SitesBLAST
Comparing PfGW456L13_3512 Alcohol dehydrogenase (EC 1.1.1.1); Acetaldehyde dehydrogenase (EC 1.2.1.10) 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)
37% identity, 98% coverage: 7:387/387 of query aligns to 1:382/382 of 3bfjA
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
40% identity, 90% coverage: 34:383/387 of query aligns to 29:378/382 of 3ox4A
- binding fe (ii) ion: D193 (= D198), H197 (= H202), H262 (= H267), H276 (= H281)
- binding nicotinamide-adenine-dinucleotide: D38 (= D43), F40 (≠ G45), M41 (≠ V46), N70 (= N75), G96 (= G101), G97 (= G102), S98 (= S103), T137 (= T142), T138 (= T143), T141 (= T146), F148 (= F153), I150 (= I155), L178 (≠ T183), G181 (≠ S186), M182 (= M187), L186 (= L191), H197 (= H202), H266 (= H271), H276 (= H281)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
40% identity, 90% coverage: 34:383/387 of query aligns to 29:378/382 of 3owoA
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
35% identity, 97% coverage: 11:387/387 of query aligns to 5:381/381 of P31005
- G13 (= G19) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G21) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D94) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G101) 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 (= S103) 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 (= D106) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K109) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
36% identity, 97% coverage: 9:383/387 of query aligns to 4:378/382 of 2bi4A
- binding fe (iii) ion: D195 (= D198), H199 (= H202), H262 (= H267), H276 (= H281)
- binding nicotinamide-adenine-dinucleotide: D38 (= D43), T40 (≠ G45), L41 (≠ V46), P69 (= P74), N70 (= N75), G96 (= G101), G97 (= G102), S98 (= S103), D101 (= D106), T139 (= T142), T140 (= T143), T143 (= T146), V152 (≠ I155), K161 (= K164), M180 (≠ T183), M181 (≠ T184), G183 (≠ S186), M184 (= M187), P185 (≠ D188), L188 (= L191), D195 (= D198), H199 (= H202), H262 (= H267), H266 (= H271), H276 (= H281)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
36% identity, 97% coverage: 9:383/387 of query aligns to 4:378/382 of P0A9S1
- G16 (= G21) mutation to D: No effect on enzyme activity.
- D38 (= D43) mutation to G: Enzyme can now use NADP.
- G96 (= G101) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D198) mutation to L: Complete loss of iron-binding.
- H199 (= H202) 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
36% identity, 97% coverage: 9:383/387 of query aligns to 4:378/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D43), T40 (≠ G45), L41 (≠ V46), P69 (= P74), N70 (= N75), G96 (= G101), G97 (= G102), S98 (= S103), T139 (= T142), T140 (= T143), T143 (= T146), V152 (≠ I155), K161 (= K164), M181 (≠ T184), G183 (≠ S186), M184 (= M187), P185 (≠ D188), L188 (= L191), H276 (= H281)
- binding fe (ii) ion: L258 (= L263), C361 (= C366)
- binding zinc ion: D195 (= D198), H199 (= H202), H262 (= H267), H276 (= H281)
7qlqAAA Lactaldehyde reductase
36% identity, 97% coverage: 9:383/387 of query aligns to 3:377/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D43), T39 (≠ G45), L40 (≠ V46), P68 (= P74), N69 (= N75), G95 (= G101), G96 (= G102), S97 (= S103), D100 (= D106), T138 (= T142), T139 (= T143), T142 (= T146), V151 (≠ I155), K160 (= K164), G182 (≠ S186), M183 (= M187), P184 (≠ D188), L187 (= L191), T191 (= T195), H275 (= H281)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ F153), V162 (≠ S166), V164 (= V168), H198 (= H202), F252 (= F258), S253 (= S259), H261 (= H267), H275 (= H281), C360 (= C366)
- binding fe (iii) ion: D194 (= D198), H198 (= H202), H261 (= H267), H275 (= H281)
7qlgAAA Lactaldehyde reductase
36% identity, 97% coverage: 9:383/387 of query aligns to 3:377/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D198), H198 (= H202), H261 (= H267), H275 (= H281)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D43), T39 (≠ G45), L40 (≠ V46), P68 (= P74), N69 (= N75), G95 (= G101), G96 (= G102), S97 (= S103), D100 (= D106), T138 (= T142), T139 (= T143), T142 (= T146), A144 (= A148), T147 (≠ S151), N149 (≠ F153), V151 (≠ I155), K160 (= K164), M180 (≠ T184), G182 (≠ S186), M183 (= M187), L187 (= L191), D194 (= D198), H198 (= H202), H275 (= H281)
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
36% identity, 97% coverage: 9:383/387 of query aligns to 5:379/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D43), T41 (≠ G45), L42 (≠ V46), P70 (= P74), N71 (= N75), G97 (= G101), G98 (= G102), S99 (= S103), D102 (= D106), T140 (= T142), T141 (= T143), T144 (= T146), A146 (= A148), T149 (≠ S151), N151 (≠ F153), Y152 (≠ V154), V153 (≠ I155), K162 (= K164), M182 (≠ T184), G184 (≠ S186), C185 (≠ M187), P186 (≠ D188), L189 (= L191), H200 (= H202), F254 (= F258), H277 (= H281)
- binding zinc ion: D196 (= D198), H200 (= H202), H263 (= H267), H277 (= H281)
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
31% identity, 97% coverage: 12:387/387 of query aligns to 7:400/403 of 3zdrA
5yvmA Crystal structure of the archaeal halo-thermophilic red sea brine pool alcohol dehydrogenase adh/d1 bound to nzq (see paper)
31% identity, 97% coverage: 13:387/387 of query aligns to 12:403/403 of 5yvmA