SitesBLAST
Comparing WP_066328438.1 NCBI__GCF_900100165.1:WP_066328438.1 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)
33% identity, 97% coverage: 14:380/380 of query aligns to 13:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D191), H197 (= H195), H262 (= H260), H276 (= H274)
- binding nicotinamide-adenine-dinucleotide: D38 (≠ I39), F40 (≠ E41), M41 (≠ L42), N70 (≠ E69), G96 (= G95), G97 (= G96), S98 (= S97), T137 (= T136), T138 (= T137), F148 (≠ N147), I150 (= I149), G181 (≠ L179), M182 (≠ L180), L186 (≠ V184), H276 (= H274)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
33% identity, 97% coverage: 14:380/380 of query aligns to 13:382/382 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)
33% identity, 97% coverage: 14:380/380 of query aligns to 14:383/383 of P0DJA2
- D39 (≠ I39) binding NAD(+)
- N71 (≠ E69) binding NAD(+)
- G98 (= G96) binding NAD(+)
- S99 (= S97) binding NAD(+)
- T138 (= T136) binding NAD(+)
- T139 (= T137) binding NAD(+)
- T147 (≠ S145) binding NAD(+)
- F149 (≠ N147) binding NAD(+)
- K160 (= K157) binding NAD(+)
- L179 (= L176) binding NAD(+)
- G182 (≠ L179) binding NAD(+)
- M183 (≠ L180) binding NAD(+)
- D194 (= D191) binding Fe(2+)
- H198 (= H195) binding Fe(2+)
- H263 (= H260) binding Fe(2+)
- H267 (≠ Y264) binding NAD(+)
- H277 (= H274) 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)
34% identity, 87% coverage: 50:380/380 of query aligns to 51:382/382 of 3bfjA
1rrmA Crystal structure of lactaldehyde reductase
30% identity, 100% coverage: 1:380/380 of query aligns to 1:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (≠ I39), T40 (≠ E41), L41 (= L42), N70 (≠ E69), G96 (= G95), G97 (= G96), S98 (= S97), T139 (= T136), T140 (= T137), T143 (= T140), V152 (≠ I149), K161 (≠ V158), G183 (≠ L179), M184 (≠ L180), L188 (≠ V184), H276 (= H274)
- binding fe (ii) ion: L258 (≠ T256), C361 (≠ L359)
- binding zinc ion: D195 (= D191), H199 (= H195), H262 (= H260), H276 (= H274)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
30% identity, 100% coverage: 1:380/380 of query aligns to 1:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D191), H199 (= H195), H262 (= H260), H276 (= H274)
- binding nicotinamide-adenine-dinucleotide: D38 (≠ I39), T40 (≠ E41), L41 (= L42), G96 (= G95), G97 (= G96), S98 (= S97), T139 (= T136), T140 (= T137), V152 (≠ I149), K161 (≠ V158), G183 (≠ L179), M184 (≠ L180), L188 (≠ V184), D195 (= D191), H199 (= H195), H262 (= H260), H276 (= H274)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
30% identity, 100% coverage: 1:380/380 of query aligns to 1:382/382 of P0A9S1
- 1:9 (vs. 1:10, 40% identical) mutation to M: Loss of enzyme activity, loss of dimerization.
- G16 (= G17) mutation to D: No effect on enzyme activity.
- D38 (≠ I39) mutation to G: Enzyme can now use NADP.
- G96 (= G95) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D191) mutation to L: Complete loss of iron-binding.
- H199 (= H195) mutation H->A,F: Complete loss of iron-binding.
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
30% identity, 100% coverage: 1:380/380 of query aligns to 2:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (≠ I39), T41 (≠ E41), L42 (= L42), P70 (≠ G68), G97 (= G95), G98 (= G96), S99 (= S97), D102 (= D100), T140 (= T136), T141 (= T137), T144 (= T140), T149 (≠ S145), N151 (= N147), V153 (≠ I149), K162 (≠ V158), G184 (≠ L179), C185 (≠ L180), L189 (≠ V184), H277 (= H274)
- binding zinc ion: D196 (= D191), H200 (= H195), H263 (= H260), H277 (= H274)
7qlgAAA Lactaldehyde reductase (see paper)
30% identity, 99% coverage: 5:380/380 of query aligns to 4:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D191), H198 (= H195), H261 (= H260), H275 (= H274)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (≠ I39), T39 (≠ E41), L40 (= L42), N69 (≠ E69), G95 (= G95), G96 (= G96), S97 (= S97), D100 (= D100), T138 (= T136), T139 (= T137), T142 (= T140), T147 (≠ S145), N149 (= N147), K160 (≠ V158), L187 (≠ V184), H198 (= H195), H275 (= H274)
7qlqAAA Lactaldehyde reductase (see paper)
30% identity, 99% coverage: 5:380/380 of query aligns to 4:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (≠ I39), T39 (≠ E41), L40 (= L42), G95 (= G95), G96 (= G96), S97 (= S97), T138 (= T136), T139 (= T137), T142 (= T140), K160 (≠ V158), G182 (≠ L179), M183 (≠ L180), L187 (≠ V184), H275 (= H274)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ N147), V164 (≠ I161), H198 (= H195), F252 (≠ L251), S253 (≠ G252), H261 (= H260), C360 (≠ L359)
- binding fe (iii) ion: D194 (= D191), H198 (= H195), H261 (= H260), H275 (= H274)
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
30% identity, 98% coverage: 9:380/380 of query aligns to 7:381/381 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 (= D88) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G95) 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 (= S97) 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 (= D100) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K103) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
32% identity, 83% coverage: 66:380/380 of query aligns to 66:400/403 of 3zdrA