SitesBLAST
Comparing Ga0059261_0516 FitnessBrowser__Korea:Ga0059261_0516 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4jz6A Crystal structure of a salicylaldehyde dehydrogenase from pseudomonas putida g7 complexed with salicylaldehyde (see paper)
50% identity, 98% coverage: 11:478/478 of query aligns to 19:484/484 of 4jz6A
- active site: N150 (= N142), K173 (= K165), E251 (= E242), C285 (= C276), E380 (= E374), F458 (= F452)
- binding salicylaldehyde: W97 (= W89), G151 (≠ A143), V154 (≠ I146), R247 (≠ P238), C248 (≠ V239), I284 (= I275), C285 (= C276), M286 (= M277), Y447 (≠ F441), Y455 (= Y449)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
35% identity, 99% coverage: 7:478/478 of query aligns to 19:485/490 of 5ekcE
- active site: N154 (= N142), K177 (= K165), E252 (= E242), C286 (= C276), E381 (= E374), E459 (≠ F452)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (= I138), T151 (≠ A139), P152 (= P140), W153 (= W141), K177 (= K165), S180 (≠ E168), G210 (≠ A200), G214 (≠ V204), F228 (= F218), G230 (= G220), E231 (≠ S221), T234 (≠ V224), N331 (≠ D320), R333 (≠ K322), Q334 (≠ T323)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
35% identity, 99% coverage: 7:478/478 of query aligns to 12:478/482 of 5ek6A
- active site: N147 (= N142), K170 (= K165), E245 (= E242), C279 (= C276), E374 (= E374), E452 (≠ F452)
- binding 2-methylpropanal: I152 (≠ L147), K155 (≠ R150), T222 (= T219), E245 (= E242), F441 (= F441)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (= I138), T144 (≠ A139), W146 (= W141), N147 (= N142), I152 (≠ L147), K170 (= K165), A172 (≠ S167), S173 (≠ E168), P202 (≠ A196), G203 (≠ A200), G207 (≠ V204), F221 (= F218), T222 (= T219), G223 (= G220), E224 (≠ S221), T227 (≠ V224), I231 (= I228), E245 (= E242), L246 (= L243), C279 (= C276), E374 (= E374)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
35% identity, 99% coverage: 7:478/478 of query aligns to 12:478/482 of 4h73A
- active site: N147 (= N142), K170 (= K165), E245 (= E242), C279 (= C276), E374 (= E374), E452 (≠ F452)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (= I138), T144 (≠ A139), P145 (= P140), W146 (= W141), K170 (= K165), A172 (≠ S167), S173 (≠ E168), G203 (≠ A200), G207 (≠ V204), F221 (= F218), G223 (= G220), E224 (≠ S221), T227 (≠ V224)
Q8NMB0 Vanillin dehydrogenase; Aromatic aldehyde dehydrogenase; EC 1.2.1.67; EC 1.2.1.64; EC 1.2.1.96 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
41% identity, 95% coverage: 15:470/478 of query aligns to 30:482/484 of Q8NMB0
- N157 (= N142) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 2.3-fold decreased affinity for vanillin compared to the wild type.
- K180 (= K165) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 5-fold decreased affinity for vanillin compared to the wild type.
- E199 (= E183) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 78% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 5-fold decreased affinity for NAD(+), 2.5-fold decreased affinity for NADP(+) and 1.5-fold decreased affinity for vanillin compared to the wild type.
- E258 (= E242) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 24% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 3.5-fold decreased affinity for NAD(+), 5-fold decreased affinity for NADP(+) and 3.7-fold decreased affinity for vanillin compared to the wild type.
- C292 (= C276) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 7-fold decreased affinity for NADP(+) and 8-fold decreased affinity for vanillin compared to the wild type.
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
36% identity, 95% coverage: 17:469/478 of query aligns to 32:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
35% identity, 95% coverage: 17:469/478 of query aligns to 31:479/481 of 3jz4A
- active site: N156 (= N142), K179 (= K165), E254 (= E242), C288 (= C276), E385 (= E374), E462 (≠ F452)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P140), W155 (= W141), K179 (= K165), A181 (≠ S167), S182 (≠ E168), A212 (= A200), G216 (≠ V204), G232 (= G220), S233 (= S221), I236 (≠ V224), C288 (= C276), K338 (≠ H326), E385 (= E374), F387 (= F376)
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
35% identity, 95% coverage: 17:470/478 of query aligns to 29:486/487 of Q9H2A2
- R109 (≠ L96) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N142) mutation to A: Complete loss of activity.
- R451 (≠ H434) mutation to A: Complete loss of activity.
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
36% identity, 96% coverage: 10:470/478 of query aligns to 27:487/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I138), T159 (≠ A139), P160 (= P140), W161 (= W141), K185 (= K165), E188 (= E168), G218 (≠ A200), G222 (≠ V204), F236 (= F218), S239 (= S221), V242 (= V224)
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
36% identity, 96% coverage: 10:470/478 of query aligns to 28:488/489 of 7a6qB
- active site: N163 (= N142), E262 (= E242), C296 (= C276), E470 (≠ F452)
- binding nicotinamide-adenine-dinucleotide: I159 (= I138), W162 (= W141), K186 (= K165), E189 (= E168), G219 (≠ A200), G223 (≠ V204), S240 (= S221), V243 (= V224), K342 (= K322)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (= A14), T33 (≠ R15), C34 (≠ L16), P36 (= P18), D103 (≠ E82), E189 (= E168), Q190 (= Q169), F218 (≠ D199), I339 (≠ V319), D340 (= D320)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ L96), D141 (= D119), N143 (≠ G122), N451 (≠ T432), L453 (≠ H434), A455 (= A437)
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
36% identity, 96% coverage: 10:470/478 of query aligns to 28:488/489 of 7a6qA
- active site: N163 (= N142), E262 (= E242), C296 (= C276), E470 (≠ F452)
- binding nicotinamide-adenine-dinucleotide: I159 (= I138), T160 (≠ A139), W162 (= W141), K186 (= K165), A188 (≠ S167), E189 (= E168), G219 (≠ A200), G223 (≠ V204), S240 (= S221), V243 (= V224), K342 (= K322), K346 (≠ H326)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ L96), D141 (= D119), N143 (≠ G122), N451 (≠ T432), L453 (≠ H434), Y454 (≠ E436)
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
36% identity, 96% coverage: 10:470/478 of query aligns to 28:488/489 of 5fhzA
- active site: N163 (= N142), K186 (= K165), E262 (= E242), C296 (= C276), E393 (= E374), E470 (≠ F452)
- binding nicotinamide-adenine-dinucleotide: I159 (= I138), T160 (≠ A139), W162 (= W141), K186 (= K165), E189 (= E168), G219 (≠ A200), G223 (≠ V204), F237 (= F218), G239 (= G220), S240 (= S221), T241 (= T222), V243 (= V224), G264 (= G244), Q343 (≠ T323), E393 (= E374)
- binding retinoic acid: G118 (≠ L96), R121 (≠ S99), F164 (≠ A143), M168 (≠ L147), W171 (≠ R150), C295 (≠ I275), C296 (= C276), L453 (≠ H434)
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)
36% identity, 96% coverage: 10:470/478 of query aligns to 46:506/512 of P47895
- R89 (≠ S50) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K165) binding
- E207 (= E168) binding
- GSTEVG 257:262 (≠ GSTAVG 220:225) binding
- Q361 (≠ T323) binding
- E411 (= E374) binding
- A493 (≠ G457) 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
6tgwA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with a selective inhibitor (see paper)
36% identity, 96% coverage: 10:470/478 of query aligns to 20:477/478 of 6tgwA
- active site: N155 (= N142), E254 (= E242), C288 (= C276), E459 (≠ F452)
- binding methyl 5-(1,3-benzodioxol-5-yl)-2-phenyl-pyrazolo[1,5-a]pyrimidine-7-carboxylate: I106 (vs. gap), G110 (≠ L96), F156 (≠ A143), Q278 (≠ F266), F282 (≠ M270), L442 (≠ H434), A444 (= A437)
- binding nicotinamide-adenine-dinucleotide: I151 (= I138), T152 (≠ A139), P153 (= P140), W154 (= W141), K178 (= K165), G211 (≠ A200), G215 (≠ V204), F229 (= F218), G231 (= G220), S232 (= S221), V235 (= V224)
6tryA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with mf13 inhibitor compound (see paper)
35% identity, 96% coverage: 10:470/478 of query aligns to 21:476/478 of 6tryA
- active site: N156 (= N142), E255 (= E242), C289 (= C276), E458 (≠ F452)
- binding nicotinamide-adenine-dinucleotide: I152 (= I138), T153 (≠ A139), W155 (= W141), K179 (= K165), A181 (≠ S167), E182 (= E168), G212 (≠ A200), G216 (≠ V204), A217 (≠ G205), F230 (= F218), G232 (= G220), S233 (= S221), V236 (= V224), K335 (= K322)
- binding 8-(4-chlorophenyl)-2-phenyl-imidazo[1,2-a]pyridine: I107 (vs. gap), G111 (≠ L96), T115 (≠ M100), L160 (≠ I146), C288 (≠ I275), L441 (≠ H434), A443 (= A437)
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
32% identity, 95% coverage: 16:470/478 of query aligns to 41:495/503 of 1bpwA
- active site: N166 (= N142), K189 (= K165), E263 (= E242), C297 (= C276), E400 (= E374), E477 (≠ F452)
- binding nicotinamide-adenine-dinucleotide: I162 (= I138), L163 (≠ A139), W165 (= W141), N166 (= N142), K189 (= K165), G221 (≠ A196), G225 (≠ A200), T240 (= T219), G241 (= G220), S242 (= S221), T245 (≠ V224), E263 (= E242), L264 (= L243), C297 (= C276), E400 (= E374), F402 (= F376), F466 (= F441)
P56533 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABADH; Aldehyde dehydrogenase family 9 member A1; Betaine aldehyde dehydrogenase; BADH; EC 1.2.1.47; EC 1.2.1.3 from Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias) (see paper)
32% identity, 95% coverage: 16:470/478 of query aligns to 41:495/503 of P56533
6te5B Crystal structure of human aldehyde dehydrogenase 1a3 in complex with lq43 inhibitor compound (see paper)
35% identity, 96% coverage: 10:470/478 of query aligns to 22:477/479 of 6te5B
- active site: N157 (= N142), E256 (= E242), C290 (= C276), E459 (≠ F452)
- binding 6-(3,5-dimethoxyphenyl)-2-(4-methoxyphenyl)imidazo[1,2-a]pyridine: E111 (≠ M95), G112 (≠ L96), T116 (≠ M100), L442 (≠ H434), A444 (= A437)
- binding nicotinamide-adenine-dinucleotide: I153 (= I138), T154 (≠ A139), W156 (= W141), K180 (= K165), E183 (= E168), G213 (≠ A200), F231 (= F218), S234 (= S221), V237 (= V224), Q337 (≠ T323), K340 (≠ H326)
6s6wA Crystal structure of human aldh1a3 in complex with 2,6- diphenylimidazo[1,2-a]pyridine (compound ga11) and NAD+ (see paper)
36% identity, 96% coverage: 10:470/478 of query aligns to 24:474/476 of 6s6wA
- active site: N159 (= N142), E258 (= E242), C292 (= C276), E456 (≠ F452)
- binding 2,6-diphenylimidazo[1,2-a]pyridine: E113 (≠ M95), G114 (≠ L96), W167 (≠ R150), L439 (≠ H434), Y440 (≠ E436)
- binding nicotinamide-adenine-dinucleotide: I155 (= I138), T156 (≠ A139), W158 (= W141), K182 (= K165), A184 (≠ S167), G215 (≠ A200), G219 (≠ V204), A220 (≠ G205), F233 (= F218), S236 (= S221), V239 (= V224), K338 (= K322)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
36% identity, 88% coverage: 49:469/478 of query aligns to 63:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I138), T153 (≠ A139), P154 (= P140), K179 (= K165), A212 (= A200), K213 (≠ P201), F230 (= F218), T231 (= T219), G232 (= G220), S233 (= S221), V236 (= V224), W239 (≠ I227), G256 (= G244)
Query Sequence
>Ga0059261_0516 FitnessBrowser__Korea:Ga0059261_0516
MATIAPPAPGKTFARLNPVTGEVATEAQAFTVDQANEAVEAAAAAFPAWSTLGPNARRAA
LNKAAEALAAKAEDFVEAMNGEIGATEGWARFNLMLAVSMVREAAALTTQIGGEVIPSDK
PGCIAMAIREPVGVMLGIAPWNAPIILGVRAVAAPLACGNTVVLKASEQCPRTHSLIAEA
FDEALPKGAVSIVTNAPEDAPEIVGALIDNPHIRRINFTGSTAVGRIIAKRAAEHLKPVL
LELGGKAPMLVLEDADLDEAVKAAAFGAFMNQGQICMSTERIIVVDAVADAFVEKFAAKV
GTMPVGDPREGKTPLGAVVDQKTVAHVKALIGDALAAGAVQVNGGGVLEGTGGVLMPAHV
IDHVTPDMKLFRDESFGPVVGVIRARDEAHAILLANDTEYGLSASVFTRDTARGLRVARQ
IKSGICHVNGPTVHDEAQMPFGGVKASGYGRFGGKAGIDAFTELRWITIETEPGHYPI
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