SitesBLAST
Comparing Pf6N2E2_1751 Aldehyde dehydrogenase A (EC 1.2.1.22) / Glycolaldehyde dehydrogenase (EC 1.2.1.21) 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
59% identity, 98% coverage: 9:477/477 of query aligns to 8:477/477 of 2opxA
- active site: N151 (= N150), K174 (= K173), E249 (= E248), C283 (= C282), E381 (= E381), A458 (= A458)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (= F104), F152 (= F151), N284 (= N283), F312 (≠ Y311), G313 (= G312), R318 (≠ E317), D320 (≠ G319), I321 (≠ L320), A322 (≠ D321), Y362 (≠ H362), F440 (= F440), F440 (= F440), E441 (= E441)
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)
58% identity, 98% coverage: 9:477/477 of query aligns to 8:477/477 of 2impA
- active site: N151 (= N150), K174 (= K173), E249 (= E248), C283 (= C282), E381 (= E381), A458 (= A458)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I146), L148 (= L147), P149 (= P148), W150 (= W149), K174 (= K173), E177 (= E176), F178 (≠ E177), G207 (= G206), G211 (= G210), Q212 (≠ H211), S228 (= S227), A231 (≠ T230), K234 (≠ R233), R334 (≠ K333)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
58% identity, 98% coverage: 9:477/477 of query aligns to 8:477/477 of 2iluA
- active site: N151 (= N150), K174 (= K173), E249 (= E248), C283 (= C282), E381 (= E381), A458 (= A458)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I146), L148 (= L147), P149 (= P148), W150 (= W149), K174 (= K173), S176 (= S175), E177 (= E176), R206 (≠ T205), G207 (= G206), G211 (= G210), Q212 (≠ H211), S228 (= S227), A231 (≠ T230), K234 (≠ R233), I235 (= I234), N328 (= N327), R334 (≠ K333), F383 (= F383)
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)
58% identity, 98% coverage: 9:477/477 of query aligns to 10:479/479 of P25553
- L150 (= L147) binding
- R161 (= R158) binding
- KPSE 176:179 (= KPSE 173:176) binding
- F180 (≠ E177) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ H211) binding
- S230 (= S227) binding
- E251 (= E248) binding
- N286 (= N283) 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 (≠ K333) binding
- E443 (= E441) binding
- H449 (= H447) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
40% identity, 99% coverage: 6:475/477 of query aligns to 2:475/477 of 6j76A
- active site: N148 (= N150), E246 (= E248), C280 (= C282), E458 (≠ A458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I146), T145 (≠ L147), A146 (≠ P148), W147 (= W149), N148 (= N150), K171 (= K173), T173 (≠ S175), S174 (≠ E176), G204 (= G206), G208 (= G210), T223 (= T225), G224 (= G226), S225 (= S227), A228 (≠ T230), S231 (≠ R233), I232 (= I234), E246 (= E248), L247 (= L249), C280 (= C282), E381 (= E381), F383 (= F383), H447 (= H447)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
37% identity, 98% coverage: 9:475/477 of query aligns to 6:475/494 of 5izdA
- active site: N149 (= N150), K172 (= K173), E247 (= E248), C281 (= C282), E381 (= E381), E458 (≠ A458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I146), T146 (≠ L147), W148 (= W149), K172 (= K173), P173 (= P174), S174 (= S175), S175 (≠ E176), R204 (≠ T205), G205 (= G206), G209 (= G210), D210 (≠ H211), G225 (= G226), S226 (= S227), T229 (= T230)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
38% identity, 96% coverage: 19:475/477 of query aligns to 25:479/481 of 3jz4A
- active site: N156 (= N150), K179 (= K173), E254 (= E248), C288 (= C282), E385 (= E381), E462 (≠ A458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P148), W155 (= W149), K179 (= K173), A181 (≠ S175), S182 (≠ E176), A212 (≠ G206), G216 (= G210), G232 (= G226), S233 (= S227), I236 (≠ T230), C288 (= C282), K338 (= K333), E385 (= E381), F387 (= F383)
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)
38% identity, 96% coverage: 19:475/477 of query aligns to 26:480/482 of P25526
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
35% identity, 95% coverage: 20:473/477 of query aligns to 24:482/497 of P17202
- I28 (≠ H24) binding
- D96 (≠ E90) binding
- SPW 156:158 (≠ LPW 147:149) binding
- Y160 (≠ F151) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R158) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 173:176) binding
- L186 (≠ E177) binding
- SSAT 236:239 (≠ SVGT 227:230) binding
- V251 (≠ I242) binding in other chain
- L258 (= L249) binding
- W285 (≠ I276) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E381) binding
- A441 (≠ E432) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ E441) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ H447) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ R451) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
35% identity, 95% coverage: 20:473/477 of query aligns to 22:480/495 of 4v37A
- active site: N157 (= N150), K180 (= K173), E255 (= E248), A289 (≠ C282), E388 (= E381), E465 (≠ A458)
- binding 3-aminopropan-1-ol: C448 (≠ E441), W454 (≠ H447)
- binding nicotinamide-adenine-dinucleotide: I153 (= I146), S154 (≠ L147), P155 (= P148), W156 (= W149), N157 (= N150), M162 (≠ L155), K180 (= K173), S182 (= S175), E183 (= E176), G213 (= G206), G217 (= G210), A218 (≠ H211), T232 (= T225), G233 (= G226), S234 (= S227), T237 (= T230), E255 (= E248), L256 (= L249), A289 (≠ C282), E388 (= E381), F390 (= F383)
4npiA 1.94 angstroms x-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
37% identity, 98% coverage: 8:476/477 of query aligns to 5:482/483 of 4npiA
- active site: N152 (= N150), K175 (= K173), E251 (= E248), C285 (= C282), E387 (= E381), E464 (≠ A458)
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R99), L157 (= L155), W160 (≠ R158), E251 (= E248), C285 (= C282), Y445 (≠ N439), R447 (≠ E441), F453 (≠ H447)
- binding nicotinamide-adenine-dinucleotide: I148 (= I146), S149 (≠ L147), P150 (= P148), W151 (= W149), K175 (= K173), E178 (= E176), G208 (= G206), G213 (= G210), E214 (≠ H211), F227 (= F224), G229 (= G226), E230 (≠ S227), T233 (= T230), G253 (= G250), C285 (= C282), K335 (= K333), E387 (= E381), F389 (= F383)
4i2rA 2.15 angstroms x-ray crystal structure of NAD- and alternative substrate-bound 2-aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
37% identity, 98% coverage: 8:476/477 of query aligns to 5:482/483 of 4i2rA
- active site: N152 (= N150), K175 (= K173), E251 (= E248), C285 (= C282), E387 (= E381), E464 (≠ A458)
- binding (2E,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R99), L157 (= L155), C285 (= C282), Y445 (≠ N439), R447 (≠ E441), F453 (≠ H447)
- binding nicotinamide-adenine-dinucleotide: I148 (= I146), S149 (≠ L147), W151 (= W149), N152 (= N150), K175 (= K173), E178 (= E176), G208 (= G206), F227 (= F224), T228 (= T225), G229 (= G226), E230 (≠ S227), T233 (= T230), E251 (= E248), L252 (= L249), G253 (= G250), C285 (= C282), E387 (= E381), F389 (= F383)
4i25A 2.00 angstroms x-ray crystal structure of NAD- and substrate-bound 2- aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
37% identity, 98% coverage: 8:476/477 of query aligns to 5:482/483 of 4i25A
- active site: N152 (= N150), K175 (= K173), E251 (= E248), C285 (= C282), E387 (= E381), E464 (≠ A458)
- binding (2E,4E)-2-amino-6-oxohexa-2,4-dienoic acid: R103 (= R99), L157 (= L155), C285 (= C282), Y445 (≠ N439), R447 (≠ E441), F453 (≠ H447)
- binding nicotinamide-adenine-dinucleotide: I148 (= I146), S149 (≠ L147), P150 (= P148), W151 (= W149), N152 (= N150), K175 (= K173), E178 (= E176), G208 (= G206), G213 (= G210), F227 (= F224), T228 (= T225), G229 (= G226), E230 (≠ S227), T233 (= T230), E251 (= E248), L252 (= L249), C285 (= C282), E387 (= E381), F389 (= F383)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
37% identity, 98% coverage: 9:476/477 of query aligns to 9:481/489 of 4cazA
- active site: N152 (= N150), K175 (= K173), E251 (= E248), C285 (= C282), E386 (= E381), E463 (≠ A458)
- 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: I148 (= I146), G149 (≠ L147), W151 (= W149), N152 (= N150), K175 (= K173), E178 (= E176), G208 (= G206), G212 (= G210), F226 (= F224), T227 (= T225), G228 (= G226), G229 (≠ S227), T232 (= T230), V236 (≠ I234), E251 (= E248), L252 (= L249), C285 (= C282), E386 (= E381), F388 (= F383)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
37% identity, 98% coverage: 9:476/477 of query aligns to 9:481/489 of 2woxA
- active site: N152 (= N150), K175 (= K173), E251 (= E248), C285 (= C282), E386 (= E381), E463 (≠ A458)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I146), G149 (≠ L147), W151 (= W149), N152 (= N150), K175 (= K173), S177 (= S175), E178 (= E176), G208 (= G206), G212 (= G210), F226 (= F224), T227 (= T225), G228 (= G226), G229 (≠ S227), T232 (= T230), V236 (≠ I234), E251 (= E248), L252 (= L249), C285 (= C282), E386 (= E381), F388 (= F383)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
37% identity, 98% coverage: 9:476/477 of query aligns to 9:481/489 of 2wmeA
- active site: N152 (= N150), K175 (= K173), E251 (= E248), C285 (= C282), E386 (= E381), E463 (≠ A458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ L147), W151 (= W149), K175 (= K173), S177 (= S175), E178 (= E176), G208 (= G206), G212 (= G210), F226 (= F224), G228 (= G226), G229 (≠ S227), T232 (= T230), V236 (≠ I234)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
37% identity, 98% coverage: 9:476/477 of query aligns to 10:482/490 of Q9HTJ1
- GAWN 150:153 (≠ LPWN 147:150) binding
- K162 (= K159) active site, Charge relay system
- KPSE 176:179 (= KPSE 173:176) binding
- G209 (= G206) binding
- GTST 230:233 (≠ SVGT 227:230) binding
- E252 (= E248) active site, Proton acceptor
- C286 (= C282) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E381) binding
- E464 (≠ A458) active site, Charge relay system
5kj5B Crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase n169d in complex with NAD+ (see paper)
37% identity, 98% coverage: 8:476/477 of query aligns to 6:483/484 of 5kj5B
- active site: D153 (≠ N150), K176 (= K173), E252 (= E248), C286 (= C282), E388 (= E381), E465 (≠ A458)
- binding nicotinamide-adenine-dinucleotide: I149 (= I146), S150 (≠ L147), P151 (= P148), W152 (= W149), D153 (≠ N150), L158 (= L155), K176 (= K173), G209 (= G206), K210 (≠ A207), G214 (= G210), F228 (= F224), T229 (= T225), G230 (= G226), E231 (≠ S227), T234 (= T230), E252 (= E248), L253 (= L249), C286 (= C282), E388 (= E381), F390 (= F383), F454 (≠ H447)
5kllA Crystal structure of 2-hydroxymuconate-6-semialdehyde derived tautomeric intermediate in 2-aminomuconate 6-semialdehyde dehydrogenase n169d (see paper)
37% identity, 98% coverage: 8:476/477 of query aligns to 5:482/483 of 5kllA
- active site: D152 (≠ N150), K175 (= K173), E251 (= E248), C285 (= C282), E387 (= E381), E464 (≠ A458)
- binding (3~{E},5~{E})-6-oxidanyl-2-oxidanylidene-hexa-3,5-dienoic acid: R103 (= R99), D152 (≠ N150), L157 (= L155), W160 (≠ R158), C285 (= C282), Y445 (≠ N439), R447 (≠ E441), F453 (≠ H447)
4ou2A A 2.15 angstroms x-ray crystal structure of e268a 2-aminomuconate 6- semialdehyde dehydrogenase catalytic intermediate from pseudomonas fluorescens (see paper)
37% identity, 98% coverage: 8:476/477 of query aligns to 5:482/483 of 4ou2A
- active site: N152 (= N150), K175 (= K173), A251 (≠ E248), C285 (= C282), E387 (= E381), E464 (≠ A458)
- binding (2Z,4E)-2,6-dihydroxyhexa-2,4-dienoic acid: R103 (= R99), L157 (= L155), C285 (= C282), Y445 (≠ N439), R447 (≠ E441), F453 (≠ H447)
- binding nicotinamide-adenine-dinucleotide: I148 (= I146), S149 (≠ L147), P150 (= P148), W151 (= W149), N152 (= N150), K175 (= K173), G208 (= G206), G213 (= G210), E214 (≠ H211), F227 (= F224), T228 (= T225), G229 (= G226), E230 (≠ S227), T233 (= T230), A251 (≠ E248), L252 (= L249), G253 (= G250), C285 (= C282), E387 (= E381), F389 (= F383)
Query Sequence
>Pf6N2E2_1751 Aldehyde dehydrogenase A (EC 1.2.1.22) / Glycolaldehyde dehydrogenase (EC 1.2.1.21)
MSHIIYQNYIANAFVASDEHLEVHNPANGQLLGRVPQGSTAEVEQAIAAARQAQRAWAAR
PAIERAGYLRKIASKVREHGERLARTITAEQGKVLELARVEVNFTADYLDYMAEWARRLE
GEVLSSDRAGESIFLLRKPLGVVAGILPWNFPFFLIARKMAPALLTGNTIVIKPSEETPI
NCFEFARLVAETDLPAGVFNVVCGTGATVGHALSGHPGIDLISFTGSVGTGSRIMAAAAP
NITKLNLELGGKAPAIVLADADLDLAIRAITASRVINTGQVCNCAERVYVERKVADAFID
GIAASMAATRYGDPLAEHGLDMGPLINRAALDKVAQMVRTASGQGAQIITGGAVADLGQG
FHYQPTVLAGCSAKMEIMRKEIFGPVLPIQIVDDLDEAIALANDSEYGLTSSIYTASLSA
AMQATRLLDFGETYINRENFEAMQGFHAGTRKSGIGGADGKHGLYEYTHTHVVYIQA
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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