SitesBLAST
Comparing GFF964 FitnessBrowser__Marino:GFF964 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)
70% identity, 98% coverage: 12:504/505 of query aligns to 3:495/495 of 5iuwA
- active site: N166 (= N175), K189 (= K198), E265 (= E274), C300 (= C309), E399 (= E408), D476 (= D485)
- binding 1h-indol-3-ylacetic acid: F167 (= F176), M170 (≠ I179), C300 (= C309), D457 (= D466), F465 (= F474)
- binding nicotinamide-adenine-dinucleotide: I162 (= I171), V163 (= V172), P164 (= P173), W165 (= W174), N166 (= N175), K189 (= K198), G222 (= G231), G226 (= G235), K227 (= K236), F240 (= F249), T241 (= T250), G242 (= G251), S243 (= S252), I246 (≠ V255), Y253 (= Y262), E265 (= E274), A266 (= A275), C300 (= C309), E399 (= E408), F401 (= F410)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
70% identity, 98% coverage: 12:504/505 of query aligns to 3:495/495 of 5iuvA
- active site: N166 (= N175), K189 (= K198), E265 (= E274), C300 (= C309), E399 (= E408), D476 (= D485)
- binding nicotinamide-adenine-dinucleotide: I162 (= I171), V163 (= V172), P164 (= P173), W165 (= W174), N166 (= N175), K189 (= K198), S191 (= S200), G222 (= G231), G226 (= G235), K227 (= K236), F240 (= F249), T241 (= T250), G242 (= G251), S243 (= S252), I246 (≠ V255), Y253 (= Y262), E265 (= E274), A266 (= A275), C300 (= C309), E399 (= E408), F401 (= F410)
7jsoA P. Syringae alda indole-3-acetaldehyde dehydrogenase c302a mutant in complex with NAD+ and iaa (see paper)
70% identity, 98% coverage: 12:504/505 of query aligns to 3:495/495 of 7jsoA
- active site: N166 (= N175), E265 (= E274), A300 (≠ C309), D476 (= D485)
- binding 1h-indol-3-ylacetic acid: F167 (= F176), W174 (= W183), V299 (= V308), A300 (≠ C309), T301 (= T310), D457 (= D466), F465 (= F474)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I162 (= I171), V163 (= V172), P164 (= P173), W165 (= W174), K189 (= K198), E192 (= E201), G222 (= G231), G226 (= G235), K227 (= K236), F240 (= F249), G242 (= G251), S243 (= S252), I246 (≠ V255), A266 (= A275), G267 (= G276), A300 (≠ C309), E399 (= E408), F401 (= F410)
7uyyA The crystal structure of the pseudomonas aeruginosa aldehyde dehydrogenase encoded by the pa4189 gene in complex with nadh (see paper)
46% identity, 97% coverage: 12:502/505 of query aligns to 6:493/496 of 7uyyA
- binding 1,4-dihydronicotinamide adenine dinucleotide: V165 (≠ I171), L166 (≠ V172), P167 (= P173), W168 (= W174), K192 (= K198), G225 (= G231), G229 (= G235), F243 (= F249), G245 (= G251), S246 (= S252), T249 (≠ V255), L252 (≠ Q258), F253 (≠ L259), Y256 (= Y262), C269 (≠ A275), G270 (= G276), C303 (= C309), H350 (≠ Q356), K353 (≠ R359), F400 (= F410)
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)
46% identity, 97% coverage: 12:502/505 of query aligns to 6:493/496 of Q9HWJ2
- L166 (≠ V172) binding NADH
- W168 (= W174) binding NADH
- K192 (= K198) binding NADH
- S246 (= S252) binding NADH
- T249 (≠ V255) binding NADH
- Y256 (= Y262) binding NADH
- C269 (≠ A275) binding NADH
- K353 (≠ R359) binding NADH
- E398 (= E408) binding NADH
- E457 (≠ G467) Important in defining aldehyde specificity; mutation E->G,Q: High decrease in catalytic efficiency with ACTAL and APAL as substrates.
O94788 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Homo sapiens (Human) (see 6 papers)
45% identity, 93% coverage: 28:498/505 of query aligns to 39:507/518 of O94788
- E50 (≠ A39) to G: in dbSNP:rs34266719
- A110 (= A98) to V: in dbSNP:rs35365164
- Q182 (≠ A170) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ VPW 172:174) binding NAD(+)
- KPAE 210:213 (≠ KPSE 198:201) binding NAD(+)
- STE 264:266 (≠ STN 252:254) binding NAD(+)
- C320 (= C309) active site, Nucleophile
- R347 (≠ W336) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ R337) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ AQLDR 355:359) binding NAD(+)
- A383 (= A372) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E408) binding NAD(+)
- E436 (≠ A427) to K: in dbSNP:rs34744827
- S461 (≠ A452) to Y: in DIH4; decreased retinoic acid biosynthetic process
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
45% identity, 93% coverage: 28:498/505 of query aligns to 13:481/492 of 6b5hA
- active site: N161 (= N175), E260 (= E274), C294 (= C309), E468 (≠ D485)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (= V126), G116 (≠ A130), F162 (= F176), W169 (= W183), Q284 (≠ S299), F288 (= F303), T295 (= T310), N449 (≠ D466), L451 (≠ G468), N452 (≠ D469), F457 (= F474)
- binding nicotinamide-adenine-dinucleotide: I157 (= I171), I158 (≠ V172), W160 (= W174), N161 (= N175), K184 (= K198), G217 (= G231), G221 (= G235), F235 (= F249), T236 (= T250), G237 (= G251), S238 (= S252), V241 (= V255), E260 (= E274), L261 (≠ A275), C294 (= C309), F393 (= F410)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
45% identity, 93% coverage: 28:498/505 of query aligns to 13:481/492 of 6b5gA
- active site: N161 (= N175), E260 (= E274), C294 (= C309), E468 (≠ D485)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F176), L165 (≠ I179), W169 (= W183), F288 (= F303), C293 (≠ V308), C294 (= C309), T295 (= T310), N449 (≠ D466), L451 (≠ G468)
- binding nicotinamide-adenine-dinucleotide: I157 (= I171), I158 (≠ V172), P159 (= P173), W160 (= W174), N161 (= N175), M166 (= M180), K184 (= K198), E187 (= E201), G217 (= G231), G221 (= G235), F235 (= F249), T236 (= T250), G237 (= G251), S238 (= S252), V241 (= V255), E260 (= E274), L261 (≠ A275), C294 (= C309), E391 (= E408), F393 (= F410)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
45% identity, 93% coverage: 28:498/505 of query aligns to 13:481/492 of 6aljA