SitesBLAST
Comparing 8501918 DvMF_2633 Aldehyde Dehydrogenase (RefSeq) to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
Q70DU8 Aldehyde dehydrogenase family 3 member H1; AtALDH4; Ath-ALDH4; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
34% identity, 95% coverage: 23:458/460 of query aligns to 34:468/484 of Q70DU8
- C45 (≠ V34) mutation to S: Decreased solubility, loss of dimerization and strongly decreased activity.
- E149 (≠ A138) mutation to D: Small effect on NAD(+) interaction, but 40% loss of efficiency. Ability to use NADP(+). 70% loss of efficiency with NAD(+); when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200.; mutation to N: Ability to use NADP(+) and 33% decreased efficiency with NAD(+). 70% loss of efficiency with NAD(+); when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200.; mutation to Q: Loss of specificity for NAD(+) and loss of 25% efficiency. 15% efficiency with NAD(+); when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200.; mutation to T: Loss of specificity and increased NADP(+) binding. Decreased catalytic efficiency. Loss of cofactor specificity and same lower efficiency with both; when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200. Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with R-178 and V-200.
- V178 (≠ A167) mutation to R: Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with T-149 and V-200.
- I200 (≠ G189) mutation to G: Changed coenzyme preference from NAD(+) to NADP(+), but impaired affinities for both cofactors. No effect on the interaction with the substrate. Impaired affinities for both cofactors and decreased catalytic efficiencies; when associated with D-149, Q-149, N-149 or T-149.; mutation to V: Also able to use NADP(+) as coenzyme, but no effect on the interaction with the substrate. 15% efficiency with NAD(+); when associated with Q-149. 70% loss of efficiency with NAD(+); when associated with D-149 or N-149. Loss of cofactor specificity and same lower efficiency with both; when associated with T-149. Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with T-149 and R-178.
- C247 (≠ L235) mutation to S: No effect on solubility, but 10% loss of activity.
- C253 (≠ R241) mutation to S: No effect on solubility, but loss of activity.
P51648 Aldehyde dehydrogenase family 3 member A2; Aldehyde dehydrogenase 10; Fatty aldehyde dehydrogenase; Microsomal aldehyde dehydrogenase; EC 1.2.1.3; EC 1.2.1.94 from Homo sapiens (Human) (see 5 papers)
31% identity, 98% coverage: 8:460/460 of query aligns to 9:461/485 of P51648
- I45 (= I45) to F: in SLS; severe loss of activity
- V64 (= V64) to D: in SLS; severe loss of activity; dbSNP:rs72547556
- L106 (≠ V106) to R: in SLS; severe loss of activity; dbSNP:rs72547558
- N112 (≠ A112) mutation to A: Loss of enzyme activity.
- P114 (= P114) to L: in SLS; severe loss of activity; dbSNP:rs72547559
- P121 (= P121) to L: in SLS; severe loss of activity; dbSNP:rs72547560
- T184 (≠ D184) to M: in SLS; severe loss of activity; dbSNP:rs72547562; to R: in SLS; severe loss of activity
- G185 (= G185) to A: in SLS; severe loss of activity; dbSNP:rs72547563
- E207 (≠ I207) active site; mutation to Q: Loss of enzyme activity.
- C214 (≠ A214) to Y: in SLS; 4% of activity; dbSNP:rs72547564
- R228 (= R228) to C: in SLS; severe loss of activity; dbSNP:rs72547566
- C237 (≠ A237) to Y: in SLS; severe loss of activity; dbSNP:rs72547567
- C241 (≠ R241) active site; mutation to S: Loss of enzyme activity.
- D245 (= D245) to N: in SLS; severe loss of activity; dbSNP:rs72547568
- K266 (≠ E266) to N: in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability; dbSNP:rs72547569
- Y279 (≠ F279) to N: in SLS; severe loss of activity; dbSNP:rs72547570
- AP 314:315 (≠ PP 320:321) natural variant: AP -> GAKSTVGA (in SLS; 8% of activity)
- P315 (= P321) to S: in SLS; common mutation in Europeans; severe loss of enzymatic activity; dbSNP:rs72547571
- E331 (= E337) mutation to Q: Loss of enzyme activity.
- S365 (≠ T371) to L: in SLS; severe loss of activity; dbSNP:rs72547573
- Y410 (≠ M416) mutation to F: Decreased enzyme activity with dodecanal and hexadecanal. No effect on enzyme activity with octanal.
- H411 (≠ A417) to Y: in SLS; severe loss of activity
- S415 (≠ G421) to N: in SLS; severe loss of activity
- F419 (= F425) to S: in SLS; severe loss of activity; dbSNP:rs72547576
- R423 (= R429) to H: in SLS; severe loss of activity; dbSNP:rs768290318
- K447 (= K451) to E: in SLS; severe loss of activity; dbSNP:rs67939114
Sites not aligning to the query:
- 445:485 mutation Missing: Decreased enzyme activity with dodecanal. Strongly decreased enzyme activity with hexadecanal. No effect on enzyme activity with octanal.
4l2oA Crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
33% identity, 93% coverage: 7:433/460 of query aligns to 9:429/446 of 4l2oA
- active site: N114 (≠ A112), K137 (≠ R135), E209 (≠ I207), C243 (≠ R241), E333 (= E337), Y412 (≠ M416)
- binding 1-[(4-fluorophenyl)sulfonyl]-2-methyl-1H-benzimidazole: E61 (≠ R59), Y65 (≠ P63), Y115 (≠ D113), N118 (≠ R116), L119 (≠ S117), M237 (≠ L235), C243 (≠ R241), I391 (≠ A395), I394 (≠ L398), T395 (≠ A399), F401 (≠ Q405), H413 (≠ A417)
- binding nicotinamide-adenine-dinucleotide: T112 (≠ H110), W113 (= W111), N114 (≠ A112), L119 (≠ S117), E140 (≠ A138), V169 (≠ A167), T186 (≠ D184), G187 (= G185), S188 (≠ D186), V191 (≠ G189), E209 (≠ I207), L210 (≠ T208), G211 (= G209), C243 (≠ R241), H289 (≠ G287), E333 (= E337), F335 (= F339), F401 (≠ Q405)
4h80A Crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
33% identity, 93% coverage: 7:433/460 of query aligns to 9:429/446 of 4h80A
- active site: N114 (≠ A112), K137 (≠ R135), E209 (≠ I207), C243 (≠ R241), E333 (= E337), Y412 (≠ M416)
- binding N-(4-{[4-(methylsulfonyl)-2-nitrophenyl]amino}phenyl)acetamide: E61 (≠ R59), Y65 (≠ P63), Y115 (≠ D113), N118 (≠ R116), W233 (= W231), T242 (≠ L240), C243 (≠ R241), V244 (≠ A242), I394 (≠ L398), T395 (≠ A399), F401 (≠ Q405)
3szbA Crystal structure of human aldh3a1 modified with the beta-elimination product of aldi-1; 1-phenyl- 2-propen-1-one (see paper)
33% identity, 93% coverage: 7:433/460 of query aligns to 9:429/447 of 3szbA
4l1oB Crystal structure of human aldh3a1 with inhibitor 1-{[4-(1,3- benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-1h-indole-2,3-dione
33% identity, 93% coverage: 7:433/460 of query aligns to 9:429/452 of 4l1oB
- active site: N114 (≠ A112), K137 (≠ R135), E209 (≠ I207), C243 (≠ R241), E333 (= E337), Y412 (≠ M416)
- binding (3S)-1-{[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-3-hydroxy-1,3-dihydro-2H-indol-2-one: Y115 (≠ D113), N118 (≠ R116), L119 (≠ S117), E209 (≠ I207), T242 (≠ L240), C243 (≠ R241), I391 (≠ A395), I394 (≠ L398), F401 (≠ Q405), H413 (≠ A417)
P30838 Aldehyde dehydrogenase, dimeric NADP-preferring; ALDHIII; Aldehyde dehydrogenase 3; Aldehyde dehydrogenase family 3 member A1; EC 1.2.1.5 from Homo sapiens (Human) (see 4 papers)
33% identity, 93% coverage: 7:433/460 of query aligns to 10:430/453 of P30838
- S134 (≠ A131) to A: in dbSNP:rs887241
- E210 (≠ I207) active site
- C244 (≠ R241) active site; mutation to S: Abolishes activity.
- P329 (= P332) to A: in allele ALDH3A1*2; dbSNP:rs2228100
8bb8A Crystal structure of human aldehyde dehydrogenase aldh3a1 in complex with octanal (see paper)
33% identity, 93% coverage: 7:433/460 of query aligns to 9:429/447 of 8bb8A
E9Q3E1 Aldehyde dehydrogenase family 3 member B2; Aldehyde dehydrogenase 8; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
32% identity, 94% coverage: 2:435/460 of query aligns to 19:445/479 of E9Q3E1
Sites not aligning to the query:
- 462 W→A: Reduces lipid droplet localization.
- 469 W→A: Reduces lipid droplet localization.
- 476 C→S: Reduces lipid droplet localization.
1ad3A Class 3 aldehyde dehydrogenase complex with nicotinamide-adenine- dinucleotide (see paper)
31% identity, 93% coverage: 7:435/460 of query aligns to 8:430/446 of 1ad3A
- active site: N113 (≠ A112), K136 (≠ R135), E208 (≠ I207), C242 (≠ R241), E332 (= E337), Y411 (≠ M416)
- binding nicotinamide-adenine-dinucleotide: A111 (≠ H110), W112 (= W111), N113 (≠ A112), E139 (≠ A138), V140 (≠ E139), V168 (≠ A167), G186 (= G185), V190 (≠ G189), H288 (≠ G287), R291 (= R290), E332 (= E337), F334 (= F339)
J3QMK6 Aldehyde dehydrogenase family 3 member B3; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
30% identity, 93% coverage: 7:435/460 of query aligns to 23:445/479 of J3QMK6
Sites not aligning to the query:
- 462:463 RR→AA: Reduces membrane localization.
Q80VQ0 Aldehyde dehydrogenase family 3 member B1; Aldehyde dehydrogenase 7; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7 from Mus musculus (Mouse) (see paper)
30% identity, 94% coverage: 23:455/460 of query aligns to 26:454/468 of Q80VQ0
Sites not aligning to the query:
- 462 modified: S-palmitoyl cysteine; C→S: Reduces palmitoylation.
- 462:463 CC→SS: Abolishes palmitoylation.
- 463 modified: S-palmitoyl cysteine; C→S: Reduces palmitoylation.
P43353 Aldehyde dehydrogenase family 3 member B1; Aldehyde dehydrogenase 7; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7 from Homo sapiens (Human) (see paper)
31% identity, 96% coverage: 14:455/460 of query aligns to 17:454/468 of P43353
Sites not aligning to the query:
- 463 modified: S-palmitoyl cysteine
- 465 modified: S-geranylgeranyl cysteine
Q8W033 Aldehyde dehydrogenase family 3 member I1, chloroplastic; AtALDH3; Ath-ALDH3; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 95% coverage: 23:458/460 of query aligns to 97:531/550 of Q8W033
- C114 (≠ R40) mutation to S: No effect on solubility, but loss of dimerization and 80% loss of activity.
- C142 (≠ I68) mutation to S: No effect on solubility, but decreased activity.
- V263 (≠ G189) mutation to I: No effect on substrate specificity, but decreased affinity for NADP(+) and increased affinity for NAD(+).
- C286 (≠ S212) mutation to S: No effect on solubility, but no effect on activity.
- C310 (≠ L235) mutation to S: No effect on solubility, but no effect on activity.
- C316 (≠ R241) mutation to S: No effect on solubility, but loss of activity.
5ucdA Benzaldehyde dehydrogenase, a class 3 aldehyde dehydrogenase, with bound NADP+ and benzoate adduct (see paper)
28% identity, 94% coverage: 1:433/460 of query aligns to 8:433/435 of 5ucdA
- active site: N119 (≠ A112), K142 (≠ R135), E214 (≠ I207), C248 (≠ R241), E336 (= E337), Y416 (≠ M416)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I115 (≠ Y108), G116 (≠ A109), F118 (≠ W111), N119 (≠ A112), K142 (≠ R135), S144 (= S137), E145 (≠ A138), R174 (≠ A167), F190 (≠ Y183), T191 (≠ D184), G192 (= G185), S193 (≠ D186), V196 (≠ G189), E214 (≠ I207), L215 (≠ T208), C248 (≠ R241), E336 (= E337), F338 (= F339)
5nnoA Structure of tbaldh3 complexed with NAD and an3057 aldehyde (see paper)
31% identity, 95% coverage: 23:458/460 of query aligns to 34:483/484 of 5nnoA
- active site: N123 (≠ A112), K146 (≠ R135), E218 (≠ I207), S254 (≠ R241), E360 (= E337), Y439 (≠ M416)
- binding 4-[(1-oxidanyl-3~{H}-2,1-benzoxaborol-5-yl)oxy]benzaldehyde: P74 (= P63), Y124 (≠ D113), L127 (≠ R116), T253 (≠ L240), S254 (≠ R241), G422 (≠ A399)
- binding nicotinamide-adenine-dinucleotide: I119 (≠ Y108), G120 (≠ A109), W122 (= W111), N123 (≠ A112), L128 (≠ S117), K146 (≠ R135), E149 (≠ A138), V178 (≠ A167), T181 (≠ D170), Y194 (= Y183), T195 (≠ D184), G196 (= G185), S197 (≠ D186), V200 (≠ G189), E218 (≠ I207), L219 (≠ T208), S254 (≠ R241), E360 (= E337), F362 (= F339), F428 (≠ Q405)
Q04458 Fatty aldehyde dehydrogenase HFD1; Hexadecenal dehydrogenase; EC 1.2.1.3; EC 1.2.1.64 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
27% identity, 93% coverage: 27:456/460 of query aligns to 53:491/532 of Q04458
- S241 (= S212) mutation to L: Causes Q deficiency.
- C273 (≠ R241) mutation to S: Abolishes catalytic activity.
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
29% identity, 73% coverage: 94:430/460 of query aligns to 136:474/483 of 3b4wA
- active site: N154 (≠ A112), K177 (≠ R135), E251 (≠ I207), C285 (≠ R241), E384 (= E337), E460 (≠ M416)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ Y108), V151 (≠ A109), W153 (= W111), N154 (≠ A112), K177 (≠ R135), I210 (≠ A167), G213 (≠ D170), T228 (≠ D184), G229 (= G185), S230 (≠ D186), V233 (≠ G189), E236 (≠ T192), E251 (≠ I207), L252 (≠ T208), C285 (≠ R241), E384 (= E337), F386 (= F339)
4ou2A A 2.15 angstroms x-ray crystal structure of e268a 2-aminomuconate 6- semialdehyde dehydrogenase catalytic intermediate from pseudomonas fluorescens (see paper)
24% identity, 92% coverage: 3:426/460 of query aligns to 43:474/483 of 4ou2A
- active site: N152 (≠ A112), K175 (≠ R135), A251 (≠ I207), C285 (≠ R241), E387 (= E337), E464 (≠ M416)
- binding (2Z,4E)-2,6-dihydroxyhexa-2,4-dienoic acid: R103 (≠ P63), L157 (≠ S117), C285 (≠ R241), Y445 (≠ H397), R447 (≠ A399), F453 (≠ Q405)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ Y108), S149 (≠ A109), P150 (≠ H110), W151 (= W111), N152 (≠ A112), K175 (≠ R135), G208 (= G166), G213 (≠ E171), E214 (≠ A172), F227 (≠ Y183), T228 (≠ D184), G229 (= G185), E230 (≠ D186), T233 (≠ G189), A251 (≠ I207), L252 (≠ T208), G253 (= G209), C285 (≠ R241), E387 (= E337), F389 (= F339)
4npiA 1.94 angstroms x-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
24% identity, 92% coverage: 3:426/460 of query aligns to 43:474/483 of 4npiA
- active site: N152 (≠ A112), K175 (≠ R135), E251 (≠ I207), C285 (≠ R241), E387 (= E337), E464 (≠ M416)
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (≠ P63), L157 (≠ S117), W160 (≠ V120), E251 (≠ I207), C285 (≠ R241), Y445 (≠ H397), R447 (≠ A399), F453 (≠ Q405)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ Y108), S149 (≠ A109), P150 (≠ H110), W151 (= W111), K175 (≠ R135), E178 (≠ A138), G208 (= G166), G213 (≠ E171), E214 (≠ A172), F227 (≠ Y183), G229 (= G185), E230 (≠ D186), T233 (≠ G189), G253 (= G209), C285 (≠ R241), K335 (≠ R290), E387 (= E337), F389 (= F339)
Query Sequence
>8501918 DvMF_2633 Aldehyde Dehydrogenase (RefSeq)
MAALAARQKAFIASGAVLPSGARVDALRRLREGVQGYRDRLADAIRADYGRPEHPFLVRE
VVPVLHEIDWLIKAVPGFCGGRRVLPSLGQFKARSYVRRQPLGRVVAYAHWADPFRSLLV
PLADAIGAGNAVVLRPSAEAPATAEMVTRMVRQYFEPEHVAVVGGGAETDEALLATAPDF
VWYDGDARGARTIAVLAAPTLTPYAAITGGPSAALVHGDADMAMAARRIVWAKFLHAGQL
RAAPDVLLVQRTVLDRVLDALRTELERAFGPQPRTSADFGRMVSAAGFARQAERLAIGRA
LPFGPGDAANQPDRASLYVPPTLLTDVPDDSPVLREEGFGPVLVVRPYTRLDEATAFLAG
LPALTALYAFTTAHARGERLMENTRAGAVLINDAATHLANPRLPQGGVGETGHGAMAGPA
GLATFSAPRATAVGSNFFDIPLRFAPGSDLKLKVLKRLYK
Or try a new SitesBLAST search
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