SitesBLAST
Comparing WP_041097806.1 NCBI__GCF_000828635.1:WP_041097806.1 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)
48% identity, 98% coverage: 6:476/479 of query aligns to 13:483/485 of 6x9lA
- active site: N154 (= N147), E252 (= E245), A286 (≠ C279), E462 (= E456)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), T151 (= T144), W153 (= W146), N154 (= N147), Q159 (= Q152), K177 (= K170), E180 (= E173), G210 (= G203), P211 (= P204), G214 (= G207), T229 (= T222), G230 (= G223), S231 (= S224), E252 (= E245), L253 (= L246), A286 (≠ C279), E386 (= E380), F388 (= F382), F451 (= F445)
- binding octanal: W155 (≠ Y148), S285 (≠ T278)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
44% identity, 98% coverage: 1:471/479 of query aligns to 2:449/454 of 3ty7B
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
38% identity, 98% coverage: 1:471/479 of query aligns to 13:486/491 of 5gtlA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E380), E471 (= E456)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I143), P163 (= P145), K188 (= K170), A190 (≠ S172), E191 (= E173), Q192 (≠ V174), G221 (= G203), G225 (= G207), G241 (= G223), S242 (= S224), T245 (≠ A227), L264 (= L246), C297 (= C279), E394 (= E380), F396 (= F382)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
38% identity, 98% coverage: 1:471/479 of query aligns to 13:486/491 of 5gtkA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E380), E471 (= E456)
- binding nicotinamide-adenine-dinucleotide: I161 (= I143), I162 (≠ T144), P163 (= P145), W164 (= W146), K188 (= K170), E191 (= E173), G221 (= G203), G225 (= G207), A226 (≠ E208), F239 (= F221), G241 (= G223), S242 (= S224), T245 (≠ A227), Y248 (≠ R230), L264 (= L246), C297 (= C279), Q344 (= Q326), R347 (= R329), E394 (= E380), F396 (= F382)
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)
37% identity, 97% coverage: 6:469/479 of query aligns to 9:480/497 of P17202
- I28 (≠ F25) binding K(+)
- D96 (≠ E91) binding K(+)
- SPW 156:158 (≠ TPW 144:146) binding NAD(+)
- Y160 (= Y148) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ A155) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 170:173) binding NAD(+)
- L186 (≠ V174) binding K(+)
- SSAT 236:239 (≠ STRA 224:227) binding NAD(+)
- V251 (= V239) binding in other chain
- L258 (= L246) binding NAD(+)
- W285 (≠ L273) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E380) binding NAD(+)
- A441 (≠ Q431) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ F439) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F445) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K449) binding K(+)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
37% identity, 97% coverage: 6:469/479 of query aligns to 7:478/495 of 4v37A
- active site: N157 (= N147), K180 (= K170), E255 (= E245), A289 (≠ C279), E388 (= E380), E465 (= E456)
- binding 3-aminopropan-1-ol: C448 (≠ F439), W454 (≠ F445)
- binding nicotinamide-adenine-dinucleotide: I153 (= I143), S154 (≠ T144), P155 (= P145), W156 (= W146), N157 (= N147), M162 (≠ Q152), K180 (= K170), S182 (= S172), E183 (= E173), G213 (= G203), G217 (= G207), A218 (≠ E208), T232 (= T222), G233 (= G223), S234 (= S224), T237 (≠ A227), E255 (= E245), L256 (= L246), A289 (≠ C279), E388 (= E380), F390 (= F382)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
38% identity, 98% coverage: 2:471/479 of query aligns to 1:475/489 of 4o6rA
- active site: N150 (= N147), K173 (= K170), E248 (= E245), C282 (= C279), E383 (= E380), E460 (= E456)
- binding adenosine monophosphate: I146 (= I143), V147 (≠ T144), K173 (= K170), G206 (= G203), G210 (= G207), Q211 (≠ E208), F224 (= F221), G226 (= G223), S227 (= S224), T230 (≠ A227), R233 (= R230)
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)
37% identity, 98% coverage: 8:478/479 of query aligns to 21:498/505 of 4neaA
- active site: N166 (= N147), K189 (= K170), E264 (= E245), C298 (= C279), E399 (= E380), E476 (= E456)
- binding nicotinamide-adenine-dinucleotide: P164 (= P145), K189 (= K170), E192 (= E173), G222 (= G203), G226 (= G207), G242 (= G223), G243 (≠ S224), T246 (≠ A227), H249 (≠ R230), I250 (≠ V231), C298 (= C279), E399 (= E380), F401 (= F382)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
42% identity, 97% coverage: 6:471/479 of query aligns to 7:475/483 of 3b4wA
- active site: N154 (= N147), K177 (= K170), E251 (= E245), C285 (= C279), E384 (= E380), E460 (= E456)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), V151 (≠ T144), W153 (= W146), N154 (= N147), K177 (= K170), I210 (≠ P204), G213 (= G207), T228 (= T222), G229 (= G223), S230 (= S224), V233 (≠ A227), E236 (≠ R230), E251 (= E245), L252 (= L246), C285 (= C279), E384 (= E380), F386 (= F382)
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)
37% identity, 97% coverage: 5:471/479 of query aligns to 20:491/501 of Q56YU0