SitesBLAST
Comparing Synpcc7942_0489 FitnessBrowser__SynE:Synpcc7942_0489 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)
49% identity, 96% coverage: 10:448/459 of query aligns to 5:445/453 of P30838
- S134 (≠ C139) to A: in dbSNP:rs887241
- E210 (= E215) active site
- C244 (= C249) active site; mutation to S: Abolishes activity.
- P329 (= P334) to A: in allele ALDH3A1*2; dbSNP:rs2228100
4l2oA Crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
49% identity, 96% coverage: 10:448/459 of query aligns to 4:444/446 of 4l2oA
- active site: N114 (= N120), K137 (= K143), E209 (= E215), C243 (= C249), E333 (= E339), Y412 (= Y418)
- binding 1-[(4-fluorophenyl)sulfonyl]-2-methyl-1H-benzimidazole: E61 (≠ S67), Y65 (≠ F71), Y115 (= Y121), N118 (≠ Q124), L119 (= L125), M237 (≠ F243), C243 (= C249), I391 (= I397), I394 (≠ V400), T395 (≠ G401), F401 (= F407), H413 (= H419)
- binding nicotinamide-adenine-dinucleotide: T112 (≠ P118), W113 (= W119), N114 (= N120), L119 (= L125), E140 (= E146), V169 (≠ A175), T186 (= T192), G187 (= G193), S188 (≠ G194), V191 (≠ I197), E209 (= E215), L210 (= L216), G211 (= G217), C243 (= C249), H289 (= H295), E333 (= E339), F335 (= F341), F401 (= F407)
4h80A Crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
49% identity, 96% coverage: 10:448/459 of query aligns to 4:444/446 of 4h80A
- active site: N114 (= N120), K137 (= K143), E209 (= E215), C243 (= C249), E333 (= E339), Y412 (= Y418)
- binding N-(4-{[4-(methylsulfonyl)-2-nitrophenyl]amino}phenyl)acetamide: E61 (≠ S67), Y65 (≠ F71), Y115 (= Y121), N118 (≠ Q124), W233 (= W239), T242 (= T248), C243 (= C249), V244 (≠ I250), I394 (≠ V400), T395 (≠ G401), F401 (= F407)
3szbA Crystal structure of human aldh3a1 modified with the beta-elimination product of aldi-1; 1-phenyl- 2-propen-1-one (see paper)
49% identity, 96% coverage: 10:448/459 of query aligns to 4:444/447 of 3szbA
8bb8A Crystal structure of human aldehyde dehydrogenase aldh3a1 in complex with octanal (see paper)
49% identity, 96% coverage: 10:448/459 of query aligns to 4:444/447 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)
49% identity, 96% coverage: 10:448/459 of query aligns to 4:444/452 of 4l1oB
- active site: N114 (= N120), K137 (= K143), E209 (= E215), C243 (= C249), E333 (= E339), Y412 (= Y418)
- binding (3S)-1-{[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-3-hydroxy-1,3-dihydro-2H-indol-2-one: Y115 (= Y121), N118 (≠ Q124), L119 (= L125), E209 (= E215), T242 (= T248), C243 (= C249), I391 (= I397), I394 (≠ V400), F401 (= F407), H413 (= H419)
1ad3A Class 3 aldehyde dehydrogenase complex with nicotinamide-adenine- dinucleotide (see paper)
48% identity, 96% coverage: 10:448/459 of query aligns to 3:443/446 of 1ad3A
- active site: N113 (= N120), K136 (= K143), E208 (= E215), C242 (= C249), E332 (= E339), Y411 (= Y418)
- binding nicotinamide-adenine-dinucleotide: A111 (≠ P118), W112 (= W119), N113 (= N120), E139 (= E146), V140 (≠ L147), V168 (≠ A175), G186 (= G193), V190 (≠ I197), H288 (= H295), R291 (= R298), E332 (= E339), F334 (= F341)
Q70DU8 Aldehyde dehydrogenase family 3 member H1; AtALDH4; Ath-ALDH4; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
48% identity, 98% coverage: 9:459/459 of query aligns to 12:468/484 of Q70DU8
- C45 (≠ V42) mutation to S: Decreased solubility, loss of dimerization and strongly decreased activity.
- E149 (= E146) 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 (≠ A175) 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 (= I197) 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 (≠ F243) mutation to S: No effect on solubility, but 10% loss of activity.
- C253 (= C249) mutation to S: No effect on solubility, but loss of activity.
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)
47% identity, 96% coverage: 11:452/459 of query aligns to 6:449/468 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)
46% identity, 94% coverage: 16:448/459 of query aligns to 8:442/485 of P51648
- I45 (≠ L53) to F: in SLS; severe loss of activity
- V64 (= V72) to D: in SLS; severe loss of activity; dbSNP:rs72547556
- L106 (= L114) to R: in SLS; severe loss of activity; dbSNP:rs72547558
- N112 (= N120) mutation to A: Loss of enzyme activity.
- P114 (= P122) to L: in SLS; severe loss of activity; dbSNP:rs72547559
- P121 (= P129) to L: in SLS; severe loss of activity; dbSNP:rs72547560
- T184 (= T192) to M: in SLS; severe loss of activity; dbSNP:rs72547562; to R: in SLS; severe loss of activity
- G185 (= G193) to A: in SLS; severe loss of activity; dbSNP:rs72547563
- E207 (= E215) active site; mutation to Q: Loss of enzyme activity.
- C214 (= C222) to Y: in SLS; 4% of activity; dbSNP:rs72547564
- R228 (= R236) to C: in SLS; severe loss of activity; dbSNP:rs72547566
- C237 (≠ A245) to Y: in SLS; severe loss of activity; dbSNP:rs72547567
- C241 (= C249) active site; mutation to S: Loss of enzyme activity.
- D245 (= D253) to N: in SLS; severe loss of activity; dbSNP:rs72547568
- K266 (≠ Q274) to N: in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability; dbSNP:rs72547569
- Y279 (= Y287) to N: in SLS; severe loss of activity; dbSNP:rs72547570
- AP 314:315 (= AP 322:323) natural variant: AP -> GAKSTVGA (in SLS; 8% of activity)
- P315 (= P323) to S: in SLS; common mutation in Europeans; severe loss of enzymatic activity; dbSNP:rs72547571
- E331 (= E339) mutation to Q: Loss of enzyme activity.
- S365 (= S373) to L: in SLS; severe loss of activity; dbSNP:rs72547573
- Y410 (= Y418) mutation to F: Decreased enzyme activity with dodecanal and hexadecanal. No effect on enzyme activity with octanal.
- H411 (= H419) to Y: in SLS; severe loss of activity
- S415 (= S423) to N: in SLS; severe loss of activity
- F419 (= F427) to S: in SLS; severe loss of activity; dbSNP:rs72547576
- R423 (≠ K431) 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
E9Q3E1 Aldehyde dehydrogenase family 3 member B2; Aldehyde dehydrogenase 8; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
46% identity, 96% coverage: 12:450/459 of query aligns to 20:460/479 of E9Q3E1