SitesBLAST
Comparing PfGW456L13_3205 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3205 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, 99% coverage: 5:469/471 of query aligns to 12:477/485 of 6x9lA
- active site: N154 (= N147), E252 (= E245), A286 (≠ C279), E462 (= E454)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), T151 (≠ N144), W153 (= W146), N154 (= N147), Q159 (= Q152), K177 (= K170), E180 (≠ Q173), G210 (= G203), P211 (≠ S204), G214 (= G207), T229 (= T222), G230 (= G223), S231 (= S224), E252 (= E245), L253 (= L246), A286 (≠ C279), E386 (= E378), F388 (= F380), F451 (= F443)
- binding octanal: W155 (≠ Y148), S285 (≠ T278)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
44% identity, 99% coverage: 4:469/471 of query aligns to 5:475/483 of 3b4wA
- active site: N154 (= N147), K177 (= K170), E251 (= E245), C285 (= C279), E384 (= E378), E460 (= E454)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), V151 (≠ N144), W153 (= W146), N154 (= N147), K177 (= K170), I210 (≠ S204), G213 (= G207), T228 (= T222), G229 (= G223), S230 (= S224), V233 (≠ A227), E236 (≠ R230), E251 (= E245), L252 (= L246), C285 (= C279), E384 (= E378), F386 (= F380)
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)
38% identity, 99% coverage: 5:469/471 of query aligns to 8:482/497 of P17202
- I28 (= I25) binding
- D96 (≠ E91) binding
- SPW 156:158 (≠ NPW 144:146) binding
- Y160 (= Y148) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ G155) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPSQ 170:173) binding
- L186 (≠ E174) binding
- SSAT 236:239 (≠ STGA 224:227) binding
- V251 (= V239) binding in other chain
- L258 (= L246) binding
- W285 (≠ I273) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E378) binding
- A441 (≠ Q429) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ N438) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F443) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K447) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
37% identity, 99% coverage: 5:469/471 of query aligns to 6:480/495 of 4v37A
- active site: N157 (= N147), K180 (= K170), E255 (= E245), A289 (≠ C279), E388 (= E378), E465 (= E454)
- binding 3-aminopropan-1-ol: C448 (≠ N438), W454 (≠ F443)
- binding nicotinamide-adenine-dinucleotide: I153 (= I143), S154 (≠ N144), P155 (= P145), W156 (= W146), N157 (= N147), M162 (≠ Q152), K180 (= K170), S182 (= S172), E183 (≠ Q173), G213 (= G203), G217 (= G207), A218 (≠ E208), T232 (= T222), G233 (= G223), S234 (= S224), T237 (≠ A227), E255 (= E245), L256 (= L246), A289 (≠ C279), E388 (= E378), F390 (= F380)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
39% identity, 100% coverage: 1:469/471 of query aligns to 2:449/454 of 3ty7B
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 99% coverage: 2:469/471 of query aligns to 7:487/505 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 (≠ G155) 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.
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
39% identity, 99% coverage: 2:469/471 of query aligns to 5:485/503 of Q84LK3
- N162 (= N147) 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 (≠ G155) 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).
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
40% identity, 100% coverage: 2:471/471 of query aligns to 3:480/489 of 4cazA
- active site: N152 (= N147), K175 (= K170), E251 (= E245), C285 (= C279), E386 (= E378), E463 (= E454)
- 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 (= I143), G149 (≠ N144), W151 (= W146), N152 (= N147), K175 (= K170), E178 (≠ Q173), G208 (= G203), G212 (= G207), F226 (= F221), T227 (= T222), G228 (= G223), G229 (≠ S224), T232 (≠ A227), V236 (= V231), E251 (= E245), L252 (= L246), C285 (= C279), E386 (= E378), F388 (= F380)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
40% identity, 100% coverage: 2:471/471 of query aligns to 3:480/489 of 2woxA
- active site: N152 (= N147), K175 (= K170), E251 (= E245), C285 (= C279), E386 (= E378), E463 (= E454)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I143), G149 (≠ N144), W151 (= W146), N152 (= N147), K175 (= K170), S177 (= S172), E178 (≠ Q173), G208 (= G203), G212 (= G207), F226 (= F221), T227 (= T222), G228 (= G223), G229 (≠ S224), T232 (≠ A227), V236 (= V231), E251 (= E245), L252 (= L246), C285 (= C279), E386 (= E378), F388 (= F380)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
40% identity, 100% coverage: 2:471/471 of query aligns to 3:480/489 of 2wmeA
- active site: N152 (= N147), K175 (= K170), E251 (= E245), C285 (= C279), E386 (= E378), E463 (= E454)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ N144), W151 (= W146), K175 (= K170), S177 (= S172), E178 (≠ Q173), G208 (= G203), G212 (= G207), F226 (= F221), G228 (= G223), G229 (≠ S224), T232 (≠ A227), V236 (= V231)
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)
40% identity, 100% coverage: 2:471/471 of query aligns to 4:481/490 of Q9HTJ1
- GAWN 150:153 (≠ NPWN 144:147) binding
- K162 (= K156) active site, Charge relay system
- KPSE 176:179 (≠ KPSQ 170:173) binding
- G209 (= G203) binding
- GTST 230:233 (≠ STGA 224:227) binding
- E252 (= E245) active site, Proton acceptor
- C286 (= C279) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E378) binding
- E464 (= E454) active site, Charge relay system
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, 99% coverage: 2:469/471 of query aligns to 5:485/503 of Q8VWZ1
- N27 (≠ V24) binding
- I28 (= I25) binding
- D99 (≠ E91) binding
- L189 (≠ E174) binding
- 238:245 (vs. 223:230, 38% identical) binding
- C294 (= C279) binding
- E393 (= E378) binding
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 99% coverage: 7:471/471 of query aligns to 19:488/491 of 5gtlA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E378), E471 (= E454)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I143), P163 (= P145), K188 (= K170), A190 (≠ S172), E191 (≠ Q173), Q192 (≠ E174), G221 (= G203), G225 (= G207), G241 (= G223), S242 (= S224), T245 (≠ A227), L264 (= L246), C297 (= C279), E394 (= E378), F396 (= F380)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 99% coverage: 7:471/471 of query aligns to 19:488/491 of 5gtkA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E378), E471 (= E454)
- binding nicotinamide-adenine-dinucleotide: I161 (= I143), I162 (≠ N144), P163 (= P145), W164 (= W146), K188 (= K170), E191 (≠ Q173), G221 (= G203), G225 (= G207), A226 (≠ E208), F239 (= F221), G241 (= G223), S242 (= S224), T245 (≠ A227), Y248 (≠ R230), L264 (= L246), C297 (= C279), Q344 (= Q326), R347 (≠ T329), E394 (= E378), F396 (= F380)
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
39% identity, 99% coverage: 7:471/471 of query aligns to 13:482/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (= W146), K180 (= K170), A182 (≠ S172), T212 (≠ P202), G213 (= G203), G217 (= G207), F231 (= F221), G233 (= G223), S234 (= S224), V237 (≠ A227), Q337 (= Q326), E388 (= E378), F390 (= F380)
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
38% identity, 99% coverage: 3:469/471 of query aligns to 1:480/497 of 3iwkH
- active site: N157 (= N147), K180 (= K170), E255 (= E245), C289 (= C279), E388 (= E378), E465 (= E454)
- binding nicotinamide-adenine-dinucleotide: W156 (= W146), G213 (= G203), G217 (= G207), A218 (≠ E208), G233 (= G223), S234 (= S224), T237 (≠ A227), K240 (≠ R230), C289 (= C279), Q336 (= Q326), E388 (= E378), F390 (= F380)
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)
38% identity, 100% coverage: 1:469/471 of query aligns to 6:487/505 of C0P9J6
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
38% identity, 100% coverage: 1:469/471 of query aligns to 1:482/500 of 4i8pA
- active site: N159 (= N147), K182 (= K170), E257 (= E245), C291 (= C279), E390 (= E378), E467 (= E454)
- binding nicotinamide-adenine-dinucleotide: I155 (= I143), T156 (≠ N144), P157 (= P145), W158 (= W146), N159 (= N147), M164 (≠ Q152), K182 (= K170), S184 (= S172), E185 (≠ Q173), G215 (= G203), G219 (= G207), A220 (≠ E208), T234 (= T222), G235 (= G223), S236 (= S224), T239 (≠ A227), E257 (= E245), L258 (= L246), C291 (= C279), E390 (= E378), F392 (= F380), W456 (≠ F443)
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
39% identity, 100% coverage: 2:471/471 of query aligns to 2:479/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
39% identity, 100% coverage: 2:471/471 of query aligns to 2:479/488 of 8vr0A
Query Sequence
>PfGW456L13_3205 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3205
MLNHKTLFIDGRWQTPSGRGIAEVINPATEEACGSVPLGDELDVENAVASARRAFASWSR
TPSSVRAGYIRALADQLRNRADEMAAVITTELGMPVQWCRSVQVDGPITGLEQYVELAHL
MDEVREVGNSLVIREAVGVCAFINPWNYPLHQLIGKLAPALAAGCTVVVKPSQETPLHAF
LLAQMIEDIGLPAGVFNLVSGPGSKVGEALAKHPDVDMVSFTGSTGAGVRVAQAAAPSVK
RVCLELGGKSPLLIAEDADLAAAVRYGVQDVMINSGQTCTALTRMLLPASRYAEAVELAL
AETLSLRMGDPLDPQSFLGPMCSAGQKRTVLDYIKVGQQEGARLLCGGDTPSTFERGFYV
SPTLFADVDNRMRIAQEEIFGPVLCLIPYADETQAIQIANDSPFGLSSGVWAGSAERALQ
LGRQLRAGQCFLNGAAFNYQAPFGGYKQSGNGREWGEEGLNEFVEVKAIQV
Or try a new SitesBLAST search
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