SitesBLAST
Comparing Dsui_2116 FitnessBrowser__PS:Dsui_2116 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)
1vljB Crystal structure of nadh-dependent butanol dehydrogenase a (tm0820) from thermotoga maritima at 1.78 a resolution
48% identity, 93% coverage: 1:357/382 of query aligns to 6:366/400 of 1vljB
- binding fe (iii) ion: D200 (= D195), H204 (= H199), H273 (= H269), H287 (= H283)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G45 (≠ S40), S47 (≠ R42), P76 (≠ S71), G103 (= G98), G104 (= G99), S105 (= S100), D108 (= D103), T144 (= T139), I145 (≠ L140), T148 (= T143), T150 (≠ S145), N153 (= N148), N155 (≠ G150), K166 (= K161), T188 (= T183), L189 (≠ V184), Q193 (≠ Y188), H204 (= H199), H287 (= H283)
7w9yA Crystal structure of bacillus subtilis yugj in complex with NADP and nickel (see paper)
39% identity, 100% coverage: 1:382/382 of query aligns to 3:389/389 of 7w9yA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G40 (= G39), G41 (≠ S40), S43 (≠ R42), P72 (≠ S71), N73 (= N72), G99 (= G98), G100 (= G99), S101 (= S100), T140 (= T139), L141 (= L140), T144 (= T143), K162 (= K161), T184 (= T183), V185 (= V184), P186 (≠ S185), H189 (≠ Y188), H283 (= H283)
7w9zA Crystal structure of bacillus subtilis yugj in complex with NADP and nitrate (see paper)
39% identity, 99% coverage: 3:382/382 of query aligns to 2:381/381 of 7w9zA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G37 (= G39), G38 (≠ S40), S40 (≠ R42), P69 (≠ S71), G96 (= G98), G97 (= G99), S98 (= S100), D101 (= D103), T137 (= T139), L138 (= L140), T141 (= T143), N146 (= N148), G148 (= G150), K159 (= K161), T181 (= T183), V182 (= V184), P183 (≠ S185), H186 (≠ Y188)
- binding nitrate ion: R72 (≠ V74), V73 (≠ I75), S74 (= S76), V150 (= V152), N153 (= N155), W154 (≠ E156), E155 (≠ A157), W263 (≠ Y266), H270 (= H273), H280 (= H283)
8i29A Crystal structure of butanol dehydrogenase a (yqdh) in complex with nadh from fusobacterium nucleatum
34% identity, 99% coverage: 2:381/382 of query aligns to 1:383/384 of 8i29A
- binding cobalt (ii) ion: E205 (= E202), H271 (= H269), H285 (= H283)
- binding nicotinamide-adenine-dinucleotide: A102 (≠ G99), T142 (= T139), I143 (≠ L140), A146 (≠ T143), S148 (= S145), S151 (≠ N148), S153 (≠ G150), I155 (≠ V152), T186 (= T183), I187 (≠ V184), L191 (≠ Y188)
7fjgA Crystal structure of butanol dehydrogenase a (yqdh) in complex with partial nadh from fusobacterium nucleatum
34% identity, 99% coverage: 2:381/382 of query aligns to 1:383/384 of 7fjgA
Q46856 Alcohol dehydrogenase YqhD; EC 1.1.1.2 from Escherichia coli (strain K12) (see paper)
34% identity, 92% coverage: 1:350/382 of query aligns to 1:354/387 of Q46856
- GGS 38:40 (≠ SER 40:42) binding
- 93:99 (vs. 97:103, 100% identical) binding
- T138 (= T139) binding
- N147 (= N148) binding
- K160 (= K161) binding
- YTYT 179:182 (≠ LMKT 180:183) binding
- D194 (= D195) binding
- H198 (= H199) binding
- H267 (= H269) binding
- H281 (= H283) binding
1oj7B Structural genomics, unknown function crystal structure of e. Coli k-12 yqhd (see paper)
34% identity, 92% coverage: 1:350/382 of query aligns to 4:357/390 of 1oj7B
- binding 5,6-dihydroxy-nadp: G41 (≠ S40), S43 (≠ R42), P70 (≠ S71), N71 (= N72), G97 (= G98), G98 (= G99), S99 (= S100), D102 (= D103), T141 (= T139), L142 (= L140), T145 (= T143), S147 (= S145), G152 (= G150), V154 (= V152), K163 (= K161), T185 (= T183), L186 (≠ V184), P187 (≠ S185), Q190 (≠ Y188), H201 (= H199), H270 (= H269), H284 (= H283)
- binding zinc ion: D197 (= D195), H201 (= H199), H270 (= H269), H284 (= H283)
1oj7A Structural genomics, unknown function crystal structure of e. Coli k-12 yqhd (see paper)
34% identity, 92% coverage: 1:350/382 of query aligns to 4:357/390 of 1oj7A
- binding 5,6-dihydroxy-nadp: G41 (≠ S40), S43 (≠ R42), P70 (≠ S71), N71 (= N72), G97 (= G98), G98 (= G99), S99 (= S100), D102 (= D103), T141 (= T139), L142 (= L140), T145 (= T143), S147 (= S145), N150 (= N148), G152 (= G150), K163 (= K161), T185 (= T183), L186 (≠ V184), Q190 (≠ Y188), D197 (= D195), H201 (= H199), H270 (= H269), H284 (= H283)
3bfjA Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
28% identity, 99% coverage: 4:382/382 of query aligns to 3:382/382 of 3bfjA
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)
28% identity, 97% coverage: 1:371/382 of query aligns to 1:368/383 of P0DJA2
- M1 (= M1) modified: Initiator methionine, Removed
- D39 (≠ S40) binding
- N71 (= N72) binding
- G98 (= G99) binding
- S99 (= S100) binding
- T138 (= T139) binding
- T139 (≠ L140) binding
- T147 (≠ N148) binding
- F149 (≠ G150) binding
- K160 (= K161) binding
- L179 (= L180) binding
- G182 (≠ T183) binding
- M183 (≠ V184) binding
- D194 (= D195) binding
- H198 (= H199) binding
- H263 (= H269) binding
- H267 (= H273) binding
- H277 (= H283) binding ; binding
3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor (see paper)
28% identity, 96% coverage: 5:371/382 of query aligns to 4:367/382 of 3ox4A
- binding fe (ii) ion: D193 (= D195), H197 (= H199), H262 (= H269), H276 (= H283)
- binding nicotinamide-adenine-dinucleotide: D38 (≠ S40), F40 (≠ R42), M41 (≠ I43), N70 (= N72), G96 (= G98), G97 (= G99), S98 (= S100), T137 (= T139), T138 (≠ L140), F148 (≠ G150), I150 (≠ V152), G181 (≠ T183), M182 (≠ V184), L186 (≠ Y188), H276 (= H283)
3owoA Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
28% identity, 96% coverage: 5:371/382 of query aligns to 4:367/382 of 3owoA
P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
28% identity, 99% coverage: 6:382/382 of query aligns to 4:381/381 of P31005
- G13 (= G15) mutation to A: Shows a reduced dehydrogenase activity.
- G15 (≠ D17) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
- D88 (≠ E91) 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
7qlqAAA Lactaldehyde reductase (see paper)
25% identity, 88% coverage: 14:350/382 of query aligns to 12:349/383 of 7qlqAAA
- binding adenosine-5-diphosphoribose: D37 (≠ S40), T39 (≠ R42), L40 (≠ I43), G95 (= G98), G96 (= G99), S97 (= S100), T138 (= T139), T139 (≠ L140), T142 (= T143), K160 (= K161), G182 (≠ T183), M183 (≠ V184), L187 (≠ Y188), H275 (= H283)
- binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (= G150), V164 (≠ T165), H198 (= H199), F252 (≠ Y258), S253 (≠ A259), H261 (= H269)
- binding fe (iii) ion: D194 (= D195), H198 (= H199), H261 (= H269), H275 (= H283)
Sites not aligning to the query:
7qlgAAA Lactaldehyde reductase (see paper)
25% identity, 88% coverage: 14:350/382 of query aligns to 12:349/383 of 7qlgAAA
- binding fe (iii) ion: D194 (= D195), H198 (= H199), H261 (= H269), H275 (= H283)
- binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (≠ S40), T39 (≠ R42), L40 (≠ I43), N69 (= N72), G95 (= G98), G96 (= G99), S97 (= S100), D100 (= D103), T138 (= T139), T139 (≠ L140), T142 (= T143), T147 (≠ N148), N149 (≠ G150), K160 (= K161), L187 (≠ Y188), H198 (= H199), H275 (= H283)
2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
25% identity, 92% coverage: 1:350/382 of query aligns to 1:350/382 of 2bi4A
- binding fe (iii) ion: D195 (= D195), H199 (= H199), H262 (= H269), H276 (= H283)
- binding nicotinamide-adenine-dinucleotide: D38 (≠ S40), T40 (≠ R42), L41 (≠ I43), G96 (= G98), G97 (= G99), S98 (= S100), T139 (= T139), T140 (≠ L140), V152 (= V152), K161 (= K161), G183 (≠ T183), M184 (≠ V184), L188 (≠ Y188), D195 (= D195), H199 (= H199), H262 (= H269), H276 (= H283)
P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
25% identity, 92% coverage: 1:350/382 of query aligns to 1:350/382 of P0A9S1
- 1:9 (vs. 1:9, 33% identical) mutation to M: Loss of enzyme activity, loss of dimerization.
- G16 (≠ D17) mutation to D: No effect on enzyme activity.
- D38 (≠ S40) mutation to G: Enzyme can now use NADP.
- G96 (= G98) mutation to E: Loss of NAD binding and enzyme activity.
- D195 (= D195) mutation to L: Complete loss of iron-binding.
- H199 (= H199) mutation H->A,F: Complete loss of iron-binding.
1rrmA Crystal structure of lactaldehyde reductase
25% identity, 92% coverage: 1:350/382 of query aligns to 1:350/385 of 1rrmA
- binding adenosine-5-diphosphoribose: D38 (≠ S40), T40 (≠ R42), L41 (≠ I43), N70 (= N72), G96 (= G98), G97 (= G99), S98 (= S100), T139 (= T139), T140 (≠ L140), T143 (= T143), V152 (= V152), K161 (= K161), G183 (≠ T183), M184 (≠ V184), L188 (≠ Y188), H276 (= H283)
- binding fe (ii) ion: L258 (≠ Y264)
- binding zinc ion: D195 (= D195), H199 (= H199), H262 (= H269), H276 (= H283)
Sites not aligning to the query:
5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
25% identity, 92% coverage: 1:350/382 of query aligns to 2:351/385 of 5br4A
- binding nicotinamide-adenine-dinucleotide: D39 (≠ S40), T41 (≠ R42), L42 (≠ I43), P70 (≠ S71), G97 (= G98), G98 (= G99), S99 (= S100), D102 (= D103), T140 (= T139), T141 (≠ L140), T144 (= T143), T149 (≠ N148), N151 (≠ G150), V153 (= V152), K162 (= K161), G184 (≠ T183), C185 (≠ V184), L189 (≠ Y188), H277 (= H283)
- binding zinc ion: D196 (= D195), H200 (= H199), H263 (= H269), H277 (= H283)
5yvmA Crystal structure of the archaeal halo-thermophilic red sea brine pool alcohol dehydrogenase adh/d1 bound to nzq (see paper)
25% identity, 96% coverage: 14:380/382 of query aligns to 17:402/403 of 5yvmA
- binding manganese (ii) ion: D207 (= D195), H211 (= H199), H276 (= H269), H291 (= H283)
- binding 5,6-dihydroxy-nadp: G41 (= G39), N44 (≠ R42), M45 (≠ I43), P73 (≠ S71), N74 (= N72), G100 (= G98), G101 (= G99), S102 (= S100), D105 (= D103), S151 (≠ T139), T152 (≠ L140), T155 (= T143), T160 (≠ N148), Y162 (≠ G150), V164 (= V152), K173 (= K161), E195 (≠ T183), L200 (≠ Y188), H211 (= H199), H276 (= H269), H280 (= H273), H291 (= H283)
Query Sequence
>Dsui_2116 FitnessBrowser__PS:Dsui_2116
MDNFTFFNPTQVEFGKDKEQAIGRHLAEHGIKKVLLCYGSERIKRDGLFGVVSKSLAEQG
ITFVECGGIVSNPVISKVREAIALARDHQVEAILSVGGGSVLDSSKAIAAGVPYAGDVWD
LFIGKGRIESALPVFDILTLAATGSEMNNGAVVTNEATQEKFAITSVHTYPKVSIVNPAL
MKTVSRDYLVYSAADVIAHAIEGYFTAKDEPRFQSRLVEAIINTVIETTETLLADPENYE
ARAEFAWAATQALNGLLYAGISGYSYPNHMIEHSLSALFNVPHGAGLSVVMPAWMKWYHS
RNPVQFQRFAKYVFGVETAEQGIAALEKWFDKIGTPTRLSQLGISEADLPKTIDNVLGNA
VHFGVAETYPRDVVATILKSAL
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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