SitesBLAST
Comparing Echvi_3364 FitnessBrowser__Cola:Echvi_3364 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)
42% identity, 97% coverage: 9:255/255 of query aligns to 6:252/254 of 3o4rA
- active site: G19 (= G22), S145 (= S148), F155 (≠ L158), Y158 (= Y161), K162 (= K165), K203 (≠ D206)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G18), T17 (≠ S20), D18 (≠ K21), G19 (= G22), I20 (= I23), S39 (= S42), R40 (= R43), K41 (≠ H44), N44 (≠ H47), H65 (≠ N68), V66 (= V69), N92 (= N95), A94 (≠ G97), S145 (= S148), Y158 (= Y161), K162 (= K165), P188 (= P191), G189 (= G192), L190 (≠ I193), I191 (= I194), T193 (= T196), F195 (= F198), S196 (= S199)
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)
42% identity, 97% coverage: 9:255/255 of query aligns to 30:276/278 of Q9BTZ2
- S176 (≠ E155) 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 (≠ L158) 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 (≠ V174) 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.
2zatA Crystal structure of a mammalian reductase (see paper)
43% identity, 97% coverage: 9:255/255 of query aligns to 3:249/251 of 2zatA
- active site: G16 (= G22), S142 (= S148), L152 (= L158), Y155 (= Y161), K159 (= K165), K200 (≠ D206)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A12 (≠ G18), T14 (≠ S20), D15 (≠ K21), G16 (= G22), I17 (= I23), S36 (= S42), R37 (= R43), K38 (≠ H44), N41 (≠ H47), H62 (≠ N68), N89 (= N95), A91 (≠ G97), V140 (≠ I146), S142 (= S148), Y155 (= Y161), K159 (= K165), P185 (= P191), G186 (= G192), I188 (= I194), T190 (= T196), F192 (= F198), S193 (= S199)
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, 97% coverage: 9:255/255 of query aligns to 31:277/279 of Q8WNV7
- 37:61 (vs. 15:39, 52% identical) binding
- F177 (≠ E155) 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 (= L158) 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 (= Y161) active site, Proton acceptor
- K187 (= K165) binding
- N196 (≠ V174) 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
1vl8B Crystal structure of gluconate 5-dehydrogenase (tm0441) from thermotoga maritima at 2.07 a resolution
39% identity, 98% coverage: 6:255/255 of query aligns to 1:251/252 of 1vl8B
- active site: G17 (= G22), S143 (≠ A151), I154 (≠ L158), Y157 (= Y161), K161 (= K165)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G18), R16 (≠ K21), G17 (= G22), L18 (≠ I23), S37 (= S42), R38 (= R43), C63 (= C67), D64 (≠ N68), V65 (= V69), A91 (≠ N95), A92 (= A96), G93 (= G97), I94 (≠ T98), V114 (= V119), I141 (= I146), S143 (≠ A151), Y157 (= Y161), K161 (= K165), P187 (= P191), G188 (= G192), Y190 (≠ I194), T192 (= T196), M194 (≠ F198), T195 (≠ S199)
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)
41% identity, 97% coverage: 9:255/255 of query aligns to 9:252/254 of Q9S9W2
- R43 (= R43) mutation to C: In ibr1-1; resistance to the inhibitory effect of intermediate levels of indole-3-butyric acid (IBA) on root elongation.
- S140 (= S142) mutation to F: In ibr1-8; resistance to the inhibitory effect of intermediate levels of indole-3-butyric acid (IBA) on root elongation.
5ojiA Crystal structure of the dehydrogenase/reductase sdr family member 4 (dhrs4) from caenorhabditis elegans (see paper)
39% identity, 98% coverage: 4:252/255 of query aligns to 3:255/260 of 5ojiA
- active site: G21 (= G22), S148 (= S148), Y161 (= Y161), K165 (= K165)
- binding isatin: S148 (= S148), S150 (≠ G150), Y161 (= Y161), V193 (≠ I193), S199 (= S199), L202 (= L202)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A17 (≠ G18), T19 (≠ S20), I22 (= I23), S41 (= S42), R42 (= R43), N43 (≠ H44), N46 (≠ H47), I69 (≠ V69), N95 (= N95), H96 (≠ A96), G97 (= G97), N146 (≠ I146), S148 (= S148), Y161 (= Y161), K165 (= K165), G192 (= G192), I194 (= I194), T196 (= T196), M198 (≠ F198)
5ojgA Crystal structure of the dehydrogenase/reductase sdr family member 4 (dhrs4) from caenorhabditis elegans (see paper)
39% identity, 98% coverage: 4:252/255 of query aligns to 3:255/260 of 5ojgA
- active site: G21 (= G22), S148 (= S148), Y161 (= Y161), K165 (= K165)
- binding butane-2,3-dione: S148 (= S148), Y161 (= Y161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A17 (≠ G18), T19 (≠ S20), G21 (= G22), I22 (= I23), S41 (= S42), R42 (= R43), N43 (≠ H44), N46 (≠ H47), I69 (≠ V69), N95 (= N95), H96 (≠ A96), G97 (= G97), N146 (≠ I146), S148 (= S148), Y161 (= Y161), K165 (= K165), P191 (= P191), I194 (= I194), T196 (= T196), M198 (≠ F198)
5fffA Noroxomaritidine/norcraugsodine reductase in complex with NADP+ and piperonal (see paper)
38% identity, 100% coverage: 1:254/255 of query aligns to 1:254/257 of 5fffA
- active site: K206 (≠ D206)
- binding 1,3-benzodioxole-5-carbaldehyde: Y100 (= Y101), H158 (≠ L158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G18), T20 (≠ S20), G22 (= G22), I23 (= I23), R43 (= R43), C67 (= C67), D68 (≠ N68), V69 (= V69), N96 (= N95), I146 (= I146), Y161 (= Y161), K165 (= K165), P191 (= P191), A193 (≠ I193), I194 (= I194), T196 (= T196), G198 (≠ F198), T199 (≠ S199)
5ff9B Noroxomaritidine/norcraugsodine reductase in complex with NADP+ and tyramine (see paper)
38% identity, 100% coverage: 1:254/255 of query aligns to 1:254/257 of 5ff9B
- active site: K206 (≠ D206)
- binding 4-(2-aminoethyl)phenol: Y100 (= Y101), I155 (≠ E155), H158 (≠ L158)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G18), T20 (≠ S20), K21 (= K21), I23 (= I23), S42 (= S42), R43 (= R43), C67 (= C67), D68 (≠ N68), V69 (= V69), N96 (= N95), I146 (= I146), S148 (= S148), Y161 (= Y161), K165 (= K165), P191 (= P191), A193 (≠ I193), I194 (= I194), T196 (= T196), G198 (≠ F198), T199 (≠ S199)
A0A1A9TAK5 Noroxomaritidine/norcraugsodine reductase; NorRed; EC 1.1.1.- from Narcissus pseudonarcissus (Daffodil) (see paper)
38% identity, 100% coverage: 1:254/255 of query aligns to 1:254/257 of A0A1A9TAK5
P50162 Tropinone reductase 1; Tropine dehydrogenase; Tropinone reductase I; TR-I; EC 1.1.1.206 from Datura stramonium (Jimsonweed) (Common thornapple) (see paper)
38% identity, 98% coverage: 7:255/255 of query aligns to 17:269/273 of P50162
- 25:49 (vs. 15:39, 56% identical) binding
- S158 (= S148) binding
- Y171 (= Y161) active site, Proton acceptor
1ae1B Tropinone reductase-i complex with NADP (see paper)
38% identity, 98% coverage: 7:255/255 of query aligns to 2:254/258 of 1ae1B
- active site: G17 (= G22), S143 (= S148), V153 (≠ L158), Y156 (= Y161), K160 (= K165)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G18), S15 (= S20), K16 (= K21), G17 (= G22), I18 (= I23), S37 (= S42), R38 (= R43), C62 (= C67), D63 (≠ N68), L64 (≠ V69), N91 (= N95), A92 (= A96), S143 (= S148), Y156 (= Y161), K160 (= K165), P186 (= P191), I189 (= I194), T191 (vs. gap), L193 (vs. gap), V194 (vs. gap)
P50163 Tropinone reductase 2; Tropinone reductase II; TR-II; EC 1.1.1.236 from Datura stramonium (Jimsonweed) (Common thornapple) (see paper)
33% identity, 99% coverage: 3:255/255 of query aligns to 1:256/260 of P50163
- 18:41 (vs. 20:43, 54% identical) binding
- S146 (= S148) binding
- IATSL 192:196 (≠ IKTNF 194:198) binding
Q9ZW19 Tropinone reductase homolog At2g29360; EC 1.1.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 97% coverage: 7:254/255 of query aligns to 14:261/271 of Q9ZW19
- S209 (≠ L202) mutation to Y: Loss of activity with quinuclidinone and decreased activity with cyclohexanones.
2ae2A Tropinone reductase-ii complexed with NADP+ and pseudotropine (see paper)
34% identity, 98% coverage: 7:255/255 of query aligns to 4:255/259 of 2ae2A
- active site: G19 (= G22), S145 (= S148), Y158 (= Y161), K162 (= K165)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G18), S17 (= S20), R18 (≠ K21), G19 (= G22), I20 (= I23), S39 (= S42), R40 (= R43), C64 (= C67), L66 (≠ V69), N93 (= N95), G95 (= G97), I116 (≠ V119), I143 (= I146), S145 (= S148), Y158 (= Y161), K162 (= K165), P188 (= P191), G189 (= G192), V190 (≠ I193), I191 (= I194), T193 (= T196), S194 (≠ N197), L195 (≠ F198), V196 (≠ S199)
- binding pseudotropine: S145 (= S148), E155 (≠ L158), Y158 (= Y161), L195 (≠ F198)
1ipfA Tropinone reductase-ii complexed with NADPH and tropinone (see paper)
34% identity, 98% coverage: 7:255/255 of query aligns to 4:255/259 of 1ipfA
- active site: G19 (= G22), S145 (= S148), Y158 (= Y161), K162 (= K165)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G18), R18 (≠ K21), G19 (= G22), I20 (= I23), S39 (= S42), R40 (= R43), C64 (= C67), D65 (≠ N68), L66 (≠ V69), N93 (= N95), S145 (= S148), Y158 (= Y161), K162 (= K165), P188 (= P191), V190 (≠ I193), I191 (= I194), T193 (= T196), S194 (≠ N197), L195 (≠ F198), V196 (≠ S199)
- binding 8-methyl-8-azabicyclo[3,2,1]octan-3-one: S147 (≠ G150), E155 (≠ L158), Y158 (= Y161)
1ipeA Tropinone reductase-ii complexed with NADPH (see paper)
34% identity, 98% coverage: 7:255/255 of query aligns to 4:255/259 of 1ipeA
- active site: G19 (= G22), S145 (= S148), Y158 (= Y161), K162 (= K165)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G18), S17 (= S20), R18 (≠ K21), G19 (= G22), I20 (= I23), S39 (= S42), R40 (= R43), C64 (= C67), D65 (≠ N68), L66 (≠ V69), N93 (= N95), I116 (≠ V119), S145 (= S148), Y158 (= Y161), K162 (= K165), P188 (= P191), I191 (= I194), T193 (= T196), S194 (≠ N197), L195 (≠ F198), V196 (≠ S199)
A7DY56 Tropinone reductase; EC 1.1.1.206; EC 1.1.1.236 from Cochlearia officinalis (Common scurvygrass) (see paper)
35% identity, 98% coverage: 5:254/255 of query aligns to 12:261/273 of A7DY56
- Y209 (≠ L202) mutation to S: Loss of tropinone or nortropinone reduction, but faster reduction of cyclohexanones.
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
34% identity, 97% coverage: 9:255/255 of query aligns to 3:247/248 of 6ixmC
- active site: G16 (= G22), S142 (= S148), Y155 (= Y161), K159 (= K165)
- binding nicotinamide-adenine-dinucleotide: G12 (= G18), S15 (≠ K21), G16 (= G22), I17 (= I23), D36 (≠ S42), I37 (≠ R43), A61 (≠ C67), D62 (≠ N68), T63 (≠ V69), N89 (= N95), A90 (= A96), M140 (≠ I146), S142 (= S148), Y155 (= Y161), K159 (= K165), P185 (= P191), A186 (≠ G192), Y187 (≠ I193), I188 (= I194), L192 (≠ F198)
Query Sequence
>Echvi_3364 FitnessBrowser__Cola:Echvi_3364
MDLSSLFSLNNKVALITGASKGIGLSIAEFFAAAGAKVVICSRHQEHLDEIAKKLYEKGY
DIMGIACNVGRPNELVQLVEKTIEAYGQIDILVNNAGTNPYMGPVHETTLELFDKIMDVN
VKAPFELSKLCLPHLRKSSQASIINISSIGALSPEPQLGIYSVSKSALHSLTKVCAKEWG
QQKIRVNAICPGIIKTNFSKALWGNDQIMDVIMKRLAIKRLGKTEEIAALALFLASPAAS
YISGSIFTVDGGFTS
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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