SitesBLAST
Comparing Pf1N1B4_2542 Alcohol dehydrogenase (EC 1.1.1.1) 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)
43% identity, 96% coverage: 15:382/382 of query aligns to 14:382/382 of 3bfjA
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)
37% identity, 100% coverage: 1:382/382 of query aligns to 1:383/383 of P0DJA2
- M1 (= M1) modified: Initiator methionine, Removed
- D39 (= D39) binding
- N71 (≠ D69) binding
- G98 (= G96) binding
- S99 (= S97) binding
- T138 (= T136) binding
- T139 (= T137) binding
- T147 (= T145) binding
- F149 (≠ V147) binding
- K160 (= K158) binding
- L179 (≠ M177) binding
- G182 (≠ T180) binding
- M183 (≠ C181) binding
- D194 (= D192) binding
- H198 (= H196) binding
- H263 (= H261) binding
- H267 (≠ Y265) binding
- H277 (= H275) binding ; binding
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
37% identity, 99% coverage: 4:382/382 of query aligns to 3:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D192), H197 (= H196), H262 (= H261), H276 (= H275)
- binding nicotinamide-adenine-dinucleotide: D38 (= D39), F40 (≠ A41), M41 (≠ L42), N70 (≠ D69), G96 (= G95), G97 (= G96), S98 (= S97), T137 (= T136), T138 (= T137), F148 (≠ V147), I150 (= I149), G181 (≠ T180), M182 (≠ C181), L186 (≠ V185), H276 (= H275)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
37% identity, 99% coverage: 4:382/382 of query aligns to 3:382/382 of 3owoA
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
36% identity, 99% coverage: 3:381/382 of query aligns to 1:380/381 of P31005
- M1 (≠ L3) modified: Initiator methionine, Removed
- 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.
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
39% identity, 96% coverage: 15:382/382 of query aligns to 15:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D39), T41 (≠ A41), L42 (= L42), P70 (= P68), G97 (= G95), G98 (= G96), S99 (= S97), D102 (= D100), T140 (= T136), T141 (= T137), T144 (= T140), T149 (= T145), N151 (≠ V147), V153 (≠ I149), K162 (= K158), G184 (≠ T180), C185 (= C181), L189 (≠ V185), H277 (= H275)
- binding zinc ion: D196 (= D192), H200 (= H196), H263 (= H261), H277 (= H275)
7qlqAAA Lactaldehyde reductase (see paper)
39% identity, 96% coverage: 15:382/382 of query aligns to 13:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D39), T39 (≠ A41), L40 (= L42), G95 (= G95), G96 (= G96), S97 (= S97), T138 (= T136), T139 (= T137), T142 (= T140), K160 (= K158), G182 (≠ T180), M183 (≠ C181), L187 (≠ V185), H275 (= H275)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ V147), V164 (= V162), H198 (= H196), F252 (= F252), S253 (≠ G253), H261 (= H261), C360 (≠ L361)
- binding fe (iii) ion: D194 (= D192), H198 (= H196), H261 (= H261), H275 (= H275)
7qlgAAA Lactaldehyde reductase (see paper)
39% identity, 96% coverage: 15:382/382 of query aligns to 13:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D192), H198 (= H196), H261 (= H261), H275 (= H275)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D39), T39 (≠ A41), L40 (= L42), N69 (≠ D69), G95 (= G95), G96 (= G96), S97 (= S97), D100 (= D100), T138 (= T136), T139 (= T137), T142 (= T140), T147 (= T145), N149 (≠ V147), K160 (= K158), L187 (≠ V185), H198 (= H196), H275 (= H275)
1rrmA Crystal structure of lactaldehyde reductase
39% identity, 96% coverage: 15:382/382 of query aligns to 14:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D39), T40 (≠ A41), L41 (= L42), N70 (≠ D69), G96 (= G95), G97 (= G96), S98 (= S97), T139 (= T136), T140 (= T137), T143 (= T140), V152 (≠ I149), K161 (= K158), G183 (≠ T180), M184 (≠ C181), L188 (≠ V185), H276 (= H275)
- binding fe (ii) ion: L258 (≠ V257), C361 (≠ L361)
- binding zinc ion: D195 (= D192), H199 (= H196), H262 (= H261), H276 (= H275)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
39% identity, 96% coverage: 15:382/382 of query aligns to 14:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D192), H199 (= H196), H262 (= H261), H276 (= H275)
- binding nicotinamide-adenine-dinucleotide: D38 (= D39), T40 (≠ A41), L41 (= L42), G96 (= G95), G97 (= G96), S98 (= S97), T139 (= T136), T140 (= T137), V152 (≠ I149), K161 (= K158), G183 (≠ T180), M184 (≠ C181), L188 (≠ V185), D195 (= D192), H199 (= H196), H262 (= H261), H276 (= H275)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
39% identity, 96% coverage: 15:382/382 of query aligns to 14:382/382 of P0A9S1
- G16 (= G17) mutation to D: No effect on enzyme activity.
- D38 (= D39) mutation to G: Enzyme can now use NADP.
- G96 (= G95) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D192) mutation to L: Complete loss of iron-binding.
- H199 (= H196) 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.
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
35% identity, 100% coverage: 2:382/382 of query aligns to 1:400/403 of 3zdrA
Q59104 4-hydroxybutyrate dehydrogenase; 4HbD; Gamma-hydroxybutyrate dehydrogenase; GHBDH; EC 1.1.1.61 from Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha) (see paper)
34% identity, 95% coverage: 17:377/382 of query aligns to 15:377/382 of Q59104
- D193 (= D192) mutation to A: Retains very low activity.
- H197 (= H196) mutation to A: Loss of activity.
- H261 (= H261) mutation to A: Loss of activity.
- H265 (≠ Y265) 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 (= H275) mutation to A: Retains very low activity.
6jkpA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense in complex with NAD+ (see paper)
32% identity, 90% coverage: 35:379/382 of query aligns to 35:370/376 of 6jkpA
- binding nicotinamide-adenine-dinucleotide: F42 (≠ L42), G96 (= G96), D100 (= D100), T137 (= T136), T138 (= T137), T141 (= T140), S143 (= S142), T146 (= T145), S181 (≠ T180), V182 (≠ C181), P183 (= P182)
6jkoA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense (see paper)
32% identity, 90% coverage: 35:379/382 of query aligns to 35:370/376 of 6jkoA
1vhdA Crystal structure of an iron containing alcohol dehydrogenase (see paper)
40% identity, 65% coverage: 57:306/382 of query aligns to 58:302/361 of 1vhdA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: E69 (≠ P68), N70 (≠ D69), G96 (= G95), G97 (= G96), S98 (= S97), D101 (= D100), T137 (= T136), T138 (= T137), T141 (= T140), S143 (= S142), T146 (= T145), Y148 (≠ V147), I150 (= I149), K158 (= K158), S178 (≠ T180), M179 (≠ C181), L183 (≠ V185), D190 (= D192), H194 (= H196), H271 (= H275)
- binding zinc ion: D190 (= D192), H194 (= H196), H257 (= H261), H271 (= H275)
Sites not aligning to the query:
1o2dA Crystal structure of alcohol dehydrogenase, iron-containing (tm0920) from thermotoga maritima at 1.30 a resolution (see paper)
40% identity, 65% coverage: 57:306/382 of query aligns to 57:301/359 of 1o2dA
- binding fe (iii) ion: D189 (= D192), H193 (= H196), H256 (= H261), H270 (= H275)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: E68 (≠ P68), N69 (≠ D69), G95 (= G95), G96 (= G96), S97 (= S97), D100 (= D100), T136 (= T136), T137 (= T137), T140 (= T140), S142 (= S142), Y147 (≠ V147), I149 (= I149), K157 (= K158), S177 (≠ T180), M178 (≠ C181), L182 (≠ V185), D189 (= D192), H193 (= H196), H270 (= H275)
Sites not aligning to the query:
A0A0S1X9S7 Alcohol dehydrogenase; EC 1.1.1.1 from Thermococcus barophilus (see paper)
34% identity, 82% coverage: 69:382/382 of query aligns to 67:376/378 of A0A0S1X9S7
- D195 (= D192) mutation to A: Disrupts the overall structure of the enzyme. Lack of acetaldehyde reduction activity and displays weak ethanol oxidation activity.
- H199 (= H196) mutation to A: Disrupts the overall structure of the enzyme. Retains 10% of ethanol oxidation and acetaldehyde reduction activities.
- H262 (= H261) mutation to A: Disrupts the overall structure of the enzyme. Displays weak ethanol oxidation and acetaldehyde reduction activities.
- H266 (≠ Y265) mutation to A: Disrupts the overall structure of the enzyme. Displays higher acetaldehyde reduction activity (134%) but lower ethanol oxidation activity (36%).
- H274 (= H275) mutation to A: Disrupts the overall structure of the enzyme. Retains 20% of ethanol oxidation and acetaldehyde reduction activities.
6c75B Structure of iron containing alcohol dehydrogenase from thermococcus thioreducens in a monoclinic crystal form (see paper)
35% identity, 80% coverage: 6:310/382 of query aligns to 2:310/378 of 6c75B
6c75A Structure of iron containing alcohol dehydrogenase from thermococcus thioreducens in a monoclinic crystal form (see paper)
35% identity, 80% coverage: 6:310/382 of query aligns to 2:310/378 of 6c75A
- binding fe (iii) ion: D193 (= D192), H197 (= H196), H260 (= H261), H272 (= H275)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S33 (≠ D39), S35 (≠ A41), G91 (= G95), G92 (= G96), S93 (= S97), D96 (= D100), S139 (≠ T136), T140 (= T137), A143 (≠ T140), S148 (≠ T145), V152 (≠ I149), K159 (= K158), T181 (= T180), M182 (≠ C181), P183 (= P182), V186 (= V185), F251 (= F252), H272 (= H275)
Query Sequence
>Pf1N1B4_2542 Alcohol dehydrogenase (EC 1.1.1.1)
MSLSSFKIAHKLITGAGAIEQLAAELTRLDIDNPLIVTDAALVKSGTVELALAQLGERSY
EIFDRVLPDPEIAIVEDCMRVYREGGHDGLIGLGGGSAIDIAKSVAAYAGYHGALEDLFG
IDQVPRKGPPLIAIPTTAGTGSEVTNVAILSDKIAQLKKGIVSDYLLPDVALISPQMTLT
CPRSVTAASGVDALVHAIESYLSLNASPITDALAIGAIKLITKALPKAYANPSHLQARED
MATASLMAGMAFGNAGVGAVHALAYPLGGRFNIAHGVSNALLLPYVMTWNKMACVERMQD
IAEAMGVKTAHLSANEAADKAVEAMTELCAAVEIPLGLRSFGVPEDAIPAMAVEAAGIER
LMRNNPRKLSTVDIEKIYRAAY
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory