SitesBLAST
Comparing WP_083529425.1 NCBI__GCF_001482365.1:WP_083529425.1 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)
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)
47% identity, 87% coverage: 44:485/506 of query aligns to 2:445/453 of P30838
- S134 (≠ T174) to A: in dbSNP:rs887241
- E210 (= E249) active site
- C244 (= C283) active site; mutation to S: Abolishes activity.
- P329 (= P370) to A: in allele ALDH3A1*2; dbSNP:rs2228100
8bb8A Crystal structure of human aldehyde dehydrogenase aldh3a1 in complex with octanal (see paper)
47% identity, 87% coverage: 44:485/506 of query aligns to 1:444/447 of 8bb8A
4l1oB Crystal structure of human aldh3a1 with inhibitor 1-{[4-(1,3- benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-1h-indole-2,3-dione (see paper)
47% identity, 87% coverage: 44:485/506 of query aligns to 1:444/452 of 4l1oB
- active site: N114 (= N155), K137 (= K178), E209 (= E249), C243 (= C283), E333 (= E375), Y412 (= Y454)
- binding (3S)-1-{[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-3-hydroxy-1,3-dihydro-2H-indol-2-one: Y115 (= Y156), N118 (≠ Q159), L119 (= L160), E209 (= E249), T242 (= T282), C243 (= C283), I391 (≠ L433), I394 (≠ L436), F401 (= F443), H413 (= H455)
3szbA Crystal structure of human aldh3a1 modified with the beta-elimination product of aldi-1; 1-phenyl- 2-propen-1-one (see paper)
47% identity, 87% coverage: 44:485/506 of query aligns to 1:444/447 of 3szbA
4l2oA Crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
47% identity, 87% coverage: 44:485/506 of query aligns to 1:444/446 of 4l2oA
- active site: N114 (= N155), K137 (= K178), E209 (= E249), C243 (= C283), E333 (= E375), Y412 (= Y454)
- binding 1-[(4-fluorophenyl)sulfonyl]-2-methyl-1H-benzimidazole: E61 (≠ T102), Y65 (≠ F106), Y115 (= Y156), N118 (≠ Q159), L119 (= L160), M237 (≠ L277), C243 (= C283), I391 (≠ L433), I394 (≠ L436), T395 (≠ S437), F401 (= F443), H413 (= H455)
- binding nicotinamide-adenine-dinucleotide: T112 (≠ P153), W113 (= W154), N114 (= N155), L119 (= L160), E140 (= E181), V169 (= V209), T186 (= T226), G187 (= G227), S188 (≠ N228), V191 (= V231), E209 (= E249), L210 (= L250), G211 (= G251), C243 (= C283), H289 (= H329), E333 (= E375), F335 (= F377), F401 (= F443)
4h80A Crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
47% identity, 87% coverage: 44:485/506 of query aligns to 1:444/446 of 4h80A
- active site: N114 (= N155), K137 (= K178), E209 (= E249), C243 (= C283), E333 (= E375), Y412 (= Y454)
- binding N-(4-{[4-(methylsulfonyl)-2-nitrophenyl]amino}phenyl)acetamide: E61 (≠ T102), Y65 (≠ F106), Y115 (= Y156), N118 (≠ Q159), W233 (= W273), T242 (= T282), C243 (= C283), V244 (= V284), I394 (≠ L436), T395 (≠ S437), F401 (= F443)
1ad3A Class 3 aldehyde dehydrogenase complex with nicotinamide-adenine- dinucleotide (see paper)
46% identity, 85% coverage: 45:472/506 of query aligns to 1:429/446 of 1ad3A
- active site: N113 (= N155), K136 (= K178), E208 (= E249), C242 (= C283), E332 (= E375), Y411 (= Y454)
- binding nicotinamide-adenine-dinucleotide: A111 (≠ P153), W112 (= W154), N113 (= N155), E139 (= E181), V140 (= V182), V168 (= V209), G186 (= G227), V190 (= V231), H288 (= H329), R291 (= R332), E332 (= E375), F334 (= F377)
E9Q3E1 Aldehyde dehydrogenase family 3 member B2; Aldh3B2; Aldehyde dehydrogenase 8; Long-chain fatty aldehyde dehydrogenase; EC 1.2.1.3; EC 1.2.1.48 from Mus musculus (Mouse) (see paper)
46% identity, 87% coverage: 64:503/506 of query aligns to 37:476/479 of E9Q3E1
- W462 (≠ L489) mutation to A: Reduces lipid droplet localization.
- W469 (≠ A496) mutation to A: Reduces lipid droplet localization.
- C476 (≠ A503) mutation to S: Reduces lipid droplet localization.
Q80VQ0 Aldehyde dehydrogenase family 3 member B1; Aldehyde dehydrogenase 7; Long-chain fatty aldehyde dehydrogenase; Medium-chain fatty aldehyde dehydrogenase; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7; EC 1.2.1.48 from Mus musculus (Mouse) (see paper)
46% identity, 85% coverage: 64:495/506 of query aligns to 24:457/468 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)
44% identity, 87% coverage: 46:485/506 of query aligns to 1:442/485 of P51648
- I45 (≠ L88) to F: in SLS; severe loss of activity
- V64 (≠ T107) to D: in SLS; severe loss of activity; dbSNP:rs72547556
- L106 (= L149) to R: in SLS; severe loss of activity; dbSNP:rs72547558
- N112 (= N155) mutation to A: Loss of enzyme activity.
- P114 (= P157) to L: in SLS; severe loss of activity; dbSNP:rs72547559
- P121 (= P164) to L: in SLS; severe loss of activity; dbSNP:rs72547560
- T184 (= T226) to M: in SLS; severe loss of activity; dbSNP:rs72547562; to R: in SLS; severe loss of activity
- G185 (= G227) to A: in SLS; severe loss of activity; dbSNP:rs72547563
- E207 (= E249) active site; mutation to Q: Loss of enzyme activity.
- C214 (≠ A256) to Y: in SLS; 4% of activity; dbSNP:rs72547564
- R228 (= R270) to C: in SLS; severe loss of activity; dbSNP:rs72547566
- C237 (≠ A279) to Y: in SLS; severe loss of activity; dbSNP:rs72547567
- C241 (= C283) active site; mutation to S: Loss of enzyme activity.
- D245 (= D287) to N: in SLS; severe loss of activity; dbSNP:rs72547568
- K266 (≠ R308) to N: in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability; dbSNP:rs72547569
- Y279 (= Y321) to N: in SLS; severe loss of activity; dbSNP:rs72547570
- AP 314:315 (= AP 359:360) natural variant: AP -> GAKSTVGA (in SLS; 8% of activity)
- P315 (= P360) to S: in SLS; common mutation in Europeans; severe loss of enzymatic activity; dbSNP:rs72547571
- E331 (= E375) mutation to Q: Loss of enzyme activity.
- S365 (= S409) to L: in SLS; severe loss of activity; dbSNP:rs72547573
- Y410 (= Y454) mutation to F: Decreased enzyme activity with dodecanal and hexadecanal. No effect on enzyme activity with octanal.
- H411 (= H455) to Y: in SLS; severe loss of activity
- S415 (= S459) to N: in SLS; severe loss of activity
- F419 (= F463) to S: in SLS; severe loss of activity; dbSNP:rs72547576
- R423 (= R467) 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
P43353 Aldehyde dehydrogenase family 3 member B1; Aldehyde dehydrogenase 7; Long-chain fatty aldehyde dehydrogenase; Medium-chain fatty aldehyde dehydrogenase; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7; EC 1.2.1.48 from Homo sapiens (Human) (see paper)
46% identity, 86% coverage: 64:498/506 of query aligns to 24:458/468 of P43353