SitesBLAST
Comparing AO353_15035 AO353_15035 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)
5iuwA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ and iaa (see paper)
53% identity, 99% coverage: 7:495/496 of query aligns to 7:495/495 of 5iuwA
- active site: N166 (= N166), K189 (= K189), E265 (= E265), C300 (= C300), E399 (= E399), D476 (= D476)
- binding 1h-indol-3-ylacetic acid: F167 (= F167), M170 (≠ D170), C300 (= C300), D457 (= D457), F465 (= F465)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ V162), V163 (= V163), P164 (= P164), W165 (= W165), N166 (= N166), K189 (= K189), G222 (= G222), G226 (= G226), K227 (= K227), F240 (= F240), T241 (= T241), G242 (= G242), S243 (= S243), I246 (≠ V246), Y253 (= Y253), E265 (= E265), A266 (≠ C266), C300 (= C300), E399 (= E399), F401 (= F401)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
53% identity, 99% coverage: 7:495/496 of query aligns to 7:495/495 of 5iuvA
- active site: N166 (= N166), K189 (= K189), E265 (= E265), C300 (= C300), E399 (= E399), D476 (= D476)
- binding nicotinamide-adenine-dinucleotide: I162 (≠ V162), V163 (= V163), P164 (= P164), W165 (= W165), N166 (= N166), K189 (= K189), S191 (≠ A191), G222 (= G222), G226 (= G226), K227 (= K227), F240 (= F240), T241 (= T241), G242 (= G242), S243 (= S243), I246 (≠ V246), Y253 (= Y253), E265 (= E265), A266 (≠ C266), C300 (= C300), E399 (= E399), F401 (= F401)
7jsoA P. Syringae alda indole-3-acetaldehyde dehydrogenase c302a mutant in complex with NAD+ and iaa (see paper)
53% identity, 99% coverage: 7:495/496 of query aligns to 7:495/495 of 7jsoA
- active site: N166 (= N166), E265 (= E265), A300 (≠ C300), D476 (= D476)
- binding 1h-indol-3-ylacetic acid: F167 (= F167), W174 (= W174), V299 (= V299), A300 (≠ C300), T301 (≠ S301), D457 (= D457), F465 (= F465)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I162 (≠ V162), V163 (= V163), P164 (= P164), W165 (= W165), K189 (= K189), E192 (= E192), G222 (= G222), G226 (= G226), K227 (= K227), F240 (= F240), G242 (= G242), S243 (= S243), I246 (≠ V246), A266 (≠ C266), G267 (= G267), A300 (≠ C300), E399 (= E399), F401 (= F401)
7uyyA The crystal structure of the pseudomonas aeruginosa aldehyde dehydrogenase encoded by the pa4189 gene in complex with nadh (see paper)
49% identity, 99% coverage: 5:493/496 of query aligns to 8:493/496 of 7uyyA
- binding 1,4-dihydronicotinamide adenine dinucleotide: V165 (= V162), L166 (≠ V163), P167 (= P164), W168 (= W165), K192 (= K189), G225 (= G222), G229 (= G226), F243 (= F240), G245 (= G242), S246 (= S243), T249 (≠ V246), L252 (≠ Y249), F253 (= F250), Y256 (= Y253), C269 (= C266), G270 (= G267), C303 (= C300), H350 (≠ Q347), K353 (≠ R350), F400 (= F401)
O94788 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Homo sapiens (Human) (see 6 papers)
43% identity, 96% coverage: 18:495/496 of query aligns to 38:513/518 of O94788
- E50 (≠ Q30) to G: in dbSNP:rs34266719
- A110 (= A89) to V: in dbSNP:rs35365164
- Q182 (≠ A161) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ VPW 163:165) binding
- KPAE 210:213 (= KPAE 189:192) binding
- STE 264:266 (= STE 243:245) binding
- C320 (= C300) active site, Nucleophile
- R347 (≠ W327) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ Q328) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ RQTAR 346:350) binding
- A383 (= A363) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E399) binding
- E436 (≠ Q418) to K: in dbSNP:rs34744827
- S461 (≠ A443) to Y: in DIH4; decreased retinoic acid biosynthetic process
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
43% identity, 96% coverage: 18:495/496 of query aligns to 12:487/492 of 6b5hA
- active site: N161 (= N166), E260 (= E265), C294 (= C300), E468 (≠ D476)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ I117), G116 (= G121), F162 (= F167), W169 (= W174), Q284 (≠ F290), F288 (= F294), T295 (≠ S301), N449 (≠ D457), L451 (= L459), N452 (≠ D460), F457 (= F465)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V162), I158 (≠ V163), W160 (= W165), N161 (= N166), K184 (= K189), G217 (= G222), G221 (= G226), F235 (= F240), T236 (= T241), G237 (= G242), S238 (= S243), V241 (= V246), E260 (= E265), L261 (≠ C266), C294 (= C300), F393 (= F401)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
43% identity, 96% coverage: 18:495/496 of query aligns to 12:487/492 of 6b5gA
- active site: N161 (= N166), E260 (= E265), C294 (= C300), E468 (≠ D476)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F167), L165 (≠ D170), W169 (= W174), F288 (= F294), C293 (≠ V299), C294 (= C300), T295 (≠ S301), N449 (≠ D457), L451 (= L459)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V162), I158 (≠ V163), P159 (= P164), W160 (= W165), N161 (= N166), M166 (= M171), K184 (= K189), E187 (= E192), G217 (= G222), G221 (= G226), F235 (= F240), T236 (= T241), G237 (= G242), S238 (= S243), V241 (= V246), E260 (= E265), L261 (≠ C266), C294 (= C300), E391 (= E399), F393 (= F401)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
43% identity, 96% coverage: 18:495/496 of query aligns to 12:487/492 of 6aljA
- active site: N161 (= N166), E260 (= E265), C294 (= C300), E468 (≠ D476)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (= G121), F162 (= F167), L165 (≠ D170), M166 (= M171), W169 (= W174), E260 (= E265), C293 (≠ V299), C294 (= C300), L451 (= L459), N452 (≠ D460), A453 (≠ V461)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V162), I158 (≠ V163), P159 (= P164), W160 (= W165), N161 (= N166), K184 (= K189), E187 (= E192), G217 (= G222), G221 (= G226), F235 (= F240), G237 (= G242), S238 (= S243), V241 (= V246), Q341 (= Q347), K344 (≠ R350), E391 (= E399), F393 (= F401)
Q63639 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Rattus norvegicus (Rat) (see paper)
43% identity, 96% coverage: 18:495/496 of query aligns to 38:513/518 of Q63639
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
45% identity, 97% coverage: 18:496/496 of query aligns to 11:489/494 of 4pz2B
- active site: N159 (= N166), K182 (= K189), E258 (= E265), C292 (= C300), E392 (= E399), D469 (= D476)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ V162), I156 (≠ V163), P157 (= P164), W158 (= W165), N159 (= N166), M164 (= M171), K182 (= K189), A184 (= A191), E185 (= E192), G215 (= G222), G219 (= G226), F233 (= F240), T234 (= T241), G235 (= G242), S236 (= S243), V239 (= V246), E258 (= E265), L259 (≠ C266), C292 (= C300), E392 (= E399), F394 (= F401)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
44% identity, 95% coverage: 18:490/496 of query aligns to 6:475/486 of 4pxlA
- active site: N154 (= N166), K177 (= K189), E253 (= E265), C287 (= C300), E384 (= E399), D461 (= D476)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ V162), V151 (= V163), P152 (= P164), W153 (= W165), K177 (= K189), E180 (= E192), G210 (= G222), G214 (= G226), A215 (≠ K227), F228 (= F240), G230 (= G242), S231 (= S243), V234 (= V246), E253 (= E265), G255 (= G267), C287 (= C300), Q334 (= Q347), K337 (≠ R350), E384 (= E399), F386 (= F401)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
41% identity, 98% coverage: 12:496/496 of query aligns to 11:491/491 of 5gtlA
- active site: N165 (= N166), K188 (= K189), E263 (= E265), C297 (= C300), E394 (= E399), E471 (≠ D476)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (≠ V162), P163 (= P164), K188 (= K189), A190 (= A191), E191 (= E192), Q192 (= Q193), G221 (= G222), G225 (= G226), G241 (= G242), S242 (= S243), T245 (≠ V246), L264 (≠ C266), C297 (= C300), E394 (= E399), F396 (= F401)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
41% identity, 98% coverage: 12:496/496 of query aligns to 11:491/491 of 5gtkA
- active site: N165 (= N166), K188 (= K189), E263 (= E265), C297 (= C300), E394 (= E399), E471 (≠ D476)
- binding nicotinamide-adenine-dinucleotide: I161 (≠ V162), I162 (≠ V163), P163 (= P164), W164 (= W165), K188 (= K189), E191 (= E192), G221 (= G222), G225 (= G226), A226 (≠ K227), F239 (= F240), G241 (= G242), S242 (= S243), T245 (≠ V246), Y248 (= Y249), L264 (≠ C266), C297 (= C300), Q344 (= Q347), R347 (= R350), E394 (= E399), F396 (= F401)
5ac0A Ovis aries aldehyde dehydrogenase 1a1 in complex with a duocarmycin analog (see paper)
42% identity, 97% coverage: 14:495/496 of query aligns to 9:489/494 of 5ac0A
- active site: N163 (= N166), K186 (= K189), E262 (= E265), C296 (= C300), E393 (= E399), E470 (≠ D476)
- binding 1-[(1S)-1-methyl-5-oxidanyl-1,2-dihydrobenzo[e]indol-3-yl]hexan-1-one: M114 (≠ I117), F164 (= F167), W171 (= W174), Y290 (≠ F294), C295 (≠ V299), C296 (= C300)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ V162), I160 (≠ V163), P161 (= P164), W162 (= W165), K186 (= K189), E189 (= E192), G219 (= G222), G223 (= G226), A224 (≠ K227), F237 (= F240), G239 (= G242), S240 (= S243), V243 (= V246), G264 (= G267), C296 (= C300), Q343 (= Q347), K346 (≠ R350), E393 (= E399)
5abmA Sheep aldehyde dehydrogenase 1a1 (see paper)
42% identity, 97% coverage: 14:495/496 of query aligns to 9:489/494 of 5abmA
- active site: N163 (= N166), K186 (= K189), E262 (= E265), C296 (= C300), E393 (= E399), E470 (≠ D476)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I159 (≠ V162), I160 (≠ V163), P161 (= P164), W162 (= W165), K186 (= K189), E189 (= E192), G219 (= G222), G223 (= G226), F237 (= F240), G239 (= G242), S240 (= S243), V243 (= V246), G264 (= G267), Q343 (= Q347), K346 (≠ R350), E393 (= E399), F395 (= F401)
1bxsA Sheep liver class 1 aldehyde dehydrogenase with NAD bound (see paper)
42% identity, 97% coverage: 14:495/496 of query aligns to 9:489/494 of 1bxsA
- active site: N163 (= N166), K186 (= K189), E262 (= E265), C296 (= C300), E393 (= E399), E470 (≠ D476)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ V162), I160 (≠ V163), P161 (= P164), W162 (= W165), K186 (= K189), E189 (= E192), G219 (= G222), G223 (= G226), F237 (= F240), G239 (= G242), S240 (= S243), V243 (= V246), L263 (≠ C266), C296 (= C300), Q343 (= Q347), K346 (≠ R350), E393 (= E399), F395 (= F401)
P51977 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Ovis aries (Sheep) (see 2 papers)
42% identity, 97% coverage: 14:495/496 of query aligns to 16:496/501 of P51977
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
41% identity, 97% coverage: 18:496/496 of query aligns to 20:496/501 of Q56YU0
- G152 (≠ A149) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A416) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
5l13A Structure of aldh2 in complex with 2p3 (see paper)
42% identity, 96% coverage: 16:490/496 of query aligns to 12:484/494 of 5l13A
- active site: N163 (= N166), K186 (= K189), E262 (= E265), C296 (= C300), E393 (= E399), E470 (≠ D476)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F167), M168 (= M171), W171 (= W174), F290 (= F294), C295 (≠ V299), C296 (= C300), C297 (≠ S301), D451 (= D457), F453 (≠ L459)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
42% identity, 96% coverage: 16:490/496 of query aligns to 12:484/494 of 4kwgA
- active site: N163 (= N166), K186 (= K189), E262 (= E265), C296 (= C300), E393 (= E399), E470 (≠ D476)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F167), M168 (= M171), C295 (≠ V299), C296 (= C300), C297 (≠ S301), D451 (= D457), F453 (≠ L459)
Query Sequence
>AO353_15035 AO353_15035 aldehyde dehydrogenase
VFELEYWQGQAAALQFPTQALIEGKQRPAQSGQTFAAINPATGAVLAEVAACGNADVDAA
VISARQAFESGVWSARSPGERKQVLLRLAELIMANREELALLDSLNMGKPVMDAYTIDVP
GAAGVFRWYAESLDKLYDQIAPSAQNVLATITREALGVVAAVVPWNFPLDMAAWKLAPAL
AAGNSVILKPAEQSPFSALRLGELALEAGVPPGVLNVLPGLGEQAGKALGLHLDIDCLVF
TGSTEVGKYFMQYSAQSNLKQVWLECGGKSANLVFADCQDLDLAAQKAAFGIFFNQGEVC
SANSRLLVERSIHDEFVERLMVQVERWQPGDPLDSSSTAGAIVDSRQTARIMKFIQQAER
QGAKRVCGGQQSIINGSDNFIQPTIFTGVTADMPLFRDEVFGPVLAVTAFDDEASALQLA
NDSVYGLAASLWTDDLNRAHRVARQLRAGTVSVNSVDALDVTVPFGGGKQSGFGRDLSLH
SFDKYTQLKTTWFQLR
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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