SitesBLAST
Comparing 3608847 FitnessBrowser__Dino:3608847 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)
1vl8B Crystal structure of gluconate 5-dehydrogenase (tm0441) from thermotoga maritima at 2.07 a resolution
41% identity, 97% coverage: 8:250/250 of query aligns to 2:252/252 of 1vl8B
- active site: G17 (= G23), S143 (= S142), I154 (≠ R152), Y157 (= Y155), K161 (= K159)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G19), R16 (= R22), G17 (= G23), L18 (≠ I24), S37 (≠ A43), R38 (= R44), C63 (vs. gap), D64 (= D69), V65 (≠ I70), A91 (≠ S92), A92 (= A93), G93 (= G94), I94 (≠ L95), V114 (= V115), I141 (= I140), S143 (= S142), Y157 (= Y155), K161 (= K159), P187 (= P185), G188 (≠ T186), Y190 (≠ I188), T192 (= T190), M194 (≠ L192), T195 (= T193)
3d3wA Structure of l-xylulose reductase with bound coenzyme, phosphate and hydroxide. (see paper)
39% identity, 95% coverage: 10:247/250 of query aligns to 5:241/244 of 3d3wA
- active site: G18 (= G23), S136 (= S142), H146 (≠ R152), Y149 (= Y155), K153 (= K159)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G14 (= G19), G16 (≠ S21), K17 (≠ R22), G18 (= G23), I19 (= I24), S38 (≠ A43), R39 (= R44), T40 (≠ G45), V59 (≠ L68), L61 (≠ I70), N83 (≠ S92), A84 (= A93), A85 (≠ G94), V106 (= V115), V134 (≠ I140), S135 (= S141), S136 (= S142), Y149 (= Y155), K153 (= K159), P179 (= P185), T180 (= T186), V182 (≠ I188), T184 (= T190), S185 (≠ P191), M186 (≠ L192), G187 (≠ T193)
1pr9A Human l-xylulose reductase holoenzyme (see paper)
39% identity, 95% coverage: 10:247/250 of query aligns to 5:241/244 of 1pr9A
- active site: G18 (= G23), S136 (= S142), H146 (≠ R152), Y149 (= Y155), K153 (= K159)
- binding dihydrogenphosphate ion: S136 (= S142), C138 (≠ M144)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G14 (= G19), G16 (≠ S21), K17 (≠ R22), G18 (= G23), I19 (= I24), S38 (≠ A43), R39 (= R44), T40 (≠ G45), L61 (≠ I70), N83 (≠ S92), A85 (≠ G94), V106 (= V115), V134 (≠ I140), Y149 (= Y155), K153 (= K159), T180 (= T186), V182 (≠ I188), T184 (= T190), M186 (≠ L192)
Q7Z4W1 L-xylulose reductase; XR; Carbonyl reductase II; Dicarbonyl/L-xylulose reductase; Kidney dicarbonyl reductase; kiDCR; Short chain dehydrogenase/reductase family 20C member 1; Sperm surface protein P34H; EC 1.1.1.10 from Homo sapiens (Human) (see 2 papers)
39% identity, 95% coverage: 10:247/250 of query aligns to 5:241/244 of Q7Z4W1
- 11:40 (vs. 16:45, 53% identical) binding
- N107 (= N116) mutation N->L,D: Loss of function. Probably due to defects in formation of the active site and binding of coenzyme.
- S136 (= S142) binding
- K153 (= K159) binding
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
Q920P0 L-xylulose reductase; XR; Dicarbonyl/L-xylulose reductase; EC 1.1.1.10 from Rattus norvegicus (Rat) (see paper)
39% identity, 95% coverage: 10:247/250 of query aligns to 5:241/244 of Q920P0
- S136 (= S142) mutation to A: Loss of activity.
- Q137 (= Q143) mutation to M: Slightly reduced activity. Loss of activity for sugars; when associated with F-143 and L-146.
- L143 (≠ G149) mutation to F: Slightly reduced activity. Loss of activity for sugars; when associated with M-137 and L-146.
- H146 (≠ R152) mutation to L: Slightly reduced activity. Loss of activity for sugars; when associated with M-137; F-143 and L-146.
- Y149 (= Y155) mutation to F: Loss of activity.
- K153 (= K159) mutation to M: Loss of activity.
- N190 (≠ T196) mutation to V: Slightly reduced activity. Loss of activity for sugars; when associated with S-191.
- W191 (≠ F197) mutation to F: Slightly reduced activity.; mutation to S: Slightly reduced activity. Loss of activity for sugars; when associated with V-190.
4hp8B Crystal structure of a putative 2-deoxy-d-gluconate 3-dehydrogenase from agrobacterium tumefaciens (target efi-506435) with bound NADP
41% identity, 96% coverage: 8:247/250 of query aligns to 4:243/246 of 4hp8B
- active site: G19 (= G23), S138 (= S142), V148 (≠ R152), Y151 (= Y155), K155 (= K159)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G19), N17 (≠ S21), T18 (≠ R22), G19 (= G23), L20 (≠ I24), R40 (= R44), R41 (≠ G45), D63 (= D69), F64 (≠ I70), N85 (≠ S92), G87 (= G94), I88 (≠ L95), I136 (= I140), Y151 (= Y155), K155 (= K159), P181 (= P185), G182 (≠ T186), I184 (= I188), T186 (= T190), N188 (≠ L192), T189 (= T193)
P08074 Carbonyl reductase [NADPH] 2; Adipocyte protein P27; AP27; Lung carbonyl reductase; LCR; NADPH-dependent carbonyl reductase 2; EC 1.1.1.184 from Mus musculus (Mouse) (see 2 papers)
38% identity, 96% coverage: 8:247/250 of query aligns to 3:241/244 of P08074
- 11:39 (vs. 16:44, 52% identical) binding
- T38 (≠ A43) mutation to R: Converts the coenzyme specificity from NADP to NAD.
1cydA Carbonyl reductase complexed with NADPH and 2-propanol (see paper)
38% identity, 96% coverage: 8:247/250 of query aligns to 1:239/242 of 1cydA
- active site: G16 (= G23), S134 (= S142), L144 (≠ R152), Y147 (= Y155), K151 (= K159)
- binding isopropyl alcohol: S134 (= S142), Y147 (= Y155), V188 (≠ T196)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G19), G14 (≠ S21), K15 (≠ R22), I17 (= I24), R37 (= R44), T38 (≠ G45), D58 (= D69), L59 (≠ I70), N81 (≠ S92), A83 (≠ G94), V104 (= V115), V132 (≠ I140), S134 (= S142), Y147 (= Y155), K151 (= K159), P177 (= P185), T178 (= T186), V179 (≠ F187), V180 (≠ I188), T182 (= T190), M184 (≠ L192), G185 (≠ T193)
2ae2A Tropinone reductase-ii complexed with NADP+ and pseudotropine (see paper)
37% identity, 96% coverage: 8:246/250 of query aligns to 4:252/259 of 2ae2A
- active site: G19 (= G23), S145 (= S142), Y158 (= Y155), K162 (= K159)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G19), S17 (= S21), R18 (= R22), G19 (= G23), I20 (= I24), S39 (≠ A43), R40 (= R44), C64 (≠ L68), L66 (≠ I70), N93 (≠ S92), G95 (= G94), I116 (≠ V115), I143 (= I140), S145 (= S142), Y158 (= Y155), K162 (= K159), P188 (= P185), G189 (≠ T186), V190 (≠ F187), I191 (= I188), T193 (= T190), S194 (≠ P191), L195 (= L192), V196 (≠ T193)
- binding pseudotropine: S145 (= S142), E155 (≠ R152), Y158 (= Y155), L195 (= L192)
1ipfA Tropinone reductase-ii complexed with NADPH and tropinone (see paper)
37% identity, 96% coverage: 8:246/250 of query aligns to 4:252/259 of 1ipfA
- active site: G19 (= G23), S145 (= S142), Y158 (= Y155), K162 (= K159)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G19), R18 (= R22), G19 (= G23), I20 (= I24), S39 (≠ A43), R40 (= R44), C64 (≠ L68), D65 (= D69), L66 (≠ I70), N93 (≠ S92), S145 (= S142), Y158 (= Y155), K162 (= K159), P188 (= P185), V190 (≠ F187), I191 (= I188), T193 (= T190), S194 (≠ P191), L195 (= L192), V196 (≠ T193)
- binding 8-methyl-8-azabicyclo[3,2,1]octan-3-one: S147 (≠ M144), E155 (≠ R152), Y158 (= Y155)
1ipeA Tropinone reductase-ii complexed with NADPH (see paper)
37% identity, 96% coverage: 8:246/250 of query aligns to 4:252/259 of 1ipeA
- active site: G19 (= G23), S145 (= S142), Y158 (= Y155), K162 (= K159)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G19), S17 (= S21), R18 (= R22), G19 (= G23), I20 (= I24), S39 (≠ A43), R40 (= R44), C64 (≠ L68), D65 (= D69), L66 (≠ I70), N93 (≠ S92), I116 (≠ V115), S145 (= S142), Y158 (= Y155), K162 (= K159), P188 (= P185), I191 (= I188), T193 (= T190), S194 (≠ P191), L195 (= L192), V196 (≠ T193)
P50163 Tropinone reductase 2; Tropinone reductase II; TR-II; EC 1.1.1.236 from Datura stramonium (Jimsonweed) (Common thornapple) (see paper)
37% identity, 96% coverage: 8:246/250 of query aligns to 5:253/260 of P50163
- 18:41 (vs. 21:44, 50% identical) binding
- S146 (= S142) binding
- IATSL 192:196 (≠ IRTPL 188:192) binding
3uf0A Crystal structure of a putative NAD(p) dependent gluconate 5- dehydrogenase from beutenbergia cavernae(efi target efi-502044) with bound NADP (low occupancy)
41% identity, 96% coverage: 8:247/250 of query aligns to 3:246/249 of 3uf0A
- active site: G18 (= G23), S141 (= S142), V151 (≠ R152), Y154 (= Y155), K158 (= K159)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G14 (= G19), S17 (≠ R22), G18 (= G23), I19 (= I24), R39 (= R44), D63 (= D69), L64 (≠ I70), N89 (≠ S92), G91 (= G94), I92 (≠ L95), I139 (= I140), A140 (≠ S141), S141 (= S142), Y154 (= Y155), K158 (= K159), P184 (= P185), G185 (≠ T186), V187 (≠ I188), T189 (= T190), N191 (≠ L192), T192 (= T193)
5u9pB Crystal structure of a gluconate 5-dehydrogenase from burkholderia cenocepacia j2315 in complex with NADP and tartrate
38% identity, 97% coverage: 8:249/250 of query aligns to 12:259/261 of 5u9pB
- active site: G27 (= G23), S152 (= S142), Y165 (= Y155), K169 (= K159)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G23 (= G19), R26 (= R22), G27 (= G23), I28 (= I24), R48 (= R44), D73 (= D69), V74 (≠ I70), N100 (≠ S92), A101 (= A93), I150 (= I140), Y165 (= Y155), K169 (= K159), P195 (= P185), F198 (≠ I188), T200 (= T190), L202 (= L192), N203 (≠ T193)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
38% identity, 95% coverage: 10:246/250 of query aligns to 3:244/247 of 4jroC
- active site: G16 (= G23), S142 (= S142), Q152 (≠ R152), Y155 (= Y155), K159 (= K159)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G19), S14 (= S21), R15 (= R22), G16 (= G23), I17 (= I24), N35 (≠ A42), Y36 (≠ A43), N37 (≠ R44), G38 (= G45), S39 (≠ Q46), N63 (≠ D69), V64 (≠ I70), N90 (≠ S92), A91 (= A93), I93 (≠ L95), I113 (≠ V115), S142 (= S142), Y155 (= Y155), K159 (= K159), P185 (= P185), I188 (= I188), T190 (= T190)
A7DY56 Tropinone reductase; EC 1.1.1.206; EC 1.1.1.236 from Cochlearia officinalis (Common scurvygrass) (see paper)
35% identity, 96% coverage: 8:248/250 of query aligns to 14:261/273 of A7DY56
- Y209 (≠ T196) mutation to S: Loss of tropinone or nortropinone reduction, but faster reduction of cyclohexanones.
Q9ZW19 Tropinone reductase homolog At2g29360; EC 1.1.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 97% coverage: 6:248/250 of query aligns to 12:261/271 of Q9ZW19
- S209 (≠ T196) mutation to Y: Loss of activity with quinuclidinone and decreased activity with cyclohexanones.
5t2uA Short chain dehydrogenase/reductase family protein (see paper)
39% identity, 95% coverage: 9:246/250 of query aligns to 3:237/241 of 5t2uA
- active site: G17 (= G23), T135 (≠ S142), T145 (≠ R152), Y148 (= Y155), K152 (= K159)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G19), G17 (= G23), R38 (= R44), D39 (≠ G45), R42 (≠ E48), D60 (= D69), L61 (≠ I70), N83 (≠ S92), A84 (= A93), Y87 (≠ A96), I133 (= I140), T135 (≠ S142), Y148 (= Y155), K152 (= K159), P178 (= P185), P180 (≠ F187), T181 (≠ I188), T183 (= T190), T185 (≠ L192), T186 (= T193)
4za2D Crystal structure of pectobacterium carotovorum 2-keto-3-deoxy-d- gluconate dehydrogenase complexed with NAD+ (see paper)
34% identity, 96% coverage: 7:247/250 of query aligns to 5:244/247 of 4za2D
- binding nicotinamide-adenine-dinucleotide: G17 (= G19), D19 (≠ S21), L22 (≠ I24), I42 (≠ Q46), D65 (= D69), M66 (≠ I70), N92 (≠ S92), A93 (= A93), G94 (= G94), L115 (≠ V115), I143 (= I140), S145 (= S142), Y158 (= Y155), K162 (= K159), G189 (≠ T186), M191 (≠ I188), T193 (= T190), N195 (≠ L192)
5b4tA Crystal structure of d-3-hydroxybutyrate dehydrogenase from alcaligenes faecalis complexed with NAD+ and a substrate d-3- hydroxybutyrate (see paper)
35% identity, 96% coverage: 10:249/250 of query aligns to 2:259/260 of 5b4tA
- active site: G15 (= G23), N114 (= N116), S142 (= S142), Y155 (= Y155), K159 (= K159), I200 (vs. gap)
- binding (3R)-3-hydroxybutanoic acid: Q94 (≠ A96), S142 (= S142), H144 (≠ M144), K152 (≠ R152), Y155 (= Y155), W187 (≠ F187), Q196 (≠ T196)
- binding nicotinamide-adenine-dinucleotide: G11 (= G19), T13 (≠ S21), G15 (= G23), I16 (= I24), F36 (≠ R44), D63 (= D69), L64 (≠ I70), N90 (≠ S92), G92 (= G94), L113 (≠ V115), I140 (= I140), Y155 (= Y155), K159 (= K159), P185 (= P185), G186 (≠ T186), W187 (≠ F187), V188 (≠ I188), T190 (= T190), L192 (= L192), V193 (≠ T193)
Query Sequence
>3608847 FitnessBrowser__Dino:3608847
MLPRTPSFRLDGQRALVTGASRGIGLGCAVALAEAGAHVVMAARGQAELDAAATEMRAEG
WSVETAVLDIADLDAQAEFFGAQAPFDCLVNSAGLARHSPALDTRPEDFDAVMSVNLRAA
YFLATNAARTMPDGGSIVQISSQMGHVGGLDRAVYCASKHGVEGMTKAMAQEFGPRGIRV
NSLCPTFIRTPLTEATFADPEKRAWIMGKIKLPRVAEIEDIMGAVVFLCSPASAMVTGTG
LLVDGGWTSG
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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