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
- G152 (vs. gap) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A397) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 97% coverage: 5:471/479 of query aligns to 6:476/486 of 4pxlA
- active site: N154 (= N147), K177 (= K170), E253 (= E245), C287 (= C279), E384 (= E380), D461 (≠ E456)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), V151 (≠ T144), P152 (= P145), W153 (= W146), K177 (= K170), E180 (= E173), G210 (= G203), G214 (= G207), A215 (≠ E208), F228 (= F221), G230 (= G223), S231 (= S224), V234 (≠ A227), E253 (= E245), G255 (= G247), C287 (= C279), Q334 (= Q326), K337 (≠ R329), E384 (= E380), F386 (= F382)
3u4jA Crystal structure of NAD-dependent aldehyde dehydrogenase from sinorhizobium meliloti
41% identity, 100% coverage: 1:477/479 of query aligns to 18:502/505 of 3u4jA
Sites not aligning to the query:
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
38% identity, 98% coverage: 4:471/479 of query aligns to 2:473/487 of 4go4A
- active site: N149 (= N147), K172 (= K170), E247 (= E245), C281 (= C279), E381 (= E380), E458 (= E456)
- 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 (≠ A227), E247 (= E245), G249 (= G247), C281 (= C279), E381 (= E380), F383 (= F382)
5iuwA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ and iaa (see paper)
40% identity, 99% coverage: 2:474/479 of query aligns to 8:494/495 of 5iuwA
- active site: N166 (= N147), K189 (= K170), E265 (= E245), C300 (= C279), E399 (= E380), D476 (≠ E456)
- binding 1h-indol-3-ylacetic acid: F167 (≠ Y148), M170 (≠ H151), C300 (= C279), D457 (vs. gap), F465 (= F445)
- binding nicotinamide-adenine-dinucleotide: I162 (= I143), V163 (≠ T144), P164 (= P145), W165 (= W146), N166 (= N147), K189 (= K170), G222 (= G203), G226 (= G207), K227 (≠ E208), F240 (= F221), T241 (= T222), G242 (= G223), S243 (= S224), I246 (≠ A227), Y253 (≠ L234), E265 (= E245), A266 (≠ L246), C300 (= C279), E399 (= E380), F401 (= F382)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
40% identity, 99% coverage: 2:474/479 of query aligns to 8:494/495 of 5iuvA
- active site: N166 (= N147), K189 (= K170), E265 (= E245), C300 (= C279), E399 (= E380), D476 (≠ E456)
- binding nicotinamide-adenine-dinucleotide: I162 (= I143), V163 (≠ T144), P164 (= P145), W165 (= W146), N166 (= N147), K189 (= K170), S191 (= S172), G222 (= G203), G226 (= G207), K227 (≠ E208), F240 (= F221), T241 (= T222), G242 (= G223), S243 (= S224), I246 (≠ A227), Y253 (≠ L234), E265 (= E245), A266 (≠ L246), C300 (= C279), E399 (= E380), F401 (= F382)
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
39% identity, 97% coverage: 7:472/479 of query aligns to 13:481/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (= W146), K180 (= K170), A182 (≠ S172), T212 (≠ Y202), G213 (= G203), G217 (= G207), F231 (= F221), G233 (= G223), S234 (= S224), V237 (≠ A227), Q337 (= Q326), E388 (= E380), F390 (= F382)
7jsoA P. Syringae alda indole-3-acetaldehyde dehydrogenase c302a mutant in complex with NAD+ and iaa (see paper)
39% identity, 99% coverage: 2:474/479 of query aligns to 8:494/495 of 7jsoA
- active site: N166 (= N147), E265 (= E245), A300 (≠ C279), D476 (≠ E456)
- binding 1h-indol-3-ylacetic acid: F167 (≠ Y148), W174 (≠ A155), V299 (≠ T278), A300 (≠ C279), T301 (= T280), D457 (vs. gap), F465 (= F445)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I162 (= I143), V163 (≠ T144), P164 (= P145), W165 (= W146), K189 (= K170), E192 (= E173), G222 (= G203), G226 (= G207), K227 (≠ E208), F240 (= F221), G242 (= G223), S243 (= S224), I246 (≠ A227), A266 (≠ L246), G267 (= G247), A300 (≠ C279), E399 (= E380), F401 (= F382)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 97% coverage: 4:469/479 of query aligns to 9:485/505 of O24174
- N164 (= N147) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
- W172 (≠ A155) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
38% identity, 97% coverage: 5:471/479 of query aligns to 11:484/494 of 4pz2B
- active site: N159 (= N147), K182 (= K170), E258 (= E245), C292 (= C279), E392 (= E380), D469 (≠ E456)
- binding nicotinamide-adenine-dinucleotide: I155 (= I143), I156 (≠ T144), P157 (= P145), W158 (= W146), N159 (= N147), M164 (≠ Q152), K182 (= K170), A184 (≠ S172), E185 (= E173), G215 (= G203), G219 (= G207), F233 (= F221), T234 (= T222), G235 (= G223), S236 (= S224), V239 (≠ A227), E258 (= E245), L259 (= L246), C292 (= C279), E392 (= E380), F394 (= F382)
7w5kA The c296a mutant of l-sorbosone dehydrogenase (sndh) from gluconobacter oxydans wsh-004 (see paper)
39% identity, 97% coverage: 7:472/479 of query aligns to 12:480/491 of 7w5kA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (= I143), T153 (= T144), P154 (= P145), W155 (= W146), N156 (= N147), I161 (≠ Q152), K179 (= K170), A181 (≠ S172), E182 (= E173), T211 (≠ Y202), G212 (= G203), G216 (= G207), Q217 (≠ E208), F230 (= F221), T231 (= T222), G232 (= G223), S233 (= S224), V236 (≠ A227), E255 (= E245), L256 (= L246), G257 (= G247), A289 (≠ C279), E387 (= E380), F389 (= F382)
Query Sequence
>WP_041097806.1 NCBI__GCF_000828635.1:WP_041097806.1
MEQRTQFYIDGQWVSPAGQGTIEVFSPTDGALLATVPQGNAADADKAVTAARGAFDAWSV
TPAAERAAYLKKIQESLKARADEIAKTITLEMGMPYKFSQRIQVGSPTASFGMYSKMLAD
FPFEEKVGNSKVVREAVGVVAAITPWNYPLHQIAAKVAAALAAGCTVVLKPSEVAPLNAF
LLAEIIHAAGVPAGVFNLITGYGPVVGEAMVTHREVDMVSFTGSTRAGTRVSELASATVK
RVALELGGKSAAIILDDADFNVAVKGVVGNCYLNSGQTCTAHTRMLVPATRYAEAAKLAV
EAAQAYRVGDPMAEGVTLGPLASKMQQDRVRDYIGKGIAEGCELLTGGADLPEGVNPDGY
YVKPTIFGKVKPDSSIAQEEIFGPVLSIISYADEEDAVSIANGTVYGLAGGVWSATDEHA
EQVARRMRTGQVEINGGTFNMYAPFGGYKQSGNGRELGKYGLEDFLEFKAMQFRPAPKG
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory