SitesBLAST
Comparing GFF4005 HP15_3945 aldehyde dehydrogenase family protein 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)
6x9lA Crystal structure of aldehyde dehydrogenasE C (aldc) mutant (c291a) from pseudomonas syringae in complexed with NAD+ and octanal (see paper)
43% identity, 98% coverage: 8:469/471 of query aligns to 15:477/485 of 6x9lA
- active site: N154 (= N146), E252 (= E244), A286 (≠ C278), E462 (= E454)
- binding nicotinamide-adenine-dinucleotide: I150 (= I142), T151 (= T143), P152 (= P144), W153 (= W145), N154 (= N146), Q159 (= Q151), K177 (= K169), P178 (= P170), S179 (= S171), E180 (= E172), G210 (= G202), P211 (≠ H203), G214 (= G206), G215 (≠ D207), T229 (= T221), G230 (= G222), S231 (= S223), R233 (= R225), A234 (≠ T226), L237 (= L229), E252 (= E244), L253 (≠ M245), G254 (= G246), A286 (≠ C278), E386 (= E378), F388 (= F380), L414 (= L406), F451 (= F443)
- binding octanal: W155 (≠ Y147), Y158 (≠ H150), Q159 (= Q151), R280 (≠ L272), S285 (≠ T277), A286 (≠ C278), S287 (≠ T279), W445 (≠ F437), F451 (= F443)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
41% identity, 100% coverage: 1:469/471 of query aligns to 2:449/454 of 3ty7B
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
40% identity, 100% coverage: 2:471/471 of query aligns to 3:477/483 of 3b4wA
- active site: N154 (= N146), K177 (= K169), E251 (= E244), C285 (= C278), E384 (= E378), E460 (= E454)
- binding nicotinamide-adenine-dinucleotide: I150 (= I142), V151 (≠ T143), A152 (≠ P144), W153 (= W145), N154 (= N146), K177 (= K169), P178 (= P170), A179 (≠ S171), G209 (= G202), I210 (≠ H203), G213 (= G206), Q214 (≠ D207), F227 (= F220), T228 (= T221), G229 (= G222), S230 (= S223), V233 (≠ T226), E236 (≠ L229), V237 (≠ I230), E251 (= E244), L252 (≠ M245), G253 (= G246), C285 (= C278), E384 (= E378), F386 (= F380), L412 (= L406), F449 (= F443)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 100% coverage: 1:469/471 of query aligns to 13:486/491 of 5gtlA
- active site: N165 (= N146), K188 (= K169), E263 (= E244), C297 (= C278), E394 (= E378), E471 (= E454)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I142), I162 (≠ T143), P163 (= P144), W164 (= W145), N165 (= N146), K188 (= K169), A190 (≠ S171), E191 (= E172), Q192 (≠ I173), G219 (= G200), F220 (≠ Y201), G221 (= G202), G225 (= G206), A226 (≠ D207), V229 (≠ I210), F239 (= F220), G241 (= G222), S242 (= S223), T245 (= T226), Y248 (≠ L229), E263 (= E244), L264 (≠ M245), G265 (= G246), C297 (= C278), Q344 (= Q325), R347 (≠ K328), E394 (= E378), F396 (= F380)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 100% coverage: 1:469/471 of query aligns to 13:486/491 of 5gtkA
- active site: N165 (= N146), K188 (= K169), E263 (= E244), C297 (= C278), E394 (= E378), E471 (= E454)
- binding nicotinamide-adenine-dinucleotide: I161 (= I142), I162 (≠ T143), P163 (= P144), W164 (= W145), N165 (= N146), K188 (= K169), A190 (≠ S171), E191 (= E172), G221 (= G202), G225 (= G206), A226 (≠ D207), V229 (≠ I210), F239 (= F220), T240 (= T221), G241 (= G222), S242 (= S223), T245 (= T226), Y248 (≠ L229), E263 (= E244), L264 (≠ M245), C297 (= C278), Q344 (= Q325), R347 (≠ K328), E394 (= E378), F396 (= F380)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
38% identity, 99% coverage: 5:469/471 of query aligns to 3:473/487 of 4go4A
- active site: N149 (= N146), K172 (= K169), E247 (= E244), C281 (= C278), E381 (= E378), E458 (= E454)
- binding nicotinamide-adenine-dinucleotide: I145 (= I142), V146 (≠ T143), P147 (= P144), W148 (= W145), N149 (= N146), F154 (≠ Q151), K172 (= K169), P173 (= P170), S174 (= S171), E175 (= E172), G205 (= G202), H206 (= H203), G209 (= G206), Q210 (≠ D207), F223 (= F220), T224 (= T221), G225 (= G222), S226 (= S223), T229 (= T226), I233 (= I230), E247 (= E244), L248 (≠ M245), G249 (= G246), C281 (= C278), E381 (= E378), F383 (= F380), L409 (= L406), F447 (= F443)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
36% identity, 98% coverage: 8:469/471 of query aligns to 7:475/489 of 4o6rA
- active site: N150 (= N146), K173 (= K169), E248 (= E244), C282 (= C278), E383 (= E378), E460 (= E454)
- binding adenosine monophosphate: I146 (= I142), V147 (≠ T143), K173 (= K169), P174 (= P170), S175 (= S171), E176 (= E172), G206 (= G202), G210 (= G206), Q211 (≠ D207), F224 (= F220), T225 (= T221), G226 (= G222), S227 (= S223), T230 (= T226), R233 (≠ L229), I234 (= I230)
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
35% identity, 99% coverage: 7:471/471 of query aligns to 12:485/487 of Q9H2A2
- R109 (≠ A107) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N146) mutation to A: Complete loss of activity.
- R451 (≠ N438) mutation to A: Complete loss of activity.
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)
36% identity, 98% coverage: 8:469/471 of query aligns to 11:482/497 of P17202
- I28 (≠ H24) binding
- D96 (≠ E90) binding
- SPW 156:158 (≠ TPW 143:145) binding
- Y160 (= Y147) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ L154) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 169:172) binding
- L186 (≠ I173) binding
- SSAT 236:239 (≠ STRT 223:226) binding
- V251 (≠ F238) binding in other chain
- L258 (≠ M245) binding
- W285 (≠ L272) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E378) binding
- A441 (≠ Q429) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (vs. gap) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F443) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G447) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3- aminopropionaldehyde
36% identity, 98% coverage: 8:469/471 of query aligns to 9:480/495 of 4v37A