SitesBLAST
Comparing WP_011766203.1 NCBI__GCF_000061505.1:WP_011766203.1 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)
45% identity, 90% coverage: 42:477/485 of query aligns to 47:482/484 of Q8NMB0
- N157 (= N154) 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 (= K177) 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 (= E196) 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 (= E252) 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 (= C286) 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.
4jz6A Crystal structure of a salicylaldehyde dehydrogenase from pseudomonas putida g7 complexed with salicylaldehyde (see paper)
37% identity, 90% coverage: 49:485/485 of query aligns to 44:484/484 of 4jz6A
- active site: N150 (= N154), K173 (= K177), E251 (= E252), C285 (= C286), E380 (= E380), F458 (≠ V459)
- binding salicylaldehyde: W97 (≠ K102), G151 (≠ F155), V154 (≠ I158), R247 (≠ K248), C248 (≠ V249), I284 (= I285), C285 (= C286), M286 (= M287), Y447 (≠ F447), Y455 (≠ N455)
6tgwA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with a selective inhibitor (see paper)
37% identity, 95% coverage: 17:477/485 of query aligns to 12:477/478 of 6tgwA
- active site: N155 (= N154), E254 (= E252), C288 (= C286), E459 (≠ R458)
- binding methyl 5-(1,3-benzodioxol-5-yl)-2-phenyl-pyrazolo[1,5-a]pyrimidine-7-carboxylate: I106 (≠ V105), G110 (≠ A109), F156 (= F155), Q278 (≠ F276), F282 (≠ L280), L442 (≠ D441), A444 (≠ P443)
- binding nicotinamide-adenine-dinucleotide: I151 (= I150), T152 (≠ A151), P153 (= P152), W154 (≠ F153), K178 (= K177), G211 (= G210), G215 (= G214), F229 (= F228), G231 (= G230), S232 (= S231), V235 (= V234)
6te5B Crystal structure of human aldehyde dehydrogenase 1a3 in complex with lq43 inhibitor compound (see paper)
36% identity, 96% coverage: 14:477/485 of query aligns to 11:477/479 of 6te5B
- active site: N157 (= N154), E256 (= E252), C290 (= C286), E459 (≠ R458)
- binding 6-(3,5-dimethoxyphenyl)-2-(4-methoxyphenyl)imidazo[1,2-a]pyridine: E111 (≠ K108), G112 (≠ A109), T116 (≠ I113), L442 (≠ D441), A444 (≠ P443)
- binding nicotinamide-adenine-dinucleotide: I153 (= I150), T154 (≠ A151), W156 (≠ F153), K180 (= K177), E183 (≠ L180), G213 (= G210), F231 (= F228), S234 (= S231), V237 (= V234), Q337 (= Q333), K340 (≠ Q336)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
36% identity, 94% coverage: 29:484/485 of query aligns to 28:484/490 of 5ekcE
- active site: N154 (= N154), K177 (= K177), E252 (= E252), C286 (= C286), E381 (= E380), E459 (≠ V459)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (= I150), T151 (≠ A151), P152 (= P152), W153 (≠ F153), K177 (= K177), S180 (≠ L180), G210 (= G210), G214 (= G214), F228 (= F228), G230 (= G230), E231 (≠ S231), T234 (≠ V234), N331 (≠ S330), R333 (≠ G332), Q334 (= Q333)
6tryA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with mf13 inhibitor compound (see paper)
37% identity, 95% coverage: 17:477/485 of query aligns to 13:476/478 of 6tryA
- active site: N156 (= N154), E255 (= E252), C289 (= C286), E458 (≠ R458)
- binding nicotinamide-adenine-dinucleotide: I152 (= I150), T153 (≠ A151), W155 (≠ F153), K179 (= K177), A181 (≠ D179), E182 (≠ L180), G212 (= G210), G216 (= G214), A217 (≠ G215), F230 (= F228), G232 (= G230), S233 (= S231), V236 (= V234), K335 (≠ G332)
- binding 8-(4-chlorophenyl)-2-phenyl-imidazo[1,2-a]pyridine: I107 (≠ V105), G111 (≠ A109), T115 (≠ I113), L160 (≠ I158), C288 (≠ I285), L441 (≠ D441), A443 (≠ P443)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
36% identity, 94% coverage: 29:484/485 of query aligns to 21:477/482 of 5ek6A
- active site: N147 (= N154), K170 (= K177), E245 (= E252), C279 (= C286), E374 (= E380), E452 (≠ V459)
- binding 2-methylpropanal: I152 (≠ L159), K155 (≠ R162), T222 (= T229), E245 (= E252), F441 (= F447)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (= I150), T144 (≠ A151), W146 (≠ F153), N147 (= N154), I152 (≠ L159), K170 (= K177), A172 (≠ D179), S173 (≠ L180), P202 (vs. gap), G203 (= G210), G207 (= G214), F221 (= F228), T222 (= T229), G223 (= G230), E224 (≠ S231), T227 (≠ V234), I231 (≠ V238), E245 (= E252), L246 (= L253), C279 (= C286), E374 (= E380)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
36% identity, 94% coverage: 29:484/485 of query aligns to 21:477/482 of 4h73A
- active site: N147 (= N154), K170 (= K177), E245 (= E252), C279 (= C286), E374 (= E380), E452 (≠ V459)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (= I150), T144 (≠ A151), P145 (= P152), W146 (≠ F153), K170 (= K177), A172 (≠ D179), S173 (≠ L180), G203 (= G210), G207 (= G214), F221 (= F228), G223 (= G230), E224 (≠ S231), T227 (≠ V234)
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: 14:477/485 of query aligns to 35:506/512 of P47895
- R89 (≠ H63) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K177) binding NAD(+)
- E207 (≠ L180) binding NAD(+)
- GSTEVG 257:262 (≠ GSTRVG 230:235) binding NAD(+)
- Q361 (= Q333) binding NAD(+)
- E411 (= E380) binding NAD(+)
- A493 (= A463) 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
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
36% identity, 96% coverage: 14:477/485 of query aligns to 17:488/489 of 7a6qB
- active site: N163 (= N154), E262 (= E252), C296 (= C286), E470 (≠ R458)
- binding nicotinamide-adenine-dinucleotide: I159 (= I150), W162 (≠ F153), K186 (= K177), E189 (≠ L180), G219 (= G210), G223 (= G214), S240 (= S231), V243 (= V234), K342 (≠ G332)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (= A27), T33 (≠ V28), C34 (≠ T29), P36 (≠ K31), D103 (≠ E95), E189 (≠ L180), Q190 (≠ R181), F218 (vs. gap), I339 (= I329), D340 (≠ S330)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ A109), D141 (≠ N132), N143 (≠ G134), N451 (≠ T438), L453 (≠ D441), A455 (≠ P443)
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
36% identity, 96% coverage: 14:477/485 of query aligns to 17:488/489 of 7a6qA
- active site: N163 (= N154), E262 (= E252), C296 (= C286), E470 (≠ R458)
- binding nicotinamide-adenine-dinucleotide: I159 (= I150), T160 (≠ A151), W162 (≠ F153), K186 (= K177), A188 (≠ D179), E189 (≠ L180), G219 (= G210), G223 (= G214), S240 (= S231), V243 (= V234), K342 (≠ G332), K346 (≠ Q336)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ A109), D141 (≠ N132), N143 (≠ G134), N451 (≠ T438), L453 (≠ D441), Y454 (≠ E442)
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
36% identity, 96% coverage: 14:477/485 of query aligns to 17:488/489 of 5fhzA
- active site: N163 (= N154), K186 (= K177), E262 (= E252), C296 (= C286), E393 (= E380), E470 (≠ R458)
- binding nicotinamide-adenine-dinucleotide: I159 (= I150), T160 (≠ A151), W162 (≠ F153), K186 (= K177), E189 (≠ L180), G219 (= G210), G223 (= G214), F237 (= F228), G239 (= G230), S240 (= S231), T241 (= T232), V243 (= V234), G264 (= G254), Q343 (= Q333), E393 (= E380)
- binding retinoic acid: G118 (≠ A109), R121 (≠ G112), F164 (= F155), M168 (≠ L159), W171 (≠ R162), C295 (≠ I285), C296 (= C286), L453 (≠ D441)
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
36% identity, 96% coverage: 14:477/485 of query aligns to 16:487/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I150), T159 (≠ A151), P160 (= P152), W161 (≠ F153), K185 (= K177), E188 (≠ L180), G218 (= G210), G222 (= G214), F236 (= F228), S239 (= S231), V242 (= V234)
P00352 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Homo sapiens (Human) (see 7 papers)
36% identity, 98% coverage: 4:477/485 of query aligns to 13:495/501 of P00352
- N121 (vs. gap) to S: in dbSNP:rs1049981
- IPWN 167:170 (≠ APFN 151:154) binding NAD(+)
- I177 (= I161) to F: in dbSNP:rs8187929
- KPAE 193:196 (≠ KPDL 177:180) binding NAD(+)
- GP 226:227 (≠ GA 210:211) binding NAD(+)
- GS 246:247 (= GS 230:231) binding NAD(+)
- E269 (= E252) active site, Proton acceptor
- ELG 269:271 (= ELG 252:254) binding NAD(+)
- C302 (≠ I285) mutation C->A,S: Does not prevent inhibition by duocarmycin analogs.
- C303 (= C286) active site, Nucleophile
- EQYDK 349:353 (≠ GQLRQ 332:336) binding NAD(+)
- EIF 400:402 (= EIF 380:382) binding NAD(+)
- G458 (≠ T438) mutation to N: No significant effect on aldehyde dehydrogenase activity. Prevents the inhibition by ALDH1A1-specific inhibitors.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
- 336:501 Mediates interaction with PRMT3
8t0tA Structure of compound 4 bound to human aldh1a1 (see paper)
36% identity, 98% coverage: 4:477/485 of query aligns to 6:488/494 of 8t0tA
7um9A Human aldh1a1 with bound compound cm38 (see paper)
36% identity, 98% coverage: 4:477/485 of query aligns to 6:488/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I150), I160 (≠ A151), P161 (= P152), W162 (≠ F153), N163 (= N154), K186 (= K177), E189 (≠ L180), G219 (= G210), G223 (= G214), F237 (= F228), T238 (= T229), G239 (= G230), S240 (= S231), V243 (= V234), E262 (= E252), G264 (= G254), Q343 (= Q333), K346 (≠ Q336), E393 (= E380), F395 (= F382)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (≠ R162), H286 (≠ F276), Y290 (≠ L280), I297 (≠ M287), G451 (≠ T438)
5l2oA Crystal structure of aldh1a1 in complex with buc22 (see paper)
36% identity, 98% coverage: 4:477/485 of query aligns to 6:488/494 of 5l2oA
5l2nA Structure of aldh1a1 in complex with buc25 (see paper)
36% identity, 98% coverage: 4:477/485 of query aligns to 6:488/494 of 5l2nA
- active site: N163 (= N154), K186 (= K177), E262 (= E252), C296 (= C286), E393 (= E380), E470 (≠ V459)
- binding 3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate: F164 (= F155), M168 (≠ L159), W171 (≠ R162), H286 (≠ F276), G287 (= G277), Y290 (≠ L280), C295 (≠ I285), C296 (= C286), I297 (≠ M287), Y450 (≠ Q437), G451 (≠ T438), V453 (≠ A440), F459 (= F447)
5l2mA Structure of aldh1a1 in complex with buc11 (see paper)
36% identity, 98% coverage: 4:477/485 of query aligns to 6:488/494 of 5l2mA
- active site: N163 (= N154), K186 (= K177), E262 (= E252), C296 (= C286), E393 (= E380), E470 (≠ V459)
- binding 2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F155), F283 (≠ C273), H286 (≠ F276), Y290 (≠ L280)
4wpnA Structure of human aldh1a1 with inhibitor cm053 (see paper)
36% identity, 98% coverage: 4:477/485 of query aligns to 6:488/494 of 4wpnA
- active site: N163 (= N154), K186 (= K177), E262 (= E252), C296 (= C286), E393 (= E380), E470 (≠ V459)
- binding 1-{[1,3-dimethyl-7-(3-methylbutyl)-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]methyl}piperidine-4-carboxamide: F164 (= F155), H286 (≠ F276), G287 (= G277), Y290 (≠ L280), C295 (≠ I285), I297 (≠ M287), G451 (≠ T438), V453 (≠ A440)
Query Sequence
>WP_011766203.1 NCBI__GCF_000061505.1:WP_011766203.1
MHTLMDQAVWQDKLMCDGWRASEARAAVTDKATGEQIGSIGVADAESVVRAAALARAAQP
AWHAMPYEDRAAIFRKAARLVEEHWEELATWIVRESGAIRPKADVELKAAAGILYEAAGM
LTEPQGLLLPSNPGRMSFARRLPHGVVGVIAPFNFPLILAIRAVAPALATGNAVVLKPDL
RTAVSGGVLIARIFEEAGLPPGVLHMLPGGADAGGALCTDPNIAMVAFTGSTRVGRTVGE
LCGRHLKKVSLELGGKNSLIVLDDADLDLAAGCAAFGAWLHQGQICMATGRILAHESIAE
QLLAKLAEKADHLPVGDPASGRVALGPIISDGQLRQIDAVVKDSVAAGARLCAGGTYDQL
FYRPTVLGGVKPGMRAFEEEIFGPVACVTTFRDEDEAVALANATEYGLSAAVISRSTGRA
LALGNRLNTGLLHINDQTVADEPHVPFGGRAASGNGGRVGGPANWEEFTQWQWVTVKDTP
PAYPF
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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