SitesBLAST
Comparing Pf6N2E2_4819 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_4819 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)
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
44% identity, 91% coverage: 35:382/382 of query aligns to 34:382/382 of 3bfjA
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
38% identity, 99% coverage: 4:382/382 of query aligns to 3:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D192), H197 (= H196), H262 (= H261), H276 (= H275)
- binding nicotinamide-adenine-dinucleotide: D38 (= D39), F40 (≠ A41), M41 (≠ L42), N70 (≠ D69), G96 (= G95), G97 (= G96), S98 (= S97), T137 (= T136), T138 (= T137), T141 (= T140), F148 (≠ V147), I150 (= I149), L178 (≠ M177), G181 (≠ T180), M182 (≠ C181), L186 (≠ V185), H197 (= H196), H266 (≠ Y265), H276 (= H275)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
38% identity, 99% coverage: 4:382/382 of query aligns to 3:382/382 of 3owoA
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
38% identity, 99% coverage: 3:381/382 of query aligns to 1:380/381 of P31005
- M1 (≠ L3) modified: Initiator methionine, Removed
- G13 (= G15) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (≠ A17) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D88) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G95) mutation to A: Shows a 10-fold decreased affinity for NAD and NADH and a strongly reduced dehydrogenase activity. Completely insensitive to the stimulating effect of the activator protein Act.
- S97 (= S97) mutation to G: Shows an increase of the dehydrogenase activity and a decrease of the affinity for NAD and NADH. Completely insensitive to the stimulating effect of the activator protein Act. It does not bind NAD.; mutation to T: Shows an increase of the dehydrogenase activity and affinity for NAD and NADH.
- D100 (= D100) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K103) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
37% identity, 100% coverage: 2:382/382 of query aligns to 1:400/403 of 3zdrA
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
38% identity, 96% coverage: 15:382/382 of query aligns to 15:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D39), T41 (≠ A41), L42 (= L42), P70 (= P68), N71 (≠ D69), G97 (= G95), G98 (= G96), S99 (= S97), D102 (= D100), T140 (= T136), T141 (= T137), T144 (= T140), A146 (≠ S142), T149 (= T145), N151 (≠ V147), Y152 (≠ A148), V153 (≠ I149), K162 (= K158), M182 (≠ T178), G184 (≠ T180), C185 (= C181), P186 (= P182), L189 (≠ V185), H200 (= H196), F254 (= F252), H277 (= H275)
- binding zinc ion: D196 (= D192), H200 (= H196), H263 (= H261), H277 (= H275)
7qlqAAA Lactaldehyde reductase (see paper)
38% identity, 96% coverage: 15:382/382 of query aligns to 13:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D39), T39 (≠ A41), L40 (= L42), P68 (= P68), N69 (≠ D69), G95 (= G95), G96 (= G96), S97 (= S97), D100 (= D100), T138 (= T136), T139 (= T137), T142 (= T140), V151 (≠ I149), K160 (= K158), G182 (≠ T180), M183 (≠ C181), P184 (= P182), L187 (≠ V185), T191 (≠ S189), H275 (= H275)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ V147), V162 (≠ G160), V164 (= V162), H198 (= H196), F252 (= F252), S253 (≠ G253), H261 (= H261), H275 (= H275), C360 (≠ L361)
- binding fe (iii) ion: D194 (= D192), H198 (= H196), H261 (= H261), H275 (= H275)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
38% identity, 96% coverage: 15:382/382 of query aligns to 14:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D192), H199 (= H196), H262 (= H261), H276 (= H275)
- binding nicotinamide-adenine-dinucleotide: D38 (= D39), T40 (≠ A41), L41 (= L42), P69 (= P68), N70 (≠ D69), G96 (= G95), G97 (= G96), S98 (= S97), D101 (= D100), T139 (= T136), T140 (= T137), T143 (= T140), V152 (≠ I149), K161 (= K158), M180 (= M177), M181 (≠ T178), G183 (≠ T180), M184 (≠ C181), P185 (= P182), L188 (≠ V185), D195 (= D192), H199 (= H196), H262 (= H261), H266 (≠ Y265), H276 (= H275)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
38% identity, 96% coverage: 15:382/382 of query aligns to 14:382/382 of P0A9S1
- G16 (≠ A17) mutation to D: No effect on enzyme activity.
- D38 (= D39) mutation to G: Enzyme can now use NADP.
- G96 (= G95) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D192) mutation to L: Complete loss of iron-binding.
- H199 (= H196) mutation H->A,F: Complete loss of iron-binding.
Sites not aligning to the query:
- 1:9 MANRMILNE→M: Loss of enzyme activity, loss of dimerization.
1rrmA Crystal structure of lactaldehyde reductase
38% identity, 96% coverage: 15:382/382 of query aligns to 14:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D39), T40 (≠ A41), L41 (= L42), P69 (= P68), N70 (≠ D69), G96 (= G95), G97 (= G96), S98 (= S97), T139 (= T136), T140 (= T137), T143 (= T140), V152 (≠ I149), K161 (= K158), M181 (≠ T178), G183 (≠ T180), M184 (≠ C181), P185 (= P182), L188 (≠ V185), H276 (= H275)
- binding fe (ii) ion: L258 (≠ V257), C361 (≠ L361)
- binding zinc ion: D195 (= D192), H199 (= H196), H262 (= H261), H276 (= H275)
7qlgAAA Lactaldehyde reductase (see paper)
38% identity, 96% coverage: 15:382/382 of query aligns to 13:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D192), H198 (= H196), H261 (= H261), H275 (= H275)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D39), T39 (≠ A41), L40 (= L42), P68 (= P68), N69 (≠ D69), G95 (= G95), G96 (= G96), S97 (= S97), D100 (= D100), T138 (= T136), T139 (= T137), T142 (= T140), A144 (≠ S142), T147 (= T145), N149 (≠ V147), V151 (≠ I149), K160 (= K158), M180 (≠ T178), G182 (≠ T180), M183 (≠ C181), L187 (≠ V185), D194 (= D192), H198 (= H196), H275 (= H275)
Q59104 4-hydroxybutyrate dehydrogenase; 4HbD; Gamma-hydroxybutyrate dehydrogenase; GHBDH; EC 1.1.1.61 from Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha) (see paper)
35% identity, 94% coverage: 18:377/382 of query aligns to 16:377/382 of Q59104