SitesBLAST
Comparing GFF3984 FitnessBrowser__Marino:GFF3984 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)
3o4rA Crystal structure of human dehydrogenase/reductase (sdr family) member 4 (dhrs4)
43% identity, 96% coverage: 8:251/255 of query aligns to 6:249/254 of 3o4rA
- active site: G19 (= G21), S145 (= S147), F155 (≠ I157), Y158 (= Y160), K162 (= K164), K203 (≠ P205)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G17), T17 (= T19), D18 (≠ K20), G19 (= G21), I20 (= I22), S39 (= S41), R40 (= R42), K41 (= K43), N44 (≠ A46), H65 (= H67), V66 (= V68), N92 (= N94), A94 (= A96), S145 (= S147), Y158 (= Y160), K162 (= K164), P188 (= P190), G189 (= G191), L190 (= L192), I191 (= I193), T193 (= T195), F195 (= F197), S196 (≠ A198)
2zatA Crystal structure of a mammalian reductase (see paper)
43% identity, 96% coverage: 8:251/255 of query aligns to 3:246/251 of 2zatA
- active site: G16 (= G21), S142 (= S147), L152 (≠ I157), Y155 (= Y160), K159 (= K164), K200 (≠ P205)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A12 (≠ G17), T14 (= T19), D15 (≠ K20), G16 (= G21), I17 (= I22), S36 (= S41), R37 (= R42), K38 (= K43), N41 (≠ A46), H62 (= H67), N89 (= N94), A91 (= A96), V140 (≠ L145), S142 (= S147), Y155 (= Y160), K159 (= K164), P185 (= P190), G186 (= G191), I188 (= I193), T190 (= T195), F192 (= F197), S193 (≠ A198)
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)
43% identity, 96% coverage: 8:251/255 of query aligns to 30:273/278 of Q9BTZ2
- S176 (≠ N154) 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 (≠ I157) 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 (≠ N173) 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)
43% identity, 96% coverage: 8:251/255 of query aligns to 31:274/279 of Q8WNV7
- 37:61 (vs. 14:38, 56% identical) binding NADP(+)
- F177 (≠ N154) 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 (≠ I157) 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 (= Y160) active site, Proton acceptor
- K187 (= K164) binding NADP(+)
- N196 (= N173) 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
5ojiA Crystal structure of the dehydrogenase/reductase sdr family member 4 (dhrs4) from caenorhabditis elegans (see paper)
39% identity, 95% coverage: 10:251/255 of query aligns to 10:255/260 of 5ojiA
- active site: G21 (= G21), S148 (= S147), Y161 (= Y160), K165 (= K164)
- binding isatin: S148 (= S147), S150 (≠ A149), Y161 (= Y160), V193 (≠ L192), S199 (≠ A198), L202 (= L201)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A17 (≠ G17), T19 (= T19), I22 (= I22), S41 (= S41), R42 (= R42), N43 (≠ K43), N46 (≠ A46), I69 (≠ V68), N95 (= N94), H96 (≠ A95), G97 (≠ A96), N146 (≠ L145), S148 (= S147), Y161 (= Y160), K165 (= K164), G192 (= G191), I194 (= I193), T196 (= T195), M198 (≠ F197)
5ojgA Crystal structure of the dehydrogenase/reductase sdr family member 4 (dhrs4) from caenorhabditis elegans (see paper)
39% identity, 95% coverage: 10:251/255 of query aligns to 10:255/260 of 5ojgA
- active site: G21 (= G21), S148 (= S147), Y161 (= Y160), K165 (= K164)
- binding butane-2,3-dione: S148 (= S147), Y161 (= Y160)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A17 (≠ G17), T19 (= T19), G21 (= G21), I22 (= I22), S41 (= S41), R42 (= R42), N43 (≠ K43), N46 (≠ A46), I69 (≠ V68), N95 (= N94), H96 (≠ A95), G97 (≠ A96), N146 (≠ L145), S148 (= S147), Y161 (= Y160), K165 (= K164), P191 (= P190), I194 (= I193), T196 (= T195), M198 (≠ F197)
Q9S9W2 Short-chain dehydrogenase/reductase SDRA; Protein INDOLE-3-BUTYRIC ACID RESPONSE 1; Short-chain dehydrogenase/reductase A; EC 1.1.-.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
39% identity, 96% coverage: 8:251/255 of query aligns to 9:249/254 of Q9S9W2
- R43 (= R42) mutation to C: In ibr1-1; resistance to the inhibitory effect of intermediate levels of indole-3-butyric acid (IBA) on root elongation.
- S140 (≠ A141) mutation to F: In ibr1-8; resistance to the inhibitory effect of intermediate levels of indole-3-butyric acid (IBA) on root elongation.
A7DY56 Tropinone reductase; EC 1.1.1.206; EC 1.1.1.236 from Cochlearia officinalis (Common scurvygrass) (see paper)
33% identity, 97% coverage: 7:254/255 of query aligns to 15:262/273 of A7DY56
- Y209 (≠ L201) mutation to S: Loss of tropinone or nortropinone reduction, but faster reduction of cyclohexanones.
1vl8B Crystal structure of gluconate 5-dehydrogenase (tm0441) from thermotoga maritima at 2.07 a resolution
35% identity, 98% coverage: 5:253/255 of query aligns to 1:250/252 of 1vl8B
- active site: G17 (= G21), S143 (= S147), I154 (= I157), Y157 (= Y160), K161 (= K164)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G17), R16 (≠ K20), G17 (= G21), L18 (≠ I22), S37 (= S41), R38 (= R42), C63 (= C66), D64 (≠ H67), V65 (= V68), A91 (≠ N94), A92 (= A95), G93 (≠ A96), I94 (≠ T97), V114 (≠ T118), I141 (≠ L145), S143 (= S147), Y157 (= Y160), K161 (= K164), P187 (= P190), G188 (= G191), Y190 (≠ I193), T192 (= T195), M194 (≠ F197), T195 (≠ A198)
Q9ZW19 Tropinone reductase homolog At2g29360; EC 1.1.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 99% coverage: 2:254/255 of query aligns to 10:262/271 of Q9ZW19
- S209 (≠ L201) mutation to Y: Loss of activity with quinuclidinone and decreased activity with cyclohexanones.
4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
32% identity, 97% coverage: 8:255/255 of query aligns to 5:254/254 of 4fn4A
- active site: G18 (= G21), S144 (= S147), Y157 (= Y160), K161 (= K164), S202 (≠ P205)
- binding nicotinamide-adenine-dinucleotide: G14 (= G17), S17 (≠ K20), G18 (= G21), I19 (= I22), E38 (≠ S41), L39 (≠ R42), R43 (≠ A46), A63 (≠ C66), D64 (≠ H67), V65 (= V68), N91 (= N94), G93 (≠ A96), I94 (≠ T97), T142 (≠ L145), S144 (= S147), Y157 (= Y160), K161 (= K164), P187 (= P190), V190 (≠ I193), T192 (= T195), N193 (≠ D196), I194 (≠ F197)
1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
36% identity, 97% coverage: 7:253/255 of query aligns to 4:251/261 of 1g6kA
- active site: G18 (= G21), S145 (= S147), Y158 (= Y160), K162 (= K164)
- binding nicotinamide-adenine-dinucleotide: T17 (≠ K20), G18 (= G21), L19 (≠ I22), R39 (= R42), D65 (≠ H67), V66 (= V68), N92 (= N94), A93 (= A95), G94 (≠ A96), M143 (≠ L145), S145 (= S147), Y158 (= Y160), P188 (= P190), G189 (= G191), I191 (= I193), T193 (= T195)
P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
36% identity, 97% coverage: 7:253/255 of query aligns to 4:251/261 of P40288
- 11:35 (vs. 14:38, 52% identical) binding NADP(+)
- E96 (≠ T97) mutation E->A,G,K: Heat stable.
- D108 (≠ A111) mutation to N: Heat stable.
- V112 (≠ I115) mutation to A: Heat stable.
- E133 (= E136) mutation to K: Heat stable.
- V183 (≠ I185) mutation to I: Heat stable.
- P194 (≠ D196) mutation to Q: Heat stable.
- E210 (= E212) mutation to K: Heat stable.
- Y217 (≠ R219) 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.
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
37% identity, 96% coverage: 8:251/255 of query aligns to 3:244/247 of 4jroC
- active site: G16 (= G21), S142 (= S147), Q152 (≠ I157), Y155 (= Y160), K159 (= K164)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G17), S14 (≠ T19), R15 (≠ K20), G16 (= G21), I17 (= I22), N35 (≠ S40), Y36 (≠ S41), N37 (≠ R42), G38 (≠ K43), S39 (≠ A44), N63 (≠ H67), V64 (= V68), N90 (= N94), A91 (= A95), I93 (≠ T97), I113 (≠ T118), S142 (= S147), Y155 (= Y160), K159 (= K164), P185 (= P190), I188 (= I193), T190 (= T195)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
36% identity, 95% coverage: 11:251/255 of query aligns to 5:243/246 of 3osuA
8w0oA Gdh-105 crystal structure
35% identity, 98% coverage: 7:255/255 of query aligns to 4:253/259 of 8w0oA
- binding nicotinamide-adenine-dinucleotide: G14 (= G17), S17 (≠ K20), G18 (= G21), L19 (≠ I22), Y39 (vs. gap), Q43 (≠ A44), D65 (≠ H67), V66 (= V68), N92 (= N94), A93 (= A95), G94 (≠ A96), M143 (≠ L145), Y158 (= Y160), K162 (= K164), P188 (= P190), G189 (= G191), I191 (= I193), T193 (= T195)
8hsaA Brucella melitensis 7-alpha-hydroxysteroid dehydrogenase mutant: 1-53 truncation/m196i/i258m/k262t-NAD+
40% identity, 96% coverage: 6:251/255 of query aligns to 3:245/248 of 8hsaA
- binding nicotinamide-adenine-dinucleotide: G14 (= G17), I19 (= I22), D38 (≠ S41), L39 (≠ R42), C63 (= C66), N64 (≠ H67), V65 (= V68), N91 (= N94), A92 (= A95), G93 (≠ A96), I140 (≠ L145), S141 (= S146), Y155 (= Y160), K159 (= K164), P185 (= P190), G186 (= G191)
2ae2A Tropinone reductase-ii complexed with NADP+ and pseudotropine (see paper)
32% identity, 96% coverage: 6:251/255 of query aligns to 4:252/259 of 2ae2A
- active site: G19 (= G21), S145 (= S147), Y158 (= Y160), K162 (= K164)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G17), S17 (≠ T19), R18 (≠ K20), G19 (= G21), I20 (= I22), S39 (= S41), R40 (= R42), C64 (= C66), L66 (≠ V68), N93 (= N94), G95 (≠ A96), I116 (≠ T118), I143 (≠ L145), S145 (= S147), Y158 (= Y160), K162 (= K164), P188 (= P190), G189 (= G191), V190 (≠ L192), I191 (= I193), T193 (= T195), S194 (≠ D196), L195 (≠ F197), V196 (≠ A198)
- binding pseudotropine: S145 (= S147), E155 (≠ I157), Y158 (= Y160), L195 (≠ F197)
1ipfA Tropinone reductase-ii complexed with NADPH and tropinone (see paper)
32% identity, 96% coverage: 6:251/255 of query aligns to 4:252/259 of 1ipfA
- active site: G19 (= G21), S145 (= S147), Y158 (= Y160), K162 (= K164)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G17), R18 (≠ K20), G19 (= G21), I20 (= I22), S39 (= S41), R40 (= R42), C64 (= C66), D65 (≠ H67), L66 (≠ V68), N93 (= N94), S145 (= S147), Y158 (= Y160), K162 (= K164), P188 (= P190), V190 (≠ L192), I191 (= I193), T193 (= T195), S194 (≠ D196), L195 (≠ F197), V196 (≠ A198)
- binding 8-methyl-8-azabicyclo[3,2,1]octan-3-one: S147 (≠ A149), E155 (≠ I157), Y158 (= Y160)
1ipeA Tropinone reductase-ii complexed with NADPH (see paper)
32% identity, 96% coverage: 6:251/255 of query aligns to 4:252/259 of 1ipeA
- active site: G19 (= G21), S145 (= S147), Y158 (= Y160), K162 (= K164)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G17), S17 (≠ T19), R18 (≠ K20), G19 (= G21), I20 (= I22), S39 (= S41), R40 (= R42), C64 (= C66), D65 (≠ H67), L66 (≠ V68), N93 (= N94), I116 (≠ T118), S145 (= S147), Y158 (= Y160), K162 (= K164), P188 (= P190), I191 (= I193), T193 (= T195), S194 (≠ D196), L195 (≠ F197), V196 (≠ A198)
Query Sequence
>GFF3984 FitnessBrowser__Marino:GFF3984
MNNPLFDMTGKVAVITGSTKGIGRAIAGEMAVCGAKVVISSRKAEACEQMAEELKAQGFE
AMAIPCHVGRKEDLQNLVKKTNEAWGSIDVLVCNAATNPVYGPTAEMTDDAWDKIMDTNV
KSTFWLTNMVLPQMAEKGEGAVVLLSSIAGLRGNTVIGTYGVSKAAEAALARNLAVEWGP
KGIRINSIAPGLIKTDFARALWEDPERAKQAEDRTPLRRIGDPVDIAGLAVFLSTKASAY
ITGQVIVADGGETIC
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