SitesBLAST
Comparing Pf6N2E2_3126 4-aminobutyraldehyde dehydrogenase (EC 1.2.1.19) 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)
4f3xA Crystal structure of putative aldehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD
64% identity, 98% coverage: 8:482/485 of query aligns to 2:476/476 of 4f3xA
- active site: N150 (= N156), K173 (= K179), E247 (= E253), C281 (= C287), E379 (= E385), D456 (= D462)
- binding nicotinamide-adenine-dinucleotide: I146 (= I152), A147 (= A153), P148 (= P154), W149 (= W155), K173 (= K179), E176 (= E182), G205 (= G211), G209 (= G215), I213 (≠ V219), I223 (≠ L229), G225 (= G231), D226 (= D232), T229 (= T235), G249 (= G255), C281 (= C287), Q328 (= Q334), R331 (= R337), E379 (= E385), F381 (= F387)
P77674 Gamma-aminobutyraldehyde dehydrogenase; ABALDH; 1-pyrroline dehydrogenase; 4-aminobutanal dehydrogenase; 5-aminopentanal dehydrogenase; EC 1.2.1.19; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
63% identity, 97% coverage: 12:481/485 of query aligns to 5:474/474 of P77674
1wndA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal structure (see paper)
63% identity, 97% coverage: 12:481/485 of query aligns to 5:474/474 of 1wndA
- active site: N149 (= N156), K172 (= K179), E246 (= E253), C280 (= C287), E378 (= E385), D455 (= D462)
- binding calcium ion: G249 (= G256), K250 (= K257), A251 (= A258), G405 (= G412), L406 (= L413), A407 (= A414), Y427 (= Y434)
1wnbB Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
63% identity, 97% coverage: 12:481/485 of query aligns to 5:474/474 of 1wnbB
- active site: N149 (= N156), K172 (= K179), E246 (= E253), C280 (= C287), E378 (= E385), D455 (= D462)
- binding betaine aldehyde: D279 (= D286), F436 (= F443), L438 (= L445)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (= I152), A146 (= A153), W148 (= W155), K172 (= K179), G204 (= G211), G208 (= G215), D209 (≠ S216), T223 (= T230), G224 (= G231), S225 (≠ D232), T228 (= T235), H231 (≠ K238), G248 (= G255), E378 (= E385)
1wnbA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
63% identity, 97% coverage: 12:481/485 of query aligns to 5:474/474 of 1wnbA
- active site: N149 (= N156), K172 (= K179), E246 (= E253), C280 (= C287), E378 (= E385), D455 (= D462)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (= I152), A146 (= A153), W148 (= W155), K172 (= K179), G204 (= G211), G208 (= G215), D209 (≠ S216), G224 (= G231), S225 (≠ D232), T228 (= T235), H231 (≠ K238), G248 (= G255), F380 (= F387)
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)
39% identity, 97% coverage: 14:485/485 of query aligns to 22:499/505 of 4neaA
- active site: N166 (= N156), K189 (= K179), E264 (= E253), C298 (= C287), E399 (= E385), E476 (≠ D462)
- binding nicotinamide-adenine-dinucleotide: P164 (= P154), K189 (= K179), E192 (= E182), G222 (= G211), G226 (= G215), G242 (= G231), G243 (≠ D232), T246 (= T235), H249 (≠ K238), I250 (= I239), C298 (= C287), E399 (= E385), F401 (= F387)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
40% identity, 97% coverage: 8:477/485 of query aligns to 2:475/489 of 4o6rA
- active site: N150 (= N156), K173 (= K179), E248 (= E253), C282 (= C287), E383 (= E385), E460 (≠ D462)
- binding adenosine monophosphate: I146 (= I152), V147 (≠ A153), K173 (= K179), G206 (= G211), G210 (= G215), Q211 (≠ S216), F224 (≠ L229), G226 (= G231), S227 (≠ D232), T230 (= T235), R233 (≠ K238)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 96% coverage: 12:477/485 of query aligns to 19:486/491 of 5gtlA
- active site: N165 (= N156), K188 (= K179), E263 (= E253), C297 (= C287), E394 (= E385), E471 (≠ D462)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I152), P163 (= P154), K188 (= K179), A190 (≠ S181), E191 (= E182), Q192 (≠ H183), G221 (= G211), G225 (= G215), G241 (= G231), S242 (≠ D232), T245 (= T235), L264 (= L254), C297 (= C287), E394 (= E385), F396 (= F387)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 96% coverage: 12:477/485 of query aligns to 19:486/491 of 5gtkA
- active site: N165 (= N156), K188 (= K179), E263 (= E253), C297 (= C287), E394 (= E385), E471 (≠ D462)
- binding nicotinamide-adenine-dinucleotide: I161 (= I152), I162 (≠ A153), P163 (= P154), W164 (= W155), K188 (= K179), E191 (= E182), G221 (= G211), G225 (= G215), A226 (≠ S216), F239 (≠ L229), G241 (= G231), S242 (≠ D232), T245 (= T235), Y248 (≠ K238), L264 (= L254), C297 (= C287), Q344 (= Q334), R347 (= R337), E394 (= E385), F396 (= F387)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
40% identity, 96% coverage: 12:477/485 of query aligns to 5:473/487 of 4go4A
- active site: N149 (= N156), K172 (= K179), E247 (= E253), C281 (= C287), E381 (= E385), E458 (≠ D462)
- binding nicotinamide-adenine-dinucleotide: I145 (= I152), V146 (≠ A153), W148 (= W155), N149 (= N156), F154 (≠ M161), K172 (= K179), G205 (= G211), G209 (= G215), Q210 (≠ S216), F223 (≠ L229), T224 (= T230), G225 (= G231), S226 (≠ D232), T229 (= T235), E247 (= E253), G249 (= G255), C281 (= C287), E381 (= E385), F383 (= F387)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
37% identity, 98% coverage: 12:484/485 of query aligns to 8:485/489 of 4cazA
- active site: N152 (= N156), K175 (= K179), E251 (= E253), C285 (= C287), E386 (= E385), E463 (≠ D462)
- 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 (= I152), G149 (≠ A153), W151 (= W155), N152 (= N156), K175 (= K179), E178 (= E182), G208 (= G211), G212 (= G215), F226 (≠ L229), T227 (= T230), G228 (= G231), G229 (≠ D232), T232 (= T235), V236 (≠ I239), E251 (= E253), L252 (= L254), C285 (= C287), E386 (= E385), F388 (= F387)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
37% identity, 98% coverage: 12:484/485 of query aligns to 8:485/489 of 2woxA
- active site: N152 (= N156), K175 (= K179), E251 (= E253), C285 (= C287), E386 (= E385), E463 (≠ D462)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I152), G149 (≠ A153), W151 (= W155), N152 (= N156), K175 (= K179), S177 (= S181), E178 (= E182), G208 (= G211), G212 (= G215), F226 (≠ L229), T227 (= T230), G228 (= G231), G229 (≠ D232), T232 (= T235), V236 (≠ I239), E251 (= E253), L252 (= L254), C285 (= C287), E386 (= E385), F388 (= F387)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
37% identity, 98% coverage: 12:484/485 of query aligns to 8:485/489 of 2wmeA
- active site: N152 (= N156), K175 (= K179), E251 (= E253), C285 (= C287), E386 (= E385), E463 (≠ D462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ A153), W151 (= W155), K175 (= K179), S177 (= S181), E178 (= E182), G208 (= G211), G212 (= G215), F226 (≠ L229), G228 (= G231), G229 (≠ D232), T232 (= T235), V236 (≠ I239)
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)
37% identity, 98% coverage: 12:484/485 of query aligns to 9:486/490 of Q9HTJ1
- GAWN 150:153 (≠ APWN 153:156) binding
- K162 (= K165) active site, Charge relay system
- KPSE 176:179 (= KPSE 179:182) binding
- G209 (= G211) binding
- GTST 230:233 (≠ DIVT 232:235) binding
- E252 (= E253) active site, Proton acceptor
- C286 (= C287) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E385) binding
- E464 (≠ D462) active site, Charge relay system
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
35% identity, 99% coverage: 1:481/485 of query aligns to 1:487/487 of Q9H2A2
- R109 (≠ A110) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N156) mutation to A: Complete loss of activity.
- R451 (≠ L445) mutation to A: Complete loss of activity.
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 97% coverage: 10:478/485 of query aligns to 20:492/501 of Q56YU0
- G152 (= G136) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A402) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
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)
37% identity, 96% coverage: 12:477/485 of query aligns to 10:482/497 of P17202
- I28 (≠ L29) binding
- D96 (≠ N95) binding
- SPW 156:158 (≠ APW 153:155) binding
- Y160 (= Y157) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W164) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 179:182) binding
- L186 (≠ H183) binding
- SSAT 236:239 (≠ DIVT 232:235) binding
- V251 (≠ L247) binding in other chain
- L258 (= L254) binding
- W285 (≠ Y281) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E385) binding
- A441 (≠ C436) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ L445) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ H451) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K455) binding
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)
38% identity, 96% coverage: 4:471/485 of query aligns to 1:469/479 of P25553
- M1 (= M4) modified: Initiator methionine, Removed
- L150 (≠ A153) binding
- R161 (≠ W164) binding
- KPSE 176:179 (= KPSE 179:182) binding
- F180 (≠ H183) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ S216) binding
- S230 (≠ D232) binding
- E251 (= E253) binding
- N286 (≠ T288) 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 (= R337) binding
- E443 (≠ L445) binding
- H449 (= H451) binding
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)
35% identity, 98% coverage: 10:484/485 of query aligns to 38:516/518 of O94788
- E50 (vs. gap) to G: in dbSNP:rs34266719
- A110 (= A78) to V: in dbSNP:rs35365164
- Q182 (≠ S151) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ APW 153:155) binding
- KPAE 210:213 (≠ KPSE 179:182) binding
- STE 264:266 (≠ DIV 232:234) binding
- C320 (= C287) active site, Nucleophile
- R347 (≠ L314) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ R315) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ RQRDR 333:337) binding
- A383 (= A357) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E385) binding
- E436 (≠ D404) to K: in dbSNP:rs34744827
- S461 (≠ A429) 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)
35% identity, 98% coverage: 10:484/485 of query aligns to 12:490/492 of 6b5hA
- active site: N161 (= N156), E260 (= E253), C294 (= C287), E468 (≠ D462)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ D106), G116 (≠ A110), F162 (≠ Y157), W169 (= W164), Q284 (≠ T277), F288 (≠ Y281), T295 (= T288), N449 (≠ F443), L451 (= L445), N452 (≠ V446), F457 (≠ H451)
- binding nicotinamide-adenine-dinucleotide: I157 (= I152), I158 (≠ A153), W160 (= W155), N161 (= N156), K184 (= K179), G217 (= G211), G221 (= G215), F235 (≠ L229), T236 (= T230), G237 (= G231), S238 (≠ D232), V241 (≠ T235), E260 (= E253), L261 (= L254), C294 (= C287), F393 (= F387)
Query Sequence
>Pf6N2E2_3126 4-aminobutyraldehyde dehydrogenase (EC 1.2.1.19)
MAGMQTPLCTALLIDGELVPGAGIVEPILNPATGEVVAHIAEASTEQVEAAILAAHRAFD
GWSRTTPQQRSNLLLDIASAIEKNADELARLESLNCGKPLYLARQDDLSATVDVFRFFAG
AVRCQTGQLSGEYLPGYTSMVRRDPIGVVASIAPWNYPIMMAAWKIAPALAAGNTLVFKP
SEHTPLSILALAPTLAQILPRGVINILCGGGEGVGSHLVSHPKVRMVSLTGDIVTGQKIL
QAAAKTLKRTHLELGGKAPVIVCNDADIQAVVEGVRTYGYYNAGQDCTAACRIYAQGAIH
DRLVAELGAAVSSLRFAGKRDADNEIGPLISTRQRDRVASFVERALGQPHIERITGAAVH
SGAGFYYQPTLLAGCKQSDEIVQREVFGPVVTVTRFDELSQAVDWANDSEYGLASSVWTQ
NLDKAMQVAARLQYGCTWINSHFMLVSEMPHGGLKRSGYGKDLSSDSLQDYSVVRHIMAR
HGQHL
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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