SitesBLAST
Comparing GFF2678 FitnessBrowser__Phaeo:GFF2678 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)
Q59104 4-hydroxybutyrate dehydrogenase; 4HbD; Gamma-hydroxybutyrate dehydrogenase; GHBDH; EC 1.1.1.61 from Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha) (see paper)
39% identity, 98% coverage: 9:381/381 of query aligns to 6:382/382 of Q59104
- D193 (= D200) mutation to A: Retains very low activity.
- H197 (= H204) mutation to A: Loss of activity.
- H261 (= H268) mutation to A: Loss of activity.
- H265 (= H272) 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 (= H282) mutation to A: Retains very low activity.
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
34% identity, 99% coverage: 6:381/381 of query aligns to 3:381/381 of P31005
- G13 (= G16) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G18) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D91) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G98) 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 (= S100) 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 (= D103) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K106) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
34% identity, 99% coverage: 6:381/381 of query aligns to 4:382/382 of 3bfjA
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
35% identity, 98% coverage: 7:380/381 of query aligns to 5:381/382 of 3ox4A
- binding fe (ii) ion: D193 (= D200), H197 (= H204), H262 (= H268), H276 (= H282)
- binding nicotinamide-adenine-dinucleotide: D38 (= D40), F40 (≠ G42), M41 (≠ L43), N70 (= N72), G96 (= G98), G97 (= G99), S98 (= S100), T137 (= T144), T138 (= T145), T141 (= T148), F148 (≠ A155), I150 (≠ V157), L178 (= L185), G181 (= G188), M182 (= M189), L186 (≠ I193), H197 (= H204), H266 (= H272), H276 (= H282)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
35% identity, 98% coverage: 7:380/381 of query aligns to 5:381/382 of 3owoA
6scgA Structure of adhe form 1 (see paper)
33% identity, 97% coverage: 10:379/381 of query aligns to 8:397/406 of 6scgA
- binding fe (iii) ion: D204 (= D200), H208 (= H204), H274 (= H268), H288 (= H282)
- binding nicotinamide-adenine-dinucleotide: D38 (= D40), F40 (≠ G42), L41 (= L43), A69 (≠ P71), D70 (≠ N72), G96 (= G98), G97 (= G99), S98 (= S100), D101 (= D103), T148 (= T144), T149 (= T145), T152 (= T148), V161 (= V157), L189 (= L185), M193 (= M189), P194 (= P190), L197 (≠ I193), H278 (= H272)
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, 97% coverage: 10:379/381 of query aligns to 457:860/891 of P0A9Q7
- D487 (= D40) binding
- D519 (≠ N72) binding
- GSPMD 546:550 (≠ GSGLD 99:103) binding
- E568 (≠ D123) mutation to K: Partially restores protein stability and resistance to MCO damage; when associated with T-267.
- V610 (= V157) binding
- K619 (= K166) binding
- D653 (= D200) binding
- H657 (= H204) binding
- F670 (≠ M217) mutation F->A,E,V: Disrupts spirosome formation. Affects the forward activity of ALDH.
- H723 (= H268) binding
- H737 (= H282) 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, 97% coverage: 10:379/381 of query aligns to 457:860/891 of P0A9Q8
7bvpA Adhe spirosome in extended conformation (see paper)
32% identity, 97% coverage: 10:379/381 of query aligns to 457:860/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: D487 (= D40), F489 (≠ G42), A518 (≠ P71), D519 (≠ N72), P520 (= P73), G546 (= G99), S547 (= S100), D550 (= D103), T597 (= T144), T598 (= T145), T601 (= T148), S603 (= S150), F608 (≠ A155), V610 (= V157), K619 (= K166), M642 (= M189), L646 (≠ I193), F714 (= F260), H737 (= H282)
- binding zinc ion: D653 (= D200), H657 (= H204), H723 (= H268), H737 (= H282)
Sites not aligning to the query:
- binding nicotinamide-adenine-dinucleotide: 110, 111, 112, 113, 114, 139, 193, 194, 195, 197, 198, 201, 212, 213, 214, 246, 335, 337, 367, 417, 418, 419
6tqmA Escherichia coli adhe structure in its compact conformation (see paper)
32% identity, 97% coverage: 10:379/381 of query aligns to 457:860/869 of 6tqmA
- binding fe (iii) ion: D653 (= D200), H657 (= H204), H723 (= H268), H737 (= H282)
- 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 (= D40), L490 (= L43), G545 (= G98), G546 (= G99), S547 (= S100), D550 (= D103), T597 (= T144), S603 (= S150), F608 (≠ A155), A609 (≠ S156), V610 (= V157), L646 (≠ I193), H727 (= H272), H737 (= H282)
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
29% identity, 98% coverage: 7:381/381 of query aligns to 5:400/403 of 3zdrA
1rrmA Crystal structure of lactaldehyde reductase
31% identity, 96% coverage: 15:380/381 of query aligns to 13:381/385 of 1rrmA