SitesBLAST
Comparing WP_068106355.1 NCBI__GCF_001653335.1:WP_068106355.1 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)
6x9lA Crystal structure of aldehyde dehydrogenasE C (aldc) mutant (c291a) from pseudomonas syringae in complexed with NAD+ and octanal (see paper)
46% identity, 99% coverage: 2:470/472 of query aligns to 9:477/485 of 6x9lA
- active site: N154 (= N147), E252 (= E245), A286 (≠ C279), E462 (= E455)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), T151 (= T144), W153 (= W146), N154 (= N147), Q159 (= Q152), K177 (= K170), E180 (= E173), G210 (= G203), P211 (≠ A204), G214 (= G207), T229 (= T222), G230 (= G223), S231 (= S224), E252 (= E245), L253 (= L246), A286 (≠ C279), E386 (= E379), F388 (= F381), F451 (= F444)
- binding octanal: W155 (≠ Y148), S285 (≠ T278)
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)
39% identity, 98% coverage: 8:470/472 of query aligns to 11:482/497 of P17202
- I28 (≠ S25) binding K(+)
- D96 (≠ E91) binding K(+)
- SPW 156:158 (≠ TAW 144:146) binding NAD(+)
- Y160 (= Y148) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ T155) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 170:173) binding NAD(+)
- L186 (≠ I174) binding K(+)
- SSAT 236:239 (≠ STRT 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 (= E379) binding NAD(+)
- A441 (≠ Q430) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ F438) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F444) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K448) binding K(+)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
39% identity, 98% coverage: 8:470/472 of query aligns to 9:480/495 of 4v37A
- active site: N157 (= N147), K180 (= K170), E255 (= E245), A289 (≠ C279), E388 (= E379), E465 (= E455)
- binding 3-aminopropan-1-ol: C448 (≠ F438), W454 (≠ F444)
- binding nicotinamide-adenine-dinucleotide: I153 (= I143), S154 (≠ T144), P155 (≠ A145), 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 (= T227), E255 (= E245), L256 (= L246), A289 (≠ C279), E388 (= E379), F390 (= F381)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
39% identity, 98% coverage: 8:470/472 of query aligns to 7:475/489 of 4o6rA
- active site: N150 (= N147), K173 (= K170), E248 (= E245), C282 (= C279), E383 (= E379), E460 (= E455)
- binding adenosine monophosphate: I146 (= I143), V147 (≠ T144), K173 (= K170), G206 (= G203), G210 (= G207), Q211 (≠ E208), F224 (= F221), G226 (= G223), S227 (= S224), T230 (= T227), R233 (= R230)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
38% identity, 100% coverage: 1:470/472 of query aligns to 2:449/454 of 3ty7B
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
39% identity, 99% coverage: 8:472/472 of query aligns to 9:477/483 of 3b4wA
- active site: N154 (= N147), K177 (= K170), E251 (= E245), C285 (= C279), E384 (= E379), E460 (= E455)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), V151 (≠ T144), W153 (= W146), N154 (= N147), K177 (= K170), I210 (≠ A204), G213 (= G207), T228 (= T222), G229 (= G223), S230 (= S224), V233 (≠ T227), E236 (≠ R230), E251 (= E245), L252 (= L246), C285 (= C279), E384 (= E379), F386 (= F381)
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, 99% coverage: 5:470/472 of query aligns to 18:491/505 of 4neaA
- active site: N166 (= N147), K189 (= K170), E264 (= E245), C298 (= C279), E399 (= E379), E476 (= E455)
- binding nicotinamide-adenine-dinucleotide: P164 (≠ A145), K189 (= K170), E192 (= E173), G222 (= G203), G226 (= G207), G242 (= G223), G243 (≠ S224), T246 (= T227), H249 (≠ R230), I250 (= I231), C298 (= C279), E399 (= E379), F401 (= F381)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
38% identity, 98% coverage: 8:470/472 of query aligns to 6:473/487 of 4go4A
- active site: N149 (= N147), K172 (= K170), E247 (= E245), C281 (= C279), E381 (= E379), E458 (= E455)
- binding nicotinamide-adenine-dinucleotide: I145 (= I143), V146 (≠ T144), W148 (= W146), N149 (= N147), F154 (≠ Q152), K172 (= K170), G205 (= G203), G209 (= G207), Q210 (≠ E208), F223 (= F221), T224 (= T222), G225 (= G223), S226 (= S224), T229 (= T227), E247 (= E245), G249 (= G247), C281 (= C279), E381 (= E379), F383 (= F381)
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
42% identity, 88% coverage: 58:470/472 of query aligns to 66:485/503 of Q84LK3
- N162 (= N147) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2-fold for Bet-ald and 8-fold for GAB-ald).
- W170 (≠ T155) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 2-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2.5-fold for Bet-ald and 6-fold for GAB-ald).; mutation to F: Slightly reduced affinity for NAD, 5-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and 1.5-fold increase in catalytic efficiency towards gamma-aminobutyraldehyde (GAB-ald).
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 98% coverage: 8:470/472 of query aligns to 13:487/505 of O24174