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Comparing Echvi_0481 FitnessBrowser__Cola:Echvi_0481 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)
P37685 Aldehyde dehydrogenase B; Acetaldehyde dehydrogenase; EC 1.2.1.4 from Escherichia coli (strain K12) (see paper)
61% identity, 99% coverage: 5:509/509 of query aligns to 8:512/512 of P37685
- R197 (≠ E194) mutation to E: Less than 10% of wild-type acetaldehyde dehydrogenase activity.
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
44% identity, 94% coverage: 25:504/509 of query aligns to 7:482/489 of 4o6rA
- active site: N150 (= N168), K173 (= K191), E248 (= E265), C282 (= C304), E383 (= E405), E460 (= E482)
- binding adenosine monophosphate: I146 (= I164), V147 (≠ I165), K173 (= K191), G206 (= G223), G210 (= G227), Q211 (≠ K228), F224 (= F241), G226 (= G243), S227 (≠ E244), T230 (= T247), R233 (≠ L250)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
42% identity, 94% coverage: 25:502/509 of query aligns to 6:478/487 of 4go4A
- active site: N149 (= N168), K172 (= K191), E247 (= E265), C281 (= C304), E381 (= E405), E458 (= E482)
- binding nicotinamide-adenine-dinucleotide: I145 (= I164), V146 (≠ I165), W148 (= W167), N149 (= N168), F154 (≠ M173), K172 (= K191), G205 (= G223), G209 (= G227), Q210 (≠ K228), F223 (= F241), T224 (= T242), G225 (= G243), S226 (≠ E244), T229 (= T247), E247 (= E265), G249 (= G267), C281 (= C304), E381 (= E405), F383 (= F407)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
44% identity, 93% coverage: 25:498/509 of query aligns to 9:477/486 of 4pxlA
- active site: N154 (= N168), K177 (= K191), E253 (= E265), C287 (= C304), E384 (= E405), D461 (≠ E482)
- binding nicotinamide-adenine-dinucleotide: I150 (= I164), V151 (≠ I165), P152 (= P166), W153 (= W167), K177 (= K191), E180 (= E194), G210 (= G223), G214 (= G227), A215 (≠ K228), F228 (= F241), G230 (= G243), S231 (≠ E244), V234 (≠ T247), E253 (= E265), G255 (= G267), C287 (= C304), Q334 (= Q351), K337 (= K354), E384 (= E405), F386 (= F407)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
41% identity, 94% coverage: 25:500/509 of query aligns to 20:489/491 of 5gtlA
- active site: N165 (= N168), K188 (= K191), E263 (= E265), C297 (= C304), E394 (= E405), E471 (= E482)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I164), P163 (= P166), K188 (= K191), A190 (= A193), E191 (= E194), Q192 (= Q195), G221 (= G223), G225 (= G227), G241 (= G243), S242 (≠ E244), T245 (= T247), L264 (= L266), C297 (= C304), E394 (= E405), F396 (= F407)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
41% identity, 94% coverage: 25:500/509 of query aligns to 20:489/491 of 5gtkA
- active site: N165 (= N168), K188 (= K191), E263 (= E265), C297 (= C304), E394 (= E405), E471 (= E482)
- binding nicotinamide-adenine-dinucleotide: I161 (= I164), I162 (= I165), P163 (= P166), W164 (= W167), K188 (= K191), E191 (= E194), G221 (= G223), G225 (= G227), A226 (≠ K228), F239 (= F241), G241 (= G243), S242 (≠ E244), T245 (= T247), Y248 (≠ L250), L264 (= L266), C297 (= C304), Q344 (= Q351), R347 (≠ K354), E394 (= E405), F396 (= F407)
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
42% identity, 96% coverage: 10:499/509 of query aligns to 9:493/501 of Q56YU0
- G152 (≠ S151) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A422) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
7radA Crystal structure analysis of aldh1b1
42% identity, 96% coverage: 9:499/509 of query aligns to 2:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I164), I159 (= I165), P160 (= P166), W161 (= W167), N162 (= N168), M167 (= M173), K185 (= K191), E188 (= E194), G218 (= G223), G222 (= G227), A223 (≠ K228), T237 (= T242), G238 (= G243), S239 (≠ E244), V242 (≠ T247), E261 (= E265), L262 (= L266), C295 (= C304), E392 (= E405), F394 (= F407)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ A119), E117 (≠ L123), F163 (= F169), E285 (= E291), F289 (= F296), N450 (≠ H463), V452 (≠ Y465)
7mjdA Crystal structure analysis of aldh1b1
42% identity, 96% coverage: 9:499/509 of query aligns to 2:486/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I164), I159 (= I165), P160 (= P166), W161 (= W167), N162 (= N168), M167 (= M173), K185 (= K191), E188 (= E194), G218 (= G223), G222 (= G227), F236 (= F241), T237 (= T242), G238 (= G243), S239 (≠ E244), V242 (≠ T247), E261 (= E265), L262 (= L266), C295 (= C304), E392 (= E405), F394 (= F407)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ L123), E285 (= E291), F289 (= F296), N450 (≠ H463), V452 (≠ Y465)
7mjcA Crystal structure analysis of aldh1b1
42% identity, 96% coverage: 9:499/509 of query aligns to 2:486/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I164), I159 (= I165), P160 (= P166), W161 (= W167), N162 (= N168), K185 (= K191), E188 (= E194), G218 (= G223), G222 (= G227), T237 (= T242), G238 (= G243), S239 (≠ E244), V242 (≠ T247), E261 (= E265), L262 (= L266), C295 (= C304), E392 (= E405), F394 (= F407)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
43% identity, 93% coverage: 25:499/509 of query aligns to 17:487/494 of 5l13A
- active site: N163 (= N168), K186 (= K191), E262 (= E265), C296 (= C304), E393 (= E405), E470 (= E482)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F169), M168 (= M173), W171 (= W176), F290 (vs. gap), C295 (≠ V303), C296 (= C304), C297 (≠ T305), D451 (≠ H463), F453 (≠ Y465)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
43% identity, 93% coverage: 25:499/509 of query aligns to 17:487/494 of 4kwgA
- active site: N163 (= N168), K186 (= K191), E262 (= E265), C296 (= C304), E393 (= E405), E470 (= E482)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F169), M168 (= M173), C295 (≠ V303), C296 (= C304), C297 (≠ T305), D451 (≠ H463), F453 (≠ Y465)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
43% identity, 93% coverage: 25:499/509 of query aligns to 17:487/494 of 4kwfA
- active site: N163 (= N168), K186 (= K191), E262 (= E265), C296 (= C304), E393 (= E405), E470 (= E482)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F169), M168 (= M173), W171 (= W176), E262 (= E265), C295 (≠ V303), C296 (= C304), C297 (≠ T305), D451 (≠ H463), F453 (≠ Y465), F459 (= F471)
3sz9A Crystal structure of human aldh2 modified with the beta-elimination product of aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one (see paper)
43% identity, 93% coverage: 25:499/509 of query aligns to 17:487/494 of 3sz9A
- active site: N163 (= N168), K186 (= K191), E262 (= E265), C296 (= C304), E393 (= E405), E470 (= E482)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F169), C295 (≠ V303), C296 (= C304), D451 (≠ H463), F453 (≠ Y465), F459 (= F471)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
43% identity, 93% coverage: 25:499/509 of query aligns to 17:487/494 of 3injA
- active site: N163 (= N168), K186 (= K191), E262 (= E265), C296 (= C304), E393 (= E405), E470 (= E482)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ L123), F164 (= F169), L167 (= L172), F286 (= F296), F290 (vs. gap), D451 (≠ H463), F453 (≠ Y465)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
43% identity, 93% coverage: 25:499/509 of query aligns to 17:487/494 of 2vleA
- active site: N163 (= N168), K186 (= K191), E262 (= E265), C296 (= C304), E393 (= E405), E470 (= E482)
- binding daidzin: M118 (≠ L123), F164 (= F169), M168 (= M173), W171 (= W176), F286 (= F296), F290 (vs. gap), C295 (≠ V303), C296 (= C304), D451 (≠ H463), V452 (≠ A464), F453 (≠ Y465)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
43% identity, 93% coverage: 25:499/509 of query aligns to 17:487/494 of 1o01B
- active site: N163 (= N168), K186 (= K191), E262 (= E265), C296 (= C304), E393 (= E405), E470 (= E482)
- binding (2e)-but-2-enal: C296 (= C304), C297 (≠ T305), F453 (≠ Y465)
- binding nicotinamide-adenine-dinucleotide: I159 (= I164), I160 (= I165), P161 (= P166), W162 (= W167), K186 (= K191), E189 (= E194), G219 (= G223), G223 (= G227), A224 (≠ K228), F237 (= F241), G239 (= G243), S240 (≠ E244), I243 (≠ T247), L263 (= L266), G264 (= G267), C296 (= C304), Q343 (= Q351), E393 (= E405), F395 (= F407)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
43% identity, 93% coverage: 25:499/509 of query aligns to 17:487/494 of 1cw3A
- active site: N163 (= N168), K186 (= K191), E262 (= E265), C296 (= C304), E393 (= E405), E470 (= E482)
- binding magnesium ion: V34 (≠ I42), D103 (= D108), Q190 (= Q195)
- binding nicotinamide-adenine-dinucleotide: I159 (= I164), I160 (= I165), P161 (= P166), W162 (= W167), K186 (= K191), G219 (= G223), G223 (= G227), A224 (≠ K228), F237 (= F241), G239 (= G243), S240 (≠ E244), I243 (≠ T247), L263 (= L266), G264 (= G267), C296 (= C304), Q343 (= Q351), K346 (= K354), E393 (= E405), F395 (= F407)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
43% identity, 93% coverage: 25:499/509 of query aligns to 19:489/496 of 4fr8C
- active site: N165 (= N168), K188 (= K191), Q264 (≠ E265), C298 (= C304), E395 (= E405), E472 (= E482)
- binding nicotinamide-adenine-dinucleotide: I161 (= I164), I162 (= I165), W164 (= W167), K188 (= K191), G221 (= G223), G225 (= G227), A226 (≠ K228), F239 (= F241), G241 (= G243), S242 (≠ E244), I245 (≠ T247), Q345 (= Q351), E395 (= E405), F397 (= F407)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
43% identity, 93% coverage: 25:499/509 of query aligns to 16:486/493 of 4fr8A
- active site: N162 (= N168), K185 (= K191), Q261 (≠ E265), C295 (= C304), E392 (= E405), E469 (= E482)
- binding nicotinamide-adenine-dinucleotide: I158 (= I164), I159 (= I165), W161 (= W167), K185 (= K191), G218 (= G223), G222 (= G227), A223 (≠ K228), F236 (= F241), G238 (= G243), S239 (≠ E244), I242 (≠ T247), Q342 (= Q351), K345 (= K354), E392 (= E405), F394 (= F407)
- binding propane-1,2,3-triyl trinitrate: F163 (= F169), L166 (= L172), W170 (= W176), F289 (vs. gap), S294 (≠ V303), C295 (= C304), D450 (≠ H463), F452 (≠ Y465)
Query Sequence
>Echvi_0481 FitnessBrowser__Cola:Echvi_0481
MSTIAQEKPATMLDRPDFKPHYDNFIGGKFVPPVDGEYFDVISPVDGQVFTKVARGKAAD
IELALDAAHKAFPAWSRTSATERSNILLKIADRIENKLEYLAAVETIDNGKPVRETINAD
LALVVDHFRYFAGVIRAEEGSIAELDQHTVSVNVKEPIGIVGQIIPWNFPMLMATWKMAP
ALAAGCCTIVKPAEQTPASIMILMEVIGDLLPAGVLNVVNGFGPEAGKPLAQSPRLDKVA
FTGETTTGRLIMQYASENLNPVTMELGGKSPNVFFPSVMDADDEFLDKCLEGAVMFALNQ
GEVCTCPSRILVHEKIYDAFMEKVIARAEAIQMGHPLDKTTMMGAQASKDQFEKILSYID
IGKQEGAEVLTGGEVAKLNSGLENGYYVKPTLLKGHNKMRVFQEEIFGPVCSVATFKDVE
EAISISNDTLYGLGAGVWTRDAHEAYQVPRAIKAGRVWVNCYHAYPAHAPFGGYKKSGFG
RETHLMMLNHYRQNKNMLISYDKNKLGFF
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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