SitesBLAST
Comparing Pf6N2E2_1102 Aldehyde dehydrogenase A (EC 1.2.1.22) to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
61% identity, 100% coverage: 3:477/477 of query aligns to 2:479/479 of P25553
- L150 (= L148) binding
- R161 (= R159) binding
- KPSE 176:179 (= KPSE 174:177) binding
- F180 (≠ E178) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ A211) 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 (≠ S333) binding
- E443 (= E441) binding
- H449 (= H447) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
61% identity, 98% coverage: 10:477/477 of query aligns to 8:477/477 of 2opxA
- active site: N151 (= N151), K174 (= K174), E249 (= E248), C283 (= C282), E381 (= E381), A458 (= A458)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: Q97 (≠ A97), L98 (= L98), V101 (= V101), F105 (= F105), F152 (= F152), F155 (= F155), D273 (= D272), I277 (= I276), N284 (= N283), F312 (≠ Y311), G313 (= G312), R318 (≠ E317), D320 (= D319), I321 (= I320), A322 (≠ E321), K359 (≠ D359), 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)
61% identity, 98% coverage: 10:477/477 of query aligns to 8:477/477 of 2impA
- active site: N151 (= N151), K174 (= K174), E249 (= E248), C283 (= C282), E381 (= E381), A458 (= A458)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I147), L148 (= L148), P149 (= P149), W150 (= W150), K174 (= K174), P175 (= P175), S176 (= S176), E177 (= E177), F178 (≠ E178), G207 (= G207), E208 (≠ Q208), G211 (= G210), Q212 (≠ A211), M225 (≠ F224), G227 (= G226), S228 (= S227), A231 (≠ T230), K234 (≠ R233), I235 (= I234), N328 (= N327), A330 (≠ H329), R334 (≠ S333)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
61% identity, 98% coverage: 10:477/477 of query aligns to 8:477/477 of 2iluA
- active site: N151 (= N151), K174 (= K174), E249 (= E248), C283 (= C282), E381 (= E381), A458 (= A458)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I147), L148 (= L148), P149 (= P149), W150 (= W150), K174 (= K174), S176 (= S176), E177 (= E177), F178 (≠ E178), R206 (≠ D206), G207 (= G207), E208 (≠ Q208), G211 (= G210), Q212 (≠ A211), M225 (≠ F224), G227 (= G226), S228 (= S227), A231 (≠ T230), K234 (≠ R233), I235 (= I234), N328 (= N327), R334 (≠ S333), F383 (= F383)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
41% identity, 98% coverage: 7:475/477 of query aligns to 2:475/477 of 6j76A
- active site: N148 (= N151), E246 (= E248), C280 (= C282), E458 (≠ A458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I147), T145 (≠ L148), A146 (≠ P149), W147 (= W150), N148 (= N151), K171 (= K174), P172 (= P175), T173 (≠ S176), S174 (≠ E177), G203 (≠ D206), G204 (= G207), R205 (≠ Q208), G208 (= G210), N209 (≠ A211), T223 (= T225), G224 (= G226), S225 (= S227), A228 (≠ T230), S231 (≠ R233), I232 (= I234), E246 (= E248), L247 (= L249), G248 (= G250), C280 (= C282), E381 (= E381), F383 (= F383), H447 (= H447)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
38% identity, 98% coverage: 10:475/477 of query aligns to 6:475/494 of 5izdA
- active site: N149 (= N151), K172 (= K174), E247 (= E248), C281 (= C282), E381 (= E381), E458 (≠ A458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I147), T146 (≠ L148), W148 (= W150), K172 (= K174), P173 (= P175), S174 (= S176), S175 (≠ E177), R204 (≠ D206), G205 (= G207), G209 (= G210), D210 (≠ A211), T224 (= T225), G225 (= G226), S226 (= S227), T229 (= T230), R232 (= R233), I233 (= I234)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
39% identity, 96% coverage: 8:467/477 of query aligns to 11:471/481 of 3jz4A
- active site: N156 (= N151), K179 (= K174), E254 (= E248), C288 (= C282), E385 (= E381), E462 (≠ A458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (= I147), P154 (= P149), W155 (= W150), N156 (= N151), K179 (= K174), A181 (≠ S176), S182 (≠ E177), S211 (≠ D206), A212 (vs. gap), G213 (= G207), G216 (= G210), F230 (= F224), T231 (= T225), G232 (= G226), S233 (= S227), I236 (≠ T230), E254 (= E248), L255 (= L249), C288 (= C282), K338 (≠ S333), 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)
39% identity, 96% coverage: 8:467/477 of query aligns to 12:472/482 of P25526
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
40% identity, 95% coverage: 22:476/477 of query aligns to 23:480/489 of 6wsbA
- active site: N152 (= N151), E250 (= E248), C284 (= C282), E462 (≠ A458)
- binding nicotinamide-adenine-dinucleotide: I148 (= I147), G149 (≠ L148), A150 (≠ P149), W151 (= W150), N152 (= N151), K175 (= K174), P176 (= P175), S177 (= S176), E178 (= E177), D207 (= D206), G208 (= G207), G211 (= G210), A212 (= A211), F225 (= F224), T226 (= T225), G227 (= G226), G228 (≠ S227), T231 (= T230), K234 (≠ R233), V235 (≠ I234), E250 (= E248), L251 (= L249), G252 (= G250), C284 (= C282), E385 (= E381), F387 (= F383)
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, 99% coverage: 4:473/477 of query aligns to 5:482/497 of P17202