SitesBLAST
Comparing Ga0059261_0516 Ga0059261_0516 vanillin dehydrogenase (EC 1.2.1.67) 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)
4jz6A Crystal structure of a salicylaldehyde dehydrogenase from pseudomonas putida g7 complexed with salicylaldehyde (see paper)
50% identity, 98% coverage: 11:478/478 of query aligns to 19:484/484 of 4jz6A
- active site: N150 (= N142), K173 (= K165), E251 (= E242), C285 (= C276), E380 (= E374), F458 (= F452)
- binding salicylaldehyde: W97 (= W89), N150 (= N142), G151 (≠ A143), V154 (≠ I146), L155 (= L147), R247 (≠ P238), C248 (≠ V239), I284 (= I275), C285 (= C276), M286 (= M277), N441 (≠ D435), Y447 (≠ F441), Y455 (= Y449)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
35% identity, 99% coverage: 7:478/478 of query aligns to 19:485/490 of 5ekcE
- active site: N154 (= N142), K177 (= K165), E252 (= E242), C286 (= C276), E381 (= E374), E459 (≠ F452)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (= I138), T151 (≠ A139), P152 (= P140), W153 (= W141), K177 (= K165), P178 (≠ A166), A179 (≠ S167), S180 (≠ E168), P209 (≠ A196), G210 (≠ A200), P211 (= P201), G214 (≠ V204), E215 (≠ G205), F228 (= F218), G230 (= G220), E231 (≠ S221), T234 (≠ V224), I238 (= I228), N331 (≠ D320), R333 (≠ K322), Q334 (≠ T323)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
35% identity, 99% coverage: 7:478/478 of query aligns to 12:478/482 of 5ek6A
- active site: N147 (= N142), K170 (= K165), E245 (= E242), C279 (= C276), E374 (= E374), E452 (≠ F452)
- binding 2-methylpropanal: I152 (≠ L147), K155 (≠ R150), T222 (= T219), E245 (= E242), E435 (≠ D435), F441 (= F441), E452 (≠ F452)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (= I138), T144 (≠ A139), P145 (= P140), W146 (= W141), N147 (= N142), I152 (≠ L147), K170 (= K165), P171 (≠ A166), A172 (≠ S167), S173 (≠ E168), P202 (≠ A196), G203 (≠ A200), P204 (= P201), G207 (≠ V204), E208 (≠ G205), F221 (= F218), T222 (= T219), G223 (= G220), E224 (≠ S221), T227 (≠ V224), I231 (= I228), E245 (= E242), L246 (= L243), G247 (= G244), C279 (= C276), E374 (= E374), F376 (= F376), L402 (= L402), F441 (= F441)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
35% identity, 99% coverage: 7:478/478 of query aligns to 12:478/482 of 4h73A
- active site: N147 (= N142), K170 (= K165), E245 (= E242), C279 (= C276), E374 (= E374), E452 (≠ F452)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (= I138), T144 (≠ A139), P145 (= P140), W146 (= W141), K170 (= K165), P171 (≠ A166), A172 (≠ S167), S173 (≠ E168), P202 (≠ A196), G203 (≠ A200), P204 (= P201), G207 (≠ V204), E208 (≠ G205), F221 (= F218), T222 (= T219), G223 (= G220), E224 (≠ S221), T227 (≠ V224), I231 (= I228)
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)
41% identity, 95% coverage: 15:470/478 of query aligns to 30:482/484 of Q8NMB0
- N157 (= N142) 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 (= K165) 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 (= E183) 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 (= E242) 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 (= C276) 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.
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)
36% identity, 95% coverage: 17:469/478 of query aligns to 32:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
35% identity, 95% coverage: 17:469/478 of query aligns to 31:479/481 of 3jz4A
- active site: N156 (= N142), K179 (= K165), E254 (= E242), C288 (= C276), E385 (= E374), E462 (≠ F452)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (= I138), P154 (= P140), W155 (= W141), N156 (= N142), K179 (= K165), A181 (≠ S167), S182 (≠ E168), S211 (≠ A196), A212 (= A200), G213 (≠ P201), G216 (≠ V204), F230 (= F218), T231 (= T219), G232 (= G220), S233 (= S221), I236 (≠ V224), E254 (= E242), L255 (= L243), C288 (= C276), K338 (≠ H326), E385 (= E374), F387 (= F376)
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, 95% coverage: 17:470/478 of query aligns to 29:486/487 of Q9H2A2
- R109 (≠ L96) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N142) mutation to A: Complete loss of activity.
- R451 (≠ H434) mutation to A: Complete loss of activity.
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
36% identity, 96% coverage: 10:470/478 of query aligns to 27:487/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I138), T159 (≠ A139), P160 (= P140), W161 (= W141), K185 (= K165), P186 (≠ A166), A187 (≠ S167), E188 (= E168), G218 (≠ A200), P219 (= P201), G222 (≠ V204), A223 (≠ G205), F236 (= F218), G238 (= G220), S239 (= S221), V242 (= V224), V246 (≠ I228)
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
36% identity, 96% coverage: 10:470/478 of query aligns to 28:488/489 of 7a6qB