SitesBLAST
Comparing WP_011384974.1 AMB_RS13050 aldehyde dehydrogenase family protein 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)
50% identity, 99% coverage: 7:479/479 of query aligns to 14:484/485 of 6x9lA
- active site: N154 (= N149), E252 (= E247), A286 (≠ C281), E462 (= E457)
- binding nicotinamide-adenine-dinucleotide: I150 (= I145), T151 (= T146), W153 (= W148), N154 (= N149), Q159 (= Q154), K177 (= K172), E180 (= E175), G210 (= G205), P211 (≠ A206), G214 (= G209), T229 (= T224), G230 (= G225), S231 (= S226), E252 (= E247), L253 (= L248), A286 (≠ C281), E386 (= E381), F388 (= F383), F451 (= F446)
- binding octanal: W155 (= W150), S285 (= S280)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
45% identity, 99% coverage: 1:474/479 of query aligns to 2:451/454 of 3ty7B
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
40% identity, 97% coverage: 7:473/479 of query aligns to 8:476/483 of 3b4wA
- active site: N154 (= N149), K177 (= K172), E251 (= E247), C285 (= C281), E384 (= E381), E460 (= E457)
- binding nicotinamide-adenine-dinucleotide: I150 (= I145), V151 (≠ T146), W153 (= W148), N154 (= N149), K177 (= K172), I210 (≠ A206), G213 (= G209), T228 (= T224), G229 (= G225), S230 (= S226), V233 (≠ A229), E236 (≠ S232), E251 (= E247), L252 (= L248), C285 (= C281), E384 (= E381), F386 (= F383)
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)
36% identity, 97% coverage: 7:472/479 of query aligns to 10:482/497 of P17202
- I28 (= I26) binding
- D96 (≠ E92) binding
- SPW 156:158 (≠ TPW 146:148) binding
- Y160 (≠ W150) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ C157) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 172:175) binding
- L186 (≠ F176) binding
- SSAT 236:239 (≠ SNLA 226:229) binding
- V251 (≠ I241) binding in other chain
- L258 (= L248) binding
- W285 (≠ G275) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E381) binding
- A441 (≠ M432) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (vs. gap) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F446) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ R450) binding
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
36% identity, 99% coverage: 1:473/479 of query aligns to 13:487/491 of 5gtlA
- active site: N165 (= N149), K188 (= K172), E263 (= E247), C297 (= C281), E394 (= E381), E471 (= E457)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I145), P163 (= P147), K188 (= K172), A190 (≠ S174), E191 (= E175), Q192 (≠ F176), G221 (= G205), G225 (= G209), G241 (= G225), S242 (= S226), T245 (≠ A229), L264 (= L248), C297 (= C281), E394 (= E381), F396 (= F383)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
36% identity, 99% coverage: 1:473/479 of query aligns to 13:487/491 of 5gtkA
- active site: N165 (= N149), K188 (= K172), E263 (= E247), C297 (= C281), E394 (= E381), E471 (= E457)
- binding nicotinamide-adenine-dinucleotide: I161 (= I145), I162 (≠ T146), P163 (= P147), W164 (= W148), K188 (= K172), E191 (= E175), G221 (= G205), G225 (= G209), A226 (≠ P210), F239 (≠ L223), G241 (= G225), S242 (= S226), T245 (≠ A229), Y248 (≠ S232), L264 (= L248), C297 (= C281), Q344 (= Q328), R347 (≠ K331), E394 (= E381), F396 (= F383)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
36% identity, 97% coverage: 7:472/479 of query aligns to 8:480/495 of 4v37A
- active site: N157 (= N149), K180 (= K172), E255 (= E247), A289 (≠ C281), E388 (= E381), E465 (= E457)
- binding 3-aminopropan-1-ol: C448 (vs. gap), W454 (≠ F446)
- binding nicotinamide-adenine-dinucleotide: I153 (= I145), S154 (≠ T146), P155 (= P147), W156 (= W148), N157 (= N149), M162 (≠ Q154), K180 (= K172), S182 (= S174), E183 (= E175), G213 (= G205), G217 (= G209), A218 (≠ P210), T232 (= T224), G233 (= G225), S234 (= S226), T237 (≠ A229), E255 (= E247), L256 (= L248), A289 (≠ C281), E388 (= E381), F390 (= F383)
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
39% identity, 97% coverage: 9:472/479 of query aligns to 15:478/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
39% identity, 97% coverage: 9:472/479 of query aligns to 14:477/481 of 3jz4A
- active site: N156 (= N149), K179 (= K172), E254 (= E247), C288 (= C281), E385 (= E381), E462 (= E457)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P147), W155 (= W148), K179 (= K172), A181 (≠ S174), S182 (≠ E175), A212 (≠ G205), G216 (= G209), G232 (= G225), S233 (= S226), I236 (≠ A229), C288 (= C281), K338 (= K331), E385 (= E381), F387 (= F383)
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 97% coverage: 6:472/479 of query aligns to 9:485/503 of Q84LK3
- N162 (= N149) 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 (≠ C157) 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).
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
37% identity, 97% coverage: 7:473/479 of query aligns to 7:474/477 of 2impA
- active site: N151 (= N149), K174 (= K172), E249 (= E247), C283 (= C281), E381 (= E381), A458 (≠ E457)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I145), L148 (≠ T146), P149 (= P147), W150 (= W148), K174 (= K172), E177 (= E175), F178 (= F176), G207 (= G205), G211 (= G209), Q212 (≠ P210), S228 (= S226), A231 (= A229), K234 (≠ S232), R334 (≠ K331)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
37% identity, 97% coverage: 7:473/479 of query aligns to 7:474/477 of 2iluA
- active site: N151 (= N149), K174 (= K172), E249 (= E247), C283 (= C281), E381 (= E381), A458 (≠ E457)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I145), L148 (≠ T146), P149 (= P147), W150 (= W148), K174 (= K172), S176 (= S174), E177 (= E175), R206 (≠ D204), G207 (= G205), G211 (= G209), Q212 (≠ P210), S228 (= S226), A231 (= A229), K234 (≠ S232), I235 (≠ V233), N328 (= N325), R334 (≠ K331), F383 (= F383)
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
37% identity, 97% coverage: 7:473/479 of query aligns to 9:476/479 of P25553
- L150 (≠ T146) binding
- R161 (≠ C157) binding
- KPSE 176:179 (= KPSE 172:175) binding
- F180 (= F176) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ P210) binding
- S230 (= S226) binding
- E251 (= E247) binding
- N286 (= N282) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (≠ K331) binding
- E443 (≠ S440) binding
- H449 (≠ F446) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
37% identity, 97% coverage: 7:473/479 of query aligns to 7:474/477 of 2opxA
- active site: N151 (= N149), K174 (= K172), E249 (= E247), C283 (= C281), E381 (= E381), A458 (≠ E457)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ R107), F152 (≠ W150), N284 (= N282), F312 (≠ V310), G313 (= G311), R318 (≠ P316), D320 (≠ T318), I321 (≠ V319), A322 (vs. gap), Y362 (≠ F362), F440 (≠ L439), F440 (≠ L439), E441 (≠ S440)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
37% identity, 97% coverage: 7:472/479 of query aligns to 12:487/505 of O24174
- N164 (= N149) 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 (≠ C157) 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.
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
37% identity, 97% coverage: 7:472/479 of query aligns to 7:482/500 of 4i8pA
- active site: N159 (= N149), K182 (= K172), E257 (= E247), C291 (= C281), E390 (= E381), E467 (= E457)
- binding nicotinamide-adenine-dinucleotide: I155 (= I145), T156 (= T146), P157 (= P147), W158 (= W148), N159 (= N149), M164 (≠ Q154), K182 (= K172), S184 (= S174), E185 (= E175), G215 (= G205), G219 (= G209), A220 (≠ P210), T234 (= T224), G235 (= G225), S236 (= S226), T239 (≠ A229), E257 (= E247), L258 (= L248), C291 (= C281), E390 (= E381), F392 (= F383), W456 (≠ F446)
C0P9J6 Aminoaldehyde dehydrogenase 1a; ZmAMADH1a; 4-trimethylammoniobutyraldehyde dehydrogenase AMADH1a; Aminobutyraldehyde dehydrogenase AMADH1a; Betaine aldehyde dehydrogenase AMADH1a; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1a; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8; EC 1.2.1.54 from Zea mays (Maize) (see paper)
37% identity, 97% coverage: 7:472/479 of query aligns to 12:487/505 of C0P9J6
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
38% identity, 97% coverage: 7:472/479 of query aligns to 8:476/486 of 4pxlA
- active site: N154 (= N149), K177 (= K172), E253 (= E247), C287 (= C281), E384 (= E381), D461 (≠ E457)
- binding nicotinamide-adenine-dinucleotide: I150 (= I145), V151 (≠ T146), P152 (= P147), W153 (= W148), K177 (= K172), E180 (= E175), G210 (= G205), G214 (= G209), A215 (≠ P210), F228 (≠ L223), G230 (= G225), S231 (= S226), V234 (≠ A229), E253 (= E247), G255 (= G249), C287 (= C281), Q334 (= Q328), K337 (= K331), E384 (= E381), F386 (= F383)
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, 97% coverage: 7:472/479 of query aligns to 10:485/503 of Q8VWZ1
- N27 (≠ D24) binding
- I28 (= I26) binding
- D99 (≠ E92) binding
- L189 (≠ F176) binding
- 238:245 (vs. 225:232, 50% identical) binding
- C294 (= C281) binding
- E393 (= E381) binding
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
37% identity, 97% coverage: 8:472/479 of query aligns to 30:501/515 of 2d4eC
- active site: N173 (= N149), K196 (= K172), E271 (= E247), C305 (= C281), E409 (= E381), E486 (= E457)
- binding nicotinamide-adenine-dinucleotide: I169 (= I145), T170 (= T146), P171 (= P147), W172 (= W148), K196 (= K172), A198 (≠ S174), G229 (= G205), G233 (= G209), A234 (≠ P210), T248 (= T224), G249 (= G225), E250 (≠ S226), T253 (≠ A229), E271 (= E247), L272 (= L248), C305 (= C281), E409 (= E381), F411 (= F383), F475 (= F446)
Query Sequence
>WP_011384974.1 AMB_RS13050 aldehyde dehydrogenase family protein
MGDCLDFYVDGAWVKPAKGSRLLDVINPATEQVSGRVALGGADDAVRAIQAAAKAFPAWA
ATPLAERLEILAKVTAGYERRLDEIAEAISLEMGAPLERLAKPAQARAGLGHFKTALSLA
KTYAFERRQGTTLVVKEPVGVVSLITPWNWPMNQIACKVAPALAAGCAMVLKPSEFAPYS
ARILAEIIHEAGVPAGVFNMVFGDGAEIGPVLSSHPLVDMVSLTGSNLAGSSVMREGAAT
IKKVSLELGGKSANIICDSADFKKAIGHAVKAMMGNTGQSCNAPSRLFVPAHRLDEAEGL
AAELCAQIKVGDPSDPETVMGPIANGRQFDKVRRMIRTGMEEGAKLVCGGPERPEGLDKG
YFVRPTVFSRVTDAMTIMREEIFGPVLSMRGYADLDDAVAGANDCVYGLSGYVYAGDLDE
ARAVARRLRTGMVHLNGALSHPGGPFGGIRQSGVGREWGEAGFEEFLESKTLFGSEPKE
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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