SitesBLAST
Comparing PfGW456L13_3604 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3604 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)
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)
53% identity, 99% coverage: 4:488/490 of query aligns to 9:494/497 of P17202
- I28 (= I23) binding
- D96 (= D90) binding
- SPW 156:158 (≠ IPW 150:152) binding
- Y160 (= Y154) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W161) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 176:179) binding
- L186 (= L180) binding
- SSAT 236:239 (≠ SVPT 230:233) binding
- V251 (≠ I245) binding in other chain
- L258 (= L252) binding
- W285 (= W279) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E384) binding
- A441 (≠ I435) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ T444) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (= W450) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K454) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
53% identity, 99% coverage: 4:488/490 of query aligns to 7:492/495 of 4v37A
- active site: N157 (= N153), K180 (= K176), E255 (= E251), A289 (≠ C285), E388 (= E384), E465 (= E461)
- binding 3-aminopropan-1-ol: C448 (≠ T444), W454 (= W450)
- binding nicotinamide-adenine-dinucleotide: I153 (= I149), S154 (≠ I150), P155 (= P151), W156 (= W152), N157 (= N153), M162 (= M158), K180 (= K176), S182 (= S178), E183 (= E179), G213 (= G209), G217 (= G213), A218 (≠ S214), T232 (= T228), G233 (= G229), S234 (= S230), T237 (= T233), E255 (= E251), L256 (= L252), A289 (≠ C285), E388 (= E384), F390 (= F386)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
55% identity, 99% coverage: 2:488/490 of query aligns to 9:499/505 of O24174
- N164 (= N153) 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 (= W161) 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)
55% identity, 99% coverage: 4:488/490 of query aligns to 9:497/503 of Q84LK3
- N162 (= N153) 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 (= W161) 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).
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)
54% identity, 99% coverage: 4:488/490 of query aligns to 9:497/503 of Q93YB2
- I28 (= I23) binding
- D99 (= D90) binding
- W161 (= W152) binding
- K185 (= K176) binding
- L189 (= L180) binding
- S239 (= S230) binding
3iwjA Crystal structure of aminoaldehyde dehydrogenase 2 from pisum sativum (psamadh2) (see paper)
54% identity, 99% coverage: 4:488/490 of query aligns to 6:494/500 of 3iwjA
- active site: N159 (= N153), K182 (= K176), E257 (= E251), C291 (= C285), E390 (= E384), E467 (= E461)
- binding glycerol: D110 (= D104), Y160 (= Y154), W167 (= W161), I290 (≠ V284), C291 (= C285), C450 (≠ T444), W456 (= W450)
- binding nicotinamide-adenine-dinucleotide: I155 (= I149), T156 (≠ I150), W158 (= W152), K182 (= K176), S184 (= S178), E185 (= E179), G215 (= G209), A220 (≠ S214), F233 (= F227), G235 (= G229), S236 (= S230), T239 (= T233), I243 (= I237)
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)
54% identity, 99% coverage: 4:488/490 of query aligns to 11:499/505 of C0P9J6
4i8pA Crystal structure of aminoaldehyde dehydrogenase 1a from zea mays (zmamadh1a) (see paper)
54% identity, 99% coverage: 4:488/490 of query aligns to 6:494/500 of 4i8pA
- active site: N159 (= N153), K182 (= K176), E257 (= E251), C291 (= C285), E390 (= E384), E467 (= E461)
- binding nicotinamide-adenine-dinucleotide: I155 (= I149), T156 (≠ I150), P157 (= P151), W158 (= W152), N159 (= N153), M164 (= M158), K182 (= K176), S184 (= S178), E185 (= E179), G215 (= G209), G219 (= G213), A220 (≠ S214), T234 (= T228), G235 (= G229), S236 (= S230), T239 (= T233), E257 (= E251), L258 (= L252), C291 (= C285), E390 (= E384), F392 (= F386), W456 (= W450)
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)
54% identity, 99% coverage: 4:488/490 of query aligns to 9:497/503 of Q8VWZ1
- N27 (≠ V22) binding
- I28 (= I23) binding
- D99 (= D90) binding
- L189 (= L180) binding
- 238:245 (vs. 229:236, 63% identical) binding
- C294 (= C285) binding
- E393 (= E384) binding
3iwkH Crystal structure of aminoaldehyde dehydrogenase 1 from pisum sativum (psamadh1) (see paper)
54% identity, 99% coverage: 4:488/490 of query aligns to 4:492/497 of 3iwkH
- active site: N157 (= N153), K180 (= K176), E255 (= E251), C289 (= C285), E388 (= E384), E465 (= E461)
- binding nicotinamide-adenine-dinucleotide: W156 (= W152), G213 (= G209), G217 (= G213), A218 (≠ S214), G233 (= G229), S234 (= S230), T237 (= T233), K240 (= K236), C289 (= C285), Q336 (= Q332), E388 (= E384), F390 (= F386)
4i9bA Structure of aminoaldehyde dehydrogenase 1 from solanum lycopersium (slamadh1) with a thiohemiacetal intermediate (see paper)
54% identity, 99% coverage: 2:488/490 of query aligns to 5:493/496 of 4i9bA
- active site: N157 (= N153), K180 (= K176), E255 (= E251), C290 (= C285), E389 (= E384), D466 (≠ E461)
- binding (2-hydroxyethoxy)acetaldehyde: C290 (= C285), W455 (= W450)
- binding nicotinamide-adenine-dinucleotide: I153 (= I149), T154 (≠ I150), W156 (= W152), K180 (= K176), S182 (= S178), E183 (= E179), G213 (= G209), G217 (= G213), G218 (≠ S214), F231 (= F227), S234 (= S230), T237 (= T233), I241 (= I237)
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)
54% identity, 99% coverage: 2:488/490 of query aligns to 10:498/504 of Q56R04
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)
43% identity, 99% coverage: 6:490/490 of query aligns to 21:505/505 of 4neaA
- active site: N166 (= N153), K189 (= K176), E264 (= E251), C298 (= C285), E399 (= E384), E476 (= E461)
- binding nicotinamide-adenine-dinucleotide: P164 (= P151), K189 (= K176), E192 (= E179), G222 (= G209), G226 (= G213), G242 (= G229), G243 (≠ S230), T246 (= T233), H249 (≠ K236), I250 (= I237), C298 (= C285), E399 (= E384), F401 (= F386)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
45% identity, 96% coverage: 5:476/490 of query aligns to 25:493/503 of O14293
- S248 (= S230) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
43% identity, 97% coverage: 4:476/490 of query aligns to 18:486/491 of 5gtlA
- active site: N165 (= N153), K188 (= K176), E263 (= E251), C297 (= C285), E394 (= E384), E471 (= E461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I149), P163 (= P151), K188 (= K176), A190 (≠ S178), E191 (= E179), Q192 (≠ L180), G221 (= G209), G225 (= G213), G241 (= G229), S242 (= S230), T245 (= T233), L264 (= L252), C297 (= C285), E394 (= E384), F396 (= F386)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
43% identity, 97% coverage: 4:476/490 of query aligns to 18:486/491 of 5gtkA
- active site: N165 (= N153), K188 (= K176), E263 (= E251), C297 (= C285), E394 (= E384), E471 (= E461)
- binding nicotinamide-adenine-dinucleotide: I161 (= I149), I162 (= I150), P163 (= P151), W164 (= W152), K188 (= K176), E191 (= E179), G221 (= G209), G225 (= G213), A226 (≠ S214), F239 (= F227), G241 (= G229), S242 (= S230), T245 (= T233), Y248 (≠ K236), L264 (= L252), C297 (= C285), Q344 (= Q332), R347 (≠ K335), E394 (= E384), F396 (= F386)
O94788 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Homo sapiens (Human) (see 6 papers)
43% identity, 97% coverage: 4:477/490 of query aligns to 39:510/518 of O94788
- E50 (≠ D15) to G: in dbSNP:rs34266719
- A110 (= A73) to V: in dbSNP:rs35365164
- Q182 (= Q148) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (= IPW 150:152) binding
- KPAE 210:213 (≠ KPSE 176:179) binding
- STE 264:266 (≠ SVP 230:232) binding
- C320 (= C285) active site, Nucleophile
- R347 (≠ I312) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ S313) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ GQYDK 331:335) binding
- A383 (= A348) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E384) binding
- E436 (≠ Q403) to K: in dbSNP:rs34744827
- S461 (≠ A428) to Y: in DIH4; decreased retinoic acid biosynthetic process
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
43% identity, 97% coverage: 4:477/490 of query aligns to 13:484/492 of 6b5hA
- active site: N161 (= N153), E260 (= E251), C294 (= C285), E468 (= E461)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (vs. gap), G116 (≠ D104), F162 (≠ Y154), W169 (= W161), Q284 (≠ F275), F288 (≠ W279), T295 (≠ S286), N449 (≠ Q442), L451 (≠ T444), N452 (≠ F445), F457 (≠ W450)
- binding nicotinamide-adenine-dinucleotide: I157 (= I149), I158 (= I150), W160 (= W152), N161 (= N153), K184 (= K176), G217 (= G209), G221 (= G213), F235 (= F227), T236 (= T228), G237 (= G229), S238 (= S230), V241 (≠ T233), E260 (= E251), L261 (= L252), C294 (= C285), F393 (= F386)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
43% identity, 97% coverage: 4:477/490 of query aligns to 13:484/492 of 6b5gA
- active site: N161 (= N153), E260 (= E251), C294 (= C285), E468 (= E461)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ Y154), L165 (= L157), W169 (= W161), F288 (≠ W279), C293 (≠ V284), C294 (= C285), T295 (≠ S286), N449 (≠ Q442), L451 (≠ T444)
- binding nicotinamide-adenine-dinucleotide: I157 (= I149), I158 (= I150), P159 (= P151), W160 (= W152), N161 (= N153), M166 (= M158), K184 (= K176), E187 (= E179), G217 (= G209), G221 (= G213), F235 (= F227), T236 (= T228), G237 (= G229), S238 (= S230), V241 (≠ T233), E260 (= E251), L261 (= L252), C294 (= C285), E391 (= E384), F393 (= F386)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
43% identity, 97% coverage: 4:477/490 of query aligns to 13:484/492 of 6aljA
- active site: N161 (= N153), E260 (= E251), C294 (= C285), E468 (= E461)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ D104), F162 (≠ Y154), L165 (= L157), M166 (= M158), W169 (= W161), E260 (= E251), C293 (≠ V284), C294 (= C285), L451 (≠ T444), N452 (≠ F445), A453 (≠ V446)
- binding nicotinamide-adenine-dinucleotide: I157 (= I149), I158 (= I150), P159 (= P151), W160 (= W152), N161 (= N153), K184 (= K176), E187 (= E179), G217 (= G209), G221 (= G213), F235 (= F227), G237 (= G229), S238 (= S230), V241 (≠ T233), Q341 (= Q332), K344 (= K335), E391 (= E384), F393 (= F386)
Query Sequence
>PfGW456L13_3604 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3604
MRDQLYINGEWVSPDLGGYLDVIDPATEQAFHRVAAGTEEDVDHAVRAARRAFDNGWGQT
SGAERGQWLEALADELESGQQALAELEVRDNGKPLPEAQWDIGDAIACFRYYAGLARELD
QQQDQPLALPDARFCCRIRHEPIGVAGQIIPWNYPLLMAAWKVAPALAAGATVVLKPSEL
TPLTALELAAAADRIGLPAGVLNLVTGLGADAGSPLTEHPGVDKLAFTGSVPTGAKIMSA
AARDIKNISLELGGKSAFIVFDDADVEAAVEWILFGIFWNQGQVCSATSRLLVQETIAAR
LIERLVEETRKISIGPGMQPGVLLGPLVSQGQYDKVLGFIDQGLASGARLLTGGRRPAHL
REGYFVEPAIFDEPGHSSILWREEVFGPVLCIKRFKTEEQALQMANASRFGLAAAVMSAD
LQRTARVANQLRAGIVWVNCSQPTFVEAPWGGMKHSGIGRELGQWGLHNYLEVKQVTEYV
SDQPWGWYLK
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