SitesBLAST
Comparing Synpcc7942_0489 Synpcc7942_0489 aldehyde dehydrogenase 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
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
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.
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)
47% identity, 96% coverage: 10:448/459 of query aligns to 5:445/468 of P43353
Sites not aligning to the query:
- 463 modified: S-palmitoyl cysteine
- 465 modified: S-geranylgeranyl cysteine
J3QMK6 Aldehyde dehydrogenase family 3 member B3; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
46% identity, 96% coverage: 11:449/459 of query aligns to 19:459/479 of J3QMK6
Sites not aligning to the query:
- 462:463 RR→AA: Reduces membrane 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)
46% identity, 98% coverage: 9:458/459 of query aligns to 75:529/550 of Q8W033
- C114 (≠ E48) mutation to S: No effect on solubility, but loss of dimerization and 80% loss of activity.
- C142 (≠ I76) mutation to S: No effect on solubility, but decreased activity.
- V263 (≠ I197) mutation to I: No effect on substrate specificity, but decreased affinity for NADP(+) and increased affinity for NAD(+).
- C286 (≠ S220) mutation to S: No effect on solubility, but no effect on activity.
- C310 (≠ F243) mutation to S: No effect on solubility, but no effect on activity.
- C316 (= C249) mutation to S: No effect on solubility, but loss of activity.
5ucdA Benzaldehyde dehydrogenase, a class 3 aldehyde dehydrogenase, with bound NADP+ and benzoate adduct (see paper)
42% identity, 93% coverage: 7:433/459 of query aligns to 5:431/435 of 5ucdA
- active site: N119 (= N120), K142 (= K143), E214 (= E215), C248 (= C249), E336 (= E339), Y416 (= Y418)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I115 (= I116), G116 (= G117), F118 (≠ W119), N119 (= N120), K142 (= K143), S144 (= S145), E145 (= E146), R174 (≠ A175), F190 (= F191), T191 (= T192), G192 (= G193), S193 (≠ G194), V196 (≠ I197), E214 (= E215), L215 (= L216), C248 (= C249), E336 (= E339), F338 (= F341)
5nnoA Structure of tbaldh3 complexed with NAD and an3057 aldehyde (see paper)
40% identity, 95% coverage: 13:449/459 of query aligns to 16:472/484 of 5nnoA
- active site: N123 (= N120), K146 (= K143), E218 (= E215), S254 (≠ C249), E360 (= E339), Y439 (= Y418)
- binding 4-[(1-oxidanyl-3~{H}-2,1-benzoxaborol-5-yl)oxy]benzaldehyde: P74 (≠ F71), Y124 (= Y121), L127 (≠ Q124), T253 (= T248), S254 (≠ C249), G422 (= G401)
- binding nicotinamide-adenine-dinucleotide: I119 (= I116), G120 (= G117), W122 (= W119), N123 (= N120), L128 (= L125), K146 (= K143), E149 (= E146), V178 (≠ A175), T181 (≠ S178), Y194 (≠ F191), T195 (= T192), G196 (= G193), S197 (≠ G194), V200 (≠ I197), E218 (= E215), L219 (= L216), S254 (≠ C249), E360 (= E339), F362 (= F341), F428 (= F407)
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)
34% identity, 92% coverage: 26:448/459 of query aligns to 44:481/532 of Q04458
- S241 (= S220) mutation to L: Causes Q deficiency.
- C273 (= C249) mutation to S: Abolishes catalytic activity.
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
33% identity, 75% coverage: 90:435/459 of query aligns to 129:484/497 of P17202
- SPW 156:158 (≠ GPW 117:119) binding
- Y160 (= Y121) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ T128) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 143:146) binding
- L186 (= L147) binding
- SSAT 236:239 (≠ GTAI 194:197) binding
- V251 (≠ L209) binding in other chain
- L258 (= L216) binding
- W285 (≠ F243) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E339) binding
- A441 (≠ S390) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ G401) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F407) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G411) binding
Sites not aligning to the query:
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
33% identity, 75% coverage: 90:435/459 of query aligns to 127:482/495 of 4v37A
- active site: N157 (= N120), K180 (= K143), E255 (= E215), A289 (≠ C249), E388 (= E339), E465 (≠ Y418)
- binding 3-aminopropan-1-ol: C448 (≠ G401), W454 (≠ F407)
- binding nicotinamide-adenine-dinucleotide: I153 (= I116), S154 (≠ G117), P155 (= P118), W156 (= W119), N157 (= N120), M162 (≠ L125), K180 (= K143), S182 (= S145), E183 (= E146), G213 (≠ A175), G217 (≠ Q179), A218 (= A180), T232 (= T192), G233 (= G193), S234 (≠ G194), T237 (≠ I197), E255 (= E215), L256 (= L216), A289 (≠ C249), E388 (= E339), F390 (= F341)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
34% identity, 72% coverage: 104:433/459 of query aligns to 137:476/490 of Q9HTJ1
- GAWN 150:153 (≠ GPWN 117:120) binding
- K162 (≠ P129) active site, Charge relay system
- KPSE 176:179 (= KPSE 143:146) binding
- G209 (≠ A175) binding
- GTST 230:233 (≠ GTAI 194:197) binding
- E252 (= E215) active site, Proton acceptor
- C286 (= C249) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E339) binding
- E464 (≠ Y418) active site, Charge relay system
Query Sequence
>Synpcc7942_0489 Synpcc7942_0489 aldehyde dehydrogenase
MTAVVLPAAAETLAALQATFDRGDTRTLAFRLARLQDLAKLVADNEAELLQALASDLRKP
ALEAYASEIYFVRDQIKLTCKHLRRWMQPEKQSISLMQQPGQAYRQAEPLGVVLIIGPWN
YPFQLLITPLIGAIAAGNCAVLKPSELAPATSSLIQRLISDRFDPDYIRVLEGDASVSQA
LITQPFDHIFFTGGTAIGRKVMAAAAENLTPVTLELGGKSPCIVDTDIDLDVAARRIAWG
KFFNAGQTCIAPDYLLVQRTVAEPFIEALIDNIQQFYGEDPQQSADYARIVSDRHWQRLN
SLLVDGTIRHGGQVDRSDRYIAPTLITDVNWRDPILQEEIFGPLLPILIYDQLDEAIAQI
RAQPKPLALYLFSRDRQVQERVLAETSAGSVCLNDTILQVGVPDAAFGGVGPSGMGGYHG
KASFETFSHYKLVLKRPFWLDLALRYPPYGDKINLFRKL
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