SitesBLAST
Comparing BPHYT_RS09875 BPHYT_RS09875 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)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
45% identity, 99% coverage: 7:480/481 of query aligns to 8:476/477 of 2opxA
- active site: N151 (= N154), K174 (≠ R177), E249 (= E251), C283 (= C285), E381 (= E385), A458 (≠ D462)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y108), F152 (≠ Y155), N284 (≠ T286), F312 (≠ S314), G313 (= G315), R318 (≠ Q320), D320 (≠ S322), I321 (≠ L323), A322 (vs. gap), Y362 (≠ F366), F440 (≠ A444), F440 (≠ A444), E441 (≠ D445)
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
45% identity, 99% coverage: 7:480/481 of query aligns to 10:478/479 of P25553
- L150 (≠ I151) binding
- R161 (= R162) binding
- KPSE 176:179 (≠ RPSN 177:180) binding
- F180 (≠ N181) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ E214) binding
- S230 (= S230) binding
- E251 (= E251) binding
- N286 (≠ T286) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (≠ S335) binding
- E443 (≠ D445) binding
- H449 (= H451) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
45% identity, 99% coverage: 7:480/481 of query aligns to 8:476/477 of 2impA
- active site: N151 (= N154), K174 (≠ R177), E249 (= E251), C283 (= C285), E381 (= E385), A458 (≠ D462)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (≠ L150), L148 (≠ I151), P149 (= P152), W150 (≠ F153), K174 (≠ R177), E177 (≠ N180), F178 (≠ N181), G207 (≠ N209), G211 (≠ A213), Q212 (≠ E214), S228 (= S230), A231 (= A233), K234 (= K236), R334 (≠ S335)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
45% identity, 99% coverage: 7:480/481 of query aligns to 8:476/477 of 2iluA
- active site: N151 (= N154), K174 (≠ R177), E249 (= E251), C283 (= C285), E381 (= E385), A458 (≠ D462)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (≠ L150), L148 (≠ I151), P149 (= P152), W150 (≠ F153), K174 (≠ R177), S176 (= S179), E177 (≠ N180), R206 (≠ M208), G207 (≠ N209), G211 (≠ A213), Q212 (≠ E214), S228 (= S230), A231 (= A233), K234 (= K236), I235 (≠ V237), N328 (= N329), R334 (≠ S335), F383 (= F387)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
37% identity, 99% coverage: 7:481/481 of query aligns to 5:477/477 of 6j76A
- active site: N148 (= N154), E246 (= E251), C280 (= C285), E458 (≠ D462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (≠ L150), T145 (≠ I151), A146 (≠ P152), W147 (≠ F153), N148 (= N154), K171 (≠ R177), T173 (≠ S179), S174 (≠ N180), G204 (≠ H210), G208 (≠ A213), T223 (= T228), G224 (= G229), S225 (= S230), A228 (= A233), S231 (≠ K236), I232 (≠ V237), E246 (= E251), L247 (= L252), C280 (= C285), E381 (= E385), F383 (= F387), H447 (= H451)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
33% identity, 99% coverage: 7:481/481 of query aligns to 6:477/494 of 5izdA
- active site: N149 (= N154), K172 (≠ R177), E247 (= E251), C281 (= C285), E381 (= E385), E458 (≠ D462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (= L150), T146 (≠ I151), W148 (≠ F153), K172 (≠ R177), P173 (= P178), S174 (= S179), S175 (≠ N180), R204 (≠ M208), G205 (≠ N209), G209 (≠ A213), D210 (≠ E214), G225 (= G229), S226 (= S230), T229 (≠ A233)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
34% identity, 98% coverage: 9:479/481 of query aligns to 15:479/481 of 3jz4A
- active site: N156 (= N154), K179 (≠ R177), E254 (= E251), C288 (= C285), E385 (= E385), E462 (≠ D462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P152), W155 (≠ F153), K179 (≠ R177), A181 (≠ S179), S182 (≠ N180), A212 (vs. gap), G216 (≠ A213), G232 (= G229), S233 (= S230), I236 (≠ A233), C288 (= C285), K338 (≠ S335), E385 (= E385), F387 (= F387)
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, 97% coverage: 10:477/481 of query aligns to 24:493/503 of O14293
- S248 (= S230) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
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)
35% identity, 96% coverage: 18:480/481 of query aligns to 48:512/518 of Q63639
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)
33% identity, 98% coverage: 9:479/481 of query aligns to 16:480/482 of P25526
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
35% identity, 96% coverage: 18:480/481 of query aligns to 22:486/492 of 6b5hA
- active site: N161 (= N154), E260 (= E251), C294 (= C285), E468 (≠ D462)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ A109), G116 (vs. gap), F162 (≠ Y155), W169 (≠ R162), Q284 (≠ A275), F288 (≠ T279), T295 (= T286), N449 (≠ P443), L451 (≠ D445), N452 (≠ P446), F457 (≠ H451)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ L150), I158 (= I151), W160 (≠ F153), N161 (= N154), K184 (≠ R177), G217 (≠ H210), G221 (vs. gap), F235 (≠ L227), T236 (= T228), G237 (= G229), S238 (= S230), V241 (≠ A233), E260 (= E251), L261 (= L252), C294 (= C285), F393 (= F387)
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)
35% identity, 96% coverage: 18:480/481 of query aligns to 22:486/492 of 6b5gA
- active site: N161 (= N154), E260 (= E251), C294 (= C285), E468 (≠ D462)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ Y155), L165 (≠ Y158), W169 (≠ R162), F288 (≠ T279), C293 (≠ L284), C294 (= C285), T295 (= T286), N449 (≠ P443), L451 (≠ D445)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ L150), I158 (= I151), P159 (= P152), W160 (≠ F153), N161 (= N154), M166 (≠ T159), K184 (≠ R177), E187 (≠ N180), G217 (≠ H210), G221 (vs. gap), F235 (≠ L227), T236 (= T228), G237 (= G229), S238 (= S230), V241 (≠ A233), E260 (= E251), L261 (= L252), C294 (= C285), E391 (= E385), F393 (= F387)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
35% identity, 96% coverage: 18:480/481 of query aligns to 22:486/492 of 6aljA
- active site: N161 (= N154), E260 (= E251), C294 (= C285), E468 (≠ D462)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (vs. gap), F162 (≠ Y155), L165 (≠ Y158), M166 (≠ T159), W169 (≠ R162), E260 (= E251), C293 (≠ L284), C294 (= C285), L451 (≠ D445), N452 (≠ P446), A453 (≠ Y447)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ L150), I158 (= I151), P159 (= P152), W160 (≠ F153), N161 (= N154), K184 (≠ R177), E187 (≠ N180), G217 (≠ H210), G221 (vs. gap), F235 (≠ L227), G237 (= G229), S238 (= S230), V241 (≠ A233), Q341 (≠ S332), K344 (≠ S335), E391 (= E385), F393 (= F387)
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)
35% identity, 96% coverage: 18:480/481 of query aligns to 48:512/518 of O94788
- E50 (≠ A20) to G: in dbSNP:rs34266719
- A110 (= A77) to V: in dbSNP:rs35365164
- Q182 (≠ C149) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ IPF 151:153) binding
- KPAE 210:213 (≠ RPSN 177:180) binding
- STE 264:266 (≠ SVG 230:232) binding
- C320 (= C285) active site, Nucleophile
- R347 (≠ V312) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ E313) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ ASRQS 331:335) binding
- A383 (= A348) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E385) binding
- E436 (= E404) to K: in dbSNP:rs34744827
- S461 (≠ A429) to Y: in DIH4; decreased retinoic acid biosynthetic process
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
33% identity, 100% coverage: 1:480/481 of query aligns to 11:488/489 of 7a6qB
- active site: N163 (= N154), E262 (= E251), C296 (= C285), E470 (≠ D462)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ L150), W162 (≠ F153), K186 (≠ R177), E189 (≠ N180), G219 (≠ N209), G223 (≠ A213), S240 (= S230), V243 (≠ A233), K342 (≠ A331)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (= A26), T33 (≠ V27), C34 (= C28), P36 (= P30), D103 (≠ E94), E189 (≠ N180), Q190 (≠ N181), F218 (≠ M208), I339 (≠ V328), D340 (≠ N329)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ A109), D141 (= D131), N143 (= N136), N451 (≠ P443), L453 (≠ D445), A455 (≠ Y447)
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
33% identity, 100% coverage: 1:480/481 of query aligns to 11:488/489 of 7a6qA
- active site: N163 (= N154), E262 (= E251), C296 (= C285), E470 (≠ D462)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ L150), T160 (≠ I151), W162 (≠ F153), K186 (≠ R177), A188 (≠ S179), E189 (≠ N180), G219 (≠ N209), G223 (≠ A213), S240 (= S230), V243 (≠ A233), K342 (≠ A331), K346 (≠ S335)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ A109), D141 (= D131), N143 (= N136), N451 (≠ P443), L453 (≠ D445), Y454 (≠ P446)
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
33% identity, 100% coverage: 1:480/481 of query aligns to 11:488/489 of 5fhzA
- active site: N163 (= N154), K186 (≠ R177), E262 (= E251), C296 (= C285), E393 (= E385), E470 (≠ D462)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ L150), T160 (≠ I151), W162 (≠ F153), K186 (≠ R177), E189 (≠ N180), G219 (≠ N209), G223 (≠ A213), F237 (≠ L227), G239 (= G229), S240 (= S230), T241 (≠ V231), V243 (≠ A233), G264 (= G253), Q343 (≠ S332), E393 (= E385)
- binding retinoic acid: G118 (≠ A109), R121 (≠ Q111), F164 (≠ Y155), M168 (≠ T159), W171 (≠ R162), C295 (≠ L284), C296 (= C285), L453 (≠ D445)
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
33% identity, 100% coverage: 1:480/481 of query aligns to 10:487/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (≠ L150), T159 (≠ I151), P160 (= P152), W161 (≠ F153), K185 (≠ R177), E188 (≠ N180), G218 (≠ N209), G222 (≠ A213), F236 (≠ L227), S239 (= S230), V242 (≠ A233)
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)
33% identity, 100% coverage: 1:480/481 of query aligns to 29:506/512 of P47895
- R89 (= R62) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (≠ R177) binding
- E207 (≠ N180) binding
- GSTEVG 257:262 (≠ GSVGAG 229:234) binding
- Q361 (≠ S332) binding
- E411 (= E385) binding
- A493 (≠ G467) 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)
33% identity, 100% coverage: 1:480/481 of query aligns to 3:477/478 of 6tgwA
- active site: N155 (= N154), E254 (= E251), C288 (= C285), E459 (≠ D462)
- binding methyl 5-(1,3-benzodioxol-5-yl)-2-phenyl-pyrazolo[1,5-a]pyrimidine-7-carboxylate: I106 (≠ E105), G110 (≠ A109), F156 (≠ Y155), Q278 (≠ A275), F282 (≠ T279), L442 (≠ D445), A444 (≠ Y447)
- binding nicotinamide-adenine-dinucleotide: I151 (≠ L150), T152 (≠ I151), P153 (= P152), W154 (≠ F153), K178 (≠ R177), G211 (≠ N209), G215 (≠ A213), F229 (≠ L227), G231 (= G229), S232 (= S230), V235 (≠ A233)
Query Sequence
>BPHYT_RS09875 BPHYT_RS09875 aldehyde dehydrogenase
MRLDRNFANGRFIEPAADTASRELIAVCNPATEAVIAHVTGATQAEVIAAVDAAAVAQKG
WRKLPQAERAVYLHKLADALTECAPAIGAALALESGKSVADATNEAIYASQITRYHAEWA
RRIEGEVIPSDAPDENLVLHREPIGVVACLIPFNYPVYTFMRKVAPALIAGNTVVVRPSN
NTPTSAFEIAKAVEKAGLPAGVVNILAMNHATAEVLCTHPKVGMITLTGSVGAGRKVLDY
CKANIAKPSLELGGKTPAIIEADADLEKAARDLVASKTTHCGQLCTAIERVYVQESVHDR
FVALLKKHMSAVESGDRSEQPSLMGPLVNEASRQSIHAMVERAVAAGATLETGGKLPTPG
QGKGFFYPATLLSNCRQDMEIIQEETFGPVMPVVKYRTLDEALEMANDHQFGLSSVLYTE
NYRGAMKVANGIEAGELYVNRTPADPYQGFHAGWKRSGLGGDDGKHGMLEFTQTRLVVMK
Y
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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