SitesBLAST
Comparing PfGW456L13_1795 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1795 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)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
46% identity, 98% coverage: 9:480/482 of query aligns to 11:489/505 of O24174
- N164 (= N155) 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 (= W163) 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.
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)
43% identity, 100% coverage: 1:482/482 of query aligns to 1:486/497 of P17202
- I28 (= I26) binding
- D96 (≠ N92) binding
- SPW 156:158 (≠ VPW 152:154) binding
- Y160 (≠ F156) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W163) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 178:181) binding
- L186 (≠ V182) binding
- SSAT 236:239 (≠ SNAV 232:235) binding
- V251 (= V247) binding in other chain
- L258 (= L254) binding
- W285 (≠ F281) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E386) binding
- A441 (≠ L437) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ I446) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (= W452) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K456) binding
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)
46% identity, 100% coverage: 1:482/482 of query aligns to 1:489/503 of Q93YB2
- I28 (= I26) binding
- D99 (≠ N92) binding
- W161 (= W154) binding
- K185 (= K178) binding
- L189 (≠ V182) binding
- S239 (= S232) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
43% identity, 100% coverage: 3:482/482 of query aligns to 1:484/495 of 4v37A
- active site: N157 (= N155), K180 (= K178), E255 (= E253), A289 (≠ C287), E388 (= E386), E465 (= E463)
- binding 3-aminopropan-1-ol: C448 (≠ I446), W454 (= W452)
- binding nicotinamide-adenine-dinucleotide: I153 (= I151), S154 (≠ V152), P155 (= P153), W156 (= W154), N157 (= N155), M162 (≠ T160), K180 (= K178), S182 (= S180), E183 (= E181), G213 (= G211), G217 (= G215), A218 (= A216), T232 (= T230), G233 (= G231), S234 (= S232), T237 (≠ V235), E255 (= E253), L256 (= L254), A289 (≠ C287), E388 (= E386), F390 (= F388)
3iwjA Crystal structure of aminoaldehyde dehydrogenase 2 from pisum sativum (psamadh2) (see paper)
46% identity, 99% coverage: 4:482/482 of query aligns to 1:486/500 of 3iwjA
- active site: N159 (= N155), K182 (= K178), E257 (= E253), C291 (= C287), E390 (= E386), E467 (= E463)
- binding glycerol: D110 (= D106), Y160 (≠ F156), W167 (= W163), I290 (≠ M286), C291 (= C287), C450 (≠ I446), W456 (= W452)
- binding nicotinamide-adenine-dinucleotide: I155 (= I151), T156 (≠ V152), W158 (= W154), K182 (= K178), S184 (= S180), E185 (= E181), G215 (= G211), A220 (= A216), F233 (= F229), G235 (= G231), S236 (= S232), T239 (≠ V235), I243 (≠ V239)
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)
45% identity, 100% coverage: 1:480/482 of query aligns to 1:487/503 of Q8VWZ1
- N27 (≠ V25) binding
- I28 (= I26) binding
- D99 (≠ N92) binding
- L189 (≠ V182) binding
- 238:245 (vs. 231:238, 50% identical) binding
- C294 (= C287) binding
- E393 (= E386) binding
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
46% identity, 98% coverage: 10:480/482 of query aligns to 5:482/497 of 3iwkH
- active site: N157 (= N155), K180 (= K178), E255 (= E253), C289 (= C287), E388 (= E386), E465 (= E463)
- binding nicotinamide-adenine-dinucleotide: W156 (= W154), G213 (= G211), G217 (= G215), A218 (= A216), G233 (= G231), S234 (= S232), T237 (≠ V235), K240 (≠ Q238), C289 (= C287), Q336 (= Q334), E388 (= E386), F390 (= F388)
4i9bA Structure of aminoaldehyde dehydrogenase 1 from solanum lycopersium (slamadh1) with a thiohemiacetal intermediate (see paper)
45% identity, 97% coverage: 10:478/482 of query aligns to 8:481/496 of 4i9bA
- active site: N157 (= N155), K180 (= K178), E255 (= E253), C290 (= C287), E389 (= E386), D466 (≠ E463)
- binding (2-hydroxyethoxy)acetaldehyde: C290 (= C287), W455 (= W452)
- binding nicotinamide-adenine-dinucleotide: I153 (= I151), T154 (≠ V152), W156 (= W154), K180 (= K178), S182 (= S180), E183 (= E181), G213 (= G211), G217 (= G215), G218 (≠ A216), F231 (= F229), S234 (= S232), T237 (≠ V235), I241 (≠ V239)
Q56R04 Aminoaldehyde dehydrogenase 1; SlAMADH1; 4-trimethylammoniobutyraldehyde dehydrogenase AMADH1; Aminobutyraldehyde dehydrogenase AMADH1; Betaine aldehyde dehydrogenase AMADH1; Gamma-guanidinobutyraldehyde dehydrogenase AMADH1; 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 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) (see paper)
45% identity, 97% coverage: 10:478/482 of query aligns to 13:486/504 of Q56R04
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)
45% identity, 99% coverage: 7:482/482 of query aligns to 9:491/505 of C0P9J6
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
45% identity, 99% coverage: 7:482/482 of query aligns to 4:486/500 of 4i8pA
- active site: N159 (= N155), K182 (= K178), E257 (= E253), C291 (= C287), E390 (= E386), E467 (= E463)
- binding nicotinamide-adenine-dinucleotide: I155 (= I151), T156 (≠ V152), P157 (= P153), W158 (= W154), N159 (= N155), M164 (≠ T160), K182 (= K178), S184 (= S180), E185 (= E181), G215 (= G211), G219 (= G215), A220 (= A216), T234 (= T230), G235 (= G231), S236 (= S232), T239 (≠ V235), E257 (= E253), L258 (= L254), C291 (= C287), E390 (= E386), F392 (= F388), W456 (= W452)
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
44% identity, 97% coverage: 10:478/482 of query aligns to 10:485/503 of Q84LK3
- N162 (= N155) 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 (= W163) 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).
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)
40% identity, 97% coverage: 11:479/482 of query aligns to 21:492/505 of 4neaA
- active site: N166 (= N155), K189 (= K178), E264 (= E253), C298 (= C287), E399 (= E386), E476 (= E463)
- binding nicotinamide-adenine-dinucleotide: P164 (= P153), K189 (= K178), E192 (= E181), G222 (= G211), G226 (= G215), G242 (= G231), G243 (≠ S232), T246 (≠ V235), H249 (≠ Q238), I250 (≠ V239), C298 (= C287), E399 (= E386), F401 (= F388)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
43% identity, 98% coverage: 10:482/482 of query aligns to 18:491/496 of 4fr8C
- active site: N165 (= N155), K188 (= K178), Q264 (≠ E253), C298 (= C287), E395 (= E386), E472 (= E463)
- binding nicotinamide-adenine-dinucleotide: I161 (= I151), I162 (≠ V152), W164 (= W154), K188 (= K178), G221 (= G211), G225 (= G215), A226 (= A216), F239 (= F229), G241 (= G231), S242 (= S232), I245 (≠ V235), Q345 (= Q334), E395 (= E386), F397 (= F388)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
43% identity, 98% coverage: 10:482/482 of query aligns to 15:488/493 of 4fr8A
- active site: N162 (= N155), K185 (= K178), Q261 (≠ E253), C295 (= C287), E392 (= E386), E469 (= E463)
- binding nicotinamide-adenine-dinucleotide: I158 (= I151), I159 (≠ V152), W161 (= W154), K185 (= K178), G218 (= G211), G222 (= G215), A223 (= A216), F236 (= F229), G238 (= G231), S239 (= S232), I242 (≠ V235), Q342 (= Q334), K345 (≠ R337), E392 (= E386), F394 (= F388)
- binding propane-1,2,3-triyl trinitrate: F163 (= F156), L166 (≠ V159), W170 (= W163), F289 (= F281), S294 (≠ M286), C295 (= C287), D450 (≠ Q444), F452 (≠ I446)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
43% identity, 98% coverage: 10:482/482 of query aligns to 16:489/494 of 5l13A
- active site: N163 (= N155), K186 (= K178), E262 (= E253), C296 (= C287), E393 (= E386), E470 (= E463)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F156), M168 (≠ T160), W171 (= W163), F290 (= F281), C295 (≠ M286), C296 (= C287), C297 (≠ S288), D451 (≠ Q444), F453 (≠ I446)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
43% identity, 98% coverage: 10:482/482 of query aligns to 16:489/494 of 4kwgA
- active site: N163 (= N155), K186 (= K178), E262 (= E253), C296 (= C287), E393 (= E386), E470 (= E463)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F156), M168 (≠ T160), C295 (≠ M286), C296 (= C287), C297 (≠ S288), D451 (≠ Q444), F453 (≠ I446)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
43% identity, 98% coverage: 10:482/482 of query aligns to 16:489/494 of 4kwfA
- active site: N163 (= N155), K186 (= K178), E262 (= E253), C296 (= C287), E393 (= E386), E470 (= E463)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F156), M168 (≠ T160), W171 (= W163), E262 (= E253), C295 (≠ M286), C296 (= C287), C297 (≠ S288), D451 (≠ Q444), F453 (≠ I446), F459 (≠ W452)
3sz9A Crystal structure of human aldh2 modified with the beta-elimination product of aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one (see paper)
43% identity, 98% coverage: 10:482/482 of query aligns to 16:489/494 of 3sz9A
- active site: N163 (= N155), K186 (= K178), E262 (= E253), C296 (= C287), E393 (= E386), E470 (= E463)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F156), C295 (≠ M286), C296 (= C287), D451 (≠ Q444), F453 (≠ I446), F459 (≠ W452)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
43% identity, 98% coverage: 10:482/482 of query aligns to 16:489/494 of 3injA
- active site: N163 (= N155), K186 (= K178), E262 (= E253), C296 (= C287), E393 (= E386), E470 (= E463)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ D106), F164 (= F156), L167 (≠ V159), F286 (≠ G277), F290 (= F281), D451 (≠ Q444), F453 (≠ I446)
Query Sequence
>PfGW456L13_1795 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1795
MSFPTTLDGLYINGQWSAGNEHLRVINPATEALLTTVNGGDERAVDQAVSAATQAFADWS
KTSGAERGAILRKIATGVQANREKLMHLQSSNNGKPQFEAAIDVDDVIATFEYYAGLAEG
LDAKQDSAVELPTDDFSARLRREPCGVVGLIVPWNFPMVTTAWKLAPALAAGCCVVLKPS
EVTPLPELELAAIIAEAGVPAGVFNLVCGTGLAVGAPLSADPRIAKVSFTGSNAVGVQVM
QRAAETVKGVSLELGGKSSLLVLADADPELAVEVACGGGFFNAGQMCSATSRVLVADELA
DEFLNRVKARAEAIRVADPFDPNVEMGALVNQAQYQRVLGHIDRGLSAGAKLVCGGNRPA
DLPRGYFLQPTVFTEVPLDSALWNEEIFGPVICVRRFASEAEAIALANDSQFGLVASVVT
RNAQTADRVANALQAGLVWINAPQVIFPQTAWGGYKQSSIGRELGPWGLQAFQEIKHVIR
AV
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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