SitesBLAST
Comparing BWI76_RS22480 FitnessBrowser__Koxy:BWI76_RS22480 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)
1rrmA Crystal structure of lactaldehyde reductase
70% identity, 100% coverage: 1:383/383 of query aligns to 1:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D38), T40 (≠ D40), L41 (= L41), N70 (= N70), G96 (= G96), G97 (= G97), S98 (= S98), T139 (= T139), T140 (= T140), T143 (= T143), V152 (= V152), K161 (= K161), G183 (≠ S183), M184 (= M184), L188 (= L188), H276 (= H276)
- binding fe (ii) ion: L258 (= L258), C361 (= C362)
- binding zinc ion: D195 (= D195), H199 (= H199), H262 (= H262), H276 (= H276)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
70% identity, 100% coverage: 1:383/383 of query aligns to 1:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D195), H199 (= H199), H262 (= H262), H276 (= H276)
- binding nicotinamide-adenine-dinucleotide: D38 (= D38), T40 (≠ D40), L41 (= L41), G96 (= G96), G97 (= G97), S98 (= S98), T139 (= T139), T140 (= T140), V152 (= V152), K161 (= K161), G183 (≠ S183), M184 (= M184), L188 (= L188), D195 (= D195), H199 (= H199), H262 (= H262), H276 (= H276)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
70% identity, 100% coverage: 1:383/383 of query aligns to 1:382/382 of P0A9S1
- 1:9 (vs. 1:9, 89% identical) mutation to M: Loss of enzyme activity, loss of dimerization.
- G16 (= G16) mutation to D: No effect on enzyme activity.
- D38 (= D38) mutation to G: Enzyme can now use NADP.
- G96 (= G96) 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.
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
69% identity, 100% coverage: 1:383/383 of query aligns to 2:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D38), T41 (≠ D40), L42 (= L41), P70 (= P69), G97 (= G96), G98 (= G97), S99 (= S98), D102 (= D101), T140 (= T139), T141 (= T140), T144 (= T143), T149 (= T148), N151 (= N150), V153 (= V152), K162 (= K161), G184 (≠ S183), C185 (≠ M184), L189 (= L188), H277 (= H276)
- binding zinc ion: D196 (= D195), H200 (= H199), H263 (= H262), H277 (= H276)
7qlgAAA Lactaldehyde reductase (see paper)
69% identity, 100% coverage: 2:383/383 of query aligns to 1:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D195), H198 (= H199), H261 (= H262), H275 (= H276)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D38), T39 (≠ D40), L40 (= L41), N69 (= N70), G95 (= G96), G96 (= G97), S97 (= S98), D100 (= D101), T138 (= T139), T139 (= T140), T142 (= T143), T147 (= T148), N149 (= N150), K160 (= K161), L187 (= L188), H198 (= H199), H275 (= H276)
7qlqAAA Lactaldehyde reductase (see paper)
69% identity, 100% coverage: 2:383/383 of query aligns to 1:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D38), T39 (≠ D40), L40 (= L41), G95 (= G96), G96 (= G97), S97 (= S98), T138 (= T139), T139 (= T140), T142 (= T143), K160 (= K161), G182 (≠ S183), M183 (= M184), L187 (= L188), H275 (= H276)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ N150), V164 (≠ Y165), H198 (= H199), F252 (= F253), S253 (= S254), H261 (= H262), C360 (= C362)
- binding fe (iii) ion: D194 (= D195), H198 (= H199), H261 (= H262), H275 (= H276)
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
40% identity, 99% coverage: 3:383/383 of query aligns to 6:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D195), H197 (= H199), H262 (= H262), H276 (= H276)
- binding nicotinamide-adenine-dinucleotide: D38 (= D38), F40 (≠ D40), M41 (≠ L41), N70 (= N70), G96 (= G96), G97 (= G97), S98 (= S98), T137 (= T139), T138 (= T140), F148 (≠ N150), I150 (≠ V152), G181 (≠ S183), M182 (= M184), L186 (= L188), H276 (= H276)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
40% identity, 99% coverage: 3:383/383 of query aligns to 6:382/382 of 3owoA
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)
40% identity, 99% coverage: 3:383/383 of query aligns to 7:383/383 of P0DJA2
- D39 (= D38) binding NAD(+)
- N71 (= N70) binding NAD(+)
- G98 (= G97) binding NAD(+)
- S99 (= S98) binding NAD(+)
- T138 (= T139) binding NAD(+)
- T139 (= T140) binding NAD(+)
- T147 (= T148) binding NAD(+)
- F149 (≠ N150) binding NAD(+)
- K160 (= K161) binding NAD(+)
- L179 (≠ M180) binding NAD(+)
- G182 (≠ S183) binding NAD(+)
- M183 (= M184) binding NAD(+)
- D194 (= D195) binding Fe(2+)
- H198 (= H199) binding Fe(2+)
- H263 (= H262) binding Fe(2+)
- H267 (= H266) binding NAD(+)
- H277 (= H276) binding Fe(2+); binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
42% identity, 99% coverage: 3:383/383 of query aligns to 3:382/382 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, 97% coverage: 11:381/383 of query aligns to 10:379/381 of P31005
- G13 (= G14) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G16) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D89) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G96) 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 (= S98) 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 (= D101) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K104) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6scgA Structure of adhe form 1 (see paper)
34% identity, 97% coverage: 7:378/383 of query aligns to 7:394/406 of 6scgA
- binding fe (iii) ion: D204 (= D195), H208 (= H199), H274 (= H262), H288 (= H276)
- binding nicotinamide-adenine-dinucleotide: D38 (= D38), F40 (≠ D40), A69 (≠ P69), D70 (≠ N70), G96 (= G96), G97 (= G97), S98 (= S98), T148 (= T139), T149 (= T140), T152 (= T143), V161 (= V152), L197 (= L188), H278 (= H266)
8uhwB The structure of the clostridium thermocellum adhe spirosome
35% identity, 97% coverage: 9:379/383 of query aligns to 454:853/859 of 8uhwB
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
34% identity, 92% coverage: 32:383/383 of query aligns to 29:400/403 of 3zdrA
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)
33% identity, 97% coverage: 7:378/383 of query aligns to 456:857/891 of P0A9Q7
- D487 (= D38) binding NAD(+)
- D519 (≠ N70) binding NAD(+)
- GSPMD 546:550 (≠ GSPQD 97:101) binding NAD(+)
- E568 (vs. gap) mutation to K: Partially restores protein stability and resistance to MCO damage; when associated with T-267.
- V610 (= V152) binding NAD(+)
- K619 (= K161) binding NAD(+)
- D653 (= D195) binding Fe cation
- H657 (= H199) binding Fe cation
- F670 (≠ L212) mutation F->A,E,V: Disrupts spirosome formation. Affects the forward activity of ALDH.
- H723 (= H262) binding Fe cation
- H737 (= H276) binding Fe cation
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 110:115 binding NAD(+)
- 195 binding NAD(+)
- 213 binding NAD(+)
- 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 NAD(+)
- 358 modified: N6-acetyllysine
- 419 binding NAD(+)
- 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)
33% identity, 97% coverage: 7:378/383 of query aligns to 456:857/891 of P0A9Q8
- D487 (= D38) binding NAD(+)
- D519 (≠ N70) binding NAD(+)
- GSPMD 546:550 (≠ GSPQD 97:101) binding NAD(+)
- TT 597:598 (= TT 139:140) binding NAD(+)
- L638 (≠ M180) binding NAD(+)
- D653 (= D195) binding Fe cation
- H657 (= H199) binding Fe cation
- H723 (= H262) binding Fe cation
- H737 (= H276) binding Fe cation
7bvpA Adhe spirosome in extended conformation (see paper)
33% identity, 97% coverage: 7:378/383 of query aligns to 456:857/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: D487 (= D38), F489 (≠ D40), D519 (≠ N70), S547 (= S98), D550 (= D101), T597 (= T139), T598 (= T140), T601 (= T143), V610 (= V152), K619 (= K161), L646 (= L188), H737 (= H276)
- binding zinc ion: D653 (= D195), H657 (= H199), H723 (= H262), H737 (= H276)
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)
33% identity, 97% coverage: 7:378/383 of query aligns to 456:857/869 of 6tqmA
- binding fe (iii) ion: D653 (= D195), H657 (= H199), H723 (= H262), H737 (= H276)
- 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 (= D38), L490 (= L41), G545 (= G96), S547 (= S98), D550 (= D101), T597 (= T139), S603 (≠ A145), F608 (≠ N150), L646 (= L188), H727 (= H266)
5yvmA Crystal structure of the archaeal halo-thermophilic red sea brine pool alcohol dehydrogenase adh/d1 bound to nzq (see paper)
32% identity, 99% coverage: 1:381/383 of query aligns to 4:401/403 of 5yvmA
- binding manganese (ii) ion: D207 (= D195), H211 (= H199), H276 (= H262), H291 (= H276)
- binding 5,6-dihydroxy-nadp: G41 (≠ T37), N44 (≠ D40), M45 (≠ L41), P73 (= P69), N74 (= N70), G100 (= G96), G101 (= G97), S102 (= S98), D105 (= D101), S151 (≠ T139), T152 (= T140), T155 (= T143), T160 (= T148), Y162 (≠ N150), V164 (= V152), K173 (= K161), E195 (≠ S183), L200 (= L188), H211 (= H199), H276 (= H262), H280 (= H266), H291 (= H276)
A0A0S1X9S7 Alcohol dehydrogenase; EC 1.1.1.1 from Thermococcus barophilus (see paper)
29% identity, 97% coverage: 13:383/383 of query aligns to 12:376/378 of A0A0S1X9S7
- D195 (= D195) mutation to A: Disrupts the overall structure of the enzyme. Lack of acetaldehyde reduction activity and displays weak ethanol oxidation activity.
- H199 (= H199) mutation to A: Disrupts the overall structure of the enzyme. Retains 10% of ethanol oxidation and acetaldehyde reduction activities.
- H262 (= H262) mutation to A: Disrupts the overall structure of the enzyme. Displays weak ethanol oxidation and acetaldehyde reduction activities.
- H266 (= H266) mutation to A: Disrupts the overall structure of the enzyme. Displays higher acetaldehyde reduction activity (134%) but lower ethanol oxidation activity (36%).
- H274 (= H276) mutation to A: Disrupts the overall structure of the enzyme. Retains 20% of ethanol oxidation and acetaldehyde reduction activities.
Query Sequence
>BWI76_RS22480 FitnessBrowser__Koxy:BWI76_RS22480
MAYRMILNETSYFGPGSISCIVDEVKKRGFKKALVVTDKDLIRFNVATKVLAILDGAGLP
YSIFDDVVPNPTIEVVQQGVETFKQSGADYLIAIGGGSPQDTCKAIGIIINNPEFADVRS
LEGGADTKNAAVPMIAIPTTAGTAAEVTINYVITDVQNRRKFVCYDPHDIPLVAIIDAEM
MASMPASLKAATGVDALTHAIEGYITKGAWELTDMLHLKAIEVIGRSLRASVQGDAQGAE
GMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYGTPHGVANAVLLPHIMAYNAEYTGEKYR
DIAVALGNKSAATMPIAEARQAAIEAVAQLNRDVNIPARLRDVGMKEEDIDALAAAALAD
VCTGGNPRDTNLEEIKTLYRQIF
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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