SitesBLAST
Comparing WP_084938278.1 NCBI__GCF_002095475.1:WP_084938278.1 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)
31% identity, 98% coverage: 2:377/382 of query aligns to 9:382/382 of 3bfjA
7qlgAAA Lactaldehyde reductase (see paper)
29% identity, 99% coverage: 1:377/382 of query aligns to 4:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D187), H198 (= H191), H261 (= H256), H275 (= H270)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D32), T39 (≠ N34), L40 (≠ I35), N69 (≠ E64), G95 (= G90), G96 (= G91), S97 (= S92), D100 (= D95), T138 (= T131), T139 (= T132), T142 (= T135), T147 (= T140), N149 (= N142), K160 (= K153), L187 (≠ I180), H198 (= H191), H275 (= H270)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
29% identity, 99% coverage: 1:377/382 of query aligns to 5:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D187), H199 (= H191), H262 (= H256), H276 (= H270)
- binding nicotinamide-adenine-dinucleotide: D38 (= D32), T40 (≠ N34), L41 (≠ I35), G96 (= G90), G97 (= G91), S98 (= S92), T139 (= T131), T140 (= T132), V152 (≠ I144), K161 (= K153), G183 (≠ S175), M184 (= M176), L188 (≠ I180), D195 (= D187), H199 (= H191), H262 (= H256), H276 (= H270)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
29% identity, 99% coverage: 1:377/382 of query aligns to 5:382/382 of P0A9S1
- G16 (≠ Q12) mutation to D: No effect on enzyme activity.
- D38 (= D32) mutation to G: Enzyme can now use NADP.
- G96 (= G90) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D187) mutation to L: Complete loss of iron-binding.
- H199 (= H191) 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
29% identity, 99% coverage: 1:377/382 of query aligns to 5:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D32), T40 (≠ N34), L41 (≠ I35), N70 (≠ E64), G96 (= G90), G97 (= G91), S98 (= S92), T139 (= T131), T140 (= T132), T143 (= T135), V152 (≠ I144), K161 (= K153), G183 (≠ S175), M184 (= M176), L188 (≠ I180), H276 (= H270)
- binding fe (ii) ion: L258 (≠ T252), C361 (≠ R355)
- binding zinc ion: D195 (= D187), H199 (= H191), H262 (= H256), H276 (= H270)
7qlqAAA Lactaldehyde reductase (see paper)
29% identity, 99% coverage: 1:377/382 of query aligns to 4:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D32), T39 (≠ N34), L40 (≠ I35), G95 (= G90), G96 (= G91), S97 (= S92), T138 (= T131), T139 (= T132), T142 (= T135), K160 (= K153), G182 (≠ S175), M183 (= M176), L187 (≠ I180), H275 (= H270)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ N142), V164 (≠ I157), H198 (= H191), F252 (≠ I247), S253 (≠ A248), H261 (= H256), C360 (≠ R355)
- binding fe (iii) ion: D194 (= D187), H198 (= H191), H261 (= H256), H275 (= H270)
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
29% identity, 99% coverage: 1:377/382 of query aligns to 6:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D32), T41 (≠ N34), L42 (≠ I35), P70 (= P63), G97 (= G90), G98 (= G91), S99 (= S92), D102 (= D95), T140 (= T131), T141 (= T132), T144 (= T135), T149 (= T140), N151 (= N142), V153 (≠ I144), K162 (= K153), G184 (≠ S175), C185 (≠ M176), L189 (≠ I180), H277 (= H270)
- binding zinc ion: D196 (= D187), H200 (= H191), H263 (= H256), H277 (= H270)
Q59104 4-hydroxybutyrate dehydrogenase; 4HbD; Gamma-hydroxybutyrate dehydrogenase; GHBDH; EC 1.1.1.61 from Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha) (see paper)
30% identity, 92% coverage: 23:372/382 of query aligns to 28:377/382 of Q59104
- D193 (= D187) mutation to A: Retains very low activity.
- H197 (= H191) mutation to A: Loss of activity.
- H261 (= H256) mutation to A: Loss of activity.
- H265 (≠ Y260) mutation to A: 75% decrease in Vmax. Optimum pH is 9.5.; mutation to C: 95% decrease in Vmax. Optimum pH is 8.5.; mutation to D: Retains very low activity.; mutation to Y: Loss of activity.
- H280 (= H270) mutation to A: Retains very low activity.
1o2dA Crystal structure of alcohol dehydrogenase, iron-containing (tm0920) from thermotoga maritima at 1.30 a resolution (see paper)
32% identity, 91% coverage: 25:373/382 of query aligns to 29:353/359 of 1o2dA
- binding fe (iii) ion: D189 (= D187), H193 (= H191), H256 (= H256), H270 (= H270)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S38 (≠ N34), S39 (≠ I35), E68 (≠ P63), N69 (≠ E64), G95 (= G90), G96 (= G91), S97 (= S92), D100 (= D95), T136 (= T131), T137 (= T132), T140 (= T135), S142 (= S137), Y147 (≠ N142), I149 (= I144), K157 (= K153), S177 (= S175), M178 (= M176), L182 (≠ I180), D189 (= D187), H193 (= H191), H270 (= H270)
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
28% identity, 90% coverage: 10:352/382 of query aligns to 13:357/381 of P31005
- G13 (= G10) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (≠ Q12) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D83) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G90) 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 (= S92) 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 (= D95) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K98) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1vhdA Crystal structure of an iron containing alcohol dehydrogenase (see paper)
32% identity, 91% coverage: 25:373/382 of query aligns to 30:354/361 of 1vhdA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S39 (≠ N34), S40 (≠ I35), E69 (≠ P63), N70 (≠ E64), G96 (= G90), G97 (= G91), S98 (= S92), D101 (= D95), T137 (= T131), T138 (= T132), T141 (= T135), S143 (= S137), T146 (= T140), Y148 (≠ N142), I150 (= I144), K158 (= K153), S178 (= S175), M179 (= M176), L183 (≠ I180), D190 (= D187), H194 (= H191), H271 (= H270)
- binding zinc ion: D190 (= D187), H194 (= H191), H257 (= H256), H271 (= H270)
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
29% identity, 96% coverage: 12:377/382 of query aligns to 20:382/382 of 3ox4A