SitesBLAST
Comparing Dsui_0105 Dsui_0105 NAD-dependent aldehyde dehydrogenase 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)
6x9lA Crystal structure of aldehyde dehydrogenasE C (aldc) mutant (c291a) from pseudomonas syringae in complexed with NAD+ and octanal (see paper)
48% identity, 98% coverage: 6:470/476 of query aligns to 13:477/485 of 6x9lA
- active site: N154 (= N147), E252 (= E245), A286 (≠ C279), E462 (= E455)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), T151 (= T144), W153 (= W146), N154 (= N147), Q159 (= Q152), K177 (= K170), E180 (= E173), G210 (= G203), P211 (= P204), G214 (= G207), T229 (= T222), G230 (= G223), S231 (= S224), E252 (= E245), L253 (= L246), A286 (≠ C279), E386 (= E379), F388 (= F381), F451 (= F444)
- binding octanal: W155 (≠ F148), S285 (≠ A278)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
41% identity, 99% coverage: 1:470/476 of query aligns to 2:449/454 of 3ty7B
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
41% identity, 98% coverage: 6:470/476 of query aligns to 9:482/497 of P17202
- I28 (≠ E25) binding
- D96 (≠ E91) binding
- SPW 156:158 (≠ TPW 144:146) binding
- Y160 (≠ F148) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ A155) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 170:173) binding
- L186 (≠ V174) binding
- SSAT 236:239 (≠ STAA 224:227) binding
- V251 (= V239) binding in other chain
- L258 (= L246) binding
- W285 (≠ L273) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E379) binding
- A441 (≠ Q430) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ N439) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F444) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K448) binding
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
39% identity, 99% coverage: 1:470/476 of query aligns to 13:486/491 of 5gtlA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E379), E471 (= E455)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I143), P163 (= P145), K188 (= K170), A190 (≠ S172), E191 (= E173), Q192 (≠ V174), G221 (= G203), G225 (= G207), G241 (= G223), S242 (= S224), T245 (≠ A227), L264 (= L246), C297 (= C279), E394 (= E379), F396 (= F381)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
39% identity, 99% coverage: 1:470/476 of query aligns to 13:486/491 of 5gtkA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E379), E471 (= E455)
- binding nicotinamide-adenine-dinucleotide: I161 (= I143), I162 (≠ T144), P163 (= P145), W164 (= W146), K188 (= K170), E191 (= E173), G221 (= G203), G225 (= G207), A226 (≠ E208), F239 (= F221), G241 (= G223), S242 (= S224), T245 (≠ A227), Y248 (≠ R230), L264 (= L246), C297 (= C279), Q344 (= Q326), R347 (= R329), E394 (= E379), F396 (= F381)
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
42% identity, 98% coverage: 6:470/476 of query aligns to 4:480/497 of 3iwkH
- active site: N157 (= N147), K180 (= K170), E255 (= E245), C289 (= C279), E388 (= E379), E465 (= E455)
- binding nicotinamide-adenine-dinucleotide: W156 (= W146), G213 (= G203), G217 (= G207), A218 (≠ E208), G233 (= G223), S234 (= S224), T237 (≠ A227), K240 (≠ R230), C289 (= C279), Q336 (= Q326), E388 (= E379), F390 (= F381)
Q8VWZ1 Aminoaldehyde dehydrogenase 1, peroxisomal; PsAMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
42% identity, 98% coverage: 6:470/476 of query aligns to 9:485/503 of Q8VWZ1
- N27 (≠ V24) binding
- I28 (≠ E25) binding
- D99 (≠ E91) binding
- L189 (≠ V174) binding
- 238:245 (vs. 223:230, 50% identical) binding
- C294 (= C279) binding
- E393 (= E379) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
40% identity, 98% coverage: 6:470/476 of query aligns to 7:480/495 of 4v37A
- active site: N157 (= N147), K180 (= K170), E255 (= E245), A289 (≠ C279), E388 (= E379), E465 (= E455)
- binding 3-aminopropan-1-ol: C448 (≠ N439), W454 (≠ F444)
- binding nicotinamide-adenine-dinucleotide: I153 (= I143), S154 (≠ T144), P155 (= P145), W156 (= W146), N157 (= N147), M162 (≠ Q152), K180 (= K170), S182 (= S172), E183 (= E173), G213 (= G203), G217 (= G207), A218 (≠ E208), T232 (= T222), G233 (= G223), S234 (= S224), T237 (≠ A227), E255 (= E245), L256 (= L246), A289 (≠ C279), E388 (= E379), F390 (= F381)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
40% identity, 99% coverage: 2:470/476 of query aligns to 1:475/489 of 4o6rA
- active site: N150 (= N147), K173 (= K170), E248 (= E245), C282 (= C279), E383 (= E379), E460 (= E455)
- binding adenosine monophosphate: I146 (= I143), V147 (≠ T144), K173 (= K170), G206 (= G203), G210 (= G207), Q211 (≠ E208), F224 (= F221), G226 (= G223), S227 (= S224), T230 (≠ A227), R233 (= R230)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
40% identity, 99% coverage: 3:474/476 of query aligns to 4:479/483 of 3b4wA
- active site: N154 (= N147), K177 (= K170), E251 (= E245), C285 (= C279), E384 (= E379), E460 (= E455)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), V151 (≠ T144), W153 (= W146), N154 (= N147), K177 (= K170), I210 (≠ P204), G213 (= G207), T228 (= T222), G229 (= G223), S230 (= S224), V233 (≠ A227), E236 (≠ R230), E251 (= E245), L252 (= L246), C285 (= C279), E384 (= E379), F386 (= F381)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
39% identity, 98% coverage: 4:470/476 of query aligns to 2:473/487 of 4go4A
- active site: N149 (= N147), K172 (= K170), E247 (= E245), C281 (= C279), E381 (= E379), E458 (= E455)
- binding nicotinamide-adenine-dinucleotide: I145 (= I143), V146 (≠ T144), W148 (= W146), N149 (= N147), F154 (≠ Q152), K172 (= K170), G205 (= G203), G209 (= G207), Q210 (≠ E208), F223 (= F221), T224 (= T222), G225 (= G223), S226 (= S224), T229 (≠ A227), E247 (= E245), G249 (= G247), C281 (= C279), E381 (= E379), F383 (= F381)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
40% identity, 97% coverage: 7:470/476 of query aligns to 12:487/505 of O24174
- N164 (= N147) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
- W172 (≠ A155) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
40% identity, 99% coverage: 3:472/476 of query aligns to 4:475/477 of 2opxA
- active site: N151 (= N147), K174 (= K170), E249 (= E245), C283 (= C279), E381 (= E379), A458 (≠ E455)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (vs. gap), F152 (= F148), N284 (≠ S280), F312 (≠ L308), G313 (= G309), R318 (≠ E314), D320 (≠ S316), I321 (vs. gap), A322 (≠ R317), Y362 (= Y360), F440 (= F438), F440 (= F438), E441 (≠ N439)
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
39% identity, 99% coverage: 3:472/476 of query aligns to 6:477/479 of P25553
- L150 (≠ T144) binding
- R161 (≠ A155) binding
- KPSE 176:179 (= KPSE 170:173) binding
- F180 (≠ V174) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ E208) binding
- S230 (= S224) binding
- E251 (= E245) binding
- N286 (≠ S280) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (= R329) binding
- E443 (≠ N439) binding
- H449 (vs. gap) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
39% identity, 99% coverage: 3:472/476 of query aligns to 4:475/477 of 2impA
- active site: N151 (= N147), K174 (= K170), E249 (= E245), C283 (= C279), E381 (= E379), A458 (≠ E455)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I143), L148 (≠ T144), P149 (= P145), W150 (= W146), K174 (= K170), E177 (= E173), F178 (≠ V174), G207 (= G203), G211 (= G207), Q212 (≠ E208), S228 (= S224), A231 (= A227), K234 (≠ R230), R334 (= R329)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
39% identity, 99% coverage: 3:472/476 of query aligns to 4:475/477 of 2iluA
- active site: N151 (= N147), K174 (= K170), E249 (= E245), C283 (= C279), E381 (= E379), A458 (≠ E455)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I143), L148 (≠ T144), P149 (= P145), W150 (= W146), K174 (= K170), S176 (= S172), E177 (= E173), R206 (≠ Y202), G207 (= G203), G211 (= G207), Q212 (≠ E208), S228 (= S224), A231 (= A227), K234 (≠ R230), I235 (≠ V231), N328 (≠ S323), R334 (= R329), F383 (= F381)
3iwjA Crystal structure of aminoaldehyde dehydrogenase 2 from pisum sativum (psamadh2) (see paper)
40% identity, 98% coverage: 6:470/476 of query aligns to 6:482/500 of 3iwjA
- active site: N159 (= N147), K182 (= K170), E257 (= E245), C291 (= C279), E390 (= E379), E467 (= E455)
- binding glycerol: D110 (≠ T110), Y160 (≠ F148), W167 (≠ A155), I290 (≠ A278), C291 (= C279), C450 (≠ N439), W456 (≠ F444)
- binding nicotinamide-adenine-dinucleotide: I155 (= I143), T156 (= T144), W158 (= W146), K182 (= K170), S184 (= S172), E185 (= E173), G215 (= G203), A220 (≠ E208), F233 (= F221), G235 (= G223), S236 (= S224), T239 (≠ A227), I243 (≠ V231)
Q93YB2 Aminoaldehyde dehydrogenase 2, peroxisomal; PsAMADH2; Aminobutyraldehyde dehydrogenase AMADH2; Gamma-guanidinobutyraldehyde dehydrogenase AMADH2; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
40% identity, 98% coverage: 6:470/476 of query aligns to 9:485/503 of Q93YB2
- I28 (≠ E25) binding
- D99 (≠ E91) binding
- W161 (= W146) binding
- K185 (= K170) binding
- L189 (≠ V174) binding
- S239 (= S224) binding
5ac0A Ovis aries aldehyde dehydrogenase 1a1 in complex with a duocarmycin analog (see paper)
37% identity, 100% coverage: 3:476/476 of query aligns to 12:491/494 of 5ac0A
- active site: N163 (= N147), K186 (= K170), E262 (= E245), C296 (= C279), E393 (= E379), E470 (= E455)
- binding 1-[(1S)-1-methyl-5-oxidanyl-1,2-dihydrobenzo[e]indol-3-yl]hexan-1-one: M114 (≠ V102), F164 (= F148), W171 (≠ A155), Y290 (≠ L273), C295 (≠ A278), C296 (= C279)
- binding nicotinamide-adenine-dinucleotide: I159 (= I143), I160 (≠ T144), P161 (= P145), W162 (= W146), K186 (= K170), E189 (= E173), G219 (= G203), G223 (= G207), A224 (≠ E208), F237 (= F221), G239 (= G223), S240 (= S224), V243 (≠ A227), G264 (= G247), C296 (= C279), Q343 (= Q326), K346 (≠ R329), E393 (= E379)
5abmA Sheep aldehyde dehydrogenase 1a1 (see paper)
37% identity, 100% coverage: 3:476/476 of query aligns to 12:491/494 of 5abmA
- active site: N163 (= N147), K186 (= K170), E262 (= E245), C296 (= C279), E393 (= E379), E470 (= E455)
- 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: I159 (= I143), I160 (≠ T144), P161 (= P145), W162 (= W146), K186 (= K170), E189 (= E173), G219 (= G203), G223 (= G207), F237 (= F221), G239 (= G223), S240 (= S224), V243 (≠ A227), G264 (= G247), Q343 (= Q326), K346 (≠ R329), E393 (= E379), F395 (= F381)
Query Sequence
>Dsui_0105 Dsui_0105 NAD-dependent aldehyde dehydrogenase
MQQHSRFYIGGQWVAPDGNAFIDVENPATETVIARVPEGTATDADRAARAAAAAFPAWAA
LSGAERGAFLQKIADGLKARQDELGRLIASEVGMPVKLATRVQAGNPIFTFAACARIAAE
GFAEERIGQSLVLKVPTGPVACITPWNFPLHQIAAKVGAALAAGCTVVLKPSEVAPLNAF
LLAEVIEAAGLPAGVFNLVTGYGPVVGEALAAHPALAAVSFTGSTAAGKRVAAVAAATVK
RVSLELGGKSASVVLPDADLAAAVKGTVAGCFLNSGQACSALTRLLVPQERYAEAAALAV
QAAAAYTLGDPLAEGSRLGPLVSGLQRQRVRAMIEQAVADGAELLCGGSAAPEGLPTGYY
VRPTVFGRVRPDAALAREEVFGPVLAILTYRDEAEAEAIANGTDYGLAAAVWSAEEARAL
AFARRLRAGQVDINGAFFNLLAPFGGFKQSGYGRELGRHGVEDFLETQSIQLPQRQ
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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