SitesBLAST
Comparing 15537 b1415 aldehyde dehydrogenase A, NAD-linked (NCBI) 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)
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)
100% identity, 100% coverage: 1:479/479 of query aligns to 1:479/479 of P25553
- M1 (= M1) modified: Initiator methionine, Removed
- L150 (= L150) binding
- R161 (= R161) binding
- KPSE 176:179 (= KPSE 176:179) binding
- F180 (= F180) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (= Q214) binding
- S230 (= S230) binding
- E251 (= E251) binding
- N286 (= N286) 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 (= R336) binding
- E443 (= E443) binding
- H449 (= H449) binding
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)
100% identity, 100% coverage: 3:479/479 of query aligns to 1:477/477 of 2impA
- active site: N151 (= N153), K174 (= K176), E249 (= E251), C283 (= C285), E381 (= E383), A458 (= A460)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I149), L148 (= L150), P149 (= P151), W150 (= W152), K174 (= K176), E177 (= E179), F178 (= F180), G207 (= G209), G211 (= G213), Q212 (= Q214), S228 (= S230), A231 (= A233), K234 (= K236), R334 (= R336)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
100% identity, 100% coverage: 3:479/479 of query aligns to 1:477/477 of 2iluA
- active site: N151 (= N153), K174 (= K176), E249 (= E251), C283 (= C285), E381 (= E383), A458 (= A460)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I149), L148 (= L150), P149 (= P151), W150 (= W152), K174 (= K176), S176 (= S178), E177 (= E179), R206 (= R208), G207 (= G209), G211 (= G213), Q212 (= Q214), S228 (= S230), A231 (= A233), K234 (= K236), I235 (= I237), N328 (= N330), R334 (= R336), F383 (= F385)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
99% identity, 100% coverage: 3:479/479 of query aligns to 1:477/477 of 2opxA
- active site: N151 (= N153), K174 (= K176), E249 (= E251), C283 (= C285), E381 (= E383), A458 (= A460)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (= F107), F152 (= F154), N284 (= N286), F312 (= F314), G313 (= G315), R318 (= R320), D320 (= D322), I321 (= I323), A322 (= A324), Y362 (= Y364), F440 (= F442), F440 (= F442), E441 (= E443)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
44% identity, 99% coverage: 6:477/479 of query aligns to 1:475/477 of 6j76A
- active site: N148 (= N153), E246 (= E251), C280 (= C285), E458 (≠ A460)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I149), T145 (≠ L150), A146 (≠ P151), W147 (= W152), N148 (= N153), K171 (= K176), T173 (≠ S178), S174 (≠ E179), G204 (= G209), G208 (= G213), T223 (= T228), G224 (= G229), S225 (= S230), A228 (= A233), S231 (≠ K236), I232 (= I237), E246 (= E251), L247 (= L252), C280 (= C285), E381 (= E383), F383 (= F385), H447 (= H449)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
39% identity, 98% coverage: 9:477/479 of query aligns to 5:475/494 of 5izdA
- active site: N149 (= N153), K172 (= K176), E247 (= E251), C281 (= C285), E381 (= E383), E458 (≠ A460)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I149), T146 (≠ L150), W148 (= W152), K172 (= K176), P173 (= P177), S174 (= S178), S175 (≠ E179), R204 (= R208), G205 (= G209), G209 (= G213), D210 (≠ Q214), G225 (= G229), S226 (= S230), T229 (≠ A233)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
39% identity, 97% coverage: 11:477/479 of query aligns to 14:479/481 of 3jz4A
- active site: N156 (= N153), K179 (= K176), E254 (= E251), C288 (= C285), E385 (= E383), E462 (≠ A460)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P151), W155 (= W152), K179 (= K176), A181 (≠ S178), S182 (≠ E179), A212 (≠ G209), G216 (= G213), G232 (= G229), S233 (= S230), I236 (≠ A233), C288 (= C285), K338 (≠ R336), E385 (= E383), F387 (= F385)
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)
39% identity, 97% coverage: 11:477/479 of query aligns to 15:480/482 of P25526
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
36% identity, 98% coverage: 10:479/479 of query aligns to 21:495/505 of 4neaA
- active site: N166 (= N153), K189 (= K176), E264 (= E251), C298 (= C285), E399 (= E383), E476 (≠ A460)
- binding nicotinamide-adenine-dinucleotide: P164 (= P151), K189 (= K176), E192 (= E179), G222 (= G209), G226 (= G213), G242 (= G229), G243 (≠ S230), T246 (≠ A233), H249 (≠ K236), I250 (= I237), C298 (= C285), E399 (= E383), F401 (= F385)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
36% identity, 96% coverage: 10:468/479 of query aligns to 4:460/482 of 5ek6A
- active site: N147 (= N153), K170 (= K176), E245 (= E251), C279 (= C285), E374 (= E383), E452 (≠ A460)
- binding 2-methylpropanal: I152 (≠ L158), K155 (≠ R161), T222 (= T228), E245 (= E251), F441 (≠ H449)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (= I149), T144 (≠ L150), W146 (= W152), N147 (= N153), I152 (≠ L158), K170 (= K176), A172 (≠ S178), S173 (≠ E179), P202 (≠ R208), G203 (= G209), G207 (= G213), F221 (≠ M227), T222 (= T228), G223 (= G229), E224 (≠ S230), T227 (≠ A233), I231 (= I237), E245 (= E251), L246 (= L252), C279 (= C285), E374 (= E383)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
36% identity, 96% coverage: 10:468/479 of query aligns to 4:460/482 of 4h73A
- active site: N147 (= N153), K170 (= K176), E245 (= E251), C279 (= C285), E374 (= E383), E452 (≠ A460)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (= I149), T144 (≠ L150), P145 (= P151), W146 (= W152), K170 (= K176), A172 (≠ S178), S173 (≠ E179), G203 (= G209), G207 (= G213), F221 (≠ M227), G223 (= G229), E224 (≠ S230), T227 (≠ A233)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
36% identity, 96% coverage: 10:468/479 of query aligns to 11:467/490 of 5ekcE
- active site: N154 (= N153), K177 (= K176), E252 (= E251), C286 (= C285), E381 (= E383), E459 (≠ A460)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (= I149), T151 (≠ L150), P152 (= P151), W153 (= W152), K177 (= K176), S180 (≠ E179), G210 (= G209), G214 (= G213), F228 (≠ M227), G230 (= G229), E231 (≠ S230), T234 (≠ A233), N331 (= N330), R333 (≠ A332), Q334 (≠ A333)
P77674 Gamma-aminobutyraldehyde dehydrogenase; ABALDH; 1-pyrroline dehydrogenase; 4-aminobutanal dehydrogenase; 5-aminopentanal dehydrogenase; EC 1.2.1.19; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
38% identity, 99% coverage: 5:478/479 of query aligns to 1:473/474 of P77674
1wndA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal structure (see paper)
38% identity, 99% coverage: 5:478/479 of query aligns to 1:473/474 of 1wndA
- active site: N149 (= N153), K172 (= K176), E246 (= E251), C280 (= C285), E378 (= E383), D455 (≠ A460)
- binding calcium ion: G249 (= G254), K250 (= K255), A251 (= A256), G405 (= G410), L406 (= L411), A407 (≠ T412), Y427 (≠ F432)
1wnbB Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
38% identity, 99% coverage: 5:478/479 of query aligns to 1:473/474 of 1wnbB
- active site: N149 (= N153), K172 (= K176), E246 (= E251), C280 (= C285), E378 (= E383), D455 (≠ A460)
- binding betaine aldehyde: D279 (≠ V284), F436 (≠ N441), L438 (≠ E443)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (= I149), A146 (≠ L150), W148 (= W152), K172 (= K176), G204 (= G209), G208 (= G213), D209 (≠ Q214), T223 (= T228), G224 (= G229), S225 (= S230), T228 (≠ A233), H231 (≠ K236), G248 (= G253), E378 (= E383)
1wnbA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
38% identity, 99% coverage: 5:478/479 of query aligns to 1:473/474 of 1wnbA
- active site: N149 (= N153), K172 (= K176), E246 (= E251), C280 (= C285), E378 (= E383), D455 (≠ A460)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (= I149), A146 (≠ L150), W148 (= W152), K172 (= K176), G204 (= G209), G208 (= G213), D209 (≠ Q214), G224 (= G229), S225 (= S230), T228 (≠ A233), H231 (≠ K236), G248 (= G253), F380 (= F385)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
37% identity, 97% coverage: 9:475/479 of query aligns to 13:484/494 of 4pz2B
- active site: N159 (= N153), K182 (= K176), E258 (= E251), C292 (= C285), E392 (= E383), D469 (≠ A460)
- binding nicotinamide-adenine-dinucleotide: I155 (= I149), I156 (≠ L150), P157 (= P151), W158 (= W152), N159 (= N153), M164 (≠ L158), K182 (= K176), A184 (≠ S178), E185 (= E179), G215 (= G209), G219 (= G213), F233 (≠ M227), T234 (= T228), G235 (= G229), S236 (= S230), V239 (≠ A233), E258 (= E251), L259 (= L252), C292 (= C285), E392 (= E383), F394 (= F385)
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, 98% coverage: 9:478/479 of query aligns to 25:496/503 of O14293
- S248 (= S230) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
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, 98% coverage: 9:478/479 of query aligns to 34:506/512 of P47895
- R89 (≠ E61) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K176) binding
- E207 (= E179) binding
- GSTEVG 257:262 (≠ GSVSAG 229:234) binding
- Q361 (≠ A333) binding
- E411 (= E383) binding
- A493 (≠ G465) 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
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
33% identity, 98% coverage: 9:478/479 of query aligns to 16:488/489 of 7a6qB
- active site: N163 (= N153), E262 (= E251), C296 (= C285), E470 (≠ A460)
- binding nicotinamide-adenine-dinucleotide: I159 (= I149), W162 (= W152), K186 (= K176), E189 (= E179), G219 (= G209), G223 (= G213), S240 (= S230), V243 (≠ A233), K342 (≠ A332)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (≠ D25), T33 (≠ V26), C34 (≠ V27), P36 (= P29), D103 (≠ E92), E189 (= E179), Q190 (≠ F180), F218 (≠ R208), I339 (= I329), D340 (≠ N330)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ F107), D141 (= D130), N143 (= N135), N451 (= N441), L453 (≠ E443), A455 (≠ M445)
Query Sequence
>15537 b1415 aldehyde dehydrogenase A, NAD-linked (NCBI)
MSVPVQHPMYIDGQFVTWRGDAWIDVVNPATEAVISRIPDGQAEDARKAIDAAERAQPEW
EALPAIERASWLRKISAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWAR
RYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEF
TPNNAIAFAKIVDEIGLPRGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAT
AAKNITKVCLELGGKAPAIVMDDADLELAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ
FVNRLGEAMQAVQFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVAFGGKAVEG
KGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEDAISMANDSDYGLTSSIYTQNL
NVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQS
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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