SitesBLAST
Comparing WP_078716111.1 NCBI__GCF_900167125.1:WP_078716111.1 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)
42% identity, 98% coverage: 4:378/382 of query aligns to 3:378/382 of 3bfjA
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
40% identity, 99% coverage: 6:382/382 of query aligns to 4:381/381 of P31005
- G13 (= G15) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G17) 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
P0DJA2 Alcohol dehydrogenase 2; Alcohol dehydrogenase II; ADH II; EC 1.1.1.1 from Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) (see 2 papers)
37% identity, 99% coverage: 1:380/382 of query aligns to 1:381/383 of P0DJA2
- M1 (= M1) modified: Initiator methionine, Removed
- D39 (≠ K39) binding NAD(+)
- N71 (≠ D71) binding NAD(+)
- G98 (= G98) binding NAD(+)
- S99 (= S99) binding NAD(+)
- T138 (= T137) binding NAD(+)
- T139 (= T138) binding NAD(+)
- T147 (= T146) binding NAD(+)
- F149 (= F148) binding NAD(+)
- K160 (= K159) binding NAD(+)
- L179 (= L178) binding NAD(+)
- G182 (≠ T181) binding NAD(+)
- M183 (= M182) binding NAD(+)
- D194 (= D193) binding Fe(2+)
- H198 (= H197) binding Fe(2+)
- H263 (= H262) binding Fe(2+)
- H267 (≠ R266) binding NAD(+)
- H277 (= H276) binding Fe(2+); binding NAD(+)
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
37% identity, 98% coverage: 6:380/382 of query aligns to 5:380/382 of 3ox4A
- binding fe (ii) ion: D193 (= D193), H197 (= H197), H262 (= H262), H276 (= H276)
- binding nicotinamide-adenine-dinucleotide: D38 (≠ K39), F40 (≠ S41), M41 (≠ S42), N70 (≠ D71), G96 (= G97), G97 (= G98), S98 (= S99), T137 (= T137), T138 (= T138), F148 (= F148), I150 (≠ V150), G181 (≠ T181), M182 (= M182), L186 (≠ V186), H276 (= H276)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
37% identity, 98% coverage: 6:380/382 of query aligns to 5:380/382 of 3owoA
7qlqAAA Lactaldehyde reductase (see paper)
39% identity, 96% coverage: 14:380/382 of query aligns to 12:379/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (≠ G38), T39 (≠ S40), L40 (≠ S41), G95 (= G97), G96 (= G98), S97 (= S99), T138 (= T137), T139 (= T138), T142 (= T141), K160 (= K159), G182 (≠ T181), M183 (= M182), L187 (≠ V186), H275 (= H276)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ F148), V164 (≠ Q163), H198 (= H197), F252 (= F253), S253 (= S254), H261 (= H262), C360 (≠ S361)
- binding fe (iii) ion: D194 (= D193), H198 (= H197), H261 (= H262), H275 (= H276)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
38% identity, 96% coverage: 14:380/382 of query aligns to 13:380/382 of 2bi4A
- binding fe (iii) ion: D195 (= D193), H199 (= H197), H262 (= H262), H276 (= H276)
- binding nicotinamide-adenine-dinucleotide: D38 (≠ G38), T40 (≠ S40), L41 (≠ S41), G96 (= G97), G97 (= G98), S98 (= S99), T139 (= T137), T140 (= T138), V152 (= V150), K161 (= K159), G183 (≠ T181), M184 (= M182), L188 (≠ V186), D195 (= D193), H199 (= H197), H262 (= H262), H276 (= H276)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
38% identity, 96% coverage: 14:380/382 of query aligns to 13:380/382 of P0A9S1
- G16 (= G17) mutation to D: No effect on enzyme activity.
- D38 (≠ G38) mutation to G: Enzyme can now use NADP.
- G96 (= G97) 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.
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: 14:380/382 of query aligns to 13:380/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (≠ G38), T40 (≠ S40), L41 (≠ S41), N70 (≠ D71), G96 (= G97), G97 (= G98), S98 (= S99), T139 (= T137), T140 (= T138), T143 (= T141), V152 (= V150), K161 (= K159), G183 (≠ T181), M184 (= M182), L188 (≠ V186), H276 (= H276)
- binding fe (ii) ion: L258 (≠ V258), C361 (≠ S361)
- binding zinc ion: D195 (= D193), H199 (= H197), H262 (= H262), H276 (= H276)
7qlgAAA Lactaldehyde reductase (see paper)
38% identity, 96% coverage: 14:380/382 of query aligns to 12:379/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D193), H198 (= H197), H261 (= H262), H275 (= H276)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (≠ G38), T39 (≠ S40), L40 (≠ S41), N69 (≠ D71), G95 (= G97), G96 (= G98), S97 (= S99), D100 (= D102), T138 (= T137), T139 (= T138), T142 (= T141), T147 (= T146), N149 (≠ F148), K160 (= K159), L187 (≠ V186), H198 (= H197), H275 (= H276)
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
38% identity, 96% coverage: 14:380/382 of query aligns to 14:381/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (≠ G38), T41 (≠ S40), L42 (≠ S41), P70 (≠ S70), G97 (= G97), G98 (= G98), S99 (= S99), D102 (= D102), T140 (= T137), T141 (= T138), T144 (= T141), T149 (= T146), N151 (≠ F148), V153 (= V150), K162 (= K159), G184 (≠ T181), C185 (≠ M182), L189 (≠ V186), H277 (= H276)
- binding zinc ion: D196 (= D193), H200 (= H197), H263 (= H262), H277 (= H276)
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
38% identity, 98% coverage: 6:378/382 of query aligns to 5:396/403 of 3zdrA