SitesBLAST

Comparing WP_024888943.1 NCBI__GCF_000559025.1:WP_024888943.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

J3QMK6 Aldehyde dehydrogenase family 3 member B3; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
40% identity, 92% coverage: 6:440/472 of query aligns to 7:437/479 of J3QMK6

Sites not aligning to the query:

• 462:463 RR→AA: Reduces membrane localization.

E9Q3E1 Aldehyde dehydrogenase family 3 member B2; Aldehyde dehydrogenase 8; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
41% identity, 93% coverage: 20:460/472 of query aligns to 19:459/479 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)
40% identity, 90% coverage: 17:439/472 of query aligns to 1:421/446 of 1ad3A

• active site: N113 (= N129), K136 (= K152), E208 (= E224), C242 (= C258), E332 (= E350), Y411 (≠ L429)
• binding nicotinamide-adenine-dinucleotide: A111 (≠ P127), W112 (= W128), N113 (= N129), E139 (= E155), V140 (≠ H156), V168 (vs. gap), G186 (= G202), V190 (= V206), H288 (≠ E302), R291 (= R305), E332 (= E350), F334 (= F352)

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)
38% identity, 94% coverage: 15:460/472 of query aligns to 1:446/468 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.

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)
39% identity, 92% coverage: 24:459/472 of query aligns to 7:442/485 of P51648

• I45 (= I61) to F: in SLS; severe loss of activity
• V64 (≠ A81) to D: in SLS; severe loss of activity; dbSNP:rs72547556
• L106 (≠ G123) to R: in SLS; severe loss of activity; dbSNP:rs72547558
• N112 (= N129) mutation to A: Loss of enzyme activity.
• P114 (= P131) to L: in SLS; severe loss of activity; dbSNP:rs72547559
• P121 (= P138) to L: in SLS; severe loss of activity; dbSNP:rs72547560
• T184 (= T201) to M: in SLS; severe loss of activity; dbSNP:rs72547562; to R: in SLS; severe loss of activity
• G185 (= G202) to A: in SLS; severe loss of activity; dbSNP:rs72547563
• E207 (= E224) active site; mutation to Q: Loss of enzyme activity.
• C214 (≠ A231) to Y: in SLS; 4% of activity; dbSNP:rs72547564
• R228 (= R245) to C: in SLS; severe loss of activity; dbSNP:rs72547566
• C237 (≠ A254) to Y: in SLS; severe loss of activity; dbSNP:rs72547567
• C241 (= C258) active site; mutation to S: Loss of enzyme activity.
• D245 (= D262) to N: in SLS; severe loss of activity; dbSNP:rs72547568
• K266 (≠ E283) to N: in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability; dbSNP:rs72547569
• Y279 (= Y294) to N: in SLS; severe loss of activity; dbSNP:rs72547570
• AP 314:315 (≠ PP 333:334) natural variant: AP -> GAKSTVGA (in SLS; 8% of activity)
• P315 (= P334) to S: in SLS; common mutation in Europeans; severe loss of enzymatic activity; dbSNP:rs72547571
• E331 (= E350) mutation to Q: Loss of enzyme activity.
• S365 (= S384) to L: in SLS; severe loss of activity; dbSNP:rs72547573
• Y410 (≠ L429) mutation to F: Decreased enzyme activity with dodecanal and hexadecanal. No effect on enzyme activity with octanal.
• H411 (= H430) to Y: in SLS; severe loss of activity
• S415 (≠ G434) to N: in SLS; severe loss of activity
• F419 (≠ L438) to S: in SLS; severe loss of activity; dbSNP:rs72547576
• R423 (≠ L442) 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

Q70DU8 Aldehyde dehydrogenase family 3 member H1; AtALDH4; Ath-ALDH4; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
39% identity, 93% coverage: 35:471/472 of query aligns to 30:469/484 of Q70DU8

• C45 (≠ L50) mutation to S: Decreased solubility, loss of dimerization and strongly decreased activity.
• E149 (= E155) 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 (≠ P184) 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 (≠ V206) 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 (≠ F252) mutation to S: No effect on solubility, but 10% loss of activity.
• C253 (= C258) mutation to S: No effect on solubility, but loss of activity.

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)
41% identity, 90% coverage: 15:439/472 of query aligns to 1:423/468 of P43353

Sites not aligning to the query:

• 463 modified: S-palmitoyl cysteine
• 465 modified: S-geranylgeranyl cysteine

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)
40% identity, 86% coverage: 36:439/472 of query aligns to 23:423/453 of P30838

• S134 (≠ H148) to A: in dbSNP:rs887241
• E210 (= E224) active site
• C244 (= C258) active site; mutation to S: Abolishes activity.
• P329 (≠ A345) to A: in allele ALDH3A1*2; dbSNP:rs2228100

8bb8A Crystal structure of human aldehyde dehydrogenase aldh3a1 in complex with octanal (see paper)
40% identity, 86% coverage: 36:439/472 of query aligns to 22:422/447 of 8bb8A

• binding octanal: Y65 (≠ T80), Y115 (= Y130), N118 (≠ V133), C243 (= C258), I394 (≠ F411), T395 (≠ A412), H413 (= H430)

4l2oA Crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
40% identity, 86% coverage: 36:439/472 of query aligns to 22:422/446 of 4l2oA

• active site: N114 (= N129), K137 (= K152), E209 (= E224), C243 (= C258), E333 (= E350), Y412 (≠ L429)
• binding 1-[(4-fluorophenyl)sulfonyl]-2-methyl-1H-benzimidazole: E61 (≠ A76), Y65 (≠ T80), Y115 (= Y130), N118 (≠ V133), L119 (= L134), M237 (≠ F252), C243 (= C258), I391 (≠ L408), I394 (≠ F411), T395 (≠ A412), F401 (= F418), H413 (= H430)
• binding nicotinamide-adenine-dinucleotide: T112 (≠ P127), W113 (= W128), N114 (= N129), L119 (= L134), E140 (= E155), V169 (vs. gap), T186 (= T201), G187 (= G202), S188 (= S203), V191 (= V206), E209 (= E224), L210 (= L225), G211 (= G226), C243 (= C258), H289 (≠ E302), E333 (= E350), F335 (= F352), F401 (= F418)

4h80A Crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
40% identity, 86% coverage: 36:439/472 of query aligns to 22:422/446 of 4h80A