SitesBLAST
Comparing AZOBR_RS28580 FitnessBrowser__azobra:AZOBR_RS28580 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)
37% identity, 98% coverage: 9:387/387 of query aligns to 5:382/382 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, 99% coverage: 6:387/387 of query aligns to 1:381/381 of P31005
- M1 (≠ V6) modified: Initiator methionine, Removed
- G13 (= G18) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (= G20) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (≠ Q93) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
- G95 (= G100) 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 (= S102) 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 (= D105) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
- K103 (= K108) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.
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)
34% identity, 98% coverage: 7:387/387 of query aligns to 4:383/383 of P0DJA2
- D39 (= D42) binding
- N71 (≠ E74) binding
- G98 (= G101) binding
- S99 (= S102) binding
- T138 (= T141) binding
- T139 (= T142) binding
- T147 (≠ S150) binding
- F149 (≠ A152) binding
- K160 (= K163) binding
- L179 (≠ A183) binding
- G182 (≠ S186) binding
- M183 (= M187) binding
- D194 (= D198) binding
- H198 (= H202) binding
- H263 (= H267) binding
- H267 (≠ M271) binding
- H277 (= H281) 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)
34% identity, 98% coverage: 7:387/387 of query aligns to 3:382/382 of 3ox4A
- binding fe (ii) ion: D193 (= D198), H197 (= H202), H262 (= H267), H276 (= H281)
- binding nicotinamide-adenine-dinucleotide: D38 (= D42), F40 (≠ A44), M41 (≠ L45), N70 (≠ E74), G96 (= G100), G97 (= G101), S98 (= S102), T137 (= T141), T138 (= T142), F148 (≠ A152), I150 (≠ V154), G181 (≠ S186), M182 (= M187), L186 (≠ V191), H276 (= H281)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
34% identity, 98% coverage: 7:387/387 of query aligns to 3:382/382 of 3owoA
1rrmA Crystal structure of lactaldehyde reductase
34% identity, 96% coverage: 17:387/387 of query aligns to 13:382/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (= D42), T40 (≠ A44), L41 (= L45), N70 (≠ E74), G96 (= G100), G97 (= G101), S98 (= S102), T139 (= T141), T140 (= T142), T143 (= T145), V152 (= V154), K161 (= K163), G183 (≠ S186), M184 (= M187), L188 (≠ V191), H276 (= H281)
- binding fe (ii) ion: L258 (= L263), C361 (≠ Y366)
- binding zinc ion: D195 (= D198), H199 (= H202), H262 (= H267), H276 (= H281)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
34% identity, 96% coverage: 17:387/387 of query aligns to 13:382/382 of 2bi4A
- binding fe (iii) ion: D195 (= D198), H199 (= H202), H262 (= H267), H276 (= H281)
- binding nicotinamide-adenine-dinucleotide: D38 (= D42), T40 (≠ A44), L41 (= L45), G96 (= G100), G97 (= G101), S98 (= S102), T139 (= T141), T140 (= T142), V152 (= V154), K161 (= K163), G183 (≠ S186), M184 (= M187), L188 (≠ V191), D195 (= D198), H199 (= H202), H262 (= H267), H276 (= H281)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
34% identity, 96% coverage: 17:387/387 of query aligns to 13:382/382 of P0A9S1
- G16 (= G20) mutation to D: No effect on enzyme activity.
- D38 (= D42) mutation to G: Enzyme can now use NADP.
- G96 (= G100) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D198) mutation to L: Complete loss of iron-binding.
- H199 (= H202) 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)
33% identity, 96% coverage: 17:387/387 of query aligns to 12:381/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (= D42), T39 (≠ A44), L40 (= L45), G95 (= G100), G96 (= G101), S97 (= S102), T138 (= T141), T139 (= T142), T142 (= T145), K160 (= K163), G182 (≠ S186), M183 (= M187), L187 (≠ V191), H275 (= H281)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ A152), V164 (≠ R167), H198 (= H202), F252 (= F258), S253 (≠ G259), H261 (= H267), C360 (≠ Y366)
- binding fe (iii) ion: D194 (= D198), H198 (= H202), H261 (= H267), H275 (= H281)
7qlgAAA Lactaldehyde reductase (see paper)
33% identity, 96% coverage: 17:387/387 of query aligns to 12:381/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D198), H198 (= H202), H261 (= H267), H275 (= H281)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D42), T39 (≠ A44), L40 (= L45), N69 (≠ E74), G95 (= G100), G96 (= G101), S97 (= S102), D100 (= D105), T138 (= T141), T139 (= T142), T142 (= T145), T147 (≠ S150), N149 (≠ A152), K160 (= K163), L187 (≠ V191), H198 (= H202), H275 (= H281)
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
33% identity, 96% coverage: 17:387/387 of query aligns to 14:383/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (= D42), T41 (≠ A44), L42 (= L45), P70 (= P73), G97 (= G100), G98 (= G101), S99 (= S102), D102 (= D105), T140 (= T141), T141 (= T142), T144 (= T145), T149 (≠ S150), N151 (≠ A152), V153 (= V154), K162 (= K163), G184 (≠ S186), C185 (≠ M187), L189 (≠ V191), H277 (= H281)
- binding zinc ion: D196 (= D198), H200 (= H202), H263 (= H267), H277 (= H281)
3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
28% identity, 98% coverage: 9:387/387 of query aligns to 5:400/403 of 3zdrA
A0A0S1X9S7 Alcohol dehydrogenase; EC 1.1.1.1 from Thermococcus barophilus (see paper)
31% identity, 98% coverage: 9:387/387 of query aligns to 4:376/378 of A0A0S1X9S7
- D195 (= D198) mutation to A: Disrupts the overall structure of the enzyme. Lack of acetaldehyde reduction activity and displays weak ethanol oxidation activity.
- H199 (= H202) mutation to A: Disrupts the overall structure of the enzyme. Retains 10% of ethanol oxidation and acetaldehyde reduction activities.
- H262 (≠ M269) mutation to A: Disrupts the overall structure of the enzyme. Displays weak ethanol oxidation and acetaldehyde reduction activities.
- H266 (≠ V273) mutation to A: Disrupts the overall structure of the enzyme. Displays higher acetaldehyde reduction activity (134%) but lower ethanol oxidation activity (36%).
- H274 (= H281) mutation to A: Disrupts the overall structure of the enzyme. Retains 20% of ethanol oxidation and acetaldehyde reduction activities.
7w9yA Crystal structure of bacillus subtilis yugj in complex with NADP and nickel (see paper)
28% identity, 93% coverage: 5:363/387 of query aligns to 2:366/389 of 7w9yA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G40 (≠ L41), G41 (≠ D42), S43 (≠ A44), P72 (= P73), N73 (≠ E74), G99 (= G100), G100 (= G101), S101 (= S102), T140 (= T141), L141 (≠ T142), T144 (= T145), K162 (= K163), T184 (≠ S186), V185 (≠ M187), P186 (= P188), H189 (≠ V191), H283 (= H281)
7w9zA Crystal structure of bacillus subtilis yugj in complex with NADP and nitrate (see paper)
28% identity, 92% coverage: 8:363/387 of query aligns to 4:363/381 of 7w9zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G37 (≠ L41), G38 (≠ D42), S40 (≠ A44), P69 (= P73), G96 (= G100), G97 (= G101), S98 (= S102), D101 (= D105), T137 (= T141), L138 (≠ T142), T141 (= T145), N146 (≠ S150), G148 (≠ A152), K159 (= K163), T181 (≠ S186), V182 (≠ M187), P183 (= P188), H186 (≠ V191)
- binding nitrate ion: R72 (≠ G76), V73 (≠ D77), S74 (≠ R78), V150 (= V154), N153 (≠ D157), W154 (≠ T158), E155 (≠ A159), W263 (≠ G264), H270 (≠ M271), H280 (= H281)
Q59104 4-hydroxybutyrate dehydrogenase; 4HbD; Gamma-hydroxybutyrate dehydrogenase; GHBDH; EC 1.1.1.61 from Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha) (see paper)
31% identity, 84% coverage: 61:387/387 of query aligns to 54:382/382 of Q59104
- D193 (= D198) mutation to A: Retains very low activity.
- H197 (= H202) mutation to A: Loss of activity.
- H261 (= H267) mutation to A: Loss of activity.
- H265 (≠ M271) 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 (= H281) mutation to A: Retains very low activity.
6scgA Structure of adhe form 1 (see paper)
31% identity, 94% coverage: 10:373/387 of query aligns to 6:385/406 of 6scgA
- binding fe (iii) ion: D204 (= D198), H208 (= H202), H274 (= H267), H288 (= H281)
- binding nicotinamide-adenine-dinucleotide: D38 (= D42), F40 (≠ A44), A69 (≠ P73), D70 (≠ E74), G96 (= G100), G97 (= G101), S98 (= S102), T148 (= T141), T149 (= T142), T152 (= T145), V161 (= V154), L197 (≠ V191), H278 (≠ M271)
6jkpA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense in complex with NAD+ (see paper)
29% identity, 91% coverage: 9:361/387 of query aligns to 6:348/376 of 6jkpA
- binding nicotinamide-adenine-dinucleotide: F42 (≠ L45), G96 (= G101), D100 (= D105), T137 (= T141), T138 (= T142), T141 (= T145), S143 (= S147), T146 (≠ S150), S181 (= S186), V182 (≠ M187), P183 (= P188)
6jkoA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense (see paper)
29% identity, 91% coverage: 9:361/387 of query aligns to 6:348/376 of 6jkoA
6c75B Structure of iron containing alcohol dehydrogenase from thermococcus thioreducens in a monoclinic crystal form (see paper)
30% identity, 98% coverage: 9:387/387 of query aligns to 2:375/378 of 6c75B
Query Sequence
>AZOBR_RS28580 FitnessBrowser__azobra:AZOBR_RS28580
MSAFPVSSFSCPTKIVFGVGAHEQLPDVLREWNATRLFVLLDPALADSAIFRRIEGLLTS
NGVALSVFTGIEPEPGDRTVQAAYERCREQDAQALLAIGGGSTIDVAKAVGILMTNGGRI
ADYEGIEKFAIRPLPLIAVPTTAGTGSEVSGACVITDTARKTKMAIRHAAFSPAQVAILD
PLAVGSMPAHVAAHAGIDAFVHAFESYLSKRATVFSDAVNLHAMTLIAGSIRPFVADRTN
VPAALDMLCGSALAAMSFGVTGLGNVHCMAMSVGALFPVPHGLANAVCLPYAAAFNVSAK
PERMARIAEILGVDTAGLPLDQAAEAAVDGLRTLCADLGIPPRLRDVGVTEDRLDEMARR
SYAADYNRWNPRHTSEPDFQDLFRAAF
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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