SitesBLAST
Comparing 202599 FitnessBrowser__MR1:202599 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)
5iuwA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ and iaa (see paper)
74% identity, 99% coverage: 6:498/498 of query aligns to 3:495/495 of 5iuwA
- active site: N166 (= N169), K189 (= K192), E265 (= E268), C300 (= C303), E399 (= E402), D476 (= D479)
- binding 1h-indol-3-ylacetic acid: F167 (= F170), M170 (≠ L173), C300 (= C303), D457 (= D460), F465 (= F468)
- binding nicotinamide-adenine-dinucleotide: I162 (= I165), V163 (= V166), P164 (= P167), W165 (= W168), N166 (= N169), K189 (= K192), G222 (= G225), G226 (= G229), K227 (= K230), F240 (= F243), T241 (= T244), G242 (= G245), S243 (= S246), I246 (= I249), Y253 (= Y256), E265 (= E268), A266 (= A269), C300 (= C303), E399 (= E402), F401 (= F404)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
74% identity, 99% coverage: 6:498/498 of query aligns to 3:495/495 of 5iuvA
- active site: N166 (= N169), K189 (= K192), E265 (= E268), C300 (= C303), E399 (= E402), D476 (= D479)
- binding nicotinamide-adenine-dinucleotide: I162 (= I165), V163 (= V166), P164 (= P167), W165 (= W168), N166 (= N169), K189 (= K192), S191 (= S194), G222 (= G225), G226 (= G229), K227 (= K230), F240 (= F243), T241 (= T244), G242 (= G245), S243 (= S246), I246 (= I249), Y253 (= Y256), E265 (= E268), A266 (= A269), C300 (= C303), E399 (= E402), F401 (= F404)
7jsoA P. Syringae alda indole-3-acetaldehyde dehydrogenase c302a mutant in complex with NAD+ and iaa (see paper)
74% identity, 99% coverage: 6:498/498 of query aligns to 3:495/495 of 7jsoA
- active site: N166 (= N169), E265 (= E268), A300 (≠ C303), D476 (= D479)
- binding 1h-indol-3-ylacetic acid: F167 (= F170), W174 (= W177), V299 (= V302), A300 (≠ C303), T301 (= T304), D457 (= D460), F465 (= F468)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I162 (= I165), V163 (= V166), P164 (= P167), W165 (= W168), K189 (= K192), E192 (= E195), G222 (= G225), G226 (= G229), K227 (= K230), F240 (= F243), G242 (= G245), S243 (= S246), I246 (= I249), A266 (= A269), G267 (= G270), A300 (≠ C303), E399 (= E402), F401 (= F404)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
47% identity, 95% coverage: 22:493/498 of query aligns to 12:483/494 of 4pz2B
- active site: N159 (= N169), K182 (= K192), E258 (= E268), C292 (= C303), E392 (= E402), D469 (= D479)
- binding nicotinamide-adenine-dinucleotide: I155 (= I165), I156 (≠ V166), P157 (= P167), W158 (= W168), N159 (= N169), M164 (= M174), K182 (= K192), A184 (≠ S194), E185 (= E195), G215 (= G225), G219 (= G229), F233 (= F243), T234 (= T244), G235 (= G245), S236 (= S246), V239 (≠ I249), E258 (= E268), L259 (≠ A269), C292 (= C303), E392 (= E402), F394 (= F404)
7uyyA The crystal structure of the pseudomonas aeruginosa aldehyde dehydrogenase encoded by the pa4189 gene in complex with nadh (see paper)
45% identity, 100% coverage: 1:496/498 of query aligns to 1:493/496 of 7uyyA
- binding 1,4-dihydronicotinamide adenine dinucleotide: V165 (≠ I165), L166 (≠ V166), P167 (= P167), W168 (= W168), K192 (= K192), G225 (= G225), G229 (= G229), F243 (= F243), G245 (= G245), S246 (= S246), T249 (≠ I249), L252 (≠ Q252), F253 (≠ L253), Y256 (= Y256), C269 (≠ A269), G270 (= G270), C303 (= C303), H350 (≠ Q350), K353 (≠ T353), F400 (= F404)
Q9HWJ2 Aminoacetaldehyde dehydrogenase; ACTAL dehydrogenase; EC 1.2.1.- from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
45% identity, 100% coverage: 1:496/498 of query aligns to 1:493/496 of Q9HWJ2
- L166 (≠ V166) binding NADH
- W168 (= W168) binding NADH
- K192 (= K192) binding NADH
- S246 (= S246) binding NADH
- T249 (≠ I249) binding NADH
- Y256 (= Y256) binding NADH
- C269 (≠ A269) binding NADH
- K353 (≠ T353) binding NADH
- E398 (= E402) binding NADH
- E457 (≠ G461) Important in defining aldehyde specificity; mutation E->G,Q: High decrease in catalytic efficiency with ACTAL and APAL as substrates.
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
46% identity, 95% coverage: 22:492/498 of query aligns to 7:474/486 of 4pxlA
- active site: N154 (= N169), K177 (= K192), E253 (= E268), C287 (= C303), E384 (= E402), D461 (= D479)
- binding nicotinamide-adenine-dinucleotide: I150 (= I165), V151 (= V166), P152 (= P167), W153 (= W168), K177 (= K192), E180 (= E195), G210 (= G225), G214 (= G229), A215 (≠ K230), F228 (= F243), G230 (= G245), S231 (= S246), V234 (≠ I249), E253 (= E268), G255 (= G270), C287 (= C303), Q334 (= Q350), K337 (≠ T353), E384 (= E402), F386 (= F404)
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, 96% coverage: 22:498/498 of query aligns to 21:495/501 of Q56YU0
- G152 (= G152) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A419) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
P05091 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Homo sapiens (Human) (see 5 papers)
44% identity, 94% coverage: 24:492/498 of query aligns to 40:506/517 of P05091
- E337 (≠ G321) to V: in dbSNP:rs1062136
- E496 (≠ L482) to K: in allele ALDH2*3; dbSNP:rs769724893
- E504 (= E490) to K: in AMEDS; allele ALDH2*2; drastic reduction of enzyme activity; dbSNP:rs671
Sites not aligning to the query:
5l13A Structure of aldh2 in complex with 2p3 (see paper)
44% identity, 94% coverage: 24:492/498 of query aligns to 17:483/494 of 5l13A