SitesBLAST
Comparing 353293 FitnessBrowser__Btheta:353293 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)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
56% identity, 100% coverage: 2:384/384 of query aligns to 3:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D194), H199 (= H198), H262 (= H263), H276 (= H277)
- binding nicotinamide-adenine-dinucleotide: D38 (= D37), T40 (≠ D39), L41 (= L40), G96 (= G95), G97 (= G96), S98 (= S97), T139 (= T138), T140 (= T139), V152 (= V151), K161 (= K160), G183 (≠ S182), M184 (= M183), L188 (= L187), D195 (= D194), H199 (= H198), H262 (= H263), H276 (= H277)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
56% identity, 100% coverage: 2:384/384 of query aligns to 3:382/382 of P0A9S1
- G16 (= G15) mutation to D: No effect on enzyme activity.
- D38 (= D37) mutation to G: Enzyme can now use NADP.
- G96 (= G95) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D194) mutation to L: Complete loss of iron-binding.
- H199 (= H198) 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
56% identity, 100% coverage: 2:384/384 of query aligns to 3:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D37), T40 (≠ D39), L41 (= L40), N70 (= N69), G96 (= G95), G97 (= G96), S98 (= S97), T139 (= T138), T140 (= T139), T143 (= T142), V152 (= V151), K161 (= K160), G183 (≠ S182), M184 (= M183), L188 (= L187), H276 (= H277)
- binding fe (ii) ion: L258 (= L259), C361 (= C363)
- binding zinc ion: D195 (= D194), H199 (= H198), H262 (= H263), H276 (= H277)
7qlgAAA Lactaldehyde reductase (see paper)
56% identity, 100% coverage: 2:384/384 of query aligns to 2:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D194), H198 (= H198), H261 (= H263), H275 (= H277)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D37), T39 (≠ D39), L40 (= L40), N69 (= N69), G95 (= G95), G96 (= G96), S97 (= S97), D100 (= D100), T138 (= T138), T139 (= T139), T142 (= T142), T147 (= T147), N149 (= N149), K160 (= K160), L187 (= L187), H198 (= H198), H275 (= H277)
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
56% identity, 100% coverage: 2:384/384 of query aligns to 4:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D37), T41 (≠ D39), L42 (= L40), P70 (≠ A68), G97 (= G95), G98 (= G96), S99 (= S97), D102 (= D100), T140 (= T138), T141 (= T139), T144 (= T142), T149 (= T147), N151 (= N149), V153 (= V151), K162 (= K160), G184 (≠ S182), C185 (≠ M183), L189 (= L187), H277 (= H277)
- binding zinc ion: D196 (= D194), H200 (= H198), H263 (= H263), H277 (= H277)
7qlqAAA Lactaldehyde reductase (see paper)
56% identity, 100% coverage: 2:384/384 of query aligns to 2:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D37), T39 (≠ D39), L40 (= L40), G95 (= G95), G96 (= G96), S97 (= S97), T138 (= T138), T139 (= T139), T142 (= T142), K160 (= K160), G182 (≠ S182), M183 (= M183), L187 (= L187), H275 (= H277)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ N149), V164 (= V164), H198 (= H198), F252 (= F254), S253 (= S255), H261 (= H263), C360 (= C363)
- binding fe (iii) ion: D194 (= D194), H198 (= H198), H261 (= H263), H275 (= H277)
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)
46% identity, 93% coverage: 28:384/384 of query aligns to 30:383/383 of P0DJA2
- D39 (= D37) binding
- N71 (= N69) binding
- G98 (= G96) binding
- S99 (= S97) binding
- T138 (= T138) binding
- T139 (= T139) binding
- T147 (= T147) binding
- F149 (≠ N149) binding
- K160 (= K160) binding
- L179 (= L179) binding
- G182 (≠ S182) binding
- M183 (= M183) binding
- D194 (= D194) binding
- H198 (= H198) binding
- H263 (= H263) binding
- H267 (= H267) binding
- H277 (= H277) binding ; binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
46% identity, 93% coverage: 28:384/384 of query aligns to 29:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D194), H197 (= H198), H262 (= H263), H276 (= H277)
- binding nicotinamide-adenine-dinucleotide: D38 (= D37), F40 (≠ D39), M41 (≠ L40), N70 (= N69), G96 (= G95), G97 (= G96), S98 (= S97), T137 (= T138), T138 (= T139), F148 (≠ N149), I150 (≠ V151), G181 (≠ S182), M182 (= M183), L186 (= L187), H276 (= H277)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
46% identity, 93% coverage: 28:384/384 of query aligns to 29:382/382 of 3owoA
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
42% identity, 98% coverage: 10:384/384 of query aligns to 11:382/382 of 3bfjA
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
39% identity, 100% coverage: 1:384/384 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 (= 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.
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
37% identity, 92% coverage: 31:384/384 of query aligns to 29:400/403 of 3zdrA
6scgA Structure of adhe form 1 (see paper)
35% identity, 97% coverage: 6:377/384 of query aligns to 7:392/406 of 6scgA
- binding fe (iii) ion: D204 (= D194), H208 (= H198), H274 (= H263), H288 (= H277)
- binding nicotinamide-adenine-dinucleotide: D38 (= D37), F40 (≠ D39), A69 (= A68), D70 (≠ N69), G96 (= G95), G97 (= G96), S98 (= S97), T148 (= T138), T149 (= T139), T152 (= T142), V161 (= V151), L197 (= L187), H278 (= H267)
7bvpA Adhe spirosome in extended conformation (see paper)
34% identity, 97% coverage: 6:377/384 of query aligns to 456:855/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: D487 (= D37), F489 (≠ D39), D519 (≠ N69), S547 (= S97), D550 (= D100), T597 (= T138), T598 (= T139), T601 (= T142), V610 (= V151), K619 (= K160), L646 (= L187), H737 (= H277)
- binding zinc ion: D653 (= D194), H657 (= H198), H723 (= H263), H737 (= H277)
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
6tqmA Escherichia coli adhe structure in its compact conformation (see paper)
34% identity, 97% coverage: 6:377/384 of query aligns to 456:855/869 of 6tqmA
- binding fe (iii) ion: D653 (= D194), H657 (= H198), H723 (= H263), H737 (= H277)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: D487 (= D37), L490 (= L40), G545 (= G95), S547 (= S97), D550 (= D100), T597 (= T138), S603 (≠ A144), F608 (≠ N149), L646 (= L187), H727 (= H267)
P0A9Q7 Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli (strain K12) (see 8 papers)
34% identity, 97% coverage: 6:377/384 of query aligns to 456:855/891 of P0A9Q7
- D487 (= D37) binding
- D519 (≠ N69) binding
- GSPMD 546:550 (≠ GSSID 96:100) binding
- E568 (vs. gap) mutation to K: Partially restores protein stability and resistance to MCO damage; when associated with T-267.
- V610 (= V151) binding
- K619 (= K160) binding
- D653 (= D194) binding
- H657 (= H198) binding
- F670 (≠ M211) mutation F->A,E,V: Disrupts spirosome formation. Affects the forward activity of ALDH.
- H723 (= H263) binding
- H737 (= H277) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 110:115 binding
- 195 binding
- 213 binding
- 267 A→T: Shows aerobic growth ability on ethanol. Shows 5-6 fold increase in acetaldehyde dehydrogenase activity, but does not affect ethanol dehydrogenase activity. Shows decreased thermal enzyme stability and increased sensitivity to MCO damage. Shows increased protein stability and resistance to MCO; when associated with K-568.
- 335 binding
- 358 modified: N6-acetyllysine
- 419 binding
- 446:449 mutation Missing: Can form dimers, but does not assemble into long filaments. Strongly affects ALDH activity, but not ADH activity.
P0A9Q8 Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli O157:H7 (see paper)
34% identity, 97% coverage: 6:377/384 of query aligns to 456:855/891 of P0A9Q8
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, 96% coverage: 15:382/384 of query aligns to 15:376/382 of Q59104
- D193 (= D194) mutation to A: Retains very low activity.
- H197 (= H198) mutation to A: Loss of activity.
- H261 (= H263) mutation to A: Loss of activity.
- H265 (= H267) 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 (= H277) mutation to A: Retains very low activity.
A0A0S1X9S7 Alcohol dehydrogenase; EC 1.1.1.1 from Thermococcus barophilus (see paper)
32% identity, 100% coverage: 2:384/384 of query aligns to 8:376/378 of A0A0S1X9S7
- D195 (= D194) mutation to A: Disrupts the overall structure of the enzyme. Lack of acetaldehyde reduction activity and displays weak ethanol oxidation activity.
- H199 (= H198) mutation to A: Disrupts the overall structure of the enzyme. Retains 10% of ethanol oxidation and acetaldehyde reduction activities.
- H262 (= H263) mutation to A: Disrupts the overall structure of the enzyme. Displays weak ethanol oxidation and acetaldehyde reduction activities.
- H266 (= H267) mutation to A: Disrupts the overall structure of the enzyme. Displays higher acetaldehyde reduction activity (134%) but lower ethanol oxidation activity (36%).
- H274 (= H277) mutation to A: Disrupts the overall structure of the enzyme. Retains 20% of ethanol oxidation and acetaldehyde reduction activities.
5yvmA Crystal structure of the archaeal halo-thermophilic red sea brine pool alcohol dehydrogenase adh/d1 bound to nzq (see paper)
32% identity, 97% coverage: 12:384/384 of query aligns to 17:403/403 of 5yvmA
- binding manganese (ii) ion: D207 (= D194), H211 (= H198), H276 (= H263), H291 (= H277)
- binding 5,6-dihydroxy-nadp: G41 (≠ D37), N44 (≠ D39), M45 (≠ L40), P73 (≠ A68), N74 (= N69), G100 (= G95), G101 (= G96), S102 (= S97), D105 (= D100), S151 (≠ T138), T152 (= T139), T155 (= T142), T160 (= T147), Y162 (≠ N149), V164 (= V151), K173 (= K160), E195 (≠ S182), L200 (= L187), H211 (= H198), H276 (= H263), H280 (= H267), H291 (= H277)
Query Sequence
>353293 FitnessBrowser__Btheta:353293
MNRIILNETSYFGAGCRSVIAVEAARRGFKKAFFVTDKDLIKFGVAAEIIKVFDDNHIPY
ELYSDVKANPTIANVQNGVAAYKASGADFIVALGGGSSIDTAKGIGIVVNNPDFADVKSL
EGVADTKHKAVPTFALPTTAGTAAEVTINYVIIDEDARKKMVCVDPNDIPAVAIVDPELM
YSMPKGLTAATGMDALTHAIESYITPGAWAMSDMFELKAIEMIAQNLKAAVDNGKDTVAR
EAMSQAQYIAGMGFSNVGLGIVHSMAHPLGAFYDTPHGVANALLLPYVMEYNAESPAAPK
YIHIAKAMGVNTDGMTETEGVKAAIEAVKALSLSIGIPQKLHEINVKEEDIPALAVAAFN
DVCTGGNPRPTSVAEIEVLYRKAF
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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