SitesBLAST
Comparing WP_225487653.1 NCBI__GCF_000021485.1:WP_225487653.1 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)
Q70DU8 Aldehyde dehydrogenase family 3 member H1; AtALDH4; Ath-ALDH4; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
34% identity, 95% coverage: 20:461/465 of query aligns to 31:469/484 of Q70DU8
- C45 (≠ L34) mutation to S: Decreased solubility, loss of dimerization and strongly decreased activity.
- E149 (≠ R139) 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 (≠ P168) 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 (≠ T190) 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 (≠ V236) mutation to S: No effect on solubility, but 10% loss of activity.
- C253 (= C242) mutation to S: No effect on solubility, but loss of activity.
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)
36% identity, 88% coverage: 21:430/465 of query aligns to 21:421/485 of P51648
- I45 (= I45) to F: in SLS; severe loss of activity
- V64 (≠ L65) to D: in SLS; severe loss of activity; dbSNP:rs72547556
- L106 (≠ G107) to R: in SLS; severe loss of activity; dbSNP:rs72547558
- N112 (= N113) mutation to A: Loss of enzyme activity.
- P114 (= P115) to L: in SLS; severe loss of activity; dbSNP:rs72547559
- P121 (= P122) to L: in SLS; severe loss of activity; dbSNP:rs72547560
- T184 (≠ S185) to M: in SLS; severe loss of activity; dbSNP:rs72547562; to R: in SLS; severe loss of activity
- G185 (= G186) to A: in SLS; severe loss of activity; dbSNP:rs72547563
- E207 (≠ S208) active site; mutation to Q: Loss of enzyme activity.
- C214 (≠ A215) to Y: in SLS; 4% of activity; dbSNP:rs72547564
- R228 (≠ S229) to C: in SLS; severe loss of activity; dbSNP:rs72547566
- C237 (≠ A238) to Y: in SLS; severe loss of activity; dbSNP:rs72547567
- C241 (= C242) active site; mutation to S: Loss of enzyme activity.
- D245 (= D246) to N: in SLS; severe loss of activity; dbSNP:rs72547568
- K266 (≠ L267) to N: in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability; dbSNP:rs72547569
- Y279 (= Y279) to N: in SLS; severe loss of activity; dbSNP:rs72547570
- AP 314:315 (≠ PP 323:324) natural variant: AP -> GAKSTVGA (in SLS; 8% of activity)
- P315 (= P324) to S: in SLS; common mutation in Europeans; severe loss of enzymatic activity; dbSNP:rs72547571
- E331 (= E340) mutation to Q: Loss of enzyme activity.
- S365 (≠ D374) to L: in SLS; severe loss of activity; dbSNP:rs72547573
- Y410 (= Y419) mutation to F: Decreased enzyme activity with dodecanal and hexadecanal. No effect on enzyme activity with octanal.
- H411 (≠ R420) to Y: in SLS; severe loss of activity
- S415 (≠ G424) to N: in SLS; severe loss of activity
- F419 (≠ L428) to S: in SLS; severe loss of activity; dbSNP:rs72547576
Sites not aligning to the query:
- 423 R → H: in SLS; severe loss of activity; dbSNP:rs768290318
- 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
Q8W033 Aldehyde dehydrogenase family 3 member I1, chloroplastic; AtALDH3; Ath-ALDH3; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 99% coverage: 1:461/465 of query aligns to 79:531/550 of Q8W033
- C114 (≠ A40) mutation to S: No effect on solubility, but loss of dimerization and 80% loss of activity.
- C142 (≠ I69) mutation to S: No effect on solubility, but decreased activity.
- V263 (≠ T190) mutation to I: No effect on substrate specificity, but decreased affinity for NADP(+) and increased affinity for NAD(+).
- C286 (≠ S213) mutation to S: No effect on solubility, but no effect on activity.
- C310 (≠ V236) mutation to S: No effect on solubility, but no effect on activity.
- C316 (= C242) mutation to S: No effect on solubility, but loss of activity.
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)
31% identity, 94% coverage: 23:460/465 of query aligns to 39:469/479 of E9Q3E1
- W462 (= W453) 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.
5ucdA Benzaldehyde dehydrogenase, a class 3 aldehyde dehydrogenase, with bound NADP+ and benzoate adduct (see paper)
33% identity, 93% coverage: 1:434/465 of query aligns to 8:431/435 of 5ucdA
- active site: N119 (= N113), K142 (= K136), E214 (≠ S208), C248 (= C242), E336 (= E340), Y416 (= Y419)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I115 (= I109), G116 (= G110), F118 (≠ W112), N119 (= N113), K142 (= K136), S144 (≠ P138), E145 (≠ R139), R174 (≠ P168), F190 (= F184), T191 (≠ S185), G192 (= G186), S193 (≠ A187), V196 (≠ T190), E214 (≠ S208), L215 (≠ M209), C248 (= C242), E336 (= E340), F338 (= F342)
1ad3A Class 3 aldehyde dehydrogenase complex with nicotinamide-adenine- dinucleotide (see paper)
31% identity, 94% coverage: 6:441/465 of query aligns to 1:433/446 of 1ad3A
- active site: N113 (= N113), K136 (= K136), E208 (≠ S208), C242 (= C242), E332 (= E340), Y411 (= Y419)
- binding nicotinamide-adenine-dinucleotide: A111 (= A111), W112 (= W112), N113 (= N113), E139 (≠ R139), V140 (≠ L140), V168 (≠ P168), G186 (= G186), V190 (≠ T190), H288 (≠ L287), R291 (= R290), E332 (= E340), F334 (= F342)
5nnoA Structure of tbaldh3 complexed with NAD and an3057 aldehyde (see paper)
35% identity, 95% coverage: 9:450/465 of query aligns to 20:472/484 of 5nnoA
- active site: N123 (= N113), K146 (= K136), E218 (≠ S208), S254 (≠ C242), E360 (= E340), Y439 (= Y419)
- binding 4-[(1-oxidanyl-3~{H}-2,1-benzoxaborol-5-yl)oxy]benzaldehyde: P74 (= P64), Y124 (= Y114), L127 (= L117), T253 (= T241), S254 (≠ C242), G422 (≠ A402)
- binding nicotinamide-adenine-dinucleotide: I119 (= I109), G120 (= G110), W122 (= W112), N123 (= N113), L128 (= L118), K146 (= K136), E149 (≠ R139), V178 (≠ P168), T181 (≠ D171), Y194 (≠ F184), T195 (≠ S185), G196 (= G186), S197 (≠ A187), V200 (≠ T190), E218 (≠ S208), L219 (≠ M209), S254 (≠ C242), E360 (= E340), F362 (= F342), F428 (= F408)
8bb8A Crystal structure of human aldehyde dehydrogenase aldh3a1 in complex with octanal (see paper)
32% identity, 87% coverage: 27:430/465 of query aligns to 29:423/447 of 8bb8A
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)
32% identity, 87% coverage: 27:430/465 of query aligns to 30:424/453 of P30838
- S134 (≠ R132) to A: in dbSNP:rs887241
- E210 (≠ S208) active site
- C244 (= C242) active site; mutation to S: Abolishes activity.
- P329 (≠ K335) to A: in allele ALDH3A1*2; dbSNP:rs2228100
4l2oA Crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
32% identity, 87% coverage: 27:430/465 of query aligns to 29:423/446 of 4l2oA
- active site: N114 (= N113), K137 (= K136), E209 (≠ S208), C243 (= C242), E333 (= E340), Y412 (= Y419)
- binding 1-[(4-fluorophenyl)sulfonyl]-2-methyl-1H-benzimidazole: E61 (vs. gap), Y65 (≠ P64), Y115 (= Y114), N118 (≠ L117), L119 (= L118), M237 (≠ V236), C243 (= C242), I391 (= I398), I394 (≠ V401), T395 (≠ A402), F401 (= F408), H413 (≠ R420)
- binding nicotinamide-adenine-dinucleotide: T112 (≠ A111), W113 (= W112), N114 (= N113), L119 (= L118), E140 (≠ R139), V169 (≠ P168), T186 (≠ S185), G187 (= G186), S188 (≠ A187), V191 (≠ T190), E209 (≠ S208), L210 (≠ M209), G211 (≠ S210), C243 (= C242), H289 (≠ L287), E333 (= E340), F335 (= F342), F401 (= F408)
4h80A Crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
32% identity, 87% coverage: 27:430/465 of query aligns to 29:423/446 of 4h80A
- active site: N114 (= N113), K137 (= K136), E209 (≠ S208), C243 (= C242), E333 (= E340), Y412 (= Y419)
- binding N-(4-{[4-(methylsulfonyl)-2-nitrophenyl]amino}phenyl)acetamide: E61 (vs. gap), Y65 (≠ P64), Y115 (= Y114), N118 (≠ L117), W233 (≠ A232), T242 (= T241), C243 (= C242), V244 (≠ I243), I394 (≠ V401), T395 (≠ A402), F401 (= F408)
3szbA Crystal structure of human aldh3a1 modified with the beta-elimination product of aldi-1; 1-phenyl- 2-propen-1-one (see paper)
32% identity, 87% coverage: 27:430/465 of query aligns to 29:423/447 of 3szbA
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)
32% identity, 87% coverage: 27:430/465 of query aligns to 29:423/452 of 4l1oB
- active site: N114 (= N113), K137 (= K136), E209 (≠ S208), C243 (= C242), E333 (= E340), Y412 (= Y419)
- binding (3S)-1-{[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-3-hydroxy-1,3-dihydro-2H-indol-2-one: Y115 (= Y114), N118 (≠ L117), L119 (= L118), E209 (≠ S208), T242 (= T241), C243 (= C242), I391 (= I398), I394 (≠ V401), F401 (= F408), H413 (≠ R420)
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)
31% identity, 95% coverage: 23:465/465 of query aligns to 26:462/468 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)
29% identity, 99% coverage: 1:460/465 of query aligns to 17:469/479 of J3QMK6
- RR 462:463 (≠ WT 453:454) mutation to AA: Reduces membrane 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)
31% identity, 98% coverage: 9:463/465 of query aligns to 12:460/468 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.
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)
29% identity, 90% coverage: 19:437/465 of query aligns to 45:467/532 of Q04458
- S241 (= S213) mutation to L: Causes Q deficiency.
- C273 (= C242) mutation to S: Abolishes catalytic activity.
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
31% identity, 74% coverage: 94:435/465 of query aligns to 135:476/483 of 3b4wA
- active site: N154 (= N113), K177 (= K136), E251 (≠ S208), C285 (= C242), E384 (= E340), E460 (≠ Y419)
- binding nicotinamide-adenine-dinucleotide: I150 (= I109), V151 (≠ G110), W153 (= W112), N154 (= N113), K177 (= K136), I210 (≠ P168), G213 (≠ D171), T228 (≠ S185), G229 (= G186), S230 (≠ A187), V233 (≠ T190), E236 (≠ V193), E251 (≠ S208), L252 (≠ M209), C285 (= C242), E384 (= E340), F386 (= F342)
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)
26% identity, 96% coverage: 4:449/465 of query aligns to 51:497/497 of P17202
- D96 (= D48) binding K(+)
- SPW 156:158 (≠ GAW 110:112) binding NAD(+)
- Y160 (= Y114) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ L121) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KGPR 136:139) binding NAD(+)
- L186 (= L140) binding K(+)
- SSAT 236:239 (≠ ATRT 187:190) binding NAD(+)
- V251 (≠ L202) binding in other chain
- L258 (≠ M209) binding NAD(+)
- W285 (≠ V236) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E340) binding NAD(+)
- A441 (≠ G391) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ G405) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F408) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G412) binding K(+)
Sites not aligning to the query:
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
26% identity, 96% coverage: 4:449/465 of query aligns to 49:495/495 of 4v37A
- active site: N157 (= N113), K180 (= K136), E255 (≠ S208), A289 (≠ C242), E388 (= E340), E465 (≠ Y419)
- binding 3-aminopropan-1-ol: C448 (≠ G405), W454 (≠ F408)
- binding nicotinamide-adenine-dinucleotide: I153 (= I109), S154 (≠ G110), P155 (≠ A111), W156 (= W112), N157 (= N113), M162 (≠ L118), K180 (= K136), S182 (≠ P138), E183 (≠ R139), G213 (≠ S167), G217 (≠ D171), A218 (≠ H172), T232 (≠ S185), G233 (= G186), S234 (≠ A187), T237 (= T190), E255 (≠ S208), L256 (≠ M209), A289 (≠ C242), E388 (= E340), F390 (= F342)
Query Sequence
>WP_225487653.1 NCBI__GCF_000021485.1:WP_225487653.1
MDELLAVQKSALRENGAIDYRQRRTLLRDLAQMLRQHGRAFSEAIARDFGRRHPRETEIY
EIYPLQAEIAYVLSHLRNWTRPRAVHTRWPFLPARSQITPQPVGVVGIIGAWNYPLLLTL
LPLISAIAAGNRAIIKGPRLAPQTMTLLAQYLRDVTSEDTIALVQGSPDVDHAFPGLPFD
HLIFSGATRTGRVIARAAARNLVPVTLSMSGKSPAIIQCDYPLATAARSIMAGKLVNAGQ
TCIAPDYCLVAADQRDDFIALAKSAALSLYPHWADNPDYTSIPNVLLWERLEGLLQDAQR
KGAILWQPSPAPALADGAQRPFPPTLLWDVQPGMKILEEETFGPILVVLTYDDIQEALDY
VRDHPAPLALYYFDRDQRRALRHCKGIAAGGVTINDTIFHVAQPGIPFGGIGLSGIGQYR
GIYGFQRLSHYQGVFRQNRLSACEWVRPPYGRWTRLLIAWLSRWG
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