SitesBLAST
Comparing GFF2063 FitnessBrowser__Marino:GFF2063 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)
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
39% identity, 92% coverage: 31:385/385 of query aligns to 30:382/382 of 3bfjA
7qlqAAA Lactaldehyde reductase (see paper)
34% identity, 94% coverage: 26:385/385 of query aligns to 24:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D39), T39 (≠ G41), L40 (= L42), G95 (= G97), G96 (= G98), S97 (= S99), T138 (= T138), T139 (= T139), T142 (= T142), K160 (= K160), G182 (= G181), M183 (≠ L182), L187 (≠ V186), H275 (= H278)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ I149), V164 (= V163), H198 (= H197), F252 (= F255), S253 (≠ A256), H261 (= H264), C360 (≠ L364)
- binding fe (iii) ion: D194 (= D193), H198 (= H197), H261 (= H264), H275 (= H278)
7qlgAAA Lactaldehyde reductase (see paper)
34% identity, 94% coverage: 26:385/385 of query aligns to 24:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D193), H198 (= H197), H261 (= H264), H275 (= H278)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D39), T39 (≠ G41), L40 (= L42), N69 (≠ D71), G95 (= G97), G96 (= G98), S97 (= S99), D100 (= D102), T138 (= T138), T139 (= T139), T142 (= T142), T147 (= T147), N149 (≠ I149), K160 (= K160), L187 (≠ V186), H198 (= H197), H275 (= H278)
1rrmA Crystal structure of lactaldehyde reductase
34% identity, 94% coverage: 26:385/385 of query aligns to 25:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D39), T40 (≠ G41), L41 (= L42), N70 (≠ D71), G96 (= G97), G97 (= G98), S98 (= S99), T139 (= T138), T140 (= T139), T143 (= T142), V152 (≠ I151), K161 (= K160), G183 (= G181), M184 (≠ L182), L188 (≠ V186), H276 (= H278)
- binding fe (ii) ion: L258 (≠ V260), C361 (≠ L364)
- binding zinc ion: D195 (= D193), H199 (= H197), H262 (= H264), H276 (= H278)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
34% identity, 94% coverage: 26:385/385 of query aligns to 25:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D193), H199 (= H197), H262 (= H264), H276 (= H278)
- binding nicotinamide-adenine-dinucleotide: D38 (= D39), T40 (≠ G41), L41 (= L42), G96 (= G97), G97 (= G98), S98 (= S99), T139 (= T138), T140 (= T139), V152 (≠ I151), K161 (= K160), G183 (= G181), M184 (≠ L182), L188 (≠ V186), D195 (= D193), H199 (= H197), H262 (= H264), H276 (= H278)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
34% identity, 94% coverage: 26:385/385 of query aligns to 25:382/382 of P0A9S1
- D38 (= D39) mutation to G: Enzyme can now use NADP.
- G96 (= G97) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D193) mutation to L: Complete loss of iron-binding.
- H199 (= H197) 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.
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
34% identity, 94% coverage: 26:385/385 of query aligns to 26:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D39), T41 (≠ G41), L42 (= L42), P70 (≠ A70), G97 (= G97), G98 (= G98), S99 (= S99), D102 (= D102), T140 (= T138), T141 (= T139), T144 (= T142), T149 (= T147), N151 (≠ I149), V153 (≠ I151), K162 (= K160), G184 (= G181), C185 (≠ L182), L189 (≠ V186), H277 (= H278)
- binding zinc ion: D196 (= D193), H200 (= H197), H263 (= H264), H277 (= H278)
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
34% identity, 92% coverage: 32:385/385 of query aligns to 31:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D193), H197 (= H197), H262 (= H264), H276 (= H278)
- binding nicotinamide-adenine-dinucleotide: D38 (= D39), F40 (≠ G41), M41 (≠ L42), N70 (≠ D71), G96 (= G97), G97 (= G98), S98 (= S99), T137 (= T138), T138 (= T139), F148 (≠ I149), I150 (= I151), G181 (= G181), M182 (≠ L182), L186 (≠ V186), H276 (= H278)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
34% identity, 92% coverage: 32:385/385 of query aligns to 31:382/382 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)
35% identity, 92% coverage: 32:385/385 of query aligns to 32:383/383 of P0DJA2
- D39 (= D39) binding
- N71 (≠ D71) binding
- G98 (= G98) binding
- S99 (= S99) binding
- T138 (= T138) binding
- T139 (= T139) binding
- T147 (= T147) binding
- F149 (≠ I149) binding
- K160 (= K159) binding
- L179 (= L178) binding
- G182 (= G181) binding
- M183 (≠ L182) binding
- D194 (= D193) binding
- H198 (= H197) binding
- H263 (= H264) binding
- H267 (≠ Y268) binding
- H277 (= H278) binding ; binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
32% identity, 100% coverage: 1:385/385 of query aligns to 1:381/381 of P31005
- M1 (= M1) modified: Initiator methionine, Removed
- G13 (≠ C14) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G17) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (= D90) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G97) 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 (= S99) 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 (= D102) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K105) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
Q59104 4-hydroxybutyrate dehydrogenase; 4HbD; Gamma-hydroxybutyrate dehydrogenase; GHBDH; EC 1.1.1.61 from Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha) (see paper)
35% identity, 90% coverage: 32:376/385 of query aligns to 30:373/382 of Q59104
- D193 (= D193) mutation to A: Retains very low activity.
- H197 (= H197) mutation to A: Loss of activity.
- H261 (= H264) mutation to A: Loss of activity.
- H265 (≠ Y268) 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 (= H278) mutation to A: Retains very low activity.
6scgA Structure of adhe form 1 (see paper)
35% identity, 83% coverage: 32:351/385 of query aligns to 31:362/406 of 6scgA
- binding fe (iii) ion: D204 (= D193), H208 (= H197), H274 (= H264), H288 (= H278)
- binding nicotinamide-adenine-dinucleotide: D38 (= D39), F40 (≠ G41), A69 (= A70), D70 (= D71), G96 (= G97), G97 (= G98), S98 (= S99), T148 (= T138), T149 (= T139), T152 (= T142), V161 (≠ I151), L197 (≠ V186), H278 (≠ Y268)
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
32% identity, 92% coverage: 33:385/385 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)
34% identity, 83% coverage: 32:351/385 of query aligns to 480:825/891 of P0A9Q7
- D487 (= D39) binding
- D519 (= D71) binding
- GSPMD 546:550 (≠ GSSMD 98:102) binding
- E568 (vs. gap) mutation to K: Partially restores protein stability and resistance to MCO damage; when associated with T-267.
- V610 (≠ I151) binding
- K619 (= K160) binding
- D653 (= D193) binding
- H657 (= H197) binding
- F670 (≠ V212) mutation F->A,E,V: Disrupts spirosome formation. Affects the forward activity of ALDH.
- H723 (= H264) binding
- H737 (= H278) 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, 83% coverage: 32:351/385 of query aligns to 480:825/891 of P0A9Q8
7bvpA Adhe spirosome in extended conformation (see paper)
34% identity, 83% coverage: 32:351/385 of query aligns to 480:825/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: D487 (= D39), F489 (≠ G41), D519 (= D71), S547 (= S99), D550 (= D102), T597 (= T138), T598 (= T139), T601 (= T142), V610 (≠ I151), K619 (= K160), L646 (≠ V186), H737 (= H278)
- binding zinc ion: D653 (= D193), H657 (= H197), H723 (= H264), H737 (= H278)
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, 83% coverage: 32:351/385 of query aligns to 480:825/869 of 6tqmA
- binding fe (iii) ion: D653 (= D193), H657 (= H197), H723 (= H264), H737 (= H278)
- 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 (= D39), L490 (= L42), G545 (= G97), S547 (= S99), D550 (= D102), T597 (= T138), S603 (= S144), F608 (≠ I149), L646 (≠ V186), H727 (≠ Y268)
1o2dA Crystal structure of alcohol dehydrogenase, iron-containing (tm0920) from thermotoga maritima at 1.30 a resolution (see paper)
36% identity, 76% coverage: 4:295/385 of query aligns to 2:287/359 of 1o2dA
- binding fe (iii) ion: D189 (= D193), H193 (= H197), H256 (= H264), H270 (= H278)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S38 (≠ P40), S39 (≠ G41), E68 (≠ A70), N69 (≠ D71), G95 (= G97), G96 (= G98), S97 (= S99), D100 (= D102), T136 (= T138), T137 (= T139), T140 (= T142), S142 (= S144), Y147 (≠ I149), I149 (= I151), K157 (= K159), S177 (≠ G181), M178 (≠ L182), L182 (≠ V186), D189 (= D193), H193 (= H197), H270 (= H278)
1vhdA Crystal structure of an iron containing alcohol dehydrogenase (see paper)
36% identity, 76% coverage: 4:295/385 of query aligns to 3:288/361 of 1vhdA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S39 (≠ P40), S40 (≠ G41), E69 (≠ A70), N70 (≠ D71), G96 (= G97), G97 (= G98), S98 (= S99), D101 (= D102), T137 (= T138), T138 (= T139), T141 (= T142), S143 (= S144), T146 (= T147), Y148 (≠ I149), I150 (= I151), K158 (= K159), S178 (≠ G181), M179 (≠ L182), L183 (≠ V186), D190 (= D193), H194 (= H197), H271 (= H278)
- binding zinc ion: D190 (= D193), H194 (= H197), H257 (= H264), H271 (= H278)
Query Sequence
>GFF2063 FitnessBrowser__Marino:GFF2063
MTAFTFNTTKSVICEPGVTHRLGQIVKEHMGKKVLLVTDPGLVKAGLLDVATNSLNEAGV
KYELFDGVVADPPVSVVEAALADAREAGVDGVIGFGGGSSMDVAKLIALLIGGEEKLDDV
YGVGQAKGKRLPLIQIPTTAGTGSEVTPISIITVGETEKKGVVAPQLLPDIALLDAELTL
GLPAHVTAATGIDAMVHAIESYTSASANNNPVSKALAREALRLLGANIETAVKDGSNVKA
RSDMLLGAMLAGQAFANSPVAAVHALAYPIGGIFHVPHGLSNALVLPHVMRFNTEICGEA
YSILATDVFPDLAGTPAAKRANQFIDRLEALSADLGLEQTLREVGIGEADLATLASDSMK
QTRLLVNNPREVSETDALAIYKAAF
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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