SitesBLAST
Comparing N515DRAFT_4224 FitnessBrowser__Dyella79:N515DRAFT_4224 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)
Q70DU8 Aldehyde dehydrogenase family 3 member H1; AtALDH4; Ath-ALDH4; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
37% identity, 94% coverage: 16:443/456 of query aligns to 34:459/484 of Q70DU8
- C45 (≠ I27) mutation to S: Decreased solubility, loss of dimerization and strongly decreased activity.
- E149 (= E132) 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 (≠ A161) 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 (≠ V183) 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 (≠ F229) mutation to S: No effect on solubility, but 10% loss of activity.
- C253 (= C235) 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)
37% identity, 94% coverage: 16:443/456 of query aligns to 23:445/485 of P51648
- I45 (= I38) to F: in SLS; severe loss of activity
- V64 (≠ S58) to D: in SLS; severe loss of activity; dbSNP:rs72547556
- L106 (≠ G100) to R: in SLS; severe loss of activity; dbSNP:rs72547558
- N112 (= N106) mutation to A: Loss of enzyme activity.
- P114 (= P108) to L: in SLS; severe loss of activity; dbSNP:rs72547559
- P121 (= P115) to L: in SLS; severe loss of activity; dbSNP:rs72547560
- T184 (= T178) to M: in SLS; severe loss of activity; dbSNP:rs72547562; to R: in SLS; severe loss of activity
- G185 (= G179) to A: in SLS; severe loss of activity; dbSNP:rs72547563
- E207 (= E201) active site; mutation to Q: Loss of enzyme activity.
- C214 (≠ A208) to Y: in SLS; 4% of activity; dbSNP:rs72547564
- R228 (= R222) to C: in SLS; severe loss of activity; dbSNP:rs72547566
- C237 (≠ A231) to Y: in SLS; severe loss of activity; dbSNP:rs72547567
- C241 (= C235) active site; mutation to S: Loss of enzyme activity.
- D245 (= D239) to N: in SLS; severe loss of activity; dbSNP:rs72547568
- K266 (≠ A260) to N: in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability; dbSNP:rs72547569
- Y279 (= Y272) to N: in SLS; severe loss of activity; dbSNP:rs72547570
- AP 314:315 (≠ TP 314:315) natural variant: AP -> GAKSTVGA (in SLS; 8% of activity)
- P315 (= P315) to S: in SLS; common mutation in Europeans; severe loss of enzymatic activity; dbSNP:rs72547571
- E331 (= E331) mutation to Q: Loss of enzyme activity.
- S365 (≠ E365) to L: in SLS; severe loss of activity; dbSNP:rs72547573
- Y410 (= Y410) mutation to F: Decreased enzyme activity with dodecanal and hexadecanal. No effect on enzyme activity with octanal.
- H411 (= H411) to Y: in SLS; severe loss of activity
- S415 (≠ G415) to N: in SLS; severe loss of activity
- F419 (= F419) to S: in SLS; severe loss of activity; dbSNP:rs72547576
- R423 (≠ K423) 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
8bb8A Crystal structure of human aldehyde dehydrogenase aldh3a1 in complex with octanal (see paper)
38% identity, 92% coverage: 16:436/456 of query aligns to 25:438/447 of 8bb8A
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)
38% identity, 92% coverage: 16:436/456 of query aligns to 26:439/453 of P30838
- S134 (≠ R125) to A: in dbSNP:rs887241
- E210 (= E201) active site
- C244 (= C235) active site; mutation to S: Abolishes activity.
- P329 (≠ A326) to A: in allele ALDH3A1*2; dbSNP:rs2228100
3szbA Crystal structure of human aldh3a1 modified with the beta-elimination product of aldi-1; 1-phenyl- 2-propen-1-one (see paper)
38% identity, 92% coverage: 16:436/456 of query aligns to 25:438/447 of 3szbA
4l2oA Crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
38% identity, 92% coverage: 16:436/456 of query aligns to 25:438/446 of 4l2oA
- active site: N114 (= N106), K137 (= K129), E209 (= E201), C243 (= C235), E333 (= E331), Y412 (= Y410)
- binding 1-[(4-fluorophenyl)sulfonyl]-2-methyl-1H-benzimidazole: E61 (≠ L53), Y65 (≠ P57), Y115 (= Y107), N118 (≠ F110), L119 (= L111), M237 (≠ F229), C243 (= C235), I391 (≠ L389), I394 (= I392), T395 (≠ A393), F401 (= F399), H413 (= H411)
- binding nicotinamide-adenine-dinucleotide: T112 (≠ P104), W113 (= W105), N114 (= N106), L119 (= L111), E140 (= E132), V169 (≠ A161), T186 (= T178), G187 (= G179), S188 (= S180), V191 (= V183), E209 (= E201), L210 (= L202), G211 (= G203), C243 (= C235), H289 (≠ Q280), E333 (= E331), F335 (= F333), F401 (= F399)
4h80A Crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
38% identity, 92% coverage: 16:436/456 of query aligns to 25:438/446 of 4h80A
- active site: N114 (= N106), K137 (= K129), E209 (= E201), C243 (= C235), E333 (= E331), Y412 (= Y410)
- binding N-(4-{[4-(methylsulfonyl)-2-nitrophenyl]amino}phenyl)acetamide: E61 (≠ L53), Y65 (≠ P57), Y115 (= Y107), N118 (≠ F110), W233 (≠ V225), T242 (= T234), C243 (= C235), V244 (≠ I236), I394 (= I392), T395 (≠ A393), F401 (= F399)
4l1oB Crystal structure of human aldh3a1 with inhibitor 1-{[4-(1,3- benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-1h-indole-2,3-dione
38% identity, 92% coverage: 16:436/456 of query aligns to 25:438/452 of 4l1oB
- active site: N114 (= N106), K137 (= K129), E209 (= E201), C243 (= C235), E333 (= E331), Y412 (= Y410)
- binding (3S)-1-{[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-3-hydroxy-1,3-dihydro-2H-indol-2-one: Y115 (= Y107), N118 (≠ F110), L119 (= L111), E209 (= E201), T242 (= T234), C243 (= C235), I391 (≠ L389), I394 (= I392), F401 (= F399), H413 (= H411)
J3QMK6 Aldehyde dehydrogenase family 3 member B3; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
36% identity, 95% coverage: 16:449/456 of query aligns to 39:467/479 of J3QMK6
- RR 462:463 (≠ RF 444:445) mutation to AA: Reduces membrane localization.
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, 100% coverage: 1:454/456 of query aligns to 11:459/468 of P43353
Sites not aligning to the query:
- 463 modified: S-palmitoyl cysteine
- 465 modified: S-geranylgeranyl cysteine
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)
35% identity, 100% coverage: 1:454/456 of query aligns to 11:459/468 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.
E9Q3E1 Aldehyde dehydrogenase family 3 member B2; Aldehyde dehydrogenase 8; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
36% identity, 95% coverage: 16:450/456 of query aligns to 39:468/479 of E9Q3E1
- W462 (≠ R444) 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.
Q8W033 Aldehyde dehydrogenase family 3 member I1, chloroplastic; AtALDH3; Ath-ALDH3; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
35% identity, 97% coverage: 12:453/456 of query aligns to 93:532/550 of Q8W033
- C114 (≠ E33) mutation to S: No effect on solubility, but loss of dimerization and 80% loss of activity.
- C142 (≠ I62) mutation to S: No effect on solubility, but decreased activity.
- V263 (= V183) mutation to I: No effect on substrate specificity, but decreased affinity for NADP(+) and increased affinity for NAD(+).
- C286 (≠ S206) mutation to S: No effect on solubility, but no effect on activity.
- C310 (≠ F229) mutation to S: No effect on solubility, but no effect on activity.
- C316 (= C235) mutation to S: No effect on solubility, but loss of activity.
1ad3A Class 3 aldehyde dehydrogenase complex with nicotinamide-adenine- dinucleotide (see paper)
38% identity, 91% coverage: 16:432/456 of query aligns to 24:433/446 of 1ad3A
- active site: N113 (= N106), K136 (= K129), E208 (= E201), C242 (= C235), E332 (= E331), Y411 (= Y410)
- binding nicotinamide-adenine-dinucleotide: A111 (≠ P104), W112 (= W105), N113 (= N106), E139 (= E132), V140 (≠ Y133), V168 (≠ A161), G186 (= G179), V190 (= V183), H288 (≠ Q280), R291 (= R283), E332 (= E331), F334 (= F333)
5ucdA Benzaldehyde dehydrogenase, a class 3 aldehyde dehydrogenase, with bound NADP+ and benzoate adduct (see paper)
36% identity, 90% coverage: 16:425/456 of query aligns to 30:431/435 of 5ucdA
- active site: N119 (= N106), K142 (= K129), E214 (= E201), C248 (= C235), E336 (= E331), Y416 (= Y410)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I115 (= I102), G116 (≠ V103), F118 (≠ W105), N119 (= N106), K142 (= K129), S144 (= S131), E145 (= E132), R174 (≠ A161), F190 (= F177), T191 (= T178), G192 (= G179), S193 (= S180), V196 (= V183), E214 (= E201), L215 (= L202), C248 (= C235), E336 (= E331), F338 (= F333)
5nnoA Structure of tbaldh3 complexed with NAD and an3057 aldehyde (see paper)
35% identity, 94% coverage: 2:428/456 of query aligns to 20:457/484 of 5nnoA
- active site: N123 (= N106), K146 (= K129), E218 (= E201), S254 (≠ C235), E360 (= E331), Y439 (= Y410)
- binding 4-[(1-oxidanyl-3~{H}-2,1-benzoxaborol-5-yl)oxy]benzaldehyde: P74 (= P57), Y124 (= Y107), L127 (≠ F110), T253 (= T234), S254 (≠ C235), G422 (≠ A393)
- binding nicotinamide-adenine-dinucleotide: I119 (= I102), G120 (≠ V103), W122 (= W105), N123 (= N106), L128 (= L111), K146 (= K129), E149 (= E132), V178 (≠ A161), T181 (≠ A164), Y194 (≠ F177), T195 (= T178), G196 (= G179), S197 (= S180), V200 (= V183), E218 (= E201), L219 (= L202), S254 (≠ C235), E360 (= E331), F362 (= F333), F428 (= F399)
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)
30% identity, 100% coverage: 1:455/456 of query aligns to 33:496/532 of Q04458
- S241 (= S206) mutation to L: Causes Q deficiency.
- C273 (= C235) mutation to S: Abolishes catalytic activity.
7radA Crystal structure analysis of aldh1b1
33% identity, 90% coverage: 15:425/456 of query aligns to 76:484/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I102), I159 (≠ V103), P160 (= P104), W161 (= W105), N162 (= N106), M167 (≠ L111), K185 (= K129), E188 (= E132), G218 (≠ A161), G222 (≠ Q165), A223 (= A166), T237 (= T178), G238 (= G179), S239 (= S180), V242 (= V183), E261 (= E201), L262 (= L202), C295 (= C235), E392 (= E331), F394 (= F333)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (= L53), E117 (≠ P57), F163 (≠ Y107), E285 (≠ V225), F289 (= F229), N450 (≠ H391), V452 (≠ A393)
7mjdA Crystal structure analysis of aldh1b1
33% identity, 90% coverage: 15:425/456 of query aligns to 76:484/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I102), I159 (≠ V103), P160 (= P104), W161 (= W105), N162 (= N106), M167 (≠ L111), K185 (= K129), E188 (= E132), G218 (≠ A161), G222 (≠ Q165), F236 (= F177), T237 (= T178), G238 (= G179), S239 (= S180), V242 (= V183), E261 (= E201), L262 (= L202), C295 (= C235), E392 (= E331), F394 (= F333)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ P57), E285 (≠ V225), F289 (= F229), N450 (≠ H391), V452 (≠ A393)
7mjcA Crystal structure analysis of aldh1b1
33% identity, 90% coverage: 15:425/456 of query aligns to 76:484/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I102), I159 (≠ V103), P160 (= P104), W161 (= W105), N162 (= N106), K185 (= K129), E188 (= E132), G218 (≠ A161), G222 (≠ Q165), T237 (= T178), G238 (= G179), S239 (= S180), V242 (= V183), E261 (= E201), L262 (= L202), C295 (= C235), E392 (= E331), F394 (= F333)
Query Sequence
>N515DRAFT_4224 FitnessBrowser__Dyella79:N515DRAFT_4224
MREAHAREPMPAWPERARRLRALNDLIGEHRGEIADAIHQDFGGRPAQETDLLEVFPSLS
AIRHALAHGRRWMKPRRSWPGLLFMPARNEIRPQPLGVVGIIVPWNYPLFLAAGPMVDAL
AAGNRVMVKMSEYTPQFSALFAQLAARYFKPEEVCVVTGDADVAQAFSALPFDHLLFTGS
TAVGRHVMRAASANLTPVTLELGGKSPAIVGPGARFANAVERILVGKLFNAGQTCIAPDY
VLLPRAQVDEFVAAARDVAARLYPQPVRNEQYASIISERQYQRLAALRDDAARDGAKLTL
LGDETDDIQRRRMTPALLTGVSESMAVMQEEIFGPLLPLVPYDDIEQAIAYVAAHPHPLA
LYLFEEDGALVDRVLARTTAGGVTINDTLYHIAQHDLPFGGVGPSGSGGYHGEAGFRTFS
HLKSVFRQARVNGAGLLNPPYGQRFKQMLAIMLKRG
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