SitesBLAST
Comparing 1937064 b3589 predicted Fe-containing alcohol dehydrogenase (NCBI) 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)
63% identity, 100% coverage: 2:383/383 of query aligns to 1:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D194), H197 (= H198), H262 (= H263), H276 (= H277)
- binding nicotinamide-adenine-dinucleotide: D38 (= D39), F40 (≠ M41), M41 (≠ L42), N70 (= N71), G96 (= G97), G97 (= G98), S98 (= S99), T137 (= T138), T138 (= T139), T141 (= T142), F148 (= F149), I150 (= I151), L178 (= L179), G181 (= G182), M182 (= M183), L186 (= L187), H197 (= H198), H266 (= H267), H276 (= H277)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
63% identity, 100% coverage: 2:383/383 of query aligns to 1:382/382 of 3owoA
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
49% identity, 99% coverage: 6:383/383 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: 4:383/383 of query aligns to 2:381/381 of P31005
- G13 (= G15) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (≠ D17) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D90) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G97) 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 (= S99) 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 (= D102) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K105) 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)
44% identity, 92% coverage: 30:383/383 of query aligns to 29:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D194), H199 (= H198), H262 (= H263), H276 (= H277)
- binding nicotinamide-adenine-dinucleotide: D38 (= D39), T40 (≠ M41), L41 (= L42), P69 (= P70), N70 (= N71), G96 (= G97), G97 (= G98), S98 (= S99), D101 (= D102), T139 (= T138), T140 (= T139), T143 (= T142), V152 (≠ I151), K161 (= K160), M180 (≠ L179), M181 (= M180), G183 (= G182), M184 (= M183), P185 (= P184), L188 (= L187), D195 (= D194), H199 (= H198), H262 (= H263), H266 (= H267), H276 (= H277)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
44% identity, 92% coverage: 30:383/383 of query aligns to 29:382/382 of P0A9S1
- D38 (= D39) mutation to G: Enzyme can now use NADP.
- G96 (= G97) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D194) mutation to L: Complete loss of iron-binding.
- H199 (= H198) 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.
- 16 G→D: No effect on enzyme activity.
1rrmA Crystal structure of lactaldehyde reductase
44% identity, 92% coverage: 30:383/383 of query aligns to 29:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D39), T40 (≠ M41), L41 (= L42), P69 (= P70), N70 (= N71), G96 (= G97), G97 (= G98), S98 (= S99), T139 (= T138), T140 (= T139), T143 (= T142), V152 (≠ I151), K161 (= K160), M181 (= M180), G183 (= G182), M184 (= M183), P185 (= P184), L188 (= L187), H276 (= H277)
- binding fe (ii) ion: L258 (= L259), C361 (= C362)
- binding zinc ion: D195 (= D194), H199 (= H198), H262 (= H263), H276 (= H277)
7qlqAAA Lactaldehyde reductase
43% identity, 96% coverage: 18:383/383 of query aligns to 19:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D39), T39 (≠ M41), L40 (= L42), P68 (= P70), N69 (= N71), G95 (= G97), G96 (= G98), S97 (= S99), D100 (= D102), T138 (= T138), T139 (= T139), T142 (= T142), V151 (≠ I151), K160 (= K160), G182 (= G182), M183 (= M183), P184 (= P184), L187 (= L187), T191 (= T191), H275 (= H277)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ F149), V162 (≠ A162), V164 (= V164), H198 (= H198), F252 (= F254), S253 (≠ N255), H261 (= H263), H275 (= H277), C360 (= C362)
- binding fe (iii) ion: D194 (= D194), H198 (= H198), H261 (= H263), H275 (= H277)
7qlgAAA Lactaldehyde reductase
44% identity, 92% coverage: 30:383/383 of query aligns to 28:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D194), H198 (= H198), H261 (= H263), H275 (= H277)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D39), T39 (≠ M41), L40 (= L42), P68 (= P70), N69 (= N71), G95 (= G97), G96 (= G98), S97 (= S99), D100 (= D102), T138 (= T138), T139 (= T139), T142 (= T142), A144 (≠ S144), T147 (= T147), N149 (≠ F149), V151 (≠ I151), K160 (= K160), M180 (= M180), G182 (= G182), M183 (= M183), L187 (= L187), D194 (= D194), H198 (= H198), H275 (= H277)
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
44% identity, 92% coverage: 30:383/383 of query aligns to 30:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D39), T41 (≠ M41), L42 (= L42), P70 (= P70), N71 (= N71), G97 (= G97), G98 (= G98), S99 (= S99), D102 (= D102), T140 (= T138), T141 (= T139), T144 (= T142), A146 (≠ S144), T149 (= T147), N151 (≠ F149), Y152 (≠ C150), V153 (≠ I151), K162 (= K160), M182 (= M180), G184 (= G182), C185 (≠ M183), P186 (= P184), L189 (= L187), H200 (= H198), F254 (= F254), H277 (= H277)
- binding zinc ion: D196 (= D194), H200 (= H198), H263 (= H263), H277 (= H277)
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
37% identity, 92% coverage: 32:383/383 of query aligns to 28:400/403 of 3zdrA
6scgA Structure of adhe form 1 (see paper)
36% identity, 91% coverage: 18:367/383 of query aligns to 17:383/406 of 6scgA