SitesBLAST
Comparing BPHYT_RS31860 FitnessBrowser__BFirm:BPHYT_RS31860 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)
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
36% identity, 92% coverage: 32:393/393 of query aligns to 27:401/403 of 3zdrA
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
34% identity, 98% coverage: 7:392/393 of query aligns to 5:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D200), H197 (= H204), H262 (= H269), H276 (= H283)
- binding nicotinamide-adenine-dinucleotide: D38 (= D40), F40 (≠ Y42), M41 (= M43), N70 (≠ D72), G96 (= G98), G97 (= G99), S98 (= S100), T137 (= T144), T138 (= T145), T141 (= T148), F148 (= F155), I150 (≠ V157), L178 (= L185), G181 (≠ D188), M182 (= M189), L186 (= L193), H197 (= H204), H266 (≠ R273), H276 (= H283)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
34% identity, 98% coverage: 7:392/393 of query aligns to 5:382/382 of 3owoA
1rrmA Crystal structure of lactaldehyde reductase
34% identity, 96% coverage: 15:393/393 of query aligns to 13:383/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D40), T40 (≠ Y42), L41 (≠ M43), P69 (≠ A71), N70 (≠ D72), G96 (= G98), G97 (= G99), S98 (= S100), T139 (= T144), T140 (= T145), T143 (= T148), V152 (= V157), K161 (= K166), M181 (≠ T186), G183 (≠ D188), M184 (= M189), P185 (= P190), L188 (= L193), H276 (= H283)
- binding fe (ii) ion: L258 (≠ V265), C361 (≠ S371)
- binding zinc ion: D195 (= D200), H199 (= H204), H262 (= H269), H276 (= H283)
7qlqAAA Lactaldehyde reductase (see paper)
35% identity, 96% coverage: 15:392/393 of query aligns to 12:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D40), T39 (≠ Y42), L40 (≠ M43), P68 (≠ A71), N69 (≠ D72), G95 (= G98), G96 (= G99), S97 (= S100), D100 (= D103), T138 (= T144), T139 (= T145), T142 (= T148), V151 (= V157), K160 (= K166), G182 (≠ D188), M183 (= M189), P184 (= P190), L187 (= L193), T191 (= T197), H275 (= H283)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ F155), V162 (≠ L168), V164 (≠ S170), H198 (= H204), F252 (≠ C260), S253 (= S261), H261 (= H269), H275 (= H283), C360 (≠ S371)
- binding fe (iii) ion: D194 (= D200), H198 (= H204), H261 (= H269), H275 (= H283)
7qlgAAA Lactaldehyde reductase (see paper)
35% identity, 96% coverage: 15:392/393 of query aligns to 12:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D200), H198 (= H204), H261 (= H269), H275 (= H283)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D40), T39 (≠ Y42), L40 (≠ M43), P68 (≠ A71), N69 (≠ D72), G95 (= G98), G96 (= G99), S97 (= S100), D100 (= D103), T138 (= T144), T139 (= T145), T142 (= T148), A144 (≠ S150), T147 (= T153), N149 (≠ F155), V151 (= V157), K160 (= K166), M180 (≠ T186), G182 (≠ D188), M183 (= M189), L187 (= L193), D194 (= D200), H198 (= H204), H275 (= H283)
6scgA Structure of adhe form 1 (see paper)
36% identity, 91% coverage: 31:387/393 of query aligns to 29:394/406 of 6scgA
- binding fe (iii) ion: D204 (= D200), H208 (= H204), H274 (= H269), H288 (= H283)
- binding nicotinamide-adenine-dinucleotide: D38 (= D40), F40 (≠ Y42), L41 (≠ M43), A69 (= A71), D70 (= D72), G96 (= G98), G97 (= G99), S98 (= S100), D101 (= D103), T148 (= T144), T149 (= T145), T152 (= T148), V161 (= V157), L189 (= L185), M193 (= M189), P194 (= P190), L197 (= L193), H278 (≠ R273)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
34% identity, 96% coverage: 15:392/393 of query aligns to 13:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D200), H199 (= H204), H262 (= H269), H276 (= H283)
- binding nicotinamide-adenine-dinucleotide: D38 (= D40), T40 (≠ Y42), L41 (≠ M43), P69 (≠ A71), N70 (≠ D72), G96 (= G98), G97 (= G99), S98 (= S100), D101 (= D103), T139 (= T144), T140 (= T145), T143 (= T148), V152 (= V157), K161 (= K166), M180 (≠ L185), M181 (≠ T186), G183 (≠ D188), M184 (= M189), P185 (= P190), L188 (= L193), D195 (= D200), H199 (= H204), H262 (= H269), H266 (≠ R273), H276 (= H283)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
34% identity, 96% coverage: 15:392/393 of query aligns to 13:382/382 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 (= D200) mutation to L: Complete loss of iron-binding.
- H199 (= H204) 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.
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
34% identity, 96% coverage: 15:392/393 of query aligns to 14:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D40), T41 (≠ Y42), L42 (≠ M43), P70 (≠ A71), N71 (≠ D72), G97 (= G98), G98 (= G99), S99 (= S100), D102 (= D103), T140 (= T144), T141 (= T145), T144 (= T148), A146 (≠ S150), T149 (= T153), N151 (≠ F155), Y152 (≠ T156), V153 (= V157), K162 (= K166), M182 (≠ T186), G184 (≠ D188), C185 (≠ M189), P186 (= P190), L189 (= L193), H200 (= H204), F254 (≠ C260), H277 (= H283)
- binding zinc ion: D196 (= D200), H200 (= H204), H263 (= H269), H277 (= H283)
7bvpA Adhe spirosome in extended conformation (see paper)
35% identity, 91% coverage: 31:387/393 of query aligns to 478:857/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: D487 (= D40), F489 (≠ Y42), A518 (= A71), D519 (= D72), P520 (= P73), G546 (= G99), S547 (= S100), D550 (= D103), T597 (= T144), T598 (= T145), T601 (= T148), S603 (= S150), F608 (= F155), V610 (= V157), K619 (= K166), M642 (= M189), L646 (= L193), F714 (≠ C260), H737 (= H283)
- binding zinc ion: D653 (= D200), H657 (= H204), H723 (= H269), H737 (= H283)
Sites not aligning to the query:
- binding nicotinamide-adenine-dinucleotide: 110, 111, 112, 113, 114, 139, 193, 194, 195, 197, 198, 201, 212, 213, 214, 246, 335, 337, 367, 417, 418, 419
6tqmA Escherichia coli adhe structure in its compact conformation (see paper)
35% identity, 91% coverage: 31:387/393 of query aligns to 478:857/869 of 6tqmA