SitesBLAST
Comparing CA265_RS21385 CA265_RS21385 aldehyde dehydrogenase family protein 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)
45% identity, 94% coverage: 20:455/465 of query aligns to 19:450/453 of P30838
- S134 (≠ C135) to A: in dbSNP:rs887241
- E210 (= E211) active site
- C244 (= C245) active site; mutation to S: Abolishes activity.
- P329 (≠ A336) to A: in allele ALDH3A1*2; dbSNP:rs2228100
4l1oB Crystal structure of human aldh3a1 with inhibitor 1-{[4-(1,3- benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-1h-indole-2,3-dione
45% identity, 94% coverage: 20:455/465 of query aligns to 18:449/452 of 4l1oB
- active site: N114 (= N116), K137 (= K139), E209 (= E211), C243 (= C245), E333 (= E341), Y412 (≠ C420)
- binding (3S)-1-{[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-3-hydroxy-1,3-dihydro-2H-indol-2-one: Y115 (= Y117), N118 (≠ Q120), L119 (= L121), E209 (= E211), T242 (= T244), C243 (= C245), I391 (≠ L399), I394 (= I402), F401 (= F409), H413 (= H421)
3szbA Crystal structure of human aldh3a1 modified with the beta-elimination product of aldi-1; 1-phenyl- 2-propen-1-one (see paper)
45% identity, 93% coverage: 20:450/465 of query aligns to 18:444/447 of 3szbA
4l2oA Crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
45% identity, 93% coverage: 20:450/465 of query aligns to 18:444/446 of 4l2oA
- active site: N114 (= N116), K137 (= K139), E209 (= E211), C243 (= C245), E333 (= E341), Y412 (≠ C420)
- binding 1-[(4-fluorophenyl)sulfonyl]-2-methyl-1H-benzimidazole: E61 (≠ T63), Y65 (≠ F67), Y115 (= Y117), N118 (≠ Q120), L119 (= L121), M237 (≠ V239), C243 (= C245), I391 (≠ L399), I394 (= I402), T395 (≠ G403), F401 (= F409), H413 (= H421)
- binding nicotinamide-adenine-dinucleotide: T112 (≠ P114), W113 (= W115), N114 (= N116), L119 (= L121), E140 (= E142), V169 (≠ A171), T186 (= T188), G187 (= G189), S188 (= S190), V191 (≠ I193), E209 (= E211), L210 (= L212), G211 (= G213), C243 (= C245), H289 (≠ Q292), E333 (= E341), F335 (= F343), F401 (= F409)
4h80A Crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
45% identity, 93% coverage: 20:450/465 of query aligns to 18:444/446 of 4h80A
- active site: N114 (= N116), K137 (= K139), E209 (= E211), C243 (= C245), E333 (= E341), Y412 (≠ C420)
- binding N-(4-{[4-(methylsulfonyl)-2-nitrophenyl]amino}phenyl)acetamide: E61 (≠ T63), Y65 (≠ F67), Y115 (= Y117), N118 (≠ Q120), W233 (= W235), T242 (= T244), C243 (= C245), V244 (≠ I246), I394 (= I402), T395 (≠ G403), F401 (= F409)
8bb8A Crystal structure of human aldehyde dehydrogenase aldh3a1 in complex with octanal (see paper)
45% identity, 93% coverage: 20:450/465 of query aligns to 18:444/447 of 8bb8A
1ad3A Class 3 aldehyde dehydrogenase complex with nicotinamide-adenine- dinucleotide (see paper)
46% identity, 91% coverage: 27:450/465 of query aligns to 24:443/446 of 1ad3A
- active site: N113 (= N116), K136 (= K139), E208 (= E211), C242 (= C245), E332 (= E341), Y411 (≠ C420)
- binding nicotinamide-adenine-dinucleotide: A111 (≠ P114), W112 (= W115), N113 (= N116), E139 (= E142), V140 (≠ L143), V168 (≠ A171), G186 (= G189), V190 (≠ I193), H288 (≠ Q292), R291 (= R295), E332 (= E341), F334 (= F343)
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)
43% identity, 94% coverage: 20:454/465 of query aligns to 19:449/468 of P43353
Sites not aligning to the query:
- 463 modified: S-palmitoyl cysteine
- 465 modified: S-geranylgeranyl cysteine
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)
43% identity, 93% coverage: 20:450/465 of query aligns to 16:442/485 of P51648
- I45 (≠ L49) to F: in SLS; severe loss of activity
- V64 (≠ T68) to D: in SLS; severe loss of activity; dbSNP:rs72547556
- L106 (= L110) to R: in SLS; severe loss of activity; dbSNP:rs72547558
- N112 (= N116) mutation to A: Loss of enzyme activity.
- P114 (= P118) to L: in SLS; severe loss of activity; dbSNP:rs72547559
- P121 (= P125) to L: in SLS; severe loss of activity; dbSNP:rs72547560
- T184 (= T188) to M: in SLS; severe loss of activity; dbSNP:rs72547562; to R: in SLS; severe loss of activity
- G185 (= G189) to A: in SLS; severe loss of activity; dbSNP:rs72547563
- E207 (= E211) active site; mutation to Q: Loss of enzyme activity.
- C214 (≠ A218) to Y: in SLS; 4% of activity; dbSNP:rs72547564
- R228 (≠ K232) to C: in SLS; severe loss of activity; dbSNP:rs72547566
- C237 (≠ A241) to Y: in SLS; severe loss of activity; dbSNP:rs72547567
- C241 (= C245) active site; mutation to S: Loss of enzyme activity.
- D245 (= D249) to N: in SLS; severe loss of activity; dbSNP:rs72547568
- K266 (= K271) to N: in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability; dbSNP:rs72547569
- Y279 (= Y284) to N: in SLS; severe loss of activity; dbSNP:rs72547570
- AP 314:315 (≠ TP 324:325) natural variant: AP -> GAKSTVGA (in SLS; 8% of activity)
- P315 (= P325) to S: in SLS; common mutation in Europeans; severe loss of enzymatic activity; dbSNP:rs72547571
- E331 (= E341) mutation to Q: Loss of enzyme activity.
- S365 (= S375) to L: in SLS; severe loss of activity; dbSNP:rs72547573
- Y410 (≠ C420) mutation to F: Decreased enzyme activity with dodecanal and hexadecanal. No effect on enzyme activity with octanal.
- H411 (= H421) to Y: in SLS; severe loss of activity
- S415 (≠ G425) to N: in SLS; severe loss of activity
- F419 (= F429) to S: in SLS; severe loss of activity; dbSNP:rs72547576
- R423 (= R433) 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
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)
42% identity, 94% coverage: 18:454/465 of query aligns to 17:449/468 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.
E9Q3E1 Aldehyde dehydrogenase family 3 member B2; Aldehyde dehydrogenase 8; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
43% identity, 95% coverage: 20:460/465 of query aligns to 32:469/479 of E9Q3E1
- W462 (vs. gap) mutation to A: Reduces lipid droplet localization.
- W469 (= W460) mutation to A: Reduces lipid droplet localization.
Sites not aligning to the query:
- 476 C→S: Reduces lipid droplet localization.
J3QMK6 Aldehyde dehydrogenase family 3 member B3; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
42% identity, 96% coverage: 14:460/465 of query aligns to 25:469/479 of J3QMK6
- RR 462:463 (≠ SK 453:454) mutation to AA: Reduces membrane localization.
Q70DU8 Aldehyde dehydrogenase family 3 member H1; AtALDH4; Ath-ALDH4; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
41% identity, 94% coverage: 27:465/465 of query aligns to 34:469/484 of Q70DU8
- C45 (≠ L38) mutation to S: Decreased solubility, loss of dimerization and strongly decreased activity.
- E149 (= E142) 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 (≠ A171) 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 (= I193) 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 (≠ V239) mutation to S: No effect on solubility, but 10% loss of activity.
- C253 (= C245) mutation to S: No effect on solubility, but loss of activity.
Q8W033 Aldehyde dehydrogenase family 3 member I1, chloroplastic; AtALDH3; Ath-ALDH3; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 100% coverage: 3:465/465 of query aligns to 80:532/550 of Q8W033
- C114 (≠ E44) mutation to S: No effect on solubility, but loss of dimerization and 80% loss of activity.
- C142 (≠ I72) mutation to S: No effect on solubility, but decreased activity.
- V263 (≠ I193) mutation to I: No effect on substrate specificity, but decreased affinity for NADP(+) and increased affinity for NAD(+).
- C286 (≠ S216) mutation to S: No effect on solubility, but no effect on activity.
- C310 (≠ V239) mutation to S: No effect on solubility, but no effect on activity.
- C316 (= C245) mutation to S: No effect on solubility, but loss of activity.
5nnoA Structure of tbaldh3 complexed with NAD and an3057 aldehyde (see paper)
41% identity, 93% coverage: 23:453/465 of query aligns to 30:474/484 of 5nnoA
- active site: N123 (= N116), K146 (= K139), E218 (= E211), S254 (≠ C245), E360 (= E341), Y439 (≠ C420)
- binding 4-[(1-oxidanyl-3~{H}-2,1-benzoxaborol-5-yl)oxy]benzaldehyde: P74 (≠ F67), Y124 (= Y117), L127 (≠ Q120), T253 (= T244), S254 (≠ C245), G422 (= G403)
- binding nicotinamide-adenine-dinucleotide: I119 (= I112), G120 (≠ A113), W122 (= W115), N123 (= N116), L128 (= L121), K146 (= K139), E149 (= E142), V178 (≠ A171), T181 (≠ S174), Y194 (≠ F187), T195 (= T188), G196 (= G189), S197 (= S190), V200 (≠ I193), E218 (= E211), L219 (= L212), S254 (≠ C245), E360 (= E341), F362 (= F343), F428 (= F409)
5ucdA Benzaldehyde dehydrogenase, a class 3 aldehyde dehydrogenase, with bound NADP+ and benzoate adduct (see paper)
39% identity, 93% coverage: 4:435/465 of query aligns to 7:431/435 of 5ucdA
- active site: N119 (= N116), K142 (= K139), E214 (= E211), C248 (= C245), E336 (= E341), Y416 (≠ C420)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I115 (= I112), G116 (≠ A113), F118 (≠ W115), N119 (= N116), K142 (= K139), S144 (= S141), E145 (= E142), R174 (≠ A171), F190 (= F187), T191 (= T188), G192 (= G189), S193 (= S190), V196 (≠ I193), E214 (= E211), L215 (= L212), C248 (= C245), E336 (= E341), F338 (= F343)
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)
35% identity, 95% coverage: 11:454/465 of query aligns to 33:485/532 of Q04458
- S241 (= S216) mutation to L: Causes Q deficiency.
- C273 (= C245) mutation to S: Abolishes catalytic activity.
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
35% identity, 73% coverage: 103:442/465 of query aligns to 158:500/503 of O14293
- S248 (= S190) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
P47895 Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; Aldehyde dehydrogenase 6; Aldehyde dehydrogenase family 1 member A3; ALDH1A3; EC 1.2.1.36 from Homo sapiens (Human) (see 2 papers)
31% identity, 90% coverage: 20:438/465 of query aligns to 89:506/512 of P47895
- R89 (= R20) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K139) binding
- E207 (= E142) binding
- GSTEVG 257:262 (≠ GSTAIG 189:194) binding
- Q361 (= Q292) binding
- E411 (= E341) binding
- A493 (≠ G425) to P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
31% identity, 90% coverage: 20:438/465 of query aligns to 70:487/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I112), T159 (≠ A113), P160 (= P114), W161 (= W115), K185 (= K139), E188 (= E142), G218 (≠ D170), G222 (≠ S174), F236 (= F187), S239 (= S190), V242 (≠ I193)
Query Sequence
>CA265_RS21385 CA265_RS21385 aldehyde dehydrogenase family protein
MEEQIKSVFDLQQKHKFELRKTDAKTRIGKLKLLKQALEKAEEEIYAALEADLRKNRFET
AVTELFFTYAEIDHAIKKLQGWMKPKSVARTMSNLFASNKIYYEPKGVCLIIAPWNYPLQ
LIMSPLVSAIAAGNCVILKPSELSAATADVISKLISNTFEAEEIACFEGDAEVSTALLKL
PFDHIFFTGSTAIGKVVMEAAAKNLTSVTLELGGKSPAIVDETCDLKKAAEKIAWGKLVN
AGQTCIAPDYVLIKENISADFEMYYQAAVQKMFFNEAAINKNDYAKIINIKQFQRLNKLI
EEAIRDGAVLAFGGKSDEQNLTITPTLLTSVAESSAIMQEEIFGPVLPVITYQNLQEAID
VVNRKAKPLALYIFSDSTTNQNKIISETSAGGTCVNDVLVHIGNPDLPFGGVNNSGIGSC
HGIFGFKTFSHERAVVFQSKLDLTKMIYPPYASKMGLLKWLKKLM
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