SitesBLAST
Comparing WP_003942060.1 NCBI__GCF_002893965.1:WP_003942060.1 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)
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
41% identity, 94% coverage: 25:401/401 of query aligns to 5:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D212), H197 (= H216), H262 (= H281), H276 (= H295)
- binding nicotinamide-adenine-dinucleotide: D38 (= D57), F40 (≠ G59), M41 (≠ L60), N70 (= N89), G96 (= G115), G97 (= G116), S98 (= S117), T137 (= T156), T138 (= T157), F148 (= F167), I150 (= I169), G181 (≠ T200), M182 (= M201), L186 (= L205), H276 (= H295)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
41% identity, 94% coverage: 25:401/401 of query aligns to 5:382/382 of 3owoA
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)
41% identity, 94% coverage: 25:401/401 of query aligns to 6:383/383 of P0DJA2
- D39 (= D57) binding NAD(+)
- N71 (= N89) binding NAD(+)
- G98 (= G116) binding NAD(+)
- S99 (= S117) binding NAD(+)
- T138 (= T156) binding NAD(+)
- T139 (= T157) binding NAD(+)
- T147 (≠ S165) binding NAD(+)
- F149 (= F167) binding NAD(+)
- K160 (= K178) binding NAD(+)
- L179 (= L197) binding NAD(+)
- G182 (≠ T200) binding NAD(+)
- M183 (= M201) binding NAD(+)
- D194 (= D212) binding Fe(2+)
- H198 (= H216) binding Fe(2+)
- H263 (= H281) binding Fe(2+)
- H267 (= H285) binding NAD(+)
- H277 (= H295) binding Fe(2+); binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
38% identity, 95% coverage: 21:401/401 of query aligns to 1:382/382 of 3bfjA
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
37% identity, 94% coverage: 25:401/401 of query aligns to 5:381/381 of P31005
- G13 (= G33) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G35) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D108) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G115) 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 (= S117) 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 (= D120) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K123) 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)
35% identity, 92% coverage: 32:400/401 of query aligns to 13:381/382 of 2bi4A
- binding fe (iii) ion: D195 (= D212), H199 (= H216), H262 (= H281), H276 (= H295)
- binding nicotinamide-adenine-dinucleotide: D38 (= D57), T40 (≠ G59), L41 (= L60), G96 (= G115), G97 (= G116), S98 (= S117), T139 (= T156), T140 (= T157), V152 (≠ I169), K161 (= K178), G183 (≠ T200), M184 (= M201), L188 (= L205), D195 (= D212), H199 (= H216), H262 (= H281), H276 (= H295)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
35% identity, 92% coverage: 32:400/401 of query aligns to 13:381/382 of P0A9S1
- G16 (= G35) mutation to D: No effect on enzyme activity.
- D38 (= D57) mutation to G: Enzyme can now use NADP.
- G96 (= G115) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D212) mutation to L: Complete loss of iron-binding.
- H199 (= H216) 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
35% identity, 92% coverage: 32:400/401 of query aligns to 13:381/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D57), T40 (≠ G59), L41 (= L60), N70 (= N89), G96 (= G115), G97 (= G116), S98 (= S117), T139 (= T156), T140 (= T157), T143 (= T160), V152 (≠ I169), K161 (= K178), G183 (≠ T200), M184 (= M201), L188 (= L205), H276 (= H295)
- binding fe (ii) ion: L258 (= L277), C361 (= C380)
- binding zinc ion: D195 (= D212), H199 (= H216), H262 (= H281), H276 (= H295)
7qlqAAA Lactaldehyde reductase (see paper)
35% identity, 92% coverage: 32:400/401 of query aligns to 12:380/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D57), T39 (≠ G59), L40 (= L60), G95 (= G115), G96 (= G116), S97 (= S117), T138 (= T156), T139 (= T157), T142 (= T160), K160 (= K178), G182 (≠ T200), M183 (= M201), L187 (= L205), H275 (= H295)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ F167), V164 (≠ I182), H198 (= H216), F252 (= F272), S253 (≠ T273), H261 (= H281), C360 (= C380)
- binding fe (iii) ion: D194 (= D212), H198 (= H216), H261 (= H281), H275 (= H295)
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
35% identity, 92% coverage: 32:400/401 of query aligns to 14:382/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D57), T41 (≠ G59), L42 (= L60), P70 (= P88), G97 (= G115), G98 (= G116), S99 (= S117), D102 (= D120), T140 (= T156), T141 (= T157), T144 (= T160), T149 (≠ S165), N151 (≠ F167), V153 (≠ I169), K162 (= K178), G184 (≠ T200), C185 (≠ M201), L189 (= L205), H277 (= H295)
- binding zinc ion: D196 (= D212), H200 (= H216), H263 (= H281), H277 (= H295)
7qlgAAA Lactaldehyde reductase (see paper)
35% identity, 92% coverage: 32:400/401 of query aligns to 12:380/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D212), H198 (= H216), H261 (= H281), H275 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D57), T39 (≠ G59), L40 (= L60), N69 (= N89), G95 (= G115), G96 (= G116), S97 (= S117), D100 (= D120), T138 (= T156), T139 (= T157), T142 (= T160), T147 (≠ S165), N149 (≠ F167), K160 (= K178), L187 (= L205), H198 (= H216), H275 (= H295)
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
35% identity, 88% coverage: 51:401/401 of query aligns to 29:400/403 of 3zdrA