162), V185 (≠ T191)
- binding (2S)-1-[3-{[(2R)-2-hydroxypropyl]oxy}-2,2-bis({[(2R)-2-hydroxypropyl]oxy}methyl)propoxy]propan-2-ol: P93 (vs. gap), N94 (= N94), S95 (≠ G95), D98 (≠ G98)
5itvD Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
37% identity, 96% coverage: 4:249/255 of query aligns to 5:223/227 of 5itvD
- active site: G18 (= G17), S141 (= S144), Y154 (= Y158), K158 (= K162)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), S17 (= S16), G18 (= G17), I19 (= I18), D38 (≠ A37), I39 (≠ R38), T61 (≠ G62), D62 (= D63), I63 (≠ V64), N89 (= N90), T139 (= T142), S141 (= S144), Y154 (= Y158), K158 (= K162), P184 (= P188), G185 (= G189), I187 (≠ T191)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
37% identity, 98% coverage: 1:250/255 of query aligns to 2:242/244 of 4nbuB
- active site: G18 (= G17), N111 (= N116), S139 (= S144), Q149 (≠ T155), Y152 (= Y158), K156 (= K162)
- binding acetoacetyl-coenzyme a: D93 (≠ E96), K98 (≠ S101), S139 (= S144), N146 (≠ F152), V147 (≠ P153), Q149 (≠ T155), Y152 (= Y158), F184 (≠ G190), M189 (= M195), K200 (≠ N211)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), N17 (≠ S16), G18 (= G17), I19 (= I18), D38 (≠ A37), F39 (≠ R38), V59 (≠ G62), D60 (= D63), V61 (= V64), N87 (= N90), A88 (≠ V91), G89 (= G92), I90 (= I93), T137 (= T142), S139 (= S144), Y152 (= Y158), K156 (= K162), P182 (= P188), F184 (≠ G190), T185 (= T191), T187 (= T193), M189 (= M195)
Query Sequence
>7025539 FitnessBrowser__ANA3:7025539
MAVLQGKVAIITGASSGIGYATAKRFAREGAKLVLGARRGAILASLVDEIITQGGEAIYL
AGDVTDEVYASDLVALAVEQYGGLDIAFNNVGINGELGVDSDALSRAEWENTLTTNLTSA
FLAAKYQLPQMLKRGAGSIIFTSSFVGYTIGFPQTAAYAASKAGMIGLTQSLAVEYGARG
IRVNALLPGGTDTPMGREFANTPEAMAFVKNLHALKRLADPAEIAQSALYLASDAASFTT
GIALLVDGGVSICKT
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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