SitesBLAST
Comparing HSERO_RS11260 HSERO_RS11260 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)
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
75% identity, 100% coverage: 3:477/477 of query aligns to 2:476/476 of 4yweA
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 99% coverage: 3:475/477 of query aligns to 18:489/491 of 5gtlA
- active site: N165 (= N148), K188 (= K171), E263 (= E246), C297 (= C280), E394 (= E379), E471 (= E457)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I144), P163 (= P146), K188 (= K171), A190 (= A173), E191 (= E174), Q192 (≠ D175), G221 (= G204), G225 (= G208), G241 (= G224), S242 (= S225), T245 (≠ V228), L264 (= L247), C297 (= C280), E394 (= E379), F396 (= F381)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 99% coverage: 3:475/477 of query aligns to 18:489/491 of 5gtkA
- active site: N165 (= N148), K188 (= K171), E263 (= E246), C297 (= C280), E394 (= E379), E471 (= E457)
- binding nicotinamide-adenine-dinucleotide: I161 (= I144), I162 (≠ V145), P163 (= P146), W164 (= W147), K188 (= K171), E191 (= E174), G221 (= G204), G225 (= G208), A226 (≠ D209), F239 (= F222), G241 (= G224), S242 (= S225), T245 (≠ V228), Y248 (≠ L231), L264 (= L247), C297 (= C280), Q344 (= Q326), R347 (= R329), E394 (= E379), F396 (= F381)
7radA Crystal structure analysis of aldh1b1
41% identity, 99% coverage: 2:475/477 of query aligns to 13:487/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I144), I159 (≠ V145), P160 (= P146), W161 (= W147), N162 (= N148), M167 (≠ I153), K185 (= K171), E188 (= E174), G218 (= G204), G222 (= G208), A223 (≠ D209), T237 (= T223), G238 (= G224), S239 (= S225), V242 (= V228), E261 (= E246), L262 (= L247), C295 (= C280), E392 (= E379), F394 (= F381)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ A103), F163 (≠ Y149), E285 (≠ N270), F289 (≠ Q274), N450 (≠ G437), V452 (≠ G440)
7mjdA Crystal structure analysis of aldh1b1
41% identity, 99% coverage: 2:475/477 of query aligns to 13:487/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I144), I159 (≠ V145), P160 (= P146), W161 (= W147), N162 (= N148), M167 (≠ I153), K185 (= K171), E188 (= E174), G218 (= G204), G222 (= G208), F236 (= F222), T237 (= T223), G238 (= G224), S239 (= S225), V242 (= V228), E261 (= E246), L262 (= L247), C295 (= C280), E392 (= E379), F394 (= F381)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ A103), E285 (≠ N270), F289 (≠ Q274), N450 (≠ G437), V452 (≠ G440)
7mjcA Crystal structure analysis of aldh1b1
41% identity, 99% coverage: 2:475/477 of query aligns to 13:487/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I144), I159 (≠ V145), P160 (= P146), W161 (= W147), N162 (= N148), K185 (= K171), E188 (= E174), G218 (= G204), G222 (= G208), T237 (= T223), G238 (= G224), S239 (= S225), V242 (= V228), E261 (= E246), L262 (= L247), C295 (= C280), E392 (= E379), F394 (= F381)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
42% identity, 98% coverage: 5:472/477 of query aligns to 9:476/486 of 4pxlA
- active site: N154 (= N148), K177 (= K171), E253 (= E246), C287 (= C280), E384 (= E379), D461 (≠ E457)
- binding nicotinamide-adenine-dinucleotide: I150 (= I144), V151 (= V145), P152 (= P146), W153 (= W147), K177 (= K171), E180 (= E174), G210 (= G204), G214 (= G208), A215 (≠ D209), F228 (= F222), G230 (= G224), S231 (= S225), V234 (= V228), E253 (= E246), G255 (= G248), C287 (= C280), Q334 (= Q326), K337 (≠ R329), E384 (= E379), F386 (= F381)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
43% identity, 98% coverage: 5:472/477 of query aligns to 14:484/494 of 4pz2B
- active site: N159 (= N148), K182 (= K171), E258 (= E246), C292 (= C280), E392 (= E379), D469 (≠ E457)
- binding nicotinamide-adenine-dinucleotide: I155 (= I144), I156 (≠ V145), P157 (= P146), W158 (= W147), N159 (= N148), M164 (≠ I153), K182 (= K171), A184 (= A173), E185 (= E174), G215 (= G204), G219 (= G208), F233 (= F222), T234 (= T223), G235 (= G224), S236 (= S225), V239 (= V228), E258 (= E246), L259 (= L247), C292 (= C280), E392 (= E379), F394 (= F381)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
42% identity, 99% coverage: 3:474/477 of query aligns to 5:477/489 of 4o6rA
- active site: N150 (= N148), K173 (= K171), E248 (= E246), C282 (= C280), E383 (= E379), E460 (= E457)
- binding adenosine monophosphate: I146 (= I144), V147 (= V145), K173 (= K171), G206 (= G204), G210 (= G208), Q211 (≠ D209), F224 (= F222), G226 (= G224), S227 (= S225), T230 (≠ V228), R233 (≠ L231)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
41% identity, 99% coverage: 2:474/477 of query aligns to 3:475/487 of 4go4A
- active site: N149 (= N148), K172 (= K171), E247 (= E246), C281 (= C280), E381 (= E379), E458 (= E457)
- binding nicotinamide-adenine-dinucleotide: I145 (= I144), V146 (= V145), W148 (= W147), N149 (= N148), F154 (≠ I153), K172 (= K171), G205 (= G204), G209 (= G208), Q210 (≠ D209), F223 (= F222), T224 (= T223), G225 (= G224), S226 (= S225), T229 (≠ V228), E247 (= E246), G249 (= G248), C281 (= C280), E381 (= E379), F383 (= F381)
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)
39% identity, 99% coverage: 5:475/477 of query aligns to 41:512/518 of O94788
- E50 (≠ T14) to G: in dbSNP:rs34266719
- A110 (= A72) to V: in dbSNP:rs35365164
- Q182 (≠ H143) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ VPW 145:147) binding
- KPAE 210:213 (= KPAE 171:174) binding
- STE 264:266 (≠ SPN 225:227) binding
- C320 (= C280) active site, Nucleophile
- R347 (≠ L307) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ Q308) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ TQQER 325:329) binding
- A383 (≠ I342) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E379) binding
- E436 (≠ A398) to K: in dbSNP:rs34744827
- S461 (≠ A423) 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)
39% identity, 99% coverage: 5:475/477 of query aligns to 15:486/492 of 6b5hA
- active site: N161 (= N148), E260 (= E246), C294 (= C280), E468 (= E457)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ A99), G116 (≠ A103), F162 (≠ Y149), W169 (≠ R156), Q284 (≠ N270), F288 (≠ Q274), T295 (≠ S281), N449 (≠ G437), L451 (≠ G439), N452 (≠ G440), F457 (= F446)
- binding nicotinamide-adenine-dinucleotide: I157 (= I144), I158 (≠ V145), W160 (= W147), N161 (= N148), K184 (= K171), G217 (= G204), G221 (= G208), F235 (= F222), T236 (= T223), G237 (= G224), S238 (= S225), V241 (= V228), E260 (= E246), L261 (= L247), C294 (= C280), F393 (= F381)
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)
39% identity, 99% coverage: 5:475/477 of query aligns to 15:486/492 of 6b5gA
- active site: N161 (= N148), E260 (= E246), C294 (= C280), E468 (= E457)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ Y149), L165 (≠ Q152), W169 (≠ R156), F288 (≠ Q274), C293 (≠ T279), C294 (= C280), T295 (≠ S281), N449 (≠ G437), L451 (≠ G439)
- binding nicotinamide-adenine-dinucleotide: I157 (= I144), I158 (≠ V145), P159 (= P146), W160 (= W147), N161 (= N148), M166 (≠ I153), K184 (= K171), E187 (= E174), G217 (= G204), G221 (= G208), F235 (= F222), T236 (= T223), G237 (= G224), S238 (= S225), V241 (= V228), E260 (= E246), L261 (= L247), C294 (= C280), E391 (= E379), F393 (= F381)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
39% identity, 99% coverage: 5:475/477 of query aligns to 15:486/492 of 6aljA
- active site: N161 (= N148), E260 (= E246), C294 (= C280), E468 (= E457)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ A103), F162 (≠ Y149), L165 (≠ Q152), M166 (≠ I153), W169 (≠ R156), E260 (= E246), C293 (≠ T279), C294 (= C280), L451 (≠ G439), N452 (≠ G440), A453 (≠ G441)
- binding nicotinamide-adenine-dinucleotide: I157 (= I144), I158 (≠ V145), P159 (= P146), W160 (= W147), N161 (= N148), K184 (= K171), E187 (= E174), G217 (= G204), G221 (= G208), F235 (= F222), G237 (= G224), S238 (= S225), V241 (= V228), Q341 (= Q326), K344 (≠ R329), E391 (= E379), F393 (= F381)
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)
39% identity, 99% coverage: 5:475/477 of query aligns to 41:512/518 of Q63639
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)
38% identity, 99% coverage: 5:474/477 of query aligns to 23:493/501 of Q56YU0
- G152 (= G128) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A396) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
38% identity, 99% coverage: 2:475/477 of query aligns to 13:487/493 of 4fr8A
- active site: N162 (= N148), K185 (= K171), Q261 (≠ E246), C295 (= C280), E392 (= E379), E469 (= E457)
- binding nicotinamide-adenine-dinucleotide: I158 (= I144), I159 (≠ V145), W161 (= W147), K185 (= K171), G218 (= G204), G222 (= G208), A223 (≠ D209), F236 (= F222), G238 (= G224), S239 (= S225), I242 (≠ V228), Q342 (= Q326), K345 (≠ R329), E392 (= E379), F394 (= F381)
- binding propane-1,2,3-triyl trinitrate: F163 (≠ Y149), L166 (≠ Q152), W170 (≠ R156), F289 (≠ Q274), S294 (≠ T279), C295 (= C280), D450 (≠ G437), F452 (≠ G439)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
38% identity, 99% coverage: 2:475/477 of query aligns to 16:490/496 of 4fr8C
- active site: N165 (= N148), K188 (= K171), Q264 (≠ E246), C298 (= C280), E395 (= E379), E472 (= E457)
- binding nicotinamide-adenine-dinucleotide: I161 (= I144), I162 (≠ V145), W164 (= W147), K188 (= K171), G221 (= G204), G225 (= G208), A226 (≠ D209), F239 (= F222), G241 (= G224), S242 (= S225), I245 (≠ V228), Q345 (= Q326), E395 (= E379), F397 (= F381)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
38% identity, 99% coverage: 2:475/477 of query aligns to 14:488/494 of 5l13A
- active site: N163 (= N148), K186 (= K171), E262 (= E246), C296 (= C280), E393 (= E379), E470 (= E457)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (≠ Y149), M168 (≠ I153), W171 (≠ R156), F290 (≠ Q274), C295 (≠ T279), C296 (= C280), C297 (≠ S281), D451 (≠ G437), F453 (≠ G439)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
38% identity, 99% coverage: 2:475/477 of query aligns to 14:488/494 of 4kwgA
- active site: N163 (= N148), K186 (= K171), E262 (= E246), C296 (= C280), E393 (= E379), E470 (= E457)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (≠ Y149), M168 (≠ I153), C295 (≠ T279), C296 (= C280), C297 (≠ S281), D451 (≠ G437), F453 (≠ G439)
Query Sequence
>HSERO_RS11260 HSERO_RS11260 aldehyde dehydrogenase
MKQHFIANRWVAPTSGESIPVLDPSDGQPFDAIARGNATDIDQAVRAARLAYEGAWGRLS
AAERSRLLMKLAYKLQDHQEELAQLEGRDCGKPMKQARADAAAIVRYFEFYAGAADKLHG
DTIPYQAGYTVLTLREPHGVTGHIVPWNYPMQIFGRCVGGALAAGNTCVVKPAEDACLSI
LRVAELAAEVGFPEGALNIVTGYGHEAGDLLVKHPDVNHISFTGSPNVGKLVVRAAAEHH
TPVTLELGGKSPQIVFEDADMEAMLPVVVNAIVQNAGQTCSAGSRLLVQRGAYEQVLERL
SGLFSQLQVGSSQMDLDCGPLIRKTQQERVAGFLSDAQRDGIALAAQGKIAAGVPTGGFY
QAPALLRDVPPRHRLAQEEVFGPVLAAMPFEDEAHAIALANGTDYGLVASVWTRDGGRQM
RLARAIRSGQVFINNYGAGGGVELPFGGVKASGHGREKGFEALYGFTVLKTIAIRHG
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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