SitesBLAST
Comparing GFF3775 PGA1_262p01790 aldehyde dehydrogenase 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)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
36% identity, 95% coverage: 20:477/483 of query aligns to 21:477/489 of 4o6rA
- active site: N150 (= N150), K173 (= K173), E248 (= E248), C282 (= C282), E383 (= E381), E460 (= E460)
- binding adenosine monophosphate: I146 (= I146), V147 (≠ S147), K173 (= K173), G206 (= G206), G210 (= G210), Q211 (= Q211), F224 (= F224), G226 (= G226), S227 (= S227), T230 (≠ V230), R233 (≠ G233)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
35% identity, 99% coverage: 6:483/483 of query aligns to 28:509/515 of 2d4eC
- active site: N173 (= N150), K196 (= K173), E271 (= E248), C305 (= C282), E409 (= E381), E486 (= E460)
- binding nicotinamide-adenine-dinucleotide: I169 (= I146), T170 (≠ S147), P171 (= P148), W172 (= W149), K196 (= K173), A198 (= A175), G229 (= G206), G233 (= G210), A234 (≠ Q211), T248 (= T225), G249 (= G226), E250 (≠ S227), T253 (≠ V230), E271 (= E248), L272 (≠ M249), C305 (= C282), E409 (= E381), F411 (= F383), F475 (= F448)
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)
33% identity, 98% coverage: 2:473/483 of query aligns to 15:489/505 of 4neaA
- active site: N166 (= N150), K189 (= K173), E264 (= E248), C298 (= C282), E399 (= E381), E476 (= E460)
- binding nicotinamide-adenine-dinucleotide: P164 (= P148), K189 (= K173), E192 (≠ N176), G222 (= G206), G226 (= G210), G242 (= G226), G243 (≠ S227), T246 (≠ V230), H249 (≠ G233), I250 (= I234), C298 (= C282), E399 (= E381), F401 (= F383)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
36% identity, 96% coverage: 12:477/483 of query aligns to 13:475/487 of 4go4A
- active site: N149 (= N150), K172 (= K173), E247 (= E248), C281 (= C282), E381 (= E381), E458 (= E460)
- binding nicotinamide-adenine-dinucleotide: I145 (= I146), V146 (≠ S147), W148 (= W149), N149 (= N150), F154 (≠ T155), K172 (= K173), G205 (= G206), G209 (= G210), Q210 (= Q211), F223 (= F224), T224 (= T225), G225 (= G226), S226 (= S227), T229 (≠ V230), E247 (= E248), G249 (= G250), C281 (= C282), E381 (= E381), F383 (= F383)
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
36% identity, 88% coverage: 56:478/483 of query aligns to 62:487/500 of 4i8pA
- active site: N159 (= N150), K182 (= K173), E257 (= E248), C291 (= C282), E390 (= E381), E467 (= E460)
- binding nicotinamide-adenine-dinucleotide: I155 (= I146), T156 (≠ S147), P157 (= P148), W158 (= W149), N159 (= N150), M164 (≠ T155), K182 (= K173), S184 (≠ A175), E185 (≠ N176), G215 (= G206), G219 (= G210), A220 (≠ Q211), T234 (= T225), G235 (= G226), S236 (= S227), T239 (≠ V230), E257 (= E248), L258 (≠ M249), C291 (= C282), E390 (= E381), F392 (= F383), W456 (≠ F448)
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)
36% identity, 88% coverage: 56:478/483 of query aligns to 67:492/505 of C0P9J6
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
37% identity, 85% coverage: 62:473/483 of query aligns to 75:485/505 of O24174
- N164 (= N150) 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 (= W158) 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.
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
35% identity, 96% coverage: 9:473/483 of query aligns to 7:478/497 of 3iwkH
- active site: N157 (= N150), K180 (= K173), E255 (= E248), C289 (= C282), E388 (= E381), E465 (= E460)
- binding nicotinamide-adenine-dinucleotide: W156 (= W149), G213 (= G206), G217 (= G210), A218 (≠ Q211), G233 (= G226), S234 (= S227), T237 (≠ V230), K240 (≠ G233), C289 (= C282), Q336 (= Q329), E388 (= E381), F390 (= 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)
35% identity, 96% coverage: 9:473/483 of query aligns to 12:483/503 of Q8VWZ1
- N27 (= N22) binding
- I28 (≠ R23) binding
- D99 (≠ E90) binding
- L189 (≠ V177) binding
- 238:245 (vs. 226:233, 38% identical) binding
- C294 (= C282) binding
- E393 (= E381) binding
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
36% identity, 91% coverage: 41:480/483 of query aligns to 58:497/503 of 1bpwA
- active site: N166 (= N150), K189 (= K173), E263 (= E248), C297 (= C282), E400 (= E381), E477 (= E460)
- binding nicotinamide-adenine-dinucleotide: I162 (= I146), L163 (≠ S147), W165 (= W149), N166 (= N150), K189 (= K173), G221 (= G206), G225 (= G210), T240 (= T225), G241 (= G226), S242 (= S227), T245 (≠ V230), E263 (= E248), L264 (≠ M249), C297 (= C282), E400 (= E381), F402 (= F383), F466 (= F448)
P56533 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABADH; Aldehyde dehydrogenase family 9 member A1; Betaine aldehyde dehydrogenase; BADH; EC 1.2.1.47; EC 1.2.1.3 from Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias) (see paper)
36% identity, 91% coverage: 41:480/483 of query aligns to 58:497/503 of P56533
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
35% identity, 85% coverage: 62:473/483 of query aligns to 73:483/503 of Q84LK3
- N162 (= N150) 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 (= W158) 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).
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)
33% identity, 93% coverage: 24:473/483 of query aligns to 29:480/497 of P17202
- D96 (≠ E90) binding
- SPW 156:158 (= SPW 147:149) binding
- Y160 (≠ F151) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W158) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAN 173:176) binding
- L186 (≠ V177) binding
- SSAT 236:239 (≠ SVPV 227:230) binding
- V251 (≠ L242) binding in other chain
- L258 (≠ M249) binding
- W285 (≠ G276) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E381) binding
- A441 (≠ C432) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ T442) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F448) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G452) binding
Sites not aligning to the query:
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
34% identity, 98% coverage: 9:480/483 of query aligns to 10:483/489 of 4cazA
- active site: N152 (= N150), K175 (= K173), E251 (= E248), C285 (= C282), E386 (= E381), E463 (= E460)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (= I146), G149 (≠ S147), W151 (= W149), N152 (= N150), K175 (= K173), E178 (≠ N176), G208 (= G206), G212 (= G210), F226 (= F224), T227 (= T225), G228 (= G226), G229 (≠ S227), T232 (≠ V230), V236 (≠ I234), E251 (= E248), L252 (≠ M249), C285 (= C282), E386 (= E381), F388 (= F383)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
34% identity, 98% coverage: 9:480/483 of query aligns to 10:483/489 of 2woxA
- active site: N152 (= N150), K175 (= K173), E251 (= E248), C285 (= C282), E386 (= E381), E463 (= E460)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I146), G149 (≠ S147), W151 (= W149), N152 (= N150), K175 (= K173), S177 (≠ A175), E178 (≠ N176), G208 (= G206), G212 (= G210), F226 (= F224), T227 (= T225), G228 (= G226), G229 (≠ S227), T232 (≠ V230), V236 (≠ I234), E251 (= E248), L252 (≠ M249), C285 (= C282), E386 (= E381), F388 (= F383)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
34% identity, 98% coverage: 9:480/483 of query aligns to 10:483/489 of 2wmeA
- active site: N152 (= N150), K175 (= K173), E251 (= E248), C285 (= C282), E386 (= E381), E463 (= E460)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ S147), W151 (= W149), K175 (= K173), S177 (≠ A175), E178 (≠ N176), G208 (= G206), G212 (= G210), F226 (= F224), G228 (= G226), G229 (≠ S227), T232 (≠ V230), V236 (≠ I234)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
34% identity, 98% coverage: 9:480/483 of query aligns to 11:484/490 of Q9HTJ1
- GAWN 150:153 (≠ SPWN 147:150) binding
- K162 (= K159) active site, Charge relay system
- KPSE 176:179 (≠ KPAN 173:176) binding
- G209 (= G206) binding
- GTST 230:233 (≠ SVPV 227:230) binding
- E252 (= E248) active site, Proton acceptor
- C286 (= C282) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E381) binding
- E464 (= E460) active site, Charge relay system
3iwjA Crystal structure of aminoaldehyde dehydrogenase 2 from pisum sativum (psamadh2) (see paper)
35% identity, 97% coverage: 9:478/483 of query aligns to 9:487/500 of 3iwjA
- active site: N159 (= N150), K182 (= K173), E257 (= E248), C291 (= C282), E390 (= E381), E467 (= E460)
- binding glycerol: D110 (≠ R104), Y160 (≠ F151), W167 (= W158), I290 (≠ K281), C291 (= C282), C450 (≠ T442), W456 (≠ F448)
- binding nicotinamide-adenine-dinucleotide: I155 (= I146), T156 (≠ S147), W158 (= W149), K182 (= K173), S184 (≠ A175), E185 (≠ N176), G215 (= G206), A220 (≠ Q211), F233 (= F224), G235 (= G226), S236 (= S227), T239 (≠ V230), I243 (= I234)
Q93YB2 Aminoaldehyde dehydrogenase 2, peroxisomal; PsAMADH2; Aminobutyraldehyde dehydrogenase AMADH2; Gamma-guanidinobutyraldehyde dehydrogenase AMADH2; EC 1.2.1.-; EC 1.2.1.19; EC 1.2.1.54 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
35% identity, 97% coverage: 9:478/483 of query aligns to 12:490/503 of Q93YB2
- I28 (≠ R23) binding
- D99 (≠ E90) binding
- W161 (= W149) binding
- K185 (= K173) binding
- L189 (≠ V177) binding
- S239 (= S227) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
33% identity, 93% coverage: 24:473/483 of query aligns to 27:478/495 of 4v37A
- active site: N157 (= N150), K180 (= K173), E255 (= E248), A289 (≠ C282), E388 (= E381), E465 (= E460)
- binding 3-aminopropan-1-ol: C448 (≠ T442), W454 (≠ F448)
- binding nicotinamide-adenine-dinucleotide: I153 (= I146), S154 (= S147), P155 (= P148), W156 (= W149), N157 (= N150), M162 (≠ T155), K180 (= K173), S182 (≠ A175), E183 (≠ N176), G213 (= G206), G217 (= G210), A218 (≠ Q211), T232 (= T225), G233 (= G226), S234 (= S227), T237 (≠ V230), E255 (= E248), L256 (≠ M249), A289 (≠ C282), E388 (= E381), F390 (= F383)
Query Sequence
>GFF3775 PGA1_262p01790 aldehyde dehydrogenase
MHDTKLNCIAGDWVAGATEIENRNPSDLNDLIGMFAQASPDQLDATLEQAQRAQVEWAGY
GIERKYNVLMAIGTEMMTRAEELGTLLAREEGKPLAEGKGEVYRAGQFFTYYAAETLRQM
GDTADSVRDGIEIDVRREPVGVVVVISPWNFPTATASWKIAPALCYGNAVVWKPANVTPA
SAVALVEIIARQDIPKGLVSLVMGAGSSIGQRLVESPKVNAISFTGSVPVGKGIAACAIQ
NLTRVQMEMGSKNALAVMDDADIDLAVSLALGGAFGGSGQKCTASSRLVVHQSIHDQFVE
KLVMGAKAMKVGHALEAGTQMGPVVSEQQLNENLAYVDLAASEGAELLCGGQRLEMATDG
YYVSPGIFVGTNNDMRINREEMFAPLACVIPVASYDEALHVVNDTNFGLTAGIVTTNLAR
ATHFRRNAQSGCVMVNLPTAGTDYHVPFGGRGDSSYGPREQGQTARDFYTIVKTAYIASG
TPQ
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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