SitesBLAST
Comparing WP_013836016.1 NCBI__GCF_000214825.1:WP_013836016.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
35% identity, 55% coverage: 85:297/388 of query aligns to 87:294/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: G97 (= G95), G98 (= G96), S99 (= S97), D102 (= D100), T140 (= T140), T141 (= T141), T144 (= T144), T149 (= T149), N151 (= N151), V153 (= V153), K162 (≠ S163), G184 (≠ H183), C185 (= C184), L189 (≠ V188), H277 (= H280)
- binding zinc ion: D196 (= D195), H200 (≠ Q199), H263 (= H266), H277 (= H280)
Sites not aligning to the query:
1rrmA Crystal structure of lactaldehyde reductase
35% identity, 55% coverage: 85:297/388 of query aligns to 86:293/385 of 1rrmA
- binding adenosine-5-diphosphoribose: G96 (= G95), G97 (= G96), S98 (= S97), T139 (= T140), T140 (= T141), T143 (= T144), V152 (= V153), K161 (≠ S163), G183 (≠ H183), M184 (≠ C184), L188 (≠ V188), H276 (= H280)
- binding fe (ii) ion: L258 (= L262)
- binding zinc ion: D195 (= D195), H199 (≠ Q199), H262 (= H266), H276 (= H280)
Sites not aligning to the query:
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
35% identity, 55% coverage: 85:297/388 of query aligns to 86:293/382 of 2bi4A
- binding fe (iii) ion: D195 (= D195), H199 (≠ Q199), H262 (= H266), H276 (= H280)
- binding nicotinamide-adenine-dinucleotide: G96 (= G95), G97 (= G96), S98 (= S97), T139 (= T140), T140 (= T141), V152 (= V153), K161 (≠ S163), G183 (≠ H183), M184 (≠ C184), L188 (≠ V188), D195 (= D195), H199 (≠ Q199), H262 (= H266), H276 (= H280)
Sites not aligning to the query:
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
35% identity, 55% coverage: 85:297/388 of query aligns to 86:293/382 of P0A9S1
- G96 (= G95) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D195) mutation to L: Complete loss of iron-binding.
- H199 (≠ Q199) 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.
- 38 D→G: Enzyme can now use NADP.
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
28% identity, 83% coverage: 68:388/388 of query aligns to 65:381/381 of P31005
- D88 (≠ E88) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G95) 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 (= S97) 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 (= D100) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K103) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 13 G→A: Shows a reduced dehydrogenase activity.
- 15 G→A: Shows almost the same dehydrogenase activity as the wild-type.
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)
27% identity, 90% coverage: 14:361/388 of query aligns to 13:354/383 of P0DJA2
- D39 (≠ G41) binding NAD(+)
- N71 (≠ S72) binding NAD(+)
- G98 (= G96) binding NAD(+)
- S99 (= S97) binding NAD(+)
- T138 (= T140) binding NAD(+)
- T139 (= T141) binding NAD(+)
- T147 (= T149) binding NAD(+)
- F149 (≠ N151) binding NAD(+)
- K160 (= K161) binding NAD(+)
- L179 (≠ F180) binding NAD(+)
- G182 (≠ H183) binding NAD(+)
- M183 (≠ C184) binding NAD(+)
- D194 (= D195) binding Fe(2+)
- H198 (≠ Q199) binding Fe(2+)
- H263 (= H266) binding Fe(2+)
- H267 (≠ G270) binding NAD(+)
- H277 (= H280) binding Fe(2+); binding NAD(+)
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)
27% identity, 90% coverage: 14:361/388 of query aligns to 12:353/382 of 3ox4A
- binding fe (ii) ion: D193 (= D195), H197 (≠ Q199), H262 (= H266), H276 (= H280)
- binding nicotinamide-adenine-dinucleotide: D38 (≠ G41), F40 (≠ Y43), M41 (≠ A44), N70 (≠ S72), G96 (= G95), G97 (= G96), S98 (= S97), T137 (= T140), T138 (= T141), F148 (≠ N151), I150 (≠ V153), G181 (≠ H183), M182 (≠ C184), L186 (≠ V188), H276 (= H280)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
27% identity, 90% coverage: 14:361/388 of query aligns to 12:353/382 of 3owoA
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
30% identity, 80% coverage: 70:380/388 of query aligns to 68:374/382 of 3bfjA
7qlgAAA Lactaldehyde reductase (see paper)
34% identity, 55% coverage: 85:297/388 of query aligns to 85:292/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D195), H198 (≠ Q199), H261 (= H266), H275 (= H280)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G95 (= G95), G96 (= G96), S97 (= S97), D100 (= D100), T138 (= T140), T139 (= T141), T142 (= T144), T147 (= T149), N149 (= N151), K160 (≠ S163), L187 (≠ V188), H198 (≠ Q199), H275 (= H280)
Sites not aligning to the query:
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
31% identity, 68% coverage: 70:331/388 of query aligns to 67:337/403 of 3zdrA
7qlqAAA Lactaldehyde reductase (see paper)
34% identity, 55% coverage: 85:297/388 of query aligns to 85:292/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: G95 (= G95), G96 (= G96), S97 (= S97), T138 (= T140), T139 (= T141), T142 (= T144), K160 (≠ S163), G182 (≠ H183), M183 (≠ C184), L187 (≠ V188), H275 (= H280)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ N151), V164 (vs. gap), H198 (≠ Q199), F252 (≠ L257), S253 (≠ A258), H261 (= H266)
- binding fe (iii) ion: D194 (= D195), H198 (≠ Q199), H261 (= H266), H275 (= H280)
Sites not aligning to the query:
Q59104 4-hydroxybutyrate dehydrogenase; 4HbD; Gamma-hydroxybutyrate dehydrogenase; GHBDH; EC 1.1.1.61 from Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha) (see paper)
28% identity, 75% coverage: 70:361/388 of query aligns to 67:354/382 of Q59104
- D193 (= D195) mutation to A: Retains very low activity.
- H197 (≠ Q199) mutation to A: Loss of activity.
- H261 (= H266) mutation to A: Loss of activity.
- H265 (≠ G270) 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 (= H280) mutation to A: Retains very low activity.
7bvpA Adhe spirosome in extended conformation (see paper)
30% identity, 83% coverage: 37:359/388 of query aligns to 489:829/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: F489 (≠ M37), D519 (≠ E70), S547 (= S97), D550 (= D100), T597 (= T140), T598 (= T141), T601 (= T144), V610 (= V153), K619 (= K162), L646 (≠ V188), H737 (= H280)
- binding zinc ion: D653 (= D195), H657 (≠ Q199), H723 (= H266), H737 (= H280)
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, 487
6tqmA Escherichia coli adhe structure in its compact conformation (see paper)
30% identity, 83% coverage: 37:359/388 of query aligns to 489:829/869 of 6tqmA
- binding fe (iii) ion: D653 (= D195), H657 (≠ Q199), H723 (= H266), H737 (= H280)
- 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: L490 (= L38), G545 (= G95), S547 (= S97), D550 (= D100), T597 (= T140), S603 (= S146), F608 (≠ N151), L646 (≠ V188), H727 (≠ G270)
Sites not aligning to the query:
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)
30% identity, 83% coverage: 37:359/388 of query aligns to 489:829/891 of P0A9Q7
- D519 (≠ E70) binding NAD(+)
- GSPMD 546:550 (≠ GSVLD 96:100) binding NAD(+)
- E568 (≠ V116) mutation to K: Partially restores protein stability and resistance to MCO damage; when associated with T-267.
- V610 (= V153) binding NAD(+)
- K619 (= K162) binding NAD(+)
- D653 (= D195) binding Fe cation
- H657 (≠ Q199) binding Fe cation
- F670 (≠ I212) mutation F->A,E,V: Disrupts spirosome formation. Affects the forward activity of ALDH.
- H723 (= H266) binding Fe cation
- H737 (= H280) 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.
- 487 binding NAD(+)
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)
30% identity, 83% coverage: 37:359/388 of query aligns to 489:829/891 of P0A9Q8
- D519 (≠ E70) binding NAD(+)
- GSPMD 546:550 (≠ GSVLD 96:100) binding NAD(+)
- TT 597:598 (= TT 140:141) binding NAD(+)
- L638 (≠ F180) binding NAD(+)
- D653 (= D195) binding Fe cation
- H657 (≠ Q199) binding Fe cation
- H723 (= H266) binding Fe cation
- H737 (= H280) binding Fe cation
Sites not aligning to the query:
6scgA Structure of adhe form 1 (see paper)
29% identity, 83% coverage: 37:359/388 of query aligns to 40:366/406 of 6scgA
- binding fe (iii) ion: D204 (= D195), H208 (≠ Q199), H274 (= H266), H288 (= H280)
- binding nicotinamide-adenine-dinucleotide: F40 (≠ M37), A69 (≠ G69), D70 (≠ E70), G96 (= G95), G97 (= G96), S98 (= S97), T148 (= T140), T149 (= T141), T152 (= T144), V161 (= V153), L197 (≠ V188), H278 (≠ G270)
Sites not aligning to the query:
A0A0S1X9S7 Alcohol dehydrogenase; EC 1.1.1.1 from Thermococcus barophilus (see paper)
28% identity, 66% coverage: 67:321/388 of query aligns to 64:306/378 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 (≠ Q199) mutation to A: Disrupts the overall structure of the enzyme. Retains 10% of ethanol oxidation and acetaldehyde reduction activities.
- H262 (= H266) mutation to A: Disrupts the overall structure of the enzyme. Displays weak ethanol oxidation and acetaldehyde reduction activities.
- H266 (≠ G270) mutation to A: Disrupts the overall structure of the enzyme. Displays higher acetaldehyde reduction activity (134%) but lower ethanol oxidation activity (36%).
- H274 (= H280) mutation to A: Disrupts the overall structure of the enzyme. Retains 20% of ethanol oxidation and acetaldehyde reduction activities.
6jkpA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense in complex with NAD+ (see paper)
25% identity, 76% coverage: 88:380/388 of query aligns to 88:365/376 of 6jkpA
Sites not aligning to the query:
Query Sequence
>WP_013836016.1 NCBI__GCF_000214825.1:WP_013836016.1
MINSFSLAQMPAIEFGWGCTDSRLADAILAQSQNQVMLISGGYADAHFVEPRLARVFECR
KVHRVVVRGEPSPAVVDKLVAEAPQGIELVIGFGGGSVLDAAKAVAGLLPERFSVVDYLE
GVGCGRKIQHTPVPFMAVPTTAGTGSETTKNAVISKLGEYKKSFRDDRLLAKQAWLDPAF
LPHCPASVLYPTAMDAFTQLLESYVTLKANPITDALAWQGMCLFKGAFDLIASNDPTCQQ
QGYGQLMLAASLSGMTLANAGLGAVHGLAGPIGAYFEAPHGVVCARLLAPITRANIEALQ
IASSEQATTALNKYVQVAELLTGHRGLAGLVAYLEQMSADYVPQGLAEFGLRADNLAPVL
ACCRAGSMLGNPLVLSDQALKQAMMAAL
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