SitesBLAST
Comparing WP_017549894.1 NCBI__GCF_000330705.1:WP_017549894.1 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)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
62% identity, 100% coverage: 1:474/476 of query aligns to 2:453/454 of 3ty7B
6x9lA Crystal structure of aldehyde dehydrogenasE C (aldc) mutant (c291a) from pseudomonas syringae in complexed with NAD+ and octanal (see paper)
42% identity, 99% coverage: 2:473/476 of query aligns to 9:480/485 of 6x9lA
- active site: N154 (= N147), E252 (= E245), A286 (≠ C279), E462 (= E455)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ V143), T151 (= T144), W153 (= W146), N154 (= N147), Q159 (= Q152), K177 (= K170), E180 (≠ V173), G210 (= G203), P211 (≠ S204), G214 (= G207), T229 (= T222), G230 (= G223), S231 (= S224), E252 (= E245), L253 (= L246), A286 (≠ C279), E386 (= E379), F388 (= F381), F451 (= F444)
- binding octanal: W155 (≠ F148), S285 (≠ V278)
Q8VWZ1 Aminoaldehyde dehydrogenase 1, peroxisomal; PsAMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
40% identity, 99% coverage: 3:473/476 of query aligns to 6:488/503 of Q8VWZ1
- N27 (≠ V24) binding Na(+)
- I28 (= I25) binding Na(+)
- D99 (≠ E91) binding Na(+)
- L189 (≠ E174) binding Na(+)
- 238:245 (vs. 223:230, 63% identical) binding NAD(+)
- C294 (= C279) binding NAD(+)
- E393 (= E379) binding NAD(+)
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
40% identity, 99% coverage: 3:473/476 of query aligns to 1:483/497 of 3iwkH
- active site: N157 (= N147), K180 (= K170), E255 (= E245), C289 (= C279), E388 (= E379), E465 (= E455)
- binding nicotinamide-adenine-dinucleotide: W156 (= W146), G213 (= G203), G217 (= G207), A218 (≠ D208), G233 (= G223), S234 (= S224), T237 (≠ A227), K240 (= K230), C289 (= C279), Q336 (= Q326), E388 (= E379), F390 (= F381)
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, 98% coverage: 4:468/476 of query aligns to 7:480/497 of P17202
- I28 (= I25) binding K(+)
- D96 (≠ E91) binding K(+)
- SPW 156:158 (≠ TPW 144:146) binding NAD(+)
- Y160 (≠ F148) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ V155) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPSV 170:173) binding NAD(+)
- L186 (≠ E174) binding K(+)
- SSAT 236:239 (≠ SESA 224:227) binding NAD(+)
- V251 (≠ F239) binding in other chain
- L258 (= L246) binding NAD(+)
- W285 (≠ D273) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E379) binding NAD(+)
- A441 (≠ S430) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ G438) 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
36% identity, 98% coverage: 4:468/476 of query aligns to 5:478/495 of 4v37A
- active site: N157 (= N147), K180 (= K170), E255 (= E245), A289 (≠ C279), E388 (= E379), E465 (= E455)
- binding 3-aminopropan-1-ol: C448 (≠ G438), W454 (≠ F444)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ V143), S154 (≠ T144), P155 (= P145), W156 (= W146), N157 (= N147), M162 (≠ Q152), K180 (= K170), S182 (= S172), E183 (≠ V173), G213 (= G203), G217 (= G207), A218 (≠ D208), T232 (= T222), G233 (= G223), S234 (= S224), T237 (≠ A227), E255 (= E245), L256 (= L246), A289 (≠ C279), E388 (= E379), F390 (= F381)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
40% identity, 98% coverage: 5:470/476 of query aligns to 6:475/483 of 3b4wA
- active site: N154 (= N147), K177 (= K170), E251 (= E245), C285 (= C279), E384 (= E379), E460 (= E455)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ V143), V151 (≠ T144), W153 (= W146), N154 (= N147), K177 (= K170), I210 (≠ S204), G213 (= G207), T228 (= T222), G229 (= G223), S230 (= S224), V233 (≠ A227), E236 (≠ K230), E251 (= E245), L252 (= L246), C285 (= C279), E384 (= E379), F386 (= F381)
P05091 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Homo sapiens (Human) (see 5 papers)
38% identity, 98% coverage: 4:470/476 of query aligns to 36:508/517 of P05091
- E337 (= E297) to V: in dbSNP:rs1062136
- E496 (≠ D458) to K: in allele ALDH2*3; dbSNP:rs769724893
- E504 (= E466) to K: in AMEDS; allele ALDH2*2; drastic reduction of enzyme activity; dbSNP:rs671
Sites not aligning to the query:
5l13A Structure of aldh2 in complex with 2p3 (see paper)
38% identity, 98% coverage: 4:470/476 of query aligns to 13:485/494 of 5l13A
- active site: N163 (= N147), K186 (= K170), E262 (= E245), C296 (= C279), E393 (= E379), E470 (= E455)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F148), M168 (≠ Q152), W171 (≠ V155), F290 (≠ D273), C295 (≠ V278), C296 (= C279), C297 (≠ D280), D451 (≠ N436), F453 (≠ G438)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
38% identity, 98% coverage: 4:470/476 of query aligns to 13:485/494 of 4kwgA