SitesBLAST
Comparing 208821 DVU3294 aldehyde dehydrogenase (NADP) family protein 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)
5n5sB Crystal structure of aldehyde dehydrogenase 21 (aldh21) from physcomitrella patens in complex with NADP+ (see paper)
33% identity, 89% coverage: 47:460/464 of query aligns to 64:477/481 of 5n5sB
- active site: N155 (= N138), K178 (= K161), E251 (= E234), C286 (= C268), E380 (= E363), E458 (≠ G441)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V151 (≠ I134), S152 (= S135), P153 (≠ A136), W154 (≠ F137), N155 (= N138), L160 (= L143), K178 (= K161), A180 (= A163), S181 (= S164), R212 (≠ A194), A215 (= A197), T230 (≠ I212), G231 (= G213), S232 (= S214), I235 (≠ V217), E251 (= E234), L252 (≠ H235), C286 (= C268), E380 (= E363), F382 (= F365), Y447 (≠ F430)
8hapB Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
31% identity, 98% coverage: 4:458/464 of query aligns to 3:463/466 of 8hapB
- binding 2'-monophosphoadenosine-5'-diphosphate: I136 (= I134), L137 (≠ S135), F139 (= F137), K163 (= K161), S165 (≠ A163), I166 (≠ S164), S196 (≠ A193), G200 (≠ A197), G216 (= G213), S217 (= S214), T220 (≠ V217), I224 (≠ L221)
8hapA Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
31% identity, 98% coverage: 4:458/464 of query aligns to 3:463/466 of 8hapA
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4s)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: I136 (= I134), L137 (≠ S135), F139 (= F137), K163 (= K161), S165 (≠ A163), I166 (≠ S164), S196 (≠ A193), G200 (≠ A197), G216 (= G213), S217 (= S214), T220 (≠ V217), I224 (≠ L221), L239 (≠ H235), C272 (= C268), E368 (= E363), F370 (= F365)
3rhdA Crystal structure of glyceraldehyde-3-phosphate dehydrogenase gapn from methanocaldococcus jannaschii dsm 2661 complexed with NADP
34% identity, 98% coverage: 3:458/464 of query aligns to 5:454/456 of 3rhdA
- active site: N133 (= N138), H156 (≠ K161), E233 (= E234), C267 (= C268), E360 (= E363), E437 (≠ G441)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I129 (= I134), T130 (≠ S135), F132 (= F137), H156 (≠ K161), S158 (≠ A163), S159 (= S164), K160 (≠ A165), G193 (≠ A194), E194 (vs. gap), G197 (≠ A197), D198 (≠ E198), F211 (= F211), S214 (= S214), V217 (= V217)
5kf0A Crystal structure of an aldedhyde dehydrogenase from burkholderia vietnamiensis
36% identity, 91% coverage: 40:459/464 of query aligns to 59:478/480 of 5kf0A
- active site: N157 (= N138), K180 (= K161), E252 (= E234), C288 (= C268), E382 (= E363), E460 (≠ G441)
- binding magnesium ion: E88 (≠ R69)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I153 (= I134), S154 (= S135), P155 (≠ A136), F156 (= F137), N157 (= N138), L162 (= L143), K180 (= K161), S183 (= S164), R184 (≠ A165), R213 (≠ A194), T231 (≠ I212), G232 (= G213), S233 (= S214), V236 (= V217), E252 (= E234), L253 (≠ H235), C288 (= C268), E382 (= E363), F384 (= F365)
Sites not aligning to the query:
5j6bA Crystal structure of aldehyde dehydrogenase from burkholderia thailandensis in covelent complex with NADPH
37% identity, 91% coverage: 40:459/464 of query aligns to 60:479/481 of 5j6bA
- active site: N158 (= N138), K181 (= K161), E253 (= E234), C289 (= C268), E383 (= E363), E461 (≠ G441)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I154 (= I134), S155 (= S135), P156 (≠ A136), F157 (= F137), N158 (= N138), L163 (= L143), K181 (= K161), A183 (= A163), S184 (= S164), R214 (≠ A194), T232 (≠ I212), G233 (= G213), S234 (= S214), V237 (= V217), L241 (= L221), E253 (= E234), L254 (≠ H235), C289 (= C268), E383 (= E363), F385 (= F365), Y450 (≠ F430)
O57693 NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde phosphate dehydrogenase (NAD(P)); GAPN; EC 1.2.1.90 from Thermoproteus tenax (see 2 papers)
34% identity, 98% coverage: 2:458/464 of query aligns to 32:490/501 of O57693
- R72 (≠ H42) binding ; binding ; binding
- R79 (= R49) binding ; binding ; binding
- G134 (= G104) binding
- RR 154:155 (≠ VR 124:125) binding ; binding
- T165 (≠ S135) binding ; binding
- N168 (= N138) binding
- Y184 (≠ A154) binding
- K191 (= K161) binding
- KPSI 191:194 (≠ KPAS 161:164) binding
- G224 (≠ A194) binding
- E228 (= E198) binding ; binding
- S244 (= S214) binding ; binding
- G265 (= G236) binding ; binding
- RCD 296:298 (≠ VCV 267:269) binding
- E395 (= E363) binding ; binding
- HG 455:456 (≠ FR 423:424) binding
1ky8A Crystal structure of the non-phosphorylating glyceraldehyde-3- phosphate dehydrogenase (see paper)
34% identity, 98% coverage: 2:458/464 of query aligns to 30:488/499 of 1ky8A
- active site: N166 (= N138), K189 (= K161), E261 (= E234), C295 (= C268), E393 (= E363), E471 (≠ G441)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I134), T163 (≠ S135), F165 (= F137), N166 (= N138), K189 (= K161), S191 (≠ A163), I192 (≠ S164), P221 (≠ A193), G222 (≠ A194), A225 (= A197), E226 (= E198), F239 (= F211), T240 (≠ I212), G241 (= G213), S242 (= S214), V245 (= V217), E261 (= E234), L262 (≠ H235), G263 (= G236), C295 (= C268), E393 (= E363), F395 (= F365)
1uxuA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
34% identity, 98% coverage: 2:458/464 of query aligns to 30:488/499 of 1uxuA
- active site: N166 (= N138), K189 (= K161), E261 (= E234), C295 (= C268), E393 (= E363), E471 (≠ G441)
- binding adenosine monophosphate: R70 (≠ H42), R77 (= R49), I131 (≠ L103), G132 (= G104), R152 (≠ V124), R153 (= R125)
- binding glyceraldehyde-3-phosphate: N166 (= N138), Y167 (≠ H139), R294 (≠ V267), C295 (= C268), D296 (≠ V269), R452 (≠ A422), H453 (≠ F423), G454 (≠ R424)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I134), T163 (≠ S135), P164 (≠ A136), F165 (= F137), K189 (= K161), S191 (≠ A163), I192 (≠ S164), P221 (≠ A193), G222 (≠ A194), E226 (= E198), G241 (= G213), S242 (= S214), V245 (= V217), E393 (= E363), F395 (= F365)
1uxtA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
34% identity, 98% coverage: 2:458/464 of query aligns to 30:488/499 of 1uxtA
- active site: N166 (= N138), K189 (= K161), E261 (= E234), C295 (= C268), E393 (= E363), E471 (≠ G441)
- binding 1-O-phosphono-alpha-D-glucopyranose: R70 (≠ H42), R77 (= R49), R152 (≠ V124), R153 (= R125)
- binding nicotinamide-adenine-dinucleotide: I162 (= I134), T163 (≠ S135), F165 (= F137), N166 (= N138), K189 (= K161), S191 (≠ A163), G222 (≠ A194), E226 (= E198), T240 (≠ I212), G241 (= G213), S242 (= S214), V245 (= V217), E261 (= E234), G263 (= G236), C295 (= C268), E393 (= E363), F395 (= F365)
1uxrA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
34% identity, 98% coverage: 2:458/464 of query aligns to 30:488/499 of 1uxrA
- active site: N166 (= N138), K189 (= K161), E261 (= E234), C295 (= C268), E393 (= E363), E471 (≠ G441)
- binding 6-O-phosphono-beta-D-fructofuranose: R70 (≠ H42), R77 (= R49), I131 (≠ L103), R152 (≠ V124)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I134), T163 (≠ S135), F165 (= F137), N166 (= N138), K189 (= K161), S191 (≠ A163), I192 (≠ S164), P221 (≠ A193), G222 (≠ A194), A225 (= A197), E226 (= E198), F239 (= F211), T240 (≠ I212), G241 (= G213), S242 (= S214), V245 (= V217), E261 (= E234), L262 (≠ H235), G263 (= G236), C295 (= C268), E393 (= E363), F395 (= F365)
1uxqA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
34% identity, 98% coverage: 2:458/464 of query aligns to 30:488/499 of 1uxqA
- active site: N166 (= N138), K189 (= K161), E261 (= E234), C295 (= C268), E393 (= E363), E471 (≠ G441)
- binding 1-O-phosphono-alpha-D-glucopyranose: R70 (≠ H42), R77 (= R49), R152 (≠ V124), R153 (= R125)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I134), T163 (≠ S135), P164 (≠ A136), F165 (= F137), N166 (= N138), K189 (= K161), S191 (≠ A163), I192 (≠ S164), P221 (≠ A193), G222 (≠ A194), A225 (= A197), E226 (= E198), T240 (≠ I212), G241 (= G213), S242 (= S214), V245 (= V217), E261 (= E234), L262 (≠ H235), G263 (= G236), C295 (= C268), E393 (= E363), F395 (= F365)
1uxnA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
34% identity, 98% coverage: 2:458/464 of query aligns to 30:488/499 of 1uxnA
- active site: N166 (= N138), K189 (= K161), E261 (= E234), C295 (= C268), E393 (= E363), E471 (≠ G441)
- binding adenosine monophosphate: R70 (≠ H42), R77 (= R49), I131 (≠ L103), G132 (= G104), R152 (≠ V124), R153 (= R125), E154 (= E126), Y182 (≠ A154)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I134), T163 (≠ S135), F165 (= F137), N166 (= N138), K189 (= K161), S191 (≠ A163), I192 (≠ S164), P221 (≠ A193), G222 (≠ A194), E226 (= E198), F239 (= F211), T240 (≠ I212), G241 (= G213), S242 (= S214), V245 (= V217), E261 (= E234), L262 (≠ H235), G263 (= G236), C295 (= C268), E393 (= E363), F395 (= F365)
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
33% identity, 98% coverage: 3:458/464 of query aligns to 27:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
33% identity, 98% coverage: 3:458/464 of query aligns to 26:479/481 of 3jz4A
- active site: N156 (= N138), K179 (= K161), E254 (= E234), C288 (= C268), E385 (= E363), E462 (≠ G441)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A136), W155 (≠ F137), K179 (= K161), A181 (= A163), S182 (= S164), A212 (= A193), G216 (≠ A197), G232 (= G213), S233 (= S214), I236 (≠ V217), C288 (= C268), K338 (≠ R318), E385 (= E363), F387 (= F365)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
33% identity, 98% coverage: 2:458/464 of query aligns to 25:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I134), T153 (≠ S135), P154 (≠ A136), K179 (= K161), A212 (= A193), K213 (≠ A194), F230 (= F211), T231 (≠ I212), G232 (= G213), S233 (= S214), V236 (= V217), W239 (≠ H220), G256 (= G236)
3rhhD Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from bacillus halodurans c-125 complexed with NADP
30% identity, 98% coverage: 4:459/464 of query aligns to 21:474/480 of 3rhhD
- active site: N155 (= N138), K178 (= K161), E251 (= E234), C285 (= C268), E378 (= E363), Q456 (≠ G441)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I151 (= I134), P153 (≠ A136), F154 (= F137), K178 (= K161), P179 (= P162), A180 (= A163), T181 (≠ S164), G211 (≠ A193), G215 (≠ A197), D216 (≠ E198), F229 (= F211), G231 (= G213), G232 (≠ S214), T235 (≠ V217)
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)
34% identity, 97% coverage: 8:459/464 of query aligns to 32:482/484 of Q8NMB0
- N157 (= N138) 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 (= K161) 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 (= E179) 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 (= E234) 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 (= C268) 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.
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
30% identity, 97% coverage: 8:459/464 of query aligns to 34:487/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I134), T159 (≠ S135), P160 (≠ A136), W161 (≠ F137), K185 (= K161), E188 (≠ S164), G218 (≠ A194), G222 (≠ E198), F236 (= F211), S239 (= S214), V242 (= V217)
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
30% identity, 97% coverage: 8:459/464 of query aligns to 35:488/489 of 7a6qB
- active site: N163 (= N138), E262 (= E234), C296 (= C268), E470 (≠ G441)
- binding nicotinamide-adenine-dinucleotide: I159 (= I134), W162 (≠ F137), K186 (= K161), E189 (≠ S164), G219 (≠ A194), G223 (≠ E198), S240 (= S214), V243 (= V217), K342 (≠ R314)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: P36 (= P9), D103 (≠ E74), E189 (≠ S164), Q190 (≠ A165), F218 (≠ A193), I339 (= I311), D340 (= D312)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ R88), D141 (≠ S116), N143 (≠ G118), N451 (≠ T421), L453 (≠ F423), A455 (≠ V425)
Sites not aligning to the query:
Query Sequence
>208821 DVU3294 aldehyde dehydrogenase (NADP) family protein
MSSITVRNPFDLSTVGEVPLMSEAEAFAALERAHALHGDPAHRIPAHERLAILERLATLM
RTHAEALVRDAVREGGKPWADSVVEVERAIDGVRWAARELAQLGGREVPMGLTPASAGRL
AFTVREPRGVVLAISAFNHPVNLIVHQAVPAFAAGCPVLVKPASATPLSCRNVLRLMHEA
GVPEAWATMLPCAAATAEKLVADPRVAFLSFIGSSRVGWHLRSKLAPGATCALEHGGAAP
VVLDASADLDAALPLLLKGGFYHAGQVCVSVQRVFAPHETARTFAERLAAAAAQLPTGDP
MRHDTAVGPLIDPREVSRVHEWVEEARAGGGTVLCGGAPLSETLYSPTVVYDPPQGCRLA
RNEVFGPVVAVFSTRDRDEAIARANDVPFIFQAAVFARDVDVALDTARRLNATGVMVNDH
TAFRVDWMPFGGRGESGMGTGGIGPAMHEMTTEKLIVLRSPAWA
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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