SitesBLAST
Comparing 16552 FitnessBrowser__Keio:16552 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)
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
37% identity, 92% coverage: 23:387/395 of query aligns to 3:373/381 of P31005
- G13 (= G33) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G35) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D108) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G115) 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 (= S117) 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 (= D120) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K123) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1rrmA Crystal structure of lactaldehyde reductase
40% identity, 92% coverage: 33:394/395 of query aligns to 14:381/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D57), T40 (≠ F59), L41 (= L60), N70 (≠ E89), G96 (= G115), G97 (= G116), S98 (= S117), T139 (= T156), T140 (= T157), T143 (= T160), V152 (= V169), K161 (= K178), G183 (= G200), M184 (≠ V201), L188 (≠ V205), H276 (= H295)
- binding fe (ii) ion: L258 (= L277), C361 (= C374)
- binding zinc ion: D195 (= D212), H199 (= H216), H262 (= H281), H276 (= H295)
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, 94% coverage: 23:394/395 of query aligns to 5:382/383 of P0DJA2
- D39 (= D57) binding
- N71 (≠ E89) binding
- G98 (= G116) binding
- S99 (= S117) binding
- T138 (= T156) binding
- T139 (= T157) binding
- T147 (= T165) binding
- F149 (≠ V167) binding
- K160 (= K178) binding
- L179 (= L197) binding
- G182 (= G200) binding
- M183 (≠ V201) binding
- D194 (= D212) binding
- H198 (= H216) binding
- H263 (= H281) binding
- H267 (= H285) binding
- H277 (= H295) binding ; binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
40% identity, 92% coverage: 33:394/395 of query aligns to 14:381/382 of 2bi4A
- binding fe (iii) ion: D195 (= D212), H199 (= H216), H262 (= H281), H276 (= H295)
- binding nicotinamide-adenine-dinucleotide: D38 (= D57), T40 (≠ F59), L41 (= L60), G96 (= G115), G97 (= G116), S98 (= S117), T139 (= T156), T140 (= T157), V152 (= V169), K161 (= K178), G183 (= G200), M184 (≠ V201), L188 (≠ V205), D195 (= D212), H199 (= H216), H262 (= H281), H276 (= H295)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
40% identity, 92% coverage: 33:394/395 of query aligns to 14:381/382 of P0A9S1
- G16 (= G35) mutation to D: No effect on enzyme activity.
- D38 (= D57) mutation to G: Enzyme can now use NADP.
- G96 (= G115) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D212) mutation to L: Complete loss of iron-binding.
- H199 (= H216) 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.
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
37% identity, 94% coverage: 23:394/395 of query aligns to 4:381/382 of 3ox4A
- binding fe (ii) ion: D193 (= D212), H197 (= H216), H262 (= H281), H276 (= H295)
- binding nicotinamide-adenine-dinucleotide: D38 (= D57), F40 (= F59), M41 (≠ L60), N70 (≠ E89), G96 (= G115), G97 (= G116), S98 (= S117), T137 (= T156), T138 (= T157), F148 (≠ V167), I150 (≠ V169), G181 (= G200), M182 (≠ V201), L186 (≠ V205), H276 (= H295)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
37% identity, 94% coverage: 23:394/395 of query aligns to 4:381/382 of 3owoA
7qlgAAA Lactaldehyde reductase (see paper)
40% identity, 92% coverage: 33:394/395 of query aligns to 13:380/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D212), H198 (= H216), H261 (= H281), H275 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D57), T39 (≠ F59), L40 (= L60), N69 (≠ E89), G95 (= G115), G96 (= G116), S97 (= S117), D100 (= D120), T138 (= T156), T139 (= T157), T142 (= T160), T147 (= T165), N149 (≠ V167), K160 (= K178), L187 (≠ V205), H198 (= H216), H275 (= H295)
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
40% identity, 92% coverage: 33:394/395 of query aligns to 15:382/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D57), T41 (≠ F59), L42 (= L60), P70 (≠ G88), G97 (= G115), G98 (= G116), S99 (= S117), D102 (= D120), T140 (= T156), T141 (= T157), T144 (= T160), T149 (= T165), N151 (≠ V167), V153 (= V169), K162 (= K178), G184 (= G200), C185 (≠ V201), L189 (≠ V205), H277 (= H295)
- binding zinc ion: D196 (= D212), H200 (= H216), H263 (= H281), H277 (= H295)
7qlqAAA Lactaldehyde reductase (see paper)
40% identity, 92% coverage: 33:394/395 of query aligns to 13:380/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D57), T39 (≠ F59), L40 (= L60), G95 (= G115), G96 (= G116), S97 (= S117), T138 (= T156), T139 (= T157), T142 (= T160), K160 (= K178), G182 (= G200), M183 (≠ V201), L187 (≠ V205), H275 (= H295)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ V167), V164 (≠ A182), H198 (= H216), F252 (= F272), S253 (= S273), H261 (= H281), C360 (= C374)
- binding fe (iii) ion: D194 (= D212), H198 (= H216), H261 (= H281), H275 (= H295)
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
35% identity, 95% coverage: 20:394/395 of query aligns to 1:381/382 of 3bfjA
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
33% identity, 94% coverage: 24:394/395 of query aligns to 5:399/403 of 3zdrA
6scgA Structure of adhe form 1 (see paper)
32% identity, 92% coverage: 25:388/395 of query aligns to 6:395/406 of 6scgA
- binding fe (iii) ion: D204 (= D212), H208 (= H216), H274 (= H281), H288 (= H295)
- binding nicotinamide-adenine-dinucleotide: D38 (= D57), F40 (= F59), A69 (≠ G88), D70 (≠ E89), G96 (= G115), G97 (= G116), S98 (= S117), T148 (= T156), T149 (= T157), T152 (= T160), V161 (= V169), L197 (≠ V205), H278 (= H285)
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)
32% identity, 90% coverage: 35:388/395 of query aligns to 465:858/891 of P0A9Q7
- D487 (= D57) binding
- D519 (≠ E89) binding
- GSPMD 546:550 (≠ GSVLD 116:120) binding
- E568 (= E138) mutation to K: Partially restores protein stability and resistance to MCO damage; when associated with T-267.
- V610 (= V169) binding
- K619 (= K178) binding
- D653 (= D212) binding
- H657 (= H216) binding
- F670 (= F229) mutation F->A,E,V: Disrupts spirosome formation. Affects the forward activity of ALDH.
- H723 (= H281) binding
- H737 (= H295) 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)
32% identity, 90% coverage: 35:388/395 of query aligns to 465:858/891 of P0A9Q8
7bvpA Adhe spirosome in extended conformation (see paper)
32% identity, 90% coverage: 35:388/395 of query aligns to 465:858/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: D487 (= D57), F489 (= F59), D519 (≠ E89), S547 (= S117), D550 (= D120), T597 (= T156), T598 (= T157), T601 (= T160), V610 (= V169), K619 (= K178), L646 (≠ V205), H737 (= H295)
- binding zinc ion: D653 (= D212), H657 (= H216), H723 (= H281), H737 (= H295)
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)
32% identity, 90% coverage: 35:388/395 of query aligns to 465:858/869 of 6tqmA
- binding fe (iii) ion: D653 (= D212), H657 (= H216), H723 (= H281), H737 (= H295)
- 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 (= D57), L490 (= L60), G545 (= G115), S547 (= S117), D550 (= D120), T597 (= T156), S603 (= S162), F608 (≠ V167), L646 (≠ V205), H727 (= H285)
A0A0S1X9S7 Alcohol dehydrogenase; EC 1.1.1.1 from Thermococcus barophilus (see paper)
36% identity, 78% coverage: 88:394/395 of query aligns to 66:375/378 of A0A0S1X9S7
- D195 (= D212) mutation to A: Disrupts the overall structure of the enzyme. Lack of acetaldehyde reduction activity and displays weak ethanol oxidation activity.
- H199 (= H216) mutation to A: Disrupts the overall structure of the enzyme. Retains 10% of ethanol oxidation and acetaldehyde reduction activities.
- H262 (= H281) mutation to A: Disrupts the overall structure of the enzyme. Displays weak ethanol oxidation and acetaldehyde reduction activities.
- H266 (= H285) mutation to A: Disrupts the overall structure of the enzyme. Displays higher acetaldehyde reduction activity (134%) but lower ethanol oxidation activity (36%).
- H274 (= H295) 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)
34% identity, 92% coverage: 33:394/395 of query aligns to 11:374/378 of 6c75B
6c75A Structure of iron containing alcohol dehydrogenase from thermococcus thioreducens in a monoclinic crystal form (see paper)
34% identity, 92% coverage: 33:394/395 of query aligns to 11:374/378 of 6c75A
- binding fe (iii) ion: D193 (= D212), H197 (= H216), H260 (= H281), H272 (= H295)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S33 (≠ D57), S35 (≠ F59), G91 (= G115), G92 (= G116), S93 (= S117), D96 (= D120), S139 (≠ T156), T140 (= T157), A143 (≠ T160), S148 (≠ T165), V152 (= V169), K159 (= K178), T181 (≠ G200), M182 (≠ V201), P183 (= P202), V186 (= V205), F251 (= F272), H272 (= H295)
Query Sequence
>16552 FitnessBrowser__Keio:16552
MQNELQTALFQAFDTLNLQRVKTFSVPPVTLCGPGSVSSCGQQAQTRGLKHLFVMADSFL
HQAGMTAGLTRSLTVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIAFGGGSVLD
AAKAVTLLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQV
LAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAM
IGKSLPKAVGYGHDLAARESMLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANA
MLLPTVMEFNRMVCRERFSQIGRALRTKKSDDRDAINAVSELIAEVGIGKRLGDVGATSA
HYGAWAQAALEDICLRSNPRTASLEQIVGLYAAAQ
Or try a new SitesBLAST search
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