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Comparing Ac3H11_4805 FitnessBrowser__acidovorax_3H11:Ac3H11_4805 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)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
40% identity, 95% coverage: 17:483/491 of query aligns to 29:507/515 of 2d4eC
- active site: N173 (= N158), K196 (= K181), E271 (= E256), C305 (= C289), E409 (= E386), E486 (= E462)
- binding nicotinamide-adenine-dinucleotide: I169 (= I154), T170 (= T155), P171 (= P156), W172 (= W157), K196 (= K181), A198 (≠ P183), G229 (= G214), G233 (= G218), A234 (= A219), T248 (= T233), G249 (= G234), E250 (≠ S235), T253 (= T238), E271 (= E256), L272 (= L257), C305 (= C289), E409 (= E386), F411 (= F388), F475 (= F451)
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)
36% identity, 95% coverage: 16:479/491 of query aligns to 11:485/487 of Q9H2A2
- R109 (= R114) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N158) mutation to A: Complete loss of activity.
- R451 (= R445) mutation to A: Complete loss of activity.
4npiA 1.94 angstroms x-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
36% identity, 94% coverage: 17:479/491 of query aligns to 5:481/483 of 4npiA
- active site: N152 (= N158), K175 (= K181), E251 (= E256), C285 (= C289), E387 (= E386), E464 (= E462)
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R114), L157 (= L163), W160 (= W166), E251 (= E256), C285 (= C289), Y445 (≠ G443), R447 (= R445), F453 (= F451)
- binding nicotinamide-adenine-dinucleotide: I148 (= I154), S149 (≠ T155), P150 (= P156), W151 (= W157), K175 (= K181), E178 (= E184), G208 (= G214), G213 (= G218), E214 (≠ A219), F227 (= F232), G229 (= G234), E230 (≠ S235), T233 (= T238), G253 (= G258), C285 (= C289), K335 (≠ R339), E387 (= E386), F389 (= F388)
4i2rA 2.15 angstroms x-ray crystal structure of NAD- and alternative substrate-bound 2-aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
36% identity, 94% coverage: 17:479/491 of query aligns to 5:481/483 of 4i2rA
- active site: N152 (= N158), K175 (= K181), E251 (= E256), C285 (= C289), E387 (= E386), E464 (= E462)
- binding (2E,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (= R114), L157 (= L163), C285 (= C289), Y445 (≠ G443), R447 (= R445), F453 (= F451)
- binding nicotinamide-adenine-dinucleotide: I148 (= I154), S149 (≠ T155), W151 (= W157), N152 (= N158), K175 (= K181), E178 (= E184), G208 (= G214), F227 (= F232), T228 (= T233), G229 (= G234), E230 (≠ S235), T233 (= T238), E251 (= E256), L252 (= L257), G253 (= G258), C285 (= C289), E387 (= E386), F389 (= F388)
4i25A 2.00 angstroms x-ray crystal structure of NAD- and substrate-bound 2- aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
36% identity, 94% coverage: 17:479/491 of query aligns to 5:481/483 of 4i25A
- active site: N152 (= N158), K175 (= K181), E251 (= E256), C285 (= C289), E387 (= E386), E464 (= E462)
- binding (2E,4E)-2-amino-6-oxohexa-2,4-dienoic acid: R103 (= R114), L157 (= L163), C285 (= C289), Y445 (≠ G443), R447 (= R445), F453 (= F451)
- binding nicotinamide-adenine-dinucleotide: I148 (= I154), S149 (≠ T155), P150 (= P156), W151 (= W157), N152 (= N158), K175 (= K181), E178 (= E184), G208 (= G214), G213 (= G218), F227 (= F232), T228 (= T233), G229 (= G234), E230 (≠ S235), T233 (= T238), E251 (= E256), L252 (= L257), C285 (= C289), E387 (= E386), F389 (= F388)
5kj5B Crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase n169d in complex with NAD+ (see paper)
36% identity, 94% coverage: 17:479/491 of query aligns to 6:482/484 of 5kj5B
- active site: D153 (≠ N158), K176 (= K181), E252 (= E256), C286 (= C289), E388 (= E386), E465 (= E462)
- binding nicotinamide-adenine-dinucleotide: I149 (= I154), S150 (≠ T155), P151 (= P156), W152 (= W157), D153 (≠ N158), L158 (= L163), K176 (= K181), G209 (= G214), K210 (≠ V215), G214 (= G218), F228 (= F232), T229 (= T233), G230 (= G234), E231 (≠ S235), T234 (= T238), E252 (= E256), L253 (= L257), C286 (= C289), E388 (= E386), F390 (= F388), F454 (= F451)
5kllA Crystal structure of 2-hydroxymuconate-6-semialdehyde derived tautomeric intermediate in 2-aminomuconate 6-semialdehyde dehydrogenase n169d (see paper)
36% identity, 94% coverage: 17:479/491 of query aligns to 5:481/483 of 5kllA
- active site: D152 (≠ N158), K175 (= K181), E251 (= E256), C285 (= C289), E387 (= E386), E464 (= E462)
- binding (3~{E},5~{E})-6-oxidanyl-2-oxidanylidene-hexa-3,5-dienoic acid: R103 (= R114), D152 (≠ N158), L157 (= L163), W160 (= W166), C285 (= C289), Y445 (≠ G443), R447 (= R445), F453 (= F451)
4ou2A A 2.15 angstroms x-ray crystal structure of e268a 2-aminomuconate 6- semialdehyde dehydrogenase catalytic intermediate from pseudomonas fluorescens (see paper)
36% identity, 94% coverage: 17:479/491 of query aligns to 5:481/483 of 4ou2A
- active site: N152 (= N158), K175 (= K181), A251 (≠ E256), C285 (= C289), E387 (= E386), E464 (= E462)
- binding (2Z,4E)-2,6-dihydroxyhexa-2,4-dienoic acid: R103 (= R114), L157 (= L163), C285 (= C289), Y445 (≠ G443), R447 (= R445), F453 (= F451)
- binding nicotinamide-adenine-dinucleotide: I148 (= I154), S149 (≠ T155), P150 (= P156), W151 (= W157), N152 (= N158), K175 (= K181), G208 (= G214), G213 (= G218), E214 (≠ A219), F227 (= F232), T228 (= T233), G229 (= G234), E230 (≠ S235), T233 (= T238), A251 (≠ E256), L252 (= L257), G253 (= G258), C285 (= C289), E387 (= E386), F389 (= F388)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
39% identity, 94% coverage: 18:479/491 of query aligns to 7:477/489 of 4o6rA
- active site: N150 (= N158), K173 (= K181), E248 (= E256), C282 (= C289), E383 (= E386), E460 (= E462)
- binding adenosine monophosphate: I146 (= I154), V147 (≠ T155), K173 (= K181), G206 (= G214), G210 (= G218), Q211 (≠ A219), F224 (= F232), G226 (= G234), S227 (= S235), T230 (= T238), R233 (≠ W241)
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, 94% coverage: 18:477/491 of query aligns to 11:482/497 of P17202
- I28 (≠ H33) binding
- D96 (= D99) binding
- SPW 156:158 (≠ TPW 155:157) binding
- Y160 (≠ A159) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W166) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPPE 181:184) binding
- L186 (≠ W185) binding
- SSAT 236:239 (≠ SVPT 235:238) binding
- V251 (≠ L250) binding in other chain
- L258 (= L257) binding
- W285 (≠ R283) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E386) binding
- A441 (≠ F436) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ R445) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F451) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K455) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
37% identity, 94% coverage: 18:477/491 of query aligns to 9:480/495 of 4v37A
- active site: N157 (= N158), K180 (= K181), E255 (= E256), A289 (≠ C289), E388 (= E386), E465 (= E462)
- binding 3-aminopropan-1-ol: C448 (≠ R445), W454 (≠ F451)
- binding nicotinamide-adenine-dinucleotide: I153 (= I154), S154 (≠ T155), P155 (= P156), W156 (= W157), N157 (= N158), M162 (≠ L163), K180 (= K181), S182 (≠ P183), E183 (= E184), G213 (= G214), G217 (= G218), A218 (= A219), T232 (= T233), G233 (= G234), S234 (= S235), T237 (= T238), E255 (= E256), L256 (= L257), A289 (≠ C289), E388 (= E386), F390 (= F388)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
36% identity, 95% coverage: 18:482/491 of query aligns to 20:491/491 of 5gtlA
- active site: N165 (= N158), K188 (= K181), E263 (= E256), C297 (= C289), E394 (= E386), E471 (= E462)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I154), P163 (= P156), K188 (= K181), A190 (≠ P183), E191 (= E184), Q192 (≠ W185), G221 (= G214), G225 (= G218), G241 (= G234), S242 (= S235), T245 (= T238), L264 (= L257), C297 (= C289), E394 (= E386), F396 (= F388)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
36% identity, 95% coverage: 18:482/491 of query aligns to 20:491/491 of 5gtkA
- active site: N165 (= N158), K188 (= K181), E263 (= E256), C297 (= C289), E394 (= E386), E471 (= E462)
- binding nicotinamide-adenine-dinucleotide: I161 (= I154), I162 (≠ T155), P163 (= P156), W164 (= W157), K188 (= K181), E191 (= E184), G221 (= G214), G225 (= G218), A226 (= A219), F239 (= F232), G241 (= G234), S242 (= S235), T245 (= T238), Y248 (≠ W241), L264 (= L257), C297 (= C289), Q344 (= Q336), R347 (= R339), E394 (= E386), F396 (= F388)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
38% identity, 94% coverage: 18:480/491 of query aligns to 9:479/486 of 4pxlA
- active site: N154 (= N158), K177 (= K181), E253 (= E256), C287 (= C289), E384 (= E386), D461 (≠ E462)
- binding nicotinamide-adenine-dinucleotide: I150 (= I154), V151 (≠ T155), P152 (= P156), W153 (= W157), K177 (= K181), E180 (= E184), G210 (= G214), G214 (= G218), A215 (= A219), F228 (= F232), G230 (= G234), S231 (= S235), V234 (≠ T238), E253 (= E256), G255 (= G258), C287 (= C289), Q334 (= Q336), K337 (≠ R339), E384 (= E386), F386 (= F388)
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
38% identity, 95% coverage: 16:479/491 of query aligns to 5:482/485 of 4u3wA
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 91% coverage: 29:477/491 of query aligns to 26:487/505 of O24174
- N164 (= N158) 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 (= W166) 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.
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
39% identity, 94% coverage: 26:488/491 of query aligns to 19:488/489 of 6wsbA
- active site: N152 (= N158), E250 (= E256), C284 (= C289), E462 (= E462)
- binding nicotinamide-adenine-dinucleotide: I148 (= I154), G149 (≠ T155), A150 (≠ P156), W151 (= W157), N152 (= N158), K175 (= K181), E178 (= E184), G208 (= G214), G211 (= G218), A212 (= A219), F225 (= F232), T226 (= T233), G227 (= G234), G228 (≠ S235), T231 (= T238), V235 (≠ I242), E250 (= E256), L251 (= L257), G252 (= G258), C284 (= C289), E385 (= E386), F387 (= F388)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
38% identity, 94% coverage: 18:479/491 of query aligns to 6:475/487 of 4go4A
- active site: N149 (= N158), K172 (= K181), E247 (= E256), C281 (= C289), E381 (= E386), E458 (= E462)
- binding nicotinamide-adenine-dinucleotide: I145 (= I154), V146 (≠ T155), W148 (= W157), N149 (= N158), F154 (≠ L163), K172 (= K181), G205 (= G214), G209 (= G218), Q210 (≠ A219), F223 (= F232), T224 (= T233), G225 (= G234), S226 (= S235), T229 (= T238), E247 (= E256), G249 (= G258), C281 (= C289), E381 (= E386), F383 (= F388)
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
38% identity, 95% coverage: 14:477/491 of query aligns to 2:480/497 of 3iwkH
- active site: N157 (= N158), K180 (= K181), E255 (= E256), C289 (= C289), E388 (= E386), E465 (= E462)
- binding nicotinamide-adenine-dinucleotide: W156 (= W157), G213 (= G214), G217 (= G218), A218 (= A219), G233 (= G234), S234 (= S235), T237 (= T238), K240 (≠ W241), C289 (= C289), Q336 (= Q336), E388 (= E386), F390 (= F388)
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)
38% identity, 95% coverage: 14:477/491 of query aligns to 7:485/503 of Q8VWZ1
- N27 (≠ L32) binding
- I28 (≠ H33) binding
- D99 (= D99) binding
- L189 (≠ W185) binding
- 238:245 (vs. 234:241, 38% identical) binding
- C294 (= C289) binding
- E393 (= E386) binding
Query Sequence
>Ac3H11_4805 FitnessBrowser__acidovorax_3H11:Ac3H11_4805
LSTDTLNVAGIAVSPHHYIDGQRVASDMRFDLHSPIDQALLGRISEGSPAHVDAAVSAAA
RAFPAWSALTAAERKPYLDRFAAEIGKRAEAFCTLESNDAGVLLSRMKHGVVPRAMLNIT
WFAEHALSLQDRPIETEQATHLVRHDPAGVVAIITPWNAPLMLATWKLGPALAAGNCVIV
KPPEWAPLTSSLLADCAHAAGLPPGVFNIVQGAGVSTGARLVSDPRLARISFTGSVPTAK
WIAQSAGANLVPCSLELGGKSAFIVLEDADIDNAAATGALMYRNAGQVCLAGTRFLVHRK
VHDAFVAALRGYVEKLTVGDPRDGATEVGPIIHPRQVERVHGFVQRAVADGATLLWGGAQ
HPFGAQYYQPTLLTDVRQDSEIVQNEVFGPVLTLQTFDSDEEAIALANGTDYGLGGVCYG
ATEHASAVAQQVRTGFIWVNSFGIRDLAAPFGGIKRSGVGREGGDWSFEFFCDVKDVVVP
KKPFRASFSHR
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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