SitesBLAST
Comparing AO356_00680 FitnessBrowser__pseudo5_N2C3_1:AO356_00680 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)
Q8NMB0 Vanillin dehydrogenase; Aromatic aldehyde dehydrogenase; EC 1.2.1.67; EC 1.2.1.64; EC 1.2.1.96 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
54% identity, 95% coverage: 15:481/492 of query aligns to 13:479/484 of Q8NMB0
- N157 (= N159) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 2.3-fold decreased affinity for vanillin compared to the wild type.
- K180 (= K182) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 5-fold decreased affinity for vanillin compared to the wild type.
- E199 (= E201) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 78% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 5-fold decreased affinity for NAD(+), 2.5-fold decreased affinity for NADP(+) and 1.5-fold decreased affinity for vanillin compared to the wild type.
- E258 (= E260) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 24% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 3.5-fold decreased affinity for NAD(+), 5-fold decreased affinity for NADP(+) and 3.7-fold decreased affinity for vanillin compared to the wild type.
- C292 (= C294) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 7-fold decreased affinity for NADP(+) and 8-fold decreased affinity for vanillin compared to the wild type.
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
37% identity, 97% coverage: 15:491/492 of query aligns to 10:484/490 of 5ekcE
- active site: N154 (= N159), K177 (= K182), E252 (= E260), C286 (= C294), E381 (= E388), E459 (≠ F466)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (= I155), T151 (≠ S156), P152 (= P157), W153 (= W158), K177 (= K182), S180 (= S185), G210 (= G216), G214 (= G220), F228 (= F234), G230 (= G236), E231 (≠ S237), T234 (≠ V240), N331 (= N338), R333 (≠ S340), Q334 (= Q341)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
37% identity, 97% coverage: 15:491/492 of query aligns to 3:477/482 of 5ek6A
- active site: N147 (= N159), K170 (= K182), E245 (= E260), C279 (= C294), E374 (= E388), E452 (≠ F466)
- binding 2-methylpropanal: I152 (≠ L164), K155 (≠ R167), T222 (= T235), E245 (= E260), F441 (= F455)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (= I155), T144 (≠ S156), W146 (= W158), N147 (= N159), I152 (≠ L164), K170 (= K182), A172 (= A184), S173 (= S185), P202 (≠ A215), G203 (= G216), G207 (= G220), F221 (= F234), T222 (= T235), G223 (= G236), E224 (≠ S237), T227 (≠ V240), I231 (≠ V244), E245 (= E260), L246 (= L261), C279 (= C294), E374 (= E388)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
37% identity, 97% coverage: 15:491/492 of query aligns to 3:477/482 of 4h73A
- active site: N147 (= N159), K170 (= K182), E245 (= E260), C279 (= C294), E374 (= E388), E452 (≠ F466)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (= I155), T144 (≠ S156), P145 (= P157), W146 (= W158), K170 (= K182), A172 (= A184), S173 (= S185), G203 (= G216), G207 (= G220), F221 (= F234), G223 (= G236), E224 (≠ S237), T227 (≠ V240)
4jz6A Crystal structure of a salicylaldehyde dehydrogenase from pseudomonas putida g7 complexed with salicylaldehyde (see paper)
37% identity, 97% coverage: 16:492/492 of query aligns to 7:484/484 of 4jz6A
- active site: N150 (= N159), K173 (= K182), E251 (= E260), C285 (= C294), E380 (= E388), F458 (= F466)
- binding salicylaldehyde: W97 (≠ K106), G151 (≠ F160), V154 (≠ Y163), R247 (= R256), C248 (≠ V257), I284 (= I293), C285 (= C294), M286 (= M295), Y447 (≠ F455), Y455 (≠ L463)
6tgwA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with a selective inhibitor (see paper)
36% identity, 95% coverage: 16:482/492 of query aligns to 9:475/478 of 6tgwA
- active site: N155 (= N159), E254 (= E260), C288 (= C294), E459 (≠ F466)
- binding methyl 5-(1,3-benzodioxol-5-yl)-2-phenyl-pyrazolo[1,5-a]pyrimidine-7-carboxylate: I106 (≠ M109), G110 (≠ F113), F156 (= F160), Q278 (≠ V284), F282 (≠ L288), L442 (≠ D449), A444 (≠ P451)
- binding nicotinamide-adenine-dinucleotide: I151 (= I155), T152 (≠ S156), P153 (= P157), W154 (= W158), K178 (= K182), G211 (= G216), G215 (= G220), F229 (= F234), G231 (= G236), S232 (= S237), V235 (= V240)
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)
36% identity, 96% coverage: 16:489/492 of query aligns to 35:511/512 of P47895
- R89 (≠ A67) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K182) binding
- E207 (≠ S185) binding
- GSTEVG 257:262 (≠ GSTDVG 236:241) binding
- Q361 (= Q341) binding
- E411 (= E388) binding
- A493 (= A471) 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
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
36% identity, 96% coverage: 16:486/492 of query aligns to 16:489/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I155), T159 (≠ S156), P160 (= P157), W161 (= W158), K185 (= K182), E188 (≠ S185), G218 (= G216), G222 (= G220), F236 (= F234), S239 (= S237), V242 (= V240)
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
36% identity, 95% coverage: 16:482/492 of query aligns to 17:486/489 of 7a6qB
- active site: N163 (= N159), E262 (= E260), C296 (= C294), E470 (≠ F466)
- binding nicotinamide-adenine-dinucleotide: I159 (= I155), W162 (= W158), K186 (= K182), E189 (≠ S185), G219 (= G216), G223 (= G220), S240 (= S237), V243 (= V240), K342 (≠ S340)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (≠ D31), T33 (≠ D32), C34 (≠ R33), P36 (= P35), D103 (≠ E99), E189 (≠ S185), Q190 (≠ D186), F218 (≠ A215), I339 (≠ V337), D340 (≠ N338)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ F113), D141 (≠ K137), N143 (≠ G139), N451 (≠ T446), L453 (≠ D449), A455 (≠ P451)
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
36% identity, 95% coverage: 16:482/492 of query aligns to 17:486/489 of 7a6qA
- active site: N163 (= N159), E262 (= E260), C296 (= C294), E470 (≠ F466)
- binding nicotinamide-adenine-dinucleotide: I159 (= I155), T160 (≠ S156), W162 (= W158), K186 (= K182), A188 (= A184), E189 (≠ S185), G219 (= G216), G223 (= G220), S240 (= S237), V243 (= V240), K342 (≠ S340), K346 (≠ G344)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ F113), D141 (≠ K137), N143 (≠ G139), N451 (≠ T446), L453 (≠ D449), Y454 (≠ Q450)
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
36% identity, 95% coverage: 16:482/492 of query aligns to 17:486/489 of 5fhzA
- active site: N163 (= N159), K186 (= K182), E262 (= E260), C296 (= C294), E393 (= E388), E470 (≠ F466)
- binding nicotinamide-adenine-dinucleotide: I159 (= I155), T160 (≠ S156), W162 (= W158), K186 (= K182), E189 (≠ S185), G219 (= G216), G223 (= G220), F237 (= F234), G239 (= G236), S240 (= S237), T241 (= T238), V243 (= V240), G264 (= G262), Q343 (= Q341), E393 (= E388)
- binding retinoic acid: G118 (≠ F113), R121 (≠ N116), F164 (= F160), M168 (≠ L164), W171 (≠ R167), C295 (≠ I293), C296 (= C294), L453 (≠ D449)
6tryA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with mf13 inhibitor compound (see paper)
36% identity, 96% coverage: 16:486/492 of query aligns to 10:478/478 of 6tryA
- active site: N156 (= N159), E255 (= E260), C289 (= C294), E458 (≠ F466)
- binding nicotinamide-adenine-dinucleotide: I152 (= I155), T153 (≠ S156), W155 (= W158), K179 (= K182), A181 (= A184), E182 (≠ S185), G212 (= G216), G216 (= G220), A217 (≠ D221), F230 (= F234), G232 (= G236), S233 (= S237), V236 (= V240), K335 (≠ S340)
- binding 8-(4-chlorophenyl)-2-phenyl-imidazo[1,2-a]pyridine: I107 (≠ M109), G111 (≠ F113), T115 (≠ L117), L160 (≠ Y163), C288 (≠ I293), L441 (≠ D449), A443 (≠ P451)
6te5B Crystal structure of human aldehyde dehydrogenase 1a3 in complex with lq43 inhibitor compound (see paper)
36% identity, 96% coverage: 16:486/492 of query aligns to 11:479/479 of 6te5B
- active site: N157 (= N159), E256 (= E260), C290 (= C294), E459 (≠ F466)
- binding 6-(3,5-dimethoxyphenyl)-2-(4-methoxyphenyl)imidazo[1,2-a]pyridine: E111 (≠ Q112), G112 (≠ F113), T116 (≠ L117), L442 (≠ D449), A444 (≠ P451)
- binding nicotinamide-adenine-dinucleotide: I153 (= I155), T154 (≠ S156), W156 (= W158), K180 (= K182), E183 (≠ S185), G213 (= G216), F231 (= F234), S234 (= S237), V237 (= V240), Q337 (= Q341), K340 (≠ G344)
6s6wA Crystal structure of human aldh1a3 in complex with 2,6- diphenylimidazo[1,2-a]pyridine (compound ga11) and NAD+ (see paper)
35% identity, 96% coverage: 16:486/492 of query aligns to 13:476/476 of 6s6wA
- active site: N159 (= N159), E258 (= E260), C292 (= C294), E456 (≠ F466)
- binding 2,6-diphenylimidazo[1,2-a]pyridine: E113 (≠ Q112), G114 (≠ F113), W167 (≠ R167), L439 (≠ D449), Y440 (≠ Q450)
- binding nicotinamide-adenine-dinucleotide: I155 (= I155), T156 (≠ S156), W158 (= W158), K182 (= K182), A184 (= A184), G215 (= G216), G219 (= G220), A220 (≠ D221), F233 (= F234), S236 (= S237), V239 (= V240), K338 (≠ S340)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
34% identity, 97% coverage: 16:492/492 of query aligns to 9:489/489 of 4cazA
- active site: N152 (= N159), K175 (= K182), E251 (= E260), C285 (= C294), E386 (= E388), E463 (≠ F466)
- 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 (= I155), G149 (≠ S156), W151 (= W158), N152 (= N159), K175 (= K182), E178 (≠ S185), G208 (= G216), G212 (= G220), F226 (= F234), T227 (= T235), G228 (= G236), G229 (≠ S237), T232 (≠ V240), V236 (= V244), E251 (= E260), L252 (= L261), C285 (= C294), E386 (= E388), F388 (= F390)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
34% identity, 97% coverage: 16:492/492 of query aligns to 9:489/489 of 2woxA
- active site: N152 (= N159), K175 (= K182), E251 (= E260), C285 (= C294), E386 (= E388), E463 (≠ F466)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I155), G149 (≠ S156), W151 (= W158), N152 (= N159), K175 (= K182), S177 (≠ A184), E178 (≠ S185), G208 (= G216), G212 (= G220), F226 (= F234), T227 (= T235), G228 (= G236), G229 (≠ S237), T232 (≠ V240), V236 (= V244), E251 (= E260), L252 (= L261), C285 (= C294), E386 (= E388), F388 (= F390)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
34% identity, 97% coverage: 16:492/492 of query aligns to 9:489/489 of 2wmeA
- active site: N152 (= N159), K175 (= K182), E251 (= E260), C285 (= C294), E386 (= E388), E463 (≠ F466)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ S156), W151 (= W158), K175 (= K182), S177 (≠ A184), E178 (≠ S185), G208 (= G216), G212 (= G220), F226 (= F234), G228 (= G236), G229 (≠ S237), T232 (≠ V240), V236 (= V244)
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)
34% identity, 97% coverage: 16:492/492 of query aligns to 10:490/490 of Q9HTJ1
- GAWN 150:153 (≠ SPWN 156:159) binding
- K162 (≠ S168) active site, Charge relay system
- KPSE 176:179 (≠ KPAS 182:185) binding
- G209 (= G216) binding
- GTST 230:233 (≠ STDV 237:240) binding
- E252 (= E260) active site, Proton acceptor
- C286 (= C294) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E388) binding
- E464 (≠ F466) active site, Charge relay system
7um9A Human aldh1a1 with bound compound cm38 (see paper)
34% identity, 95% coverage: 16:482/492 of query aligns to 17:486/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I155), I160 (≠ S156), P161 (= P157), W162 (= W158), N163 (= N159), K186 (= K182), E189 (≠ S185), G219 (= G216), G223 (= G220), F237 (= F234), T238 (= T235), G239 (= G236), S240 (= S237), V243 (= V240), E262 (= E260), G264 (= G262), Q343 (= Q341), K346 (≠ G344), E393 (= E388), F395 (= F390)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (≠ R167), H286 (≠ V284), Y290 (≠ L288), I297 (≠ M295), G451 (≠ T446)
5l2oA Crystal structure of aldh1a1 in complex with buc22 (see paper)
34% identity, 95% coverage: 16:482/492 of query aligns to 17:486/494 of 5l2oA
Query Sequence
>AO356_00680 FitnessBrowser__pseudo5_N2C3_1:AO356_00680
MTTQPLAPYAINGDQYINGTWRAGRSARRLDDRNPFNGEQLLEMPLASIADLDDAYQAAQ
KAQAPWAQLHPTQRGAQLEKLAKVIQNRREEIIDWLIHESGSTRIKASMEWQFTLNLVRE
CTTMPMQVEGRILTSYKPGEQSFVFREPLGVVGVISPWNFPLYLSMRSVVPALALGNTIV
LKPASDTAVTGGLLIAHLFEEAGFPEGSLNVVVGAGSEIGDAFVEHPVPSLISFTGSTDV
GRNVGRIATGGKHIKRVALELGGNAPLVVLDDADIDVAAHAAVVGRFLHQGQICMSVNRV
IVDRSLYADFASLVVERVRNLKTGDPTKADTVIGPVVNQSQLDGLLRKLDGARSAGLKQL
CGGPASGLVLPAHVFGEVGADQELARDETFGPLLPLLVAENQTHALALANASEYGLSSAV
FTRDMARGLNFARGIVAGMTHINDITVDDQPNAPFGGEKNSGLGRFNGHYALDEFTRAHW
VTWQPGGHHYPF
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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