SitesBLAST
Comparing SM_b20147 FitnessBrowser__Smeli:SM_b20147 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)
32% identity, 90% coverage: 37:368/368 of query aligns to 47:383/383 of P0DJA2
- N71 (≠ E60) binding
- G98 (= G87) binding
- S99 (= S88) binding
- T138 (= T127) binding
- T139 (= T128) binding
- T147 (≠ G136) binding
- F149 (≠ R138) binding
- K160 (= K149) binding
- L179 (= L168) binding
- G182 (≠ S171) binding
- M183 (≠ V172) binding
- D194 (= D183) binding
- H198 (= H187) binding
- H263 (= H252) binding
- H267 (≠ Y256) binding
- H277 (= H266) binding ; binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 39 binding
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
32% identity, 90% coverage: 37:368/368 of query aligns to 46:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D183), H197 (= H187), H262 (= H252), H276 (= H266)
- binding nicotinamide-adenine-dinucleotide: N70 (≠ E60), G96 (= G86), G97 (= G87), S98 (= S88), T137 (= T127), T138 (= T128), F148 (≠ R138), I150 (≠ L140), G181 (≠ S171), M182 (≠ V172), L186 (≠ V176), H276 (= H266)
Sites not aligning to the query:
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
32% identity, 90% coverage: 37:368/368 of query aligns to 46:382/382 of 3owoA
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
31% identity, 100% coverage: 1:368/368 of query aligns to 1:381/381 of P31005
- M1 (= M1) modified: Initiator methionine, Removed
- G13 (= G13) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G15) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D79) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G86) 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 (= S88) 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 (= D91) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K94) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
30% identity, 86% coverage: 53:368/368 of query aligns to 62:400/403 of 3zdrA
6jkpA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense in complex with NAD+ (see paper)
31% identity, 97% coverage: 6:362/368 of query aligns to 8:366/376 of 6jkpA
- binding nicotinamide-adenine-dinucleotide: F42 (vs. gap), G96 (= G87), D100 (= D91), T137 (= T127), T138 (= T128), T141 (= T131), S143 (= S133), T146 (≠ G136), S181 (= S171), V182 (= V172), P183 (= P173)
6jkoA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense (see paper)
31% identity, 97% coverage: 6:362/368 of query aligns to 8:366/376 of 6jkoA
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
31% identity, 87% coverage: 50:368/368 of query aligns to 60:382/382 of 3bfjA
A0A0S1X9S7 Alcohol dehydrogenase; EC 1.1.1.1 from Thermococcus barophilus (see paper)
30% identity, 98% coverage: 9:368/368 of query aligns to 9:376/378 of A0A0S1X9S7
- D195 (= D183) mutation to A: Disrupts the overall structure of the enzyme. Lack of acetaldehyde reduction activity and displays weak ethanol oxidation activity.
- H199 (= H187) mutation to A: Disrupts the overall structure of the enzyme. Retains 10% of ethanol oxidation and acetaldehyde reduction activities.
- H262 (= H252) mutation to A: Disrupts the overall structure of the enzyme. Displays weak ethanol oxidation and acetaldehyde reduction activities.
- H266 (≠ Y256) mutation to A: Disrupts the overall structure of the enzyme. Displays higher acetaldehyde reduction activity (134%) but lower ethanol oxidation activity (36%).
- H274 (= H266) mutation to A: Disrupts the overall structure of the enzyme. Retains 20% of ethanol oxidation and acetaldehyde reduction activities.
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
29% identity, 86% coverage: 53:368/368 of query aligns to 63:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D183), H199 (= H187), H262 (= H252), H276 (= H266)
- binding nicotinamide-adenine-dinucleotide: G96 (= G86), G97 (= G87), S98 (= S88), T139 (= T127), T140 (= T128), V152 (≠ L140), K161 (= K149), G183 (≠ S171), M184 (≠ V172), L188 (≠ V176), D195 (= D183), H199 (= H187), H262 (= H252), H276 (= H266)
Sites not aligning to the query:
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
29% identity, 86% coverage: 53:368/368 of query aligns to 63:382/382 of P0A9S1
- G96 (= G86) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D183) mutation to L: Complete loss of iron-binding.
- H199 (= H187) 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.
- 16 G→D: No effect on enzyme activity.
- 38 D→G: Enzyme can now use NADP.
1rrmA Crystal structure of lactaldehyde reductase
29% identity, 86% coverage: 53:368/368 of query aligns to 63:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: N70 (≠ E60), G96 (= G86), G97 (= G87), S98 (= S88), T139 (= T127), T140 (= T128), T143 (= T131), V152 (≠ L140), K161 (= K149), G183 (≠ S171), M184 (≠ V172), L188 (≠ V176), H276 (= H266)
- binding fe (ii) ion: L258 (≠ T248), C361 (vs. gap)
- binding zinc ion: D195 (= D183), H199 (= H187), H262 (= H252), H276 (= H266)
Sites not aligning to the query:
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
29% identity, 86% coverage: 53:368/368 of query aligns to 64:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: P70 (≠ G59), G97 (= G86), G98 (= G87), S99 (= S88), D102 (= D91), T140 (= T127), T141 (= T128), T144 (= T131), T149 (≠ G136), N151 (≠ R138), V153 (≠ L140), K162 (= K149), G184 (≠ S171), C185 (≠ V172), L189 (≠ V176), H277 (= H266)
- binding zinc ion: D196 (= D183), H200 (= H187), H263 (= H252), H277 (= H266)
Sites not aligning to the query:
7qlqAAA Lactaldehyde reductase (see paper)
29% identity, 86% coverage: 53:368/368 of query aligns to 62:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: G95 (= G86), G96 (= G87), S97 (= S88), T138 (= T127), T139 (= T128), T142 (= T131), K160 (= K149), G182 (≠ S171), M183 (≠ V172), L187 (≠ V176), H275 (= H266)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ R138), V164 (≠ E153), H198 (= H187), F252 (≠ L243), S253 (≠ G244), H261 (= H252), C360 (vs. gap)
- binding fe (iii) ion: D194 (= D183), H198 (= H187), H261 (= H252), H275 (= H266)
Sites not aligning to the query:
7qlgAAA Lactaldehyde reductase (see paper)
29% identity, 86% coverage: 53:368/368 of query aligns to 62:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D183), H198 (= H187), H261 (= H252), H275 (= H266)
- binding 1,4-dihydronicotinamide adenine dinucleotide: N69 (≠ E60), G95 (= G86), G96 (= G87), S97 (= S88), D100 (= D91), T138 (= T127), T139 (= T128), T142 (= T131), T147 (≠ G136), N149 (≠ R138), K160 (= K149), L187 (≠ V176), H198 (= H187), H275 (= H266)
Sites not aligning to the query:
6scgA Structure of adhe form 1 (see paper)
30% identity, 81% coverage: 38:334/368 of query aligns to 43:362/406 of 6scgA
- binding fe (iii) ion: D204 (= D183), H208 (= H187), H274 (= H252), H288 (= H266)
- binding nicotinamide-adenine-dinucleotide: A69 (≠ G59), D70 (≠ E60), G96 (= G86), G97 (= G87), S98 (= S88), T148 (= T127), T149 (= T128), T152 (= T131), V161 (≠ L140), L197 (≠ V176), H278 (≠ Y256)
Sites not aligning to the query:
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, 84% coverage: 50:359/368 of query aligns to 57:373/382 of Q59104
- D193 (= D183) mutation to A: Retains very low activity.
- H197 (= H187) mutation to A: Loss of activity.
- H261 (= H252) mutation to A: Loss of activity.
- H265 (≠ Y256) 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 (= H266) 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, 86% coverage: 53:368/368 of query aligns to 62:357/359 of 1o2dA
- binding fe (iii) ion: D189 (= D183), H193 (= H187), H256 (= H252), H270 (= H266)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: E68 (≠ G59), N69 (≠ E60), G95 (= G86), G96 (= G87), S97 (= S88), D100 (= D91), T136 (= T127), T137 (= T128), T140 (= T131), S142 (= S133), Y147 (≠ R138), I149 (≠ L140), K157 (= K149), S177 (= S171), M178 (≠ V172), L182 (≠ V176), D189 (= D183), H193 (= H187), H270 (= H266)
Sites not aligning to the query:
1vhdA Crystal structure of an iron containing alcohol dehydrogenase (see paper)
32% identity, 86% coverage: 53:368/368 of query aligns to 63:358/361 of 1vhdA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: E69 (≠ G59), N70 (≠ E60), G96 (= G86), G97 (= G87), S98 (= S88), D101 (= D91), T137 (= T127), T138 (= T128), T141 (= T131), S143 (= S133), T146 (≠ G136), Y148 (≠ R138), I150 (≠ L140), K158 (= K149), S178 (= S171), M179 (≠ V172), L183 (≠ V176), D190 (= D183), H194 (= H187), H271 (= H266)
- binding zinc ion: D190 (= D183), H194 (= H187), H257 (= H252), H271 (= H266)
Sites not aligning to the query:
7bvpA Adhe spirosome in extended conformation (see paper)
29% identity, 81% coverage: 38:334/368 of query aligns to 492:825/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: D519 (≠ E60), S547 (= S88), D550 (= D91), T597 (= T127), T598 (= T128), T601 (= T131), V610 (≠ L140), K619 (= K149), L646 (≠ V176), H737 (= H266)
- binding zinc ion: D653 (= D183), H657 (= H187), H723 (= H252), H737 (= H266)
Sites not aligning to the query:
- binding nicotinamide-adenine-dinucleotide: 112, 113, 139, 194, 195, 198, 212, 213, 214, 246, 335, 337, 367, 418, 419, 487, 489
Query Sequence
>SM_b20147 FitnessBrowser__Smeli:SM_b20147
MITIHQPRRLVVGAGSRGEVGAWAGQAGSTLVIATPVTSGFADSLKLSGKVTLFDAIPGE
PDITTLEAALEAARNARPDLIVGLGGGSVMDVAKLVAVLWDSGQSLADVAGPNRVAGRNT
RLAQVATTAGTGSEAGIRSLITDPGKGSKIAVESPHMIADLAVLDPELTYSVPPAVTAAT
GVDAMAHCVEAFTNRKAHTMIDGFARMGFNLVGKYLARAVRDGEDTEAREGMMLASYYGG
ICLGPVNTAAGHAISYPLGTLLHLPHGLANAIIFPHVLAFNQPSAAAKTAEVADALGLGQ
GLSQRDLLSAAKDFCAGLGIEMSLAVNGAKAADLPRFAADAHAIRRLMDNNPVDMSEADV
LEIYRAAF
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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