SitesBLAST
Comparing WP_019387402.1 NCBI__GCF_000283015.1:WP_019387402.1 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)
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)
50% identity, 96% coverage: 2:369/384 of query aligns to 1:368/383 of P0DJA2
- M1 (≠ L2) modified: Initiator methionine, Removed
- D39 (= D40) binding NAD(+)
- N71 (= N72) binding NAD(+)
- G98 (= G99) binding NAD(+)
- S99 (= S100) binding NAD(+)
- T138 (= T139) binding NAD(+)
- T139 (= T140) binding NAD(+)
- T147 (= T148) binding NAD(+)
- F149 (≠ N150) binding NAD(+)
- K160 (= K161) binding NAD(+)
- L179 (= L180) binding NAD(+)
- G182 (= G183) binding NAD(+)
- M183 (≠ K184) binding NAD(+)
- D194 (= D195) binding Fe(2+)
- H198 (= H199) binding Fe(2+)
- H263 (= H264) binding Fe(2+)
- H267 (= H268) binding NAD(+)
- H277 (= H278) binding Fe(2+); binding NAD(+)
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
51% identity, 95% coverage: 7:369/384 of query aligns to 5:367/382 of 3ox4A
- binding fe (ii) ion: D193 (= D195), H197 (= H199), H262 (= H264), H276 (= H278)
- binding nicotinamide-adenine-dinucleotide: D38 (= D40), F40 (≠ V42), M41 (≠ L43), N70 (= N72), G96 (= G98), G97 (= G99), S98 (= S100), T137 (= T139), T138 (= T140), F148 (≠ N150), I150 (≠ V152), G181 (= G183), M182 (≠ K184), L186 (= L188), H276 (= H278)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
51% identity, 95% coverage: 7:369/384 of query aligns to 5:367/382 of 3owoA
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
49% identity, 98% coverage: 9:384/384 of query aligns to 7:382/382 of 3bfjA
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
49% identity, 100% coverage: 1:383/384 of query aligns to 1:382/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D40), T41 (≠ V42), L42 (= L43), P70 (= P71), G97 (= G98), G98 (= G99), S99 (= S100), D102 (= D103), T140 (= T139), T141 (= T140), T144 (= T143), T149 (= T148), N151 (= N150), V153 (= V152), K162 (= K161), G184 (= G183), C185 (≠ K184), L189 (= L188), H277 (= H278)
- binding zinc ion: D196 (= D195), H200 (= H199), H263 (= H264), H277 (= H278)
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
47% identity, 98% coverage: 7:384/384 of query aligns to 4:381/381 of P31005
- G13 (= G16) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G18) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D91) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G98) 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 (= S100) 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 (= D103) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K106) 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)
49% identity, 98% coverage: 6:383/384 of query aligns to 4:381/382 of 2bi4A
- binding fe (iii) ion: D195 (= D195), H199 (= H199), H262 (= H264), H276 (= H278)
- binding nicotinamide-adenine-dinucleotide: D38 (= D40), T40 (≠ V42), L41 (= L43), G96 (= G98), G97 (= G99), S98 (= S100), T139 (= T139), T140 (= T140), V152 (= V152), K161 (= K161), G183 (= G183), M184 (≠ K184), L188 (= L188), D195 (= D195), H199 (= H199), H262 (= H264), H276 (= H278)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
49% identity, 98% coverage: 6:383/384 of query aligns to 4:381/382 of P0A9S1
- G16 (= G18) mutation to D: No effect on enzyme activity.
- D38 (= D40) mutation to G: Enzyme can now use NADP.
- G96 (= G98) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D195) mutation to L: Complete loss of iron-binding.
- H199 (= H199) 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
49% identity, 98% coverage: 6:383/384 of query aligns to 4:381/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D40), T40 (≠ V42), L41 (= L43), N70 (= N72), G96 (= G98), G97 (= G99), S98 (= S100), T139 (= T139), T140 (= T140), T143 (= T143), V152 (= V152), K161 (= K161), G183 (= G183), M184 (≠ K184), L188 (= L188), H276 (= H278)
- binding fe (ii) ion: L258 (= L260), C361 (= C363)
- binding zinc ion: D195 (= D195), H199 (= H199), H262 (= H264), H276 (= H278)
7qlgAAA Lactaldehyde reductase (see paper)
48% identity, 98% coverage: 6:383/384 of query aligns to 3:380/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D195), H198 (= H199), H261 (= H264), H275 (= H278)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D40), T39 (≠ V42), L40 (= L43), N69 (= N72), G95 (= G98), G96 (= G99), S97 (= S100), D100 (= D103), T138 (= T139), T139 (= T140), T142 (= T143), T147 (= T148), N149 (= N150), K160 (= K161), L187 (= L188), H198 (= H199), H275 (= H278)
7qlqAAA Lactaldehyde reductase (see paper)
48% identity, 98% coverage: 6:383/384 of query aligns to 3:380/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D40), T39 (≠ V42), L40 (= L43), G95 (= G98), G96 (= G99), S97 (= S100), T138 (= T139), T139 (= T140), T142 (= T143), K160 (= K161), G182 (= G183), M183 (≠ K184), L187 (= L188), H275 (= H278)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ N150), V164 (= V165), H198 (= H199), F252 (= F255), S253 (= S256), H261 (= H264), C360 (= C363)
- binding fe (iii) ion: D194 (= D195), H198 (= H199), H261 (= H264), H275 (= H278)
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
36% identity, 91% coverage: 34:384/384 of query aligns to 29:400/403 of 3zdrA