SitesBLAST
Comparing 6938752 FitnessBrowser__SB2B:6938752 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)
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)
37% identity, 93% coverage: 18:464/479 of query aligns to 1:442/485 of P51648
- I45 (≠ L62) to F: in SLS; severe loss of activity
- V64 (= V82) to D: in SLS; severe loss of activity; dbSNP:rs72547556
- L106 (≠ G124) to R: in SLS; severe loss of activity; dbSNP:rs72547558
- N112 (= N130) mutation to A: Loss of enzyme activity.
- P114 (= P132) to L: in SLS; severe loss of activity; dbSNP:rs72547559
- P121 (= P139) to L: in SLS; severe loss of activity; dbSNP:rs72547560
- T184 (= T202) to M: in SLS; severe loss of activity; dbSNP:rs72547562; to R: in SLS; severe loss of activity
- G185 (= G203) to A: in SLS; severe loss of activity; dbSNP:rs72547563
- E207 (= E225) active site; mutation to Q: Loss of enzyme activity.
- C214 (≠ V232) to Y: in SLS; 4% of activity; dbSNP:rs72547564
- R228 (= R246) to C: in SLS; severe loss of activity; dbSNP:rs72547566
- C237 (≠ A255) to Y: in SLS; severe loss of activity; dbSNP:rs72547567
- C241 (= C259) active site; mutation to S: Loss of enzyme activity.
- D245 (= D263) to N: in SLS; severe loss of activity; dbSNP:rs72547568
- K266 (≠ A284) to N: in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability; dbSNP:rs72547569
- Y279 (= Y296) to N: in SLS; severe loss of activity; dbSNP:rs72547570
- AP 314:315 (≠ LP 337:338) natural variant: AP -> GAKSTVGA (in SLS; 8% of activity)
- P315 (= P338) to S: in SLS; common mutation in Europeans; severe loss of enzymatic activity; dbSNP:rs72547571
- E331 (= E355) mutation to Q: Loss of enzyme activity.
- S365 (= S389) to L: in SLS; severe loss of activity; dbSNP:rs72547573
- Y410 (= Y434) mutation to F: Decreased enzyme activity with dodecanal and hexadecanal. No effect on enzyme activity with octanal.
- H411 (= H435) to Y: in SLS; severe loss of activity
- S415 (≠ G439) to N: in SLS; severe loss of activity
- F419 (= F443) to S: in SLS; severe loss of activity; dbSNP:rs72547576
- R423 (≠ K447) to H: in SLS; severe loss of activity; dbSNP:rs768290318
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.
- 447 K → E: in SLS; severe loss of activity; dbSNP:rs67939114
5ucdA Benzaldehyde dehydrogenase, a class 3 aldehyde dehydrogenase, with bound NADP+ and benzoate adduct (see paper)
37% identity, 91% coverage: 16:449/479 of query aligns to 6:431/435 of 5ucdA
- active site: N119 (= N130), K142 (= K153), E214 (= E225), C248 (= C259), E336 (= E355), Y416 (= Y434)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I115 (= I126), G116 (≠ V127), F118 (≠ W129), N119 (= N130), K142 (= K153), S144 (= S155), E145 (= E156), R174 (≠ A185), F190 (= F201), T191 (= T202), G192 (= G203), S193 (= S204), V196 (= V207), E214 (= E225), L215 (= L226), C248 (= C259), E336 (= E355), F338 (= F357)
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)
36% identity, 94% coverage: 15:464/479 of query aligns to 1:445/453 of P30838
- S134 (= S149) to A: in dbSNP:rs887241
- E210 (= E225) active site
- C244 (= C259) active site; mutation to S: Abolishes activity.
- P329 (≠ L350) to A: in allele ALDH3A1*2; dbSNP:rs2228100
8bb8A Crystal structure of human aldehyde dehydrogenase aldh3a1 in complex with octanal (see paper)
36% identity, 94% coverage: 16:464/479 of query aligns to 1:444/447 of 8bb8A
4l2oA Crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
35% identity, 94% coverage: 16:464/479 of query aligns to 1:444/446 of 4l2oA
- active site: N114 (= N130), K137 (= K153), E209 (= E225), C243 (= C259), E333 (= E355), Y412 (= Y434)
- binding 1-[(4-fluorophenyl)sulfonyl]-2-methyl-1H-benzimidazole: E61 (≠ S77), Y65 (≠ P81), Y115 (≠ F131), N118 (≠ M134), L119 (= L135), M237 (≠ L253), C243 (= C259), I391 (≠ V413), I394 (≠ V416), T395 (≠ A417), F401 (= F423), H413 (= H435)
- binding nicotinamide-adenine-dinucleotide: T112 (≠ P128), W113 (= W129), N114 (= N130), L119 (= L135), E140 (= E156), V169 (≠ A185), T186 (= T202), G187 (= G203), S188 (= S204), V191 (= V207), E209 (= E225), L210 (= L226), G211 (= G227), C243 (= C259), H289 (≠ Q304), E333 (= E355), F335 (= F357), F401 (= F423)
4h80A Crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
35% identity, 94% coverage: 16:464/479 of query aligns to 1:444/446 of 4h80A
- active site: N114 (= N130), K137 (= K153), E209 (= E225), C243 (= C259), E333 (= E355), Y412 (= Y434)
- binding N-(4-{[4-(methylsulfonyl)-2-nitrophenyl]amino}phenyl)acetamide: E61 (≠ S77), Y65 (≠ P81), Y115 (≠ F131), N118 (≠ M134), W233 (≠ Y249), T242 (≠ I258), C243 (= C259), V244 (= V260), I394 (≠ V416), T395 (≠ A417), F401 (= F423)
4l1oB Crystal structure of human aldh3a1 with inhibitor 1-{[4-(1,3- benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-1h-indole-2,3-dione
35% identity, 94% coverage: 16:464/479 of query aligns to 1:444/452 of 4l1oB
- active site: N114 (= N130), K137 (= K153), E209 (= E225), C243 (= C259), E333 (= E355), Y412 (= Y434)
- binding (3S)-1-{[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-3-hydroxy-1,3-dihydro-2H-indol-2-one: Y115 (≠ F131), N118 (≠ M134), L119 (= L135), E209 (= E225), T242 (≠ I258), C243 (= C259), I391 (≠ V413), I394 (≠ V416), F401 (= F423), H413 (= H435)
3szbA Crystal structure of human aldh3a1 modified with the beta-elimination product of aldi-1; 1-phenyl- 2-propen-1-one (see paper)
35% identity, 94% coverage: 16:464/479 of query aligns to 1:444/447 of 3szbA
1ad3A Class 3 aldehyde dehydrogenase complex with nicotinamide-adenine- dinucleotide (see paper)
36% identity, 94% coverage: 17:464/479 of query aligns to 1:443/446 of 1ad3A
- active site: N113 (= N130), K136 (= K153), E208 (= E225), C242 (= C259), E332 (= E355), Y411 (= Y434)
- binding nicotinamide-adenine-dinucleotide: A111 (≠ P128), W112 (= W129), N113 (= N130), E139 (= E156), V140 (≠ F157), V168 (≠ A185), G186 (= G203), V190 (= V207), H288 (≠ Q304), R291 (= R307), E332 (= E355), F334 (= F357)
E9Q3E1 Aldehyde dehydrogenase family 3 member B2; Aldehyde dehydrogenase 8; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
37% identity, 98% coverage: 3:473/479 of query aligns to 2:467/479 of E9Q3E1
- W462 (≠ A468) mutation to A: Reduces lipid droplet localization.
Sites not aligning to the query:
- 469 W→A: Reduces lipid droplet localization.
- 476 C→S: Reduces lipid droplet localization.
Q70DU8 Aldehyde dehydrogenase family 3 member H1; AtALDH4; Ath-ALDH4; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
36% identity, 91% coverage: 40:473/479 of query aligns to 34:465/484 of Q70DU8
- C45 (≠ L51) mutation to S: Decreased solubility, loss of dimerization and strongly decreased activity.
- E149 (= E156) 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 (≠ A185) 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 (≠ V207) 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 (≠ L253) mutation to S: No effect on solubility, but 10% loss of activity.
- C253 (= C259) mutation to S: No effect on solubility, but loss of activity.
J3QMK6 Aldehyde dehydrogenase family 3 member B3; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
37% identity, 95% coverage: 18:473/479 of query aligns to 17:467/479 of J3QMK6
- RR 462:463 (≠ AI 468:469) mutation to 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)
36% identity, 94% coverage: 17:467/479 of query aligns to 3:448/468 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)
38% identity, 93% coverage: 21:464/479 of query aligns to 7:445/468 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)
33% identity, 95% coverage: 12:465/479 of query aligns to 71:520/550 of Q8W033
- C114 (≠ A57) mutation to S: No effect on solubility, but loss of dimerization and 80% loss of activity.
- C142 (≠ I86) mutation to S: No effect on solubility, but decreased activity.
- V263 (= V207) mutation to I: No effect on substrate specificity, but decreased affinity for NADP(+) and increased affinity for NAD(+).
- C286 (≠ S230) mutation to S: No effect on solubility, but no effect on activity.
- C310 (≠ L253) mutation to S: No effect on solubility, but no effect on activity.
- C316 (= C259) mutation to S: No effect on solubility, but loss of activity.
5nnoA Structure of tbaldh3 complexed with NAD and an3057 aldehyde (see paper)
37% identity, 94% coverage: 24:473/479 of query aligns to 18:480/484 of 5nnoA
- active site: N123 (= N130), K146 (= K153), E218 (= E225), S254 (≠ C259), E360 (= E355), Y439 (= Y434)
- binding 4-[(1-oxidanyl-3~{H}-2,1-benzoxaborol-5-yl)oxy]benzaldehyde: P74 (= P81), Y124 (≠ F131), L127 (≠ M134), T253 (≠ I258), S254 (≠ C259), G422 (≠ A417)
- binding nicotinamide-adenine-dinucleotide: I119 (= I126), G120 (≠ V127), W122 (= W129), N123 (= N130), L128 (= L135), K146 (= K153), E149 (= E156), V178 (≠ A185), T181 (≠ A188), Y194 (≠ F201), T195 (= T202), G196 (= G203), S197 (= S204), V200 (= V207), E218 (= E225), L219 (= L226), S254 (≠ C259), E360 (= E355), F362 (= F357), F428 (= F423)
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)
31% identity, 94% coverage: 14:464/479 of query aligns to 19:481/532 of Q04458
- S241 (= S230) mutation to L: Causes Q deficiency.
- C273 (= C259) mutation to S: Abolishes catalytic activity.
7jwwA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
29% identity, 94% coverage: 1:449/479 of query aligns to 34:485/494 of 7jwwA
- active site: N163 (= N130), K186 (= K153), E262 (= E225), C296 (= C259), E393 (= E355), E470 (≠ Y434)
- binding 5-{4-[(Z)-2-hydroxyethenyl]phenyl}-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ P81), T122 (≠ H85), F164 (= F131), M168 (≠ L135), Y290 (≠ L253), C295 (≠ I258), C296 (= C259), I297 (≠ V260), V453 (≠ A417), F459 (= F423)
7jwvA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
29% identity, 94% coverage: 1:449/479 of query aligns to 34:485/494 of 7jwvA
- active site: N163 (= N130), K186 (= K153), E262 (= E225), C296 (= C259), E393 (= E355), E470 (≠ Y434)
- binding 5-[4-(hydroxymethyl)phenyl]-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ P81), T122 (≠ H85), F164 (= F131), M168 (≠ L135), Y290 (≠ L253), C295 (≠ I258), I297 (≠ V260), V453 (≠ A417), F459 (= F423)
7jwuA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
29% identity, 94% coverage: 1:449/479 of query aligns to 34:485/494 of 7jwuA
- active site: N163 (= N130), K186 (= K153), E262 (= E225), C296 (= C259), E393 (= E355), E470 (≠ Y434)
- binding nicotinamide-adenine-dinucleotide: I159 (= I126), I160 (≠ V127), P161 (= P128), W162 (= W129), N163 (= N130), K186 (= K153), E189 (= E156), G219 (≠ A185), G223 (vs. gap), A224 (= A189), F237 (= F201), T238 (= T202), G239 (= G203), S240 (= S204), V243 (= V207), L263 (= L226), C296 (= C259), Q343 (= Q304), K346 (≠ R307), E393 (= E355), F395 (= F357)
- binding 1-methyl-5-phenyl-6-{[(1R)-1-(pyridin-2-yl)ethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: T122 (≠ H85), F164 (= F131), W171 (≠ G138), Y290 (≠ L253), C295 (≠ I258), I297 (≠ V260), V453 (≠ A417), F459 (= F423)
Query Sequence
>6938752 FitnessBrowser__SB2B:6938752
MNAATQMQPTPSGEVAAMQQTFERQRQEFAKHSYPSLSERKNALSLLKLTLLEQQDALIN
ALSRDYGHRSADDSRISDIMPVVNHINYTLSNLKRWAKPSRRHAGILLAPASVNVTYQPK
GVVGIIVPWNFPVMLSLGPLVTAIAAGNSAMLKMSEFTPETNKVIKSLLAKTFAEKKVAV
IEGEADVAAAFSSLPFDHLLFTGSTAVGKHVMRAASANLTPVTLELGGKSPVIVAPDMDM
DTAVERMIYGKCLNAGQICVAPDYVLVPRGKEDAFIKAYQDKFAALYGKVETNKDYGAII
NERQWQRLMQVLDDAKAQGANVHSASGEPPLGTLRKLPTQLLTQVTDEMLVMQDEIFGPL
LPVVPYDSLDEALSYINARPRPLALYLMSFDTATQDKVLSSTHSGGVCINETVFHVAADD
APFGGIGPSGMGHYHGEEGFRTFSHAKTVLKRGRLNTGKLVHPPYGNAIQTLLMKVFLR
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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