SitesBLAST
Comparing PfGW456L13_2712 Alcohol dehydrogenase (EC 1.1.1.1) 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, 93% coverage: 9:366/386 of query aligns to 6:366/382 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.
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
35% identity, 98% coverage: 6:382/386 of query aligns to 4:382/382 of 3bfjA
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
34% identity, 98% coverage: 6:382/386 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
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)
31% identity, 98% coverage: 4:382/386 of query aligns to 3:383/383 of P0DJA2
- D39 (= D40) binding
- N71 (= N72) binding
- G98 (= G99) binding
- S99 (= S100) binding
- T138 (= T144) binding
- T139 (= T145) binding
- T147 (≠ G153) binding
- F149 (≠ A155) binding
- K160 (= K166) binding
- L179 (= L185) binding
- G182 (= G188) binding
- M183 (= M189) binding
- D194 (= D200) binding
- H198 (= H204) binding
- H263 (= H268) binding
- H267 (= H272) binding
- H277 (= H282) 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)
31% identity, 98% coverage: 4:382/386 of query aligns to 2:382/382 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), F148 (≠ A155), I150 (≠ V157), G181 (= G188), M182 (= M189), L186 (≠ I193), H276 (= H282)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
31% identity, 98% coverage: 4:382/386 of query aligns to 2:382/382 of 3owoA
1rrmA Crystal structure of lactaldehyde reductase
30% identity, 96% coverage: 15:384/386 of query aligns to 13:384/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D40), T40 (≠ G42), L41 (= L43), N70 (= N72), G96 (= G98), G97 (= G99), S98 (= S100), T139 (= T144), T140 (= T145), T143 (= T148), V152 (= V157), K161 (= K166), G183 (= G188), M184 (= M189), L188 (≠ I193), H276 (= H282)
- binding fe (ii) ion: L258 (= L264), C361 (≠ S361)
- binding zinc ion: D195 (= D200), H199 (= H204), H262 (= H268), H276 (= H282)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
30% identity, 95% coverage: 15:381/386 of query aligns to 13:381/382 of 2bi4A
- binding fe (iii) ion: D195 (= D200), H199 (= H204), H262 (= H268), H276 (= H282)
- binding nicotinamide-adenine-dinucleotide: D38 (= D40), T40 (≠ G42), L41 (= L43), G96 (= G98), G97 (= G99), S98 (= S100), T139 (= T144), T140 (= T145), V152 (= V157), K161 (= K166), G183 (= G188), M184 (= M189), L188 (≠ I193), D195 (= D200), H199 (= H204), H262 (= H268), H276 (= H282)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
30% identity, 95% coverage: 15:381/386 of query aligns to 13:381/382 of P0A9S1
- G16 (= G18) mutation to D: No effect on enzyme activity.
- D38 (= D40) mutation to G: Enzyme can now use NADP.
- G96 (= G98) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D200) mutation to L: Complete loss of iron-binding.
- H199 (= H204) 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.
7qlqAAA Lactaldehyde reductase (see paper)
30% identity, 95% coverage: 15:381/386 of query aligns to 12:380/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D40), T39 (≠ G42), L40 (= L43), G95 (= G98), G96 (= G99), S97 (= S100), T138 (= T144), T139 (= T145), T142 (= T148), K160 (= K166), G182 (= G188), M183 (= M189), L187 (≠ I193), H275 (= H282)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ A155), V164 (≠ F170), H198 (= H204), F252 (= F260), S253 (≠ Q261), H261 (= H268), C360 (≠ S361)
- binding fe (iii) ion: D194 (= D200), H198 (= H204), H261 (= H268), H275 (= H282)
7qlgAAA Lactaldehyde reductase (see paper)
30% identity, 95% coverage: 15:381/386 of query aligns to 12:380/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D200), H198 (= H204), H261 (= H268), H275 (= H282)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D40), T39 (≠ G42), L40 (= L43), N69 (= N72), G95 (= G98), G96 (= G99), S97 (= S100), D100 (= D103), T138 (= T144), T139 (= T145), T142 (= T148), T147 (≠ G153), N149 (≠ A155), K160 (= K166), L187 (≠ I193), H198 (= H204), H275 (= H282)
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
30% identity, 95% coverage: 15:381/386 of query aligns to 14:382/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D40), T41 (≠ G42), L42 (= L43), P70 (= P71), G97 (= G98), G98 (= G99), S99 (= S100), D102 (= D103), T140 (= T144), T141 (= T145), T144 (= T148), T149 (≠ G153), N151 (≠ A155), V153 (= V157), K162 (= K166), G184 (= G188), C185 (≠ M189), L189 (≠ I193), H277 (= H282)
- binding zinc ion: D196 (= D200), H200 (= H204), H263 (= H268), H277 (= H282)
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
30% identity, 98% coverage: 7:384/386 of query aligns to 5:402/403 of 3zdrA
6jkpA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense in complex with NAD+ (see paper)
29% identity, 96% coverage: 7:378/386 of query aligns to 4:369/376 of 6jkpA
- binding nicotinamide-adenine-dinucleotide: F42 (≠ L43), G96 (= G99), D100 (= D103), T137 (= T144), T138 (= T145), T141 (= T148), S143 (= S150), T146 (≠ G153), S181 (≠ G188), V182 (≠ M189), P183 (= P190)
6jkoA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense (see paper)
29% identity, 96% coverage: 7:378/386 of query aligns to 4:369/376 of 6jkoA
5yvmA Crystal structure of the archaeal halo-thermophilic red sea brine pool alcohol dehydrogenase adh/d1 bound to nzq (see paper)
29% identity, 99% coverage: 1:382/386 of query aligns to 2:403/403 of 5yvmA
- binding manganese (ii) ion: D207 (= D200), H211 (= H204), H276 (= H268), H291 (= H282)
- binding 5,6-dihydroxy-nadp: G41 (≠ T39), N44 (≠ G42), M45 (≠ L43), P73 (= P71), N74 (= N72), G100 (= G98), G101 (= G99), S102 (= S100), D105 (= D103), S151 (≠ T144), T152 (= T145), T155 (= T148), T160 (≠ G153), Y162 (≠ A155), V164 (= V157), K173 (= K166), E195 (≠ G188), L200 (≠ I193), H211 (= H204), H276 (= H268), H280 (= H272), H291 (= H282)
5yvrA Crystal structure of the h277a mutant of adh/d1, an archaeal halo- thermophilic red sea brine pool alcohol dehydrogenase (see paper)
29% identity, 99% coverage: 1:382/386 of query aligns to 2:403/403 of 5yvrA
- binding manganese (ii) ion: D207 (= D200), H211 (= H204), H276 (= H268), H291 (= H282)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G41 (≠ T39), S43 (= S41), N44 (≠ G42), M45 (≠ L43), G100 (= G98), G101 (= G99), S102 (= S100), D105 (= D103), S151 (≠ T144), T152 (= T145), T155 (= T148), T160 (≠ G153), Y162 (≠ A155), V164 (= V157), K173 (= K166), E195 (≠ G188), M196 (= M189), L200 (≠ I193), D207 (= D200), H211 (= H204), H291 (= H282)
6scgA Structure of adhe form 1 (see paper)
29% identity, 97% coverage: 10:385/386 of query aligns to 8:402/406 of 6scgA
- binding fe (iii) ion: D204 (= D200), H208 (= H204), H274 (= H268), H288 (= H282)
- binding nicotinamide-adenine-dinucleotide: D38 (= D40), F40 (≠ G42), A69 (≠ P71), D70 (≠ N72), G96 (= G98), G97 (= G99), S98 (= S100), T148 (= T144), T149 (= T145), T152 (= T148), V161 (= V157), L197 (≠ I193), H278 (= H272)
7bvpA Adhe spirosome in extended conformation (see paper)
28% identity, 97% coverage: 10:385/386 of query aligns to 457:865/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: D487 (= D40), F489 (≠ G42), D519 (≠ N72), S547 (= S100), D550 (= D103), T597 (= T144), T598 (= T145), T601 (= T148), V610 (= V157), K619 (= K166), L646 (≠ I193), H737 (= H282)
- binding zinc ion: D653 (= D200), H657 (= H204), H723 (= H268), H737 (= H282)
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)
28% identity, 97% coverage: 10:385/386 of query aligns to 457:865/869 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), S547 (= S100), D550 (= D103), T597 (= T144), S603 (= S150), F608 (≠ A155), L646 (≠ I193), H727 (= H272)
Query Sequence
>PfGW456L13_2712 Alcohol dehydrogenase (EC 1.1.1.1)
MNLTGNWSYPTSVRFGVGRIAELAEVCRSQGIQRPLLVTDSGLARAPITTAALDALRAAG
LGVALFCDLKPNPVEANLAGGLDAWRAGQHDGVIAFGGGSGLDMGKLIAFMSGQTRPVWD
FEDIGDYWTRADDSRIAPVIAVPTTAGTGSEVGRAAVIIDERTHTKRIIFHPKMMPRVVI
SDPALTVGMPAKITAGTGMDALSHCLEAYCAPGFHPLADGIAVEGMRLVANSLVKAVHTP
SDLEARAQMLAAAAMGATAFQKGLGGMHALSHPVGALYDTHHGMTNATFMPYVLHFNRSA
IEERITRLAAYLRLPSPGFDSFLAFVLKLRKDIGVPHTLVELGVDDRQADLIADMAIVDP
SAGGNPLPLTRDGVAKIFDAALHGRL
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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