SitesBLAST
Comparing Ga0059261_1486 FitnessBrowser__Korea:Ga0059261_1486 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)
34% identity, 97% coverage: 1:454/468 of query aligns to 4:445/453 of P30838
- S134 (≠ R134) to A: in dbSNP:rs887241
- E210 (= E210) active site
- C244 (= C244) active site; mutation to S: Abolishes activity.
- P329 (≠ T338) to A: in allele ALDH3A1*2; dbSNP:rs2228100
1ad3A Class 3 aldehyde dehydrogenase complex with nicotinamide-adenine- dinucleotide (see paper)
35% identity, 97% coverage: 1:454/468 of query aligns to 2:443/446 of 1ad3A
- active site: N113 (= N115), K136 (= K138), E208 (= E210), C242 (= C244), E332 (= E343), Y411 (= Y422)
- binding nicotinamide-adenine-dinucleotide: A111 (≠ P113), W112 (= W114), N113 (= N115), E139 (= E141), V140 (≠ F142), V168 (vs. gap), G186 (= G188), V190 (≠ I192), H288 (= H289), R291 (= R292), E332 (= E343), F334 (= F345)
8bb8A Crystal structure of human aldehyde dehydrogenase aldh3a1 in complex with octanal (see paper)
34% identity, 97% coverage: 1:454/468 of query aligns to 3:444/447 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
34% identity, 97% coverage: 1:454/468 of query aligns to 3:444/452 of 4l1oB
- active site: N114 (= N115), K137 (= K138), E209 (= E210), C243 (= C244), E333 (= E343), Y412 (= Y422)
- binding (3S)-1-{[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-3-hydroxy-1,3-dihydro-2H-indol-2-one: Y115 (≠ F116), N118 (= N119), L119 (= L120), E209 (= E210), T242 (≠ I243), C243 (= C244), I391 (= I401), I394 (≠ V404), F401 (= F411), H413 (= H423)
4l2oA Crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
34% identity, 97% coverage: 1:454/468 of query aligns to 3:444/446 of 4l2oA
- active site: N114 (= N115), K137 (= K138), E209 (= E210), C243 (= C244), E333 (= E343), Y412 (= Y422)
- binding 1-[(4-fluorophenyl)sulfonyl]-2-methyl-1H-benzimidazole: E61 (≠ T60), Y65 (≠ A64), Y115 (≠ F116), N118 (= N119), L119 (= L120), M237 (≠ L238), C243 (= C244), I391 (= I401), I394 (≠ V404), T395 (≠ S405), F401 (= F411), H413 (= H423)
- binding nicotinamide-adenine-dinucleotide: T112 (≠ P113), W113 (= W114), N114 (= N115), L119 (= L120), E140 (= E141), V169 (vs. gap), T186 (= T187), G187 (= G188), S188 (≠ A189), V191 (≠ I192), E209 (= E210), L210 (= L211), G211 (= G212), C243 (= C244), H289 (= H289), E333 (= E343), F335 (= F345), F401 (= F411)
4h80A Crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
34% identity, 97% coverage: 1:454/468 of query aligns to 3:444/446 of 4h80A
- active site: N114 (= N115), K137 (= K138), E209 (= E210), C243 (= C244), E333 (= E343), Y412 (= Y422)
- binding N-(4-{[4-(methylsulfonyl)-2-nitrophenyl]amino}phenyl)acetamide: E61 (≠ T60), Y65 (≠ A64), Y115 (≠ F116), N118 (= N119), W233 (≠ M234), T242 (≠ I243), C243 (= C244), V244 (≠ I245), I394 (≠ V404), T395 (≠ S405), F401 (= F411)
3szbA Crystal structure of human aldh3a1 modified with the beta-elimination product of aldi-1; 1-phenyl- 2-propen-1-one (see paper)
34% identity, 97% coverage: 1:454/468 of query aligns to 3:444/447 of 3szbA
E9Q3E1 Aldehyde dehydrogenase family 3 member B2; Aldehyde dehydrogenase 8; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
35% identity, 99% coverage: 5:468/468 of query aligns to 21:472/479 of E9Q3E1
- W462 (≠ K458) mutation to A: Reduces lipid droplet localization.
- W469 (≠ Q465) mutation to A: Reduces lipid droplet localization.
Sites not aligning to the query:
- 476 C→S: Reduces lipid droplet localization.
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)
35% identity, 93% coverage: 7:441/468 of query aligns to 7:429/485 of P51648
- I45 (≠ L45) to F: in SLS; severe loss of activity
- V64 (≠ S65) to D: in SLS; severe loss of activity; dbSNP:rs72547556
- L106 (≠ G109) to R: in SLS; severe loss of activity; dbSNP:rs72547558
- N112 (= N115) mutation to A: Loss of enzyme activity.
- P114 (= P117) to L: in SLS; severe loss of activity; dbSNP:rs72547559
- P121 (= P124) to L: in SLS; severe loss of activity; dbSNP:rs72547560
- T184 (= T187) to M: in SLS; severe loss of activity; dbSNP:rs72547562; to R: in SLS; severe loss of activity
- G185 (= G188) to A: in SLS; severe loss of activity; dbSNP:rs72547563
- E207 (= E210) active site; mutation to Q: Loss of enzyme activity.
- C214 (≠ A217) to Y: in SLS; 4% of activity; dbSNP:rs72547564
- R228 (= R231) to C: in SLS; severe loss of activity; dbSNP:rs72547566
- C237 (≠ A240) to Y: in SLS; severe loss of activity; dbSNP:rs72547567
- C241 (= C244) active site; mutation to S: Loss of enzyme activity.
- D245 (= D248) to N: in SLS; severe loss of activity; dbSNP:rs72547568
- K266 (≠ S269) to N: in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability; dbSNP:rs72547569
- Y279 (= Y281) to N: in SLS; severe loss of activity; dbSNP:rs72547570
- AP 314:315 (≠ PL 326:327) natural variant: AP -> GAKSTVGA (in SLS; 8% of activity)
- P315 (≠ L327) to S: in SLS; common mutation in Europeans; severe loss of enzymatic activity; dbSNP:rs72547571
- E331 (= E343) mutation to Q: Loss of enzyme activity.
- S365 (≠ G377) to L: in SLS; severe loss of activity; dbSNP:rs72547573
- Y410 (= Y422) mutation to F: Decreased enzyme activity with dodecanal and hexadecanal. No effect on enzyme activity with octanal.
- H411 (= H423) to Y: in SLS; severe loss of activity
- S415 (≠ G427) to N: in SLS; severe loss of activity
- F419 (= F431) to S: in SLS; severe loss of activity; dbSNP:rs72547576
- R423 (≠ K435) 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; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7 from Homo sapiens (Human) (see paper)
36% identity, 94% coverage: 3:441/468 of query aligns to 6:432/468 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)
34% identity, 100% coverage: 1:468/468 of query aligns to 17:472/479 of J3QMK6
- RR 462:463 (≠ KT 458:459) mutation to AA: Reduces membrane localization.
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)
35% identity, 93% coverage: 5:441/468 of query aligns to 8:432/468 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.
5ucdA Benzaldehyde dehydrogenase, a class 3 aldehyde dehydrogenase, with bound NADP+ and benzoate adduct (see paper)
33% identity, 93% coverage: 1:437/468 of query aligns to 8:431/435 of 5ucdA
- active site: N119 (= N115), K142 (= K138), E214 (= E210), C248 (= C244), E336 (= E343), Y416 (= Y422)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I115 (= I111), G116 (≠ A112), F118 (≠ W114), N119 (= N115), K142 (= K138), S144 (= S140), E145 (= E141), R174 (≠ P170), F190 (= F186), T191 (= T187), G192 (= G188), S193 (≠ A189), V196 (≠ I192), E214 (= E210), L215 (= L211), C248 (= C244), E336 (= E343), F338 (= F345)
Q70DU8 Aldehyde dehydrogenase family 3 member H1; AtALDH4; Ath-ALDH4; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
32% identity, 93% coverage: 21:457/468 of query aligns to 32:459/484 of Q70DU8
- C45 (≠ V34) mutation to S: Decreased solubility, loss of dimerization and strongly decreased activity.
- E149 (= E141) 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 (≠ P170) 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 (= I192) 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 (≠ L238) mutation to S: No effect on solubility, but 10% loss of activity.
- C253 (= C244) mutation to S: No effect on solubility, but loss of activity.
5nnoA Structure of tbaldh3 complexed with NAD and an3057 aldehyde (see paper)
36% identity, 97% coverage: 4:455/468 of query aligns to 15:472/484 of 5nnoA
- active site: N123 (= N115), K146 (= K138), E218 (= E210), S254 (≠ C244), E360 (= E343), Y439 (= Y422)
- binding 4-[(1-oxidanyl-3~{H}-2,1-benzoxaborol-5-yl)oxy]benzaldehyde: P74 (= P68), Y124 (≠ F116), L127 (≠ N119), T253 (≠ I243), S254 (≠ C244), G422 (≠ S405)
- binding nicotinamide-adenine-dinucleotide: I119 (= I111), G120 (≠ A112), W122 (= W114), N123 (= N115), L128 (= L120), K146 (= K138), E149 (= E141), V178 (≠ P170), T181 (≠ G173), Y194 (≠ F186), T195 (= T187), G196 (= G188), S197 (≠ A189), V200 (≠ I192), E218 (= E210), L219 (= L211), S254 (≠ C244), E360 (= E343), F362 (= F345), F428 (= F411)
Q8W033 Aldehyde dehydrogenase family 3 member I1, chloroplastic; AtALDH3; Ath-ALDH3; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 99% coverage: 4:467/468 of query aligns to 78:532/550 of Q8W033
- C114 (≠ R40) mutation to S: No effect on solubility, but loss of dimerization and 80% loss of activity.
- C142 (≠ L69) mutation to S: No effect on solubility, but decreased activity.
- V263 (≠ I192) mutation to I: No effect on substrate specificity, but decreased affinity for NADP(+) and increased affinity for NAD(+).
- C286 (≠ S215) mutation to S: No effect on solubility, but no effect on activity.
- C310 (≠ L238) mutation to S: No effect on solubility, but no effect on activity.
- C316 (= C244) mutation to S: No effect on solubility, but loss of activity.
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)
31% identity, 95% coverage: 20:464/468 of query aligns to 46:491/532 of Q04458
- S241 (= S215) mutation to L: Causes Q deficiency.
- C273 (= C244) 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)
28% identity, 89% coverage: 23:437/468 of query aligns to 71:482/497 of P17202
- D96 (= D48) binding
- SPW 156:158 (≠ APW 112:114) binding
- Y160 (≠ F116) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ S123) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KTSE 138:141) binding
- L186 (≠ F142) binding
- SSAT 236:239 (≠ ATGI 189:192) binding
- V251 (≠ L204) binding in other chain
- L258 (= L211) binding
- W285 (≠ L238) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E343) binding
- A441 (≠ G394) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S405) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F411) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G415) binding
Sites not aligning to the query:
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
32% identity, 73% coverage: 98:437/468 of query aligns to 154:493/503 of O14293
- S248 (≠ A189) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
P51649 Succinate-semialdehyde dehydrogenase, mitochondrial; Aldehyde dehydrogenase family 5 member A1; NAD(+)-dependent succinic semialdehyde dehydrogenase; EC 1.2.1.24 from Homo sapiens (Human) (see 5 papers)
32% identity, 73% coverage: 97:437/468 of query aligns to 187:530/535 of P51649
- R213 (≠ S123) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (≠ N133) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KTSE 138:141) binding
- T233 (= T143) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A147) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ F165) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G173) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GATGIG 188:193) binding
- R334 (≠ L238) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N239) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C244) modified: Disulfide link with 342, In inhibited form
- C342 (≠ A246) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ P279) natural variant: N -> S
- P382 (vs. gap) to L: in SSADHD; 2% of activity
- V406 (= V307) to I: in dbSNP:rs143741652
- G409 (≠ V310) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S405) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
- 93 C → F: in SSADHD; 3% of activity; dbSNP:rs765561257
- 176 G → R: in SSADHD; <1% of activity; dbSNP:rs72552281
- 180 H → Y: 83% of activity; dbSNP:rs2760118
- 182 P → L: 48% of activity; dbSNP:rs3765310
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
Query Sequence
>Ga0059261_1486 FitnessBrowser__Korea:Ga0059261_1486
MREILDRQRAAFMAELPVPIDLRRDRLRRAVAMVKDNAARFCDALSEDFGHRSPRQSMIT
DVVASVSPLKHAEKMVTRWARREKKPVMFPLGLLGARAWVEYQPKGVVGIIAPWNFPVNL
VMSPLAGVFAAGNRAMVKTSEFTPATAALFEELCPRYFDPAELAFVSGGPEVGQAFSALP
FDHLLFTGATGIGRHILHAAADNLTPVTLELGGKSPAILGRSANLAQATERVAMGKMLNA
GQICIAPDYLMVAAEQEQAAVDGLVRAASAMYPTLLSNPDYTTIINDRHFARLTAAIDDA
RAKGAEVIAVNPANEDFAASNARKLPLHIIRNATDDMTVMQEEIFGPLLPVRKYDSIDGA
IGEVNRRDRPLALYYFGNDEAERRRVLDRTISGGVSLDDTIFHVSMEELPFGGIGPSGMG
AYHGEPGFRTFSHAKSVFKQSRFDVAGLGGLKPPYGRKTDAAIKQQLG
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