SitesBLAST
Comparing SMa1415 SMa1415 aldehyde dehydrogenase 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)
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
76% identity, 99% coverage: 8:498/498 of query aligns to 2:492/492 of 7w5nA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: W156 (= W162), K180 (= K186), A182 (≠ S188), T212 (≠ S218), G213 (= G219), G217 (= G223), F231 (= F237), G233 (= G239), S234 (= S240), V237 (= V243), Q337 (= Q343), E388 (= E394), F390 (= F396)
7w5kA The c296a mutant of l-sorbosone dehydrogenase (sndh) from gluconobacter oxydans wsh-004 (see paper)
76% identity, 99% coverage: 8:498/498 of query aligns to 1:491/491 of 7w5kA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (= I159), T153 (= T160), P154 (= P161), W155 (= W162), N156 (= N163), I161 (= I168), K179 (= K186), A181 (≠ S188), E182 (= E189), T211 (≠ S218), G212 (= G219), G216 (= G223), Q217 (= Q224), F230 (= F237), T231 (= T238), G232 (= G239), S233 (= S240), V236 (= V243), E255 (= E262), L256 (= L263), G257 (= G264), A289 (≠ C296), E387 (= E394), F389 (= F396)
3u4jA Crystal structure of NAD-dependent aldehyde dehydrogenase from sinorhizobium meliloti
49% identity, 99% coverage: 4:498/498 of query aligns to 3:505/505 of 3u4jA
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)
42% identity, 94% coverage: 19:486/498 of query aligns to 22:491/501 of Q56YU0
- G152 (= G146) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A411) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
44% identity, 96% coverage: 18:497/498 of query aligns to 17:494/494 of 4pz2B
- active site: N159 (= N163), K182 (= K186), E258 (= E262), C292 (= C296), E392 (= E394), D469 (≠ E471)
- binding nicotinamide-adenine-dinucleotide: I155 (= I159), I156 (≠ T160), P157 (= P161), W158 (= W162), N159 (= N163), M164 (≠ I168), K182 (= K186), A184 (≠ S188), E185 (= E189), G215 (= G219), G219 (= G223), F233 (= F237), T234 (= T238), G235 (= G239), S236 (= S240), V239 (= V243), E258 (= E262), L259 (= L263), C292 (= C296), E392 (= E394), F394 (= F396)
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)
42% identity, 92% coverage: 36:491/498 of query aligns to 28:484/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 160:163) binding
- K162 (≠ R172) active site, Charge relay system
- KPSE 176:179 (= KPSE 186:189) binding
- G209 (= G219) binding
- GTST 230:233 (≠ STAV 240:243) binding
- E252 (= E262) active site, Proton acceptor
- C286 (= C296) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E394) binding
- E464 (= E471) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
42% identity, 92% coverage: 36:491/498 of query aligns to 27:483/489 of 4cazA
- active site: N152 (= N163), K175 (= K186), E251 (= E262), C285 (= C296), E386 (= E394), E463 (= E471)
- 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 (= I159), G149 (≠ T160), W151 (= W162), N152 (= N163), K175 (= K186), E178 (= E189), G208 (= G219), G212 (= G223), F226 (= F237), T227 (= T238), G228 (= G239), G229 (≠ S240), T232 (≠ V243), V236 (≠ C247), E251 (= E262), L252 (= L263), C285 (= C296), E386 (= E394), F388 (= F396)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
42% identity, 92% coverage: 36:491/498 of query aligns to 27:483/489 of 2woxA
- active site: N152 (= N163), K175 (= K186), E251 (= E262), C285 (= C296), E386 (= E394), E463 (= E471)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I159), G149 (≠ T160), W151 (= W162), N152 (= N163), K175 (= K186), S177 (= S188), E178 (= E189), G208 (= G219), G212 (= G223), F226 (= F237), T227 (= T238), G228 (= G239), G229 (≠ S240), T232 (≠ V243), V236 (≠ C247), E251 (= E262), L252 (= L263), C285 (= C296), E386 (= E394), F388 (= F396)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
42% identity, 92% coverage: 36:491/498 of query aligns to 27:483/489 of 2wmeA
- active site: N152 (= N163), K175 (= K186), E251 (= E262), C285 (= C296), E386 (= E394), E463 (= E471)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T160), W151 (= W162), K175 (= K186), S177 (= S188), E178 (= E189), G208 (= G219), G212 (= G223), F226 (= F237), G228 (= G239), G229 (≠ S240), T232 (≠ V243), V236 (≠ C247)
5iuwA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ and iaa (see paper)
42% identity, 95% coverage: 20:490/498 of query aligns to 21:495/495 of 5iuwA
- active site: N166 (= N163), K189 (= K186), E265 (= E262), C300 (= C296), E399 (= E394), D476 (≠ E471)
- binding 1h-indol-3-ylacetic acid: F167 (= F164), M170 (≠ L167), C300 (= C296), D457 (≠ M452), F465 (≠ L460)
- binding nicotinamide-adenine-dinucleotide: I162 (= I159), V163 (≠ T160), P164 (= P161), W165 (= W162), N166 (= N163), K189 (= K186), G222 (= G219), G226 (= G223), K227 (≠ Q224), F240 (= F237), T241 (= T238), G242 (= G239), S243 (= S240), I246 (≠ V243), Y253 (≠ A250), E265 (= E262), A266 (≠ L263), C300 (= C296), E399 (= E394), F401 (= F396)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
42% identity, 95% coverage: 20:490/498 of query aligns to 21:495/495 of 5iuvA
- active site: N166 (= N163), K189 (= K186), E265 (= E262), C300 (= C296), E399 (= E394), D476 (≠ E471)
- binding nicotinamide-adenine-dinucleotide: I162 (= I159), V163 (≠ T160), P164 (= P161), W165 (= W162), N166 (= N163), K189 (= K186), S191 (= S188), G222 (= G219), G226 (= G223), K227 (≠ Q224), F240 (= F237), T241 (= T238), G242 (= G239), S243 (= S240), I246 (≠ V243), Y253 (≠ A250), E265 (= E262), A266 (≠ L263), C300 (= C296), E399 (= E394), F401 (= F396)
7jsoA P. Syringae alda indole-3-acetaldehyde dehydrogenase c302a mutant in complex with NAD+ and iaa (see paper)
42% identity, 95% coverage: 20:490/498 of query aligns to 21:495/495 of 7jsoA
- active site: N166 (= N163), E265 (= E262), A300 (≠ C296), D476 (≠ E471)
- binding 1h-indol-3-ylacetic acid: F167 (= F164), W174 (≠ E171), V299 (≠ C295), A300 (≠ C296), T301 (≠ V297), D457 (≠ M452), F465 (≠ L460)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I162 (= I159), V163 (≠ T160), P164 (= P161), W165 (= W162), K189 (= K186), E192 (= E189), G222 (= G219), G226 (= G223), K227 (≠ Q224), F240 (= F237), G242 (= G239), S243 (= S240), I246 (≠ V243), A266 (≠ L263), G267 (= G264), A300 (≠ C296), E399 (= E394), F401 (= F396)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
42% identity, 96% coverage: 19:497/498 of query aligns to 8:486/486 of 4pxlA
- active site: N154 (= N163), K177 (= K186), E253 (= E262), C287 (= C296), E384 (= E394), D461 (≠ E471)
- binding nicotinamide-adenine-dinucleotide: I150 (= I159), V151 (≠ T160), P152 (= P161), W153 (= W162), K177 (= K186), E180 (= E189), G210 (= G219), G214 (= G223), A215 (≠ Q224), F228 (= F237), G230 (= G239), S231 (= S240), V234 (= V243), E253 (= E262), G255 (= G264), C287 (= C296), Q334 (= Q343), K337 (≠ T346), E384 (= E394), F386 (= F396)
P47895 Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; Aldehyde dehydrogenase 6; Aldehyde dehydrogenase family 1 member A3; ALDH1A3; EC 1.2.1.36 from Homo sapiens (Human) (see 2 papers)
41% identity, 98% coverage: 9:494/498 of query aligns to 16:511/512 of P47895
- R89 (≠ S71) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K186) binding
- E207 (= E189) binding
- GSTEVG 257:262 (≠ GSTAVG 239:244) binding
- Q361 (= Q343) binding
- E411 (= E394) binding
- A493 (≠ G476) to P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
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)
39% identity, 95% coverage: 19:490/498 of query aligns to 10:486/497 of P17202
- I28 (≠ H35) binding
- D96 (≠ E103) binding
- SPW 156:158 (≠ TPW 160:162) binding
- Y160 (≠ F164) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ E171) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 186:189) binding
- L186 (≠ V190) binding
- SSAT 236:239 (≠ STAV 240:243) binding
- V251 (≠ F256) binding in other chain
- L258 (= L263) binding
- W285 (≠ F290) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E394) binding
- A441 (≠ R445) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ G454) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ L460) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K464) binding
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
42% identity, 95% coverage: 20:491/498 of query aligns to 16:489/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I159), T159 (= T160), P160 (= P161), W161 (= W162), K185 (= K186), E188 (= E189), G218 (= G219), G222 (= G223), F236 (= F237), S239 (= S240), V242 (= V243)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
41% identity, 95% coverage: 18:491/498 of query aligns to 24:498/503 of O14293
- S248 (= S240) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
Q28399 Aldehyde dehydrogenase, cytosolic 1; ALDH class 1; ETA-crystallin; EC 1.2.1.3 from Elephantulus edwardii (Cape long-eared elephant shrew) (see paper)
40% identity, 96% coverage: 19:494/498 of query aligns to 23:500/501 of Q28399
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
42% identity, 95% coverage: 20:490/498 of query aligns to 17:489/489 of 7a6qB
- active site: N163 (= N163), E262 (= E262), C296 (= C296), E470 (= E471)
- binding nicotinamide-adenine-dinucleotide: I159 (= I159), W162 (= W162), K186 (= K186), E189 (= E189), G219 (= G219), G223 (= G223), S240 (= S240), V243 (= V243), K342 (≠ A342)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (≠ V33), T33 (≠ R34), C34 (≠ H35), P36 (= P37), D103 (≠ E103), E189 (= E189), Q190 (≠ V190), F218 (≠ S218), I339 (≠ T339), D340 (≠ T340)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ H117), D141 (≠ G141), N143 (≠ G143), N451 (≠ M452), L453 (≠ G454), A455 (≠ P456)
1o9jA The x-ray crystal structure of eta-crystallin (see paper)
40% identity, 96% coverage: 19:494/498 of query aligns to 16:493/494 of 1o9jA
- active site: N163 (= N163), K186 (= K186), E262 (= E262), C296 (= C296), E393 (= E394), E470 (= E471)
- binding nicotinamide-adenine-dinucleotide: I159 (= I159), F160 (≠ T160), P161 (= P161), W162 (= W162), N163 (= N163), K186 (= K186), E189 (= E189), G219 (= G219), G223 (= G223), F237 (= F237), T238 (= T238), G239 (= G239), S240 (= S240), V243 (= V243), E262 (= E262), L263 (= L263), C296 (= C296), E393 (= E394), F395 (= F396), L421 (= L422)
Query Sequence
>SMa1415 SMa1415 aldehyde dehydrogenase
MDQLNNFLSPPAAPRDFGFFVDGKWQSGHDFFVRHSPGHGVAVTRTAKCSVDDLNAAVAA
ARRAFEDRRWSGLPGGSRASVLLRVAEILRTRRDELAYWETLENGKPIAQARGEIDHCIA
CFEVGAGAARLLHGDSFNSLGDGLFGMVLREPIGVVGLITPWNFPFLILCERVPFILASG
CTMVVKPSEVTSATTLILAEVLAEAGLPDGVYNVITGSGRTIGQAMSEHPDIDMLSFTGS
TAVGRSCVHAAADSNFKKLGLELGGKNPIIVFADSDLEDAADGAAFGISFNTGQCCVSSS
RLIVERSVAREFEALLAEKMKRIRVGDPLDETTQVGAITTEAQNTTILDYIAKGKTEGAE
LVTGGTAIDLGRGQYIAPTLFSGVSREMAIARDEIFGPVLCSMTFDTVEQAVELANDTVY
GLAASVWTKNIDKALTVTRRVRAGRFWVNTMMAGGPEMPLGGFKQSGWGREAGMYGVEEY
TQVKSVHVEIGKRTHWIS
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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