SitesBLAST
Comparing AO356_04765 FitnessBrowser__pseudo5_N2C3_1:AO356_04765 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)
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
66% identity, 100% coverage: 2:382/382 of query aligns to 2:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D193), H197 (= H197), H262 (= H262), H276 (= H276)
- binding nicotinamide-adenine-dinucleotide: D38 (= D38), F40 (≠ G40), M41 (≠ L41), N70 (= N70), G96 (= G96), G97 (= G97), S98 (= S98), T137 (= T137), T138 (= T138), T141 (= T141), F148 (= F148), I150 (= I150), L178 (= L178), G181 (≠ A181), M182 (= M182), L186 (= L186), H197 (= H197), H266 (= H266), H276 (= H276)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
66% identity, 100% coverage: 2:382/382 of query aligns to 2:382/382 of 3owoA
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
50% identity, 99% coverage: 5:382/382 of query aligns to 5:382/382 of 3bfjA
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
46% identity, 99% coverage: 3:382/382 of query aligns to 2:381/381 of P31005
- G13 (= G14) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G16) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D89) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G96) 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 (= S98) 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 (= D101) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K104) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1rrmA Crystal structure of lactaldehyde reductase
41% identity, 100% coverage: 1:382/382 of query aligns to 1:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D38), T40 (≠ G40), L41 (= L41), P69 (= P69), N70 (= N70), G96 (= G96), G97 (= G97), S98 (= S98), T139 (= T137), T140 (= T138), T143 (= T141), V152 (≠ I150), K161 (= K159), M181 (= M179), G183 (≠ A181), M184 (= M182), P185 (= P183), L188 (= L186), H276 (= H276)
- binding fe (ii) ion: L258 (= L258), C361 (= C361)
- binding zinc ion: D195 (= D193), H199 (= H197), H262 (= H262), H276 (= H276)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
41% identity, 100% coverage: 1:382/382 of query aligns to 1:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D193), H199 (= H197), H262 (= H262), H276 (= H276)
- binding nicotinamide-adenine-dinucleotide: D38 (= D38), T40 (≠ G40), L41 (= L41), P69 (= P69), N70 (= N70), G96 (= G96), G97 (= G97), S98 (= S98), D101 (= D101), T139 (= T137), T140 (= T138), T143 (= T141), V152 (≠ I150), K161 (= K159), M180 (≠ L178), M181 (= M179), G183 (≠ A181), M184 (= M182), P185 (= P183), L188 (= L186), D195 (= D193), H199 (= H197), H262 (= H262), H266 (= H266), H276 (= H276)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
41% identity, 100% coverage: 1:382/382 of query aligns to 1:382/382 of P0A9S1
- 1:9 (vs. 1:9, 11% identical) mutation to M: Loss of enzyme activity, loss of dimerization.
- G16 (= G16) mutation to D: No effect on enzyme activity.
- D38 (= D38) mutation to G: Enzyme can now use NADP.
- G96 (= G96) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D193) mutation to L: Complete loss of iron-binding.
- H199 (= H197) mutation H->A,F: Complete loss of iron-binding.
7qlqAAA Lactaldehyde reductase (see paper)
42% identity, 97% coverage: 13:382/382 of query aligns to 12:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D38), T39 (≠ G40), L40 (= L41), P68 (= P69), N69 (= N70), G95 (= G96), G96 (= G97), S97 (= S98), D100 (= D101), T138 (= T137), T139 (= T138), T142 (= T141), V151 (≠ I150), K160 (= K159), G182 (≠ A181), M183 (= M182), P184 (= P183), L187 (= L186), T191 (= T190), H275 (= H276)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ F148), V162 (≠ A161), V164 (= V163), H198 (= H197), F252 (= F253), S253 (≠ N254), H261 (= H262), H275 (= H276), C360 (= C361)
- binding fe (iii) ion: D194 (= D193), H198 (= H197), H261 (= H262), H275 (= H276)
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
41% identity, 100% coverage: 1:382/382 of query aligns to 2:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D38), T41 (≠ G40), L42 (= L41), P70 (= P69), N71 (= N70), G97 (= G96), G98 (= G97), S99 (= S98), D102 (= D101), T140 (= T137), T141 (= T138), T144 (= T141), A146 (≠ S143), T149 (= T146), N151 (≠ F148), Y152 (≠ C149), V153 (≠ I150), K162 (= K159), M182 (= M179), G184 (≠ A181), C185 (≠ M182), P186 (= P183), L189 (= L186), H200 (= H197), F254 (= F253), H277 (= H276)
- binding zinc ion: D196 (= D193), H200 (= H197), H263 (= H262), H277 (= H276)
7qlgAAA Lactaldehyde reductase (see paper)
42% identity, 97% coverage: 13:382/382 of query aligns to 12:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D193), H198 (= H197), H261 (= H262), H275 (= H276)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D38), T39 (≠ G40), L40 (= L41), P68 (= P69), N69 (= N70), G95 (= G96), G96 (= G97), S97 (= S98), D100 (= D101), T138 (= T137), T139 (= T138), T142 (= T141), A144 (≠ S143), T147 (= T146), N149 (≠ F148), V151 (≠ I150), K160 (= K159), M180 (= M179), G182 (≠ A181), M183 (= M182), L187 (= L186), D194 (= D193), H198 (= H197), H275 (= H276)
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
37% identity, 92% coverage: 32:382/382 of query aligns to 29:400/403 of 3zdrA
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, 98% coverage: 1:376/382 of query aligns to 1:379/382 of Q59104