SitesBLAST
Comparing Ga0059261_3374 Ga0059261_3374 NAD-dependent aldehyde dehydrogenases 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)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
47% identity, 100% coverage: 1:473/474 of query aligns to 2:453/454 of 3ty7B
6x9lA Crystal structure of aldehyde dehydrogenasE C (aldc) mutant (c291a) from pseudomonas syringae in complexed with NAD+ and octanal (see paper)
51% identity, 98% coverage: 6:471/474 of query aligns to 13:479/485 of 6x9lA
- active site: N154 (= N147), E252 (= E245), A286 (≠ C279), E462 (= E454)
- 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 (= F443)
- binding octanal: W155 (= W148), S285 (= S278)
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)
38% identity, 97% coverage: 8:467/474 of query aligns to 11:480/497 of P17202
- I28 (= I25) binding
- D96 (≠ E91) binding
- SPW 156:158 (≠ TPW 144:146) binding
- Y160 (≠ W148) 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 (≠ E174) binding
- SSAT 236:239 (≠ STRA 224:227) binding
- V251 (= V239) binding in other chain
- L258 (= L246) binding
- W285 (≠ M273) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E379) binding
- A441 (≠ M429) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ D438) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F443) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K447) binding
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
39% identity, 99% coverage: 4:473/474 of query aligns to 13:489/489 of 7a6qB
- active site: N163 (= N147), E262 (= E245), C296 (= C279), E470 (= E454)
- binding nicotinamide-adenine-dinucleotide: I159 (= I143), W162 (= W146), K186 (= K170), E189 (= E173), G219 (= G203), G223 (= G207), S240 (= S224), V243 (≠ A227), K342 (≠ A325)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (≠ D23), T33 (≠ V24), C34 (≠ I25), P36 (= P27), D103 (≠ E91), E189 (= E173), Q190 (≠ E174), F218 (≠ D202), I339 (≠ V322), D340 (≠ N323)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ S113), D141 (vs. gap), N143 (vs. gap), N451 (≠ Q436), L453 (vs. gap), A455 (≠ P439)
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
39% identity, 99% coverage: 4:473/474 of query aligns to 13:489/489 of 7a6qA
- active site: N163 (= N147), E262 (= E245), C296 (= C279), E470 (= E454)
- binding nicotinamide-adenine-dinucleotide: I159 (= I143), T160 (= T144), W162 (= W146), K186 (= K170), A188 (≠ S172), E189 (= E173), G219 (= G203), G223 (= G207), S240 (= S224), V243 (≠ A227), K342 (≠ A325), K346 (= K329)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ S113), D141 (vs. gap), N143 (vs. gap), N451 (≠ Q436), L453 (vs. gap), Y454 (≠ D438)
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
39% identity, 99% coverage: 4:473/474 of query aligns to 13:489/489 of 5fhzA
- active site: N163 (= N147), K186 (= K170), E262 (= E245), C296 (= C279), E393 (= E379), E470 (= E454)
- binding nicotinamide-adenine-dinucleotide: I159 (= I143), T160 (= T144), W162 (= W146), K186 (= K170), E189 (= E173), G219 (= G203), G223 (= G207), F237 (= F221), G239 (= G223), S240 (= S224), T241 (= T225), V243 (≠ A227), G264 (= G247), Q343 (= Q326), E393 (= E379)
- binding retinoic acid: G118 (≠ S113), R121 (≠ N116), F164 (≠ W148), M168 (≠ Q152), W171 (≠ A155), C295 (≠ S278), C296 (= C279), L453 (vs. gap)
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
39% identity, 99% coverage: 4:473/474 of query aligns to 12:488/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I143), T159 (= T144), P160 (= P145), W161 (= W146), K185 (= K170), E188 (= E173), G218 (= G203), G222 (= G207), F236 (= F221), S239 (= S224), V242 (≠ A227)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
41% identity, 99% coverage: 4:470/474 of query aligns to 5:476/483 of 3b4wA
- active site: N154 (= N147), K177 (= K170), E251 (= E245), C285 (= C279), E384 (= E379), E460 (= E454)
- 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 (≠ Q230), E251 (= E245), L252 (= L246), C285 (= C279), E384 (= E379), F386 (= F381)
P47895 Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; Aldehyde dehydrogenase 6; Aldehyde dehydrogenase family 1 member A3; ALDH1A3; EC 1.2.1.36 from Homo sapiens (Human) (see 2 papers)
39% identity, 99% coverage: 4:473/474 of query aligns to 31:507/512 of P47895
- R89 (≠ S59) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K170) binding
- E207 (= E173) binding
- GSTEVG 257:262 (≠ GSTRAG 223:228) binding
- Q361 (= Q326) binding
- E411 (= E379) binding
- A493 (≠ G459) to P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
39% identity, 97% coverage: 8:467/474 of query aligns to 13:485/505 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.
6tgwA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with a selective inhibitor (see paper)
38% identity, 99% coverage: 4:473/474 of query aligns to 5:478/478 of 6tgwA
- active site: N155 (= N147), E254 (= E245), C288 (= C279), E459 (= E454)
- binding methyl 5-(1,3-benzodioxol-5-yl)-2-phenyl-pyrazolo[1,5-a]pyrimidine-7-carboxylate: I106 (≠ G109), G110 (≠ S113), F156 (≠ W148), Q278 (≠ F269), F282 (≠ M273), L442 (vs. gap), A444 (≠ P439)
- binding nicotinamide-adenine-dinucleotide: I151 (= I143), T152 (= T144), P153 (= P145), W154 (= W146), K178 (= K170), G211 (= G203), G215 (= G207), F229 (= F221), G231 (= G223), S232 (= S224), V235 (≠ A227)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
38% identity, 97% coverage: 8:467/474 of query aligns to 9:478/495 of 4v37A
- active site: N157 (= N147), K180 (= K170), E255 (= E245), A289 (≠ C279), E388 (= E379), E465 (= E454)
- binding 3-aminopropan-1-ol: C448 (≠ D438), W454 (≠ F443)
- 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 (≠ T208), T232 (= T222), G233 (= G223), S234 (= S224), T237 (≠ A227), E255 (= E245), L256 (= L246), A289 (≠ C279), E388 (= E379), F390 (= F381)
6te5B Crystal structure of human aldehyde dehydrogenase 1a3 in complex with lq43 inhibitor compound (see paper)
38% identity, 99% coverage: 4:473/474 of query aligns to 7:478/479 of 6te5B
- active site: N157 (= N147), E256 (= E245), C290 (= C279), E459 (= E454)
- binding 6-(3,5-dimethoxyphenyl)-2-(4-methoxyphenyl)imidazo[1,2-a]pyridine: E111 (≠ M112), G112 (≠ S113), T116 (≠ A117), L442 (vs. gap), A444 (≠ P439)
- binding nicotinamide-adenine-dinucleotide: I153 (= I143), T154 (= T144), W156 (= W146), K180 (= K170), E183 (= E173), G213 (= G203), F231 (= F221), S234 (= S224), V237 (≠ A227), Q337 (= Q326), K340 (= K329)
6tryA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with mf13 inhibitor compound (see paper)
38% identity, 99% coverage: 4:473/474 of query aligns to 6:477/478 of 6tryA
- active site: N156 (= N147), E255 (= E245), C289 (= C279), E458 (= E454)
- binding nicotinamide-adenine-dinucleotide: I152 (= I143), T153 (= T144), W155 (= W146), K179 (= K170), A181 (≠ S172), E182 (= E173), G212 (= G203), G216 (= G207), A217 (≠ T208), F230 (= F221), G232 (= G223), S233 (= S224), V236 (≠ A227), K335 (≠ A325)
- binding 8-(4-chlorophenyl)-2-phenyl-imidazo[1,2-a]pyridine: I107 (≠ G109), G111 (≠ S113), T115 (≠ A117), L160 (≠ N151), C288 (≠ S278), L441 (vs. gap), A443 (≠ P439)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
38% identity, 98% coverage: 5:469/474 of query aligns to 17:486/491 of 5gtlA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E379), E471 (= E454)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I143), P163 (= P145), K188 (= K170), A190 (≠ S172), E191 (= E173), Q192 (≠ E174), 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
38% identity, 98% coverage: 5:469/474 of query aligns to 17:486/491 of 5gtkA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E379), E471 (= E454)
- binding nicotinamide-adenine-dinucleotide: I161 (= I143), I162 (≠ T144), P163 (= P145), W164 (= W146), K188 (= K170), E191 (= E173), G221 (= G203), G225 (= G207), A226 (≠ T208), F239 (= F221), G241 (= G223), S242 (= S224), T245 (≠ A227), Y248 (≠ Q230), L264 (= L246), C297 (= C279), Q344 (= Q326), R347 (≠ K329), E394 (= E379), F396 (= F381)
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
39% identity, 99% coverage: 4:470/474 of query aligns to 11:484/492 of 6b5hA
- active site: N161 (= N147), E260 (= E245), C294 (= C279), E468 (= E454)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (vs. gap), G116 (vs. gap), F162 (≠ W148), W169 (≠ A155), Q284 (≠ F269), F288 (≠ M273), T295 (≠ I280), N449 (≠ Q436), L451 (vs. gap), N452 (≠ D438), F457 (= F443)
- binding nicotinamide-adenine-dinucleotide: I157 (= I143), I158 (≠ T144), W160 (= W146), N161 (= N147), K184 (= K170), G217 (= G203), G221 (= G207), F235 (= F221), T236 (= T222), G237 (= G223), S238 (= S224), V241 (≠ A227), E260 (= E245), L261 (= L246), C294 (= C279), F393 (= F381)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
39% identity, 99% coverage: 4:470/474 of query aligns to 11:484/492 of 6b5gA
- active site: N161 (= N147), E260 (= E245), C294 (= C279), E468 (= E454)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ W148), L165 (≠ N151), W169 (≠ A155), F288 (≠ M273), C293 (≠ S278), C294 (= C279), T295 (≠ I280), N449 (≠ Q436), L451 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: I157 (= I143), I158 (≠ T144), P159 (= P145), W160 (= W146), N161 (= N147), M166 (≠ Q152), K184 (= K170), E187 (= E173), G217 (= G203), G221 (= G207), F235 (= F221), T236 (= T222), G237 (= G223), S238 (= S224), V241 (≠ A227), E260 (= E245), L261 (= L246), C294 (= C279), E391 (= E379), F393 (= F381)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
39% identity, 99% coverage: 4:470/474 of query aligns to 11:484/492 of 6aljA
- active site: N161 (= N147), E260 (= E245), C294 (= C279), E468 (= E454)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (vs. gap), F162 (≠ W148), L165 (≠ N151), M166 (≠ Q152), W169 (≠ A155), E260 (= E245), C293 (≠ S278), C294 (= C279), L451 (vs. gap), N452 (≠ D438), A453 (≠ P439)
- binding nicotinamide-adenine-dinucleotide: I157 (= I143), I158 (≠ T144), P159 (= P145), W160 (= W146), N161 (= N147), K184 (= K170), E187 (= E173), G217 (= G203), G221 (= G207), F235 (= F221), G237 (= G223), S238 (= S224), V241 (≠ A227), Q341 (= Q326), K344 (= K329), E391 (= E379), F393 (= F381)
Q63639 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Rattus norvegicus (Rat) (see paper)
39% identity, 98% coverage: 4:469/474 of query aligns to 37:509/518 of Q63639
Query Sequence
>Ga0059261_3374 Ga0059261_3374 NAD-dependent aldehyde dehydrogenases
MRSYLKHYIGGEWVESEGGTRHDVINPATEAPVTEITLGSEADADKAVAAAKAAFDSFSR
TSVDERIALLEAILAEYKNRAGDLADAIAAEMGAPISLAKTAQVGSGIGHLMSTINALKA
FEFSEQIGQSLVVHEPIGVVALITPWNWPLNQIVAKVAPALAAGNTMVLKPSEEAPGSAA
IFAEIMDKAGVPAGVFNLVQGDGPIVGTALSRHRDVDMVSFTGSTRAGIQVAKNAAETVK
RVHQELGGKSPNVILPGADLSRAVQVGLFSVVMNSGQSCIAPARMLVHESQAAEAAQIAS
GLMKAVETGDPAQEGRHIGPVVNKAQWEKIQGLIRKGMEEGAKLETGGPGRPDGIETGYF
VKPTLFSGVRNDMTIAREEIFGPVITIIPYRDEEEAVRIANDTDYGLSAVLFGSPEEVKR
VAPRLRAGMVYINGGQPDPSLPFGGYKQSGNGREHGKFGLAEFMEVKAMVGALA
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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