SitesBLAST
Comparing WP_086509869.1 NCBI__GCF_002151265.1:WP_086509869.1 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)
5iuwA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ and iaa (see paper)
59% identity, 98% coverage: 10:499/502 of query aligns to 3:495/495 of 5iuwA
- active site: N166 (= N172), K189 (= K195), E265 (= E271), C300 (= C306), E399 (= E403), D476 (= D480)
- binding 1h-indol-3-ylacetic acid: F167 (= F173), M170 (= M176), C300 (= C306), D457 (≠ A461), F465 (= F469)
- binding nicotinamide-adenine-dinucleotide: I162 (= I168), V163 (= V169), P164 (= P170), W165 (= W171), N166 (= N172), K189 (= K195), G222 (= G228), G226 (= G232), K227 (= K233), F240 (= F246), T241 (= T247), G242 (= G248), S243 (= S249), I246 (≠ V252), Y253 (= Y259), E265 (= E271), A266 (≠ C272), C300 (= C306), E399 (= E403), F401 (= F405)
5iuvA Crystal structure of indole-3-acetaldehyde dehydrogenase in complexed with NAD+ (see paper)
59% identity, 98% coverage: 10:499/502 of query aligns to 3:495/495 of 5iuvA
- active site: N166 (= N172), K189 (= K195), E265 (= E271), C300 (= C306), E399 (= E403), D476 (= D480)
- binding nicotinamide-adenine-dinucleotide: I162 (= I168), V163 (= V169), P164 (= P170), W165 (= W171), N166 (= N172), K189 (= K195), S191 (= S197), G222 (= G228), G226 (= G232), K227 (= K233), F240 (= F246), T241 (= T247), G242 (= G248), S243 (= S249), I246 (≠ V252), Y253 (= Y259), E265 (= E271), A266 (≠ C272), C300 (= C306), E399 (= E403), F401 (= F405)
7jsoA P. Syringae alda indole-3-acetaldehyde dehydrogenase c302a mutant in complex with NAD+ and iaa (see paper)
59% identity, 98% coverage: 10:499/502 of query aligns to 3:495/495 of 7jsoA
- active site: N166 (= N172), E265 (= E271), A300 (≠ C306), D476 (= D480)
- binding 1h-indol-3-ylacetic acid: F167 (= F173), W174 (= W180), V299 (= V305), A300 (≠ C306), T301 (≠ I307), D457 (≠ A461), F465 (= F469)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I162 (= I168), V163 (= V169), P164 (= P170), W165 (= W171), K189 (= K195), E192 (= E198), G222 (= G228), G226 (= G232), K227 (= K233), F240 (= F246), G242 (= G248), S243 (= S249), I246 (≠ V252), A266 (≠ C272), G267 (= G273), A300 (≠ C306), E399 (= E403), F401 (= F405)
7uyyA The crystal structure of the pseudomonas aeruginosa aldehyde dehydrogenase encoded by the pa4189 gene in complex with nadh (see paper)
49% identity, 97% coverage: 13:497/502 of query aligns to 9:493/496 of 7uyyA
- binding 1,4-dihydronicotinamide adenine dinucleotide: V165 (≠ I168), L166 (≠ V169), P167 (= P170), W168 (= W171), K192 (= K195), G225 (= G228), G229 (= G232), F243 (= F246), G245 (= G248), S246 (= S249), T249 (≠ V252), L252 (≠ Q255), F253 (≠ L256), Y256 (= Y259), C269 (= C272), G270 (= G273), C303 (= C306), H350 (≠ Q353), K353 (≠ R356), F400 (= F405)
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)
49% identity, 97% coverage: 13:497/502 of query aligns to 9:493/496 of Q9HWJ2
- L166 (≠ V169) binding NADH
- W168 (= W171) binding NADH
- K192 (= K195) binding NADH
- S246 (= S249) binding NADH
- T249 (≠ V252) binding NADH
- Y256 (= Y259) binding NADH
- C269 (= C272) binding NADH
- K353 (≠ R356) binding NADH
- E398 (= E403) binding NADH
- E457 (≠ G462) 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)
44% identity, 95% coverage: 25:499/502 of query aligns to 38:513/518 of O94788
- E50 (= E37) to G: in dbSNP:rs34266719
- A110 (= A96) to V: in dbSNP:rs35365164
- Q182 (≠ A167) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ VPW 169:171) binding NAD(+)
- KPAE 210:213 (≠ KPSE 195:198) binding NAD(+)
- STE 264:266 (≠ STA 249:251) binding NAD(+)
- C320 (= C306) active site, Nucleophile
- R347 (≠ M333) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ Q334) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ AQHRR 352:356) binding NAD(+)
- A383 (= A369) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E403) binding NAD(+)
- E436 (≠ A422) to K: in dbSNP:rs34744827
- S461 (≠ T447) 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)
44% identity, 95% coverage: 25:499/502 of query aligns to 12:487/492 of 6b5hA
- active site: N161 (= N172), E260 (= E271), C294 (= C306), E468 (≠ D480)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (vs. gap), G116 (= G127), F162 (= F173), W169 (= W180), Q284 (≠ A296), F288 (≠ H300), T295 (≠ I307), N449 (≠ A461), L451 (≠ G463), N452 (≠ D464), F457 (= F469)
- binding nicotinamide-adenine-dinucleotide: I157 (= I168), I158 (≠ V169), W160 (= W171), N161 (= N172), K184 (= K195), G217 (= G228), G221 (= G232), F235 (= F246), T236 (= T247), G237 (= G248), S238 (= S249), V241 (= V252), E260 (= E271), L261 (≠ C272), C294 (= C306), F393 (= F405)
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)
44% identity, 95% coverage: 25:499/502 of query aligns to 12:487/492 of 6b5gA
- active site: N161 (= N172), E260 (= E271), C294 (= C306), E468 (≠ D480)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F173), L165 (≠ M176), W169 (= W180), F288 (≠ H300), C293 (≠ V305), C294 (= C306), T295 (≠ I307), N449 (≠ A461), L451 (≠ G463)
- binding nicotinamide-adenine-dinucleotide: I157 (= I168), I158 (≠ V169), P159 (= P170), W160 (= W171), N161 (= N172), M166 (= M177), K184 (= K195), E187 (= E198), G217 (= G228), G221 (= G232), F235 (= F246), T236 (= T247), G237 (= G248), S238 (= S249), V241 (= V252), E260 (= E271), L261 (≠ C272), C294 (= C306), E391 (= E403), F393 (= F405)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
44% identity, 95% coverage: 25:499/502 of query aligns to 12:487/492 of 6aljA
- active site: N161 (= N172), E260 (= E271), C294 (= C306), E468 (≠ D480)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (= G127), F162 (= F173), L165 (≠ M176), M166 (= M177), W169 (= W180), E260 (= E271), C293 (≠ V305), C294 (= C306), L451 (≠ G463), N452 (≠ D464), A453 (≠ Q465)
- binding nicotinamide-adenine-dinucleotide: I157 (= I168), I158 (≠ V169), P159 (= P170), W160 (= W171), N161 (= N172), K184 (= K195), E187 (= E198), G217 (= G228), G221 (= G232), F235 (= F246), G237 (= G248), S238 (= S249), V241 (= V252), Q341 (= Q353), K344 (≠ R356), E391 (= E403), F393 (= F405)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
47% identity, 96% coverage: 20:502/502 of query aligns to 7:491/494 of 4pz2B
- active site: N159 (= N172), K182 (= K195), E258 (= E271), C292 (= C306), E392 (= E403), D469 (= D480)
- binding nicotinamide-adenine-dinucleotide: I155 (= I168), I156 (≠ V169), P157 (= P170), W158 (= W171), N159 (= N172), M164 (= M177), K182 (= K195), A184 (≠ S197), E185 (= E198), G215 (= G228), G219 (= G232), F233 (= F246), T234 (= T247), G235 (= G248), S236 (= S249), V239 (= V252), E258 (= E271), L259 (≠ C272), C292 (= C306), E392 (= E403), F394 (= F405)
Q63639 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 Rattus norvegicus (Rat) (see paper)
44% identity, 95% coverage: 25:499/502 of query aligns to 38:513/518 of Q63639
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)
45% identity, 96% coverage: 20:502/502 of query aligns to 16:498/501 of Q56YU0
- G152 (≠ A155) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A420) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
5l13A Structure of aldh2 in complex with 2p3 (see paper)
45% identity, 94% coverage: 23:495/502 of query aligns to 12:485/494 of 5l13A
- active site: N163 (= N172), K186 (= K195), E262 (= E271), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F173), M168 (= M177), W171 (= W180), F290 (≠ H300), C295 (≠ V305), C296 (= C306), C297 (≠ I307), D451 (≠ A461), F453 (≠ G463)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
45% identity, 94% coverage: 23:495/502 of query aligns to 12:485/494 of 4kwgA
- active site: N163 (= N172), K186 (= K195), E262 (= E271), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F173), M168 (= M177), C295 (≠ V305), C296 (= C306), C297 (≠ I307), D451 (≠ A461), F453 (≠ G463)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
45% identity, 94% coverage: 23:495/502 of query aligns to 12:485/494 of 4kwfA
- active site: N163 (= N172), K186 (= K195), E262 (= E271), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F173), M168 (= M177), W171 (= W180), E262 (= E271), C295 (≠ V305), C296 (= C306), C297 (≠ I307), D451 (≠ A461), F453 (≠ G463), F459 (= F469)
3sz9A Crystal structure of human aldh2 modified with the beta-elimination product of aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one (see paper)
45% identity, 94% coverage: 23:495/502 of query aligns to 12:485/494 of 3sz9A
- active site: N163 (= N172), K186 (= K195), E262 (= E271), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F173), C295 (≠ V305), C296 (= C306), D451 (≠ A461), F453 (≠ G463), F459 (= F469)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
45% identity, 94% coverage: 23:495/502 of query aligns to 12:485/494 of 3injA
- active site: N163 (= N172), K186 (= K195), E262 (= E271), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ G127), F164 (= F173), L167 (≠ M176), F286 (≠ A296), F290 (≠ H300), D451 (≠ A461), F453 (≠ G463)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
45% identity, 94% coverage: 23:495/502 of query aligns to 12:485/494 of 2vleA
- active site: N163 (= N172), K186 (= K195), E262 (= E271), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding daidzin: M118 (≠ G127), F164 (= F173), M168 (= M177), W171 (= W180), F286 (≠ A296), F290 (≠ H300), C295 (≠ V305), C296 (= C306), D451 (≠ A461), V452 (≠ G462), F453 (≠ G463)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
45% identity, 94% coverage: 23:495/502 of query aligns to 12:485/494 of 1o01B
- active site: N163 (= N172), K186 (= K195), E262 (= E271), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding (2e)-but-2-enal: C296 (= C306), C297 (≠ I307), F453 (≠ G463)
- binding nicotinamide-adenine-dinucleotide: I159 (= I168), I160 (≠ V169), P161 (= P170), W162 (= W171), K186 (= K195), E189 (= E198), G219 (= G228), G223 (= G232), A224 (≠ K233), F237 (= F246), G239 (= G248), S240 (= S249), I243 (≠ V252), L263 (≠ C272), G264 (= G273), C296 (= C306), Q343 (= Q353), E393 (= E403), F395 (= F405)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
45% identity, 94% coverage: 23:495/502 of query aligns to 12:485/494 of 1cw3A
- active site: N163 (= N172), K186 (= K195), E262 (= E271), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding magnesium ion: V34 (≠ R45), D103 (= D113), Q190 (≠ K199)
- binding nicotinamide-adenine-dinucleotide: I159 (= I168), I160 (≠ V169), P161 (= P170), W162 (= W171), K186 (= K195), G219 (= G228), G223 (= G232), A224 (≠ K233), F237 (= F246), G239 (= G248), S240 (= S249), I243 (≠ V252), L263 (≠ C272), G264 (= G273), C296 (= C306), Q343 (= Q353), K346 (≠ R356), E393 (= E403), F395 (= F405)
Query Sequence
>WP_086509869.1 NCBI__GCF_002151265.1:WP_086509869.1
MVSRTPTPRTLADWQARAAELSFESRAFIDDSFVAAESGATFESRNPATGEILAQVASCD
EPDAARAVAVARRAFADGAWSRLAPGKRKKTLLHLADLMEAHKHELALIDTLDMGKPIAS
SLGDMAGAIACIRYQAECIDKLYGEVAPTGEETLALVLREPIGVVAAIVPWNFPLMMTAW
KIAPALAAGNSVILKPSEKSPLSALRLAQLAQEAGIPRGVFQVLPGFGHTVGKALALSME
VDCLAFTGSTAVGKQLMQYAGQSNLKRVYLECGGKSPNLVFADCKDLDTVASHAAAAIFH
NQGEVCIAGSRLLVENTIRDDFVERVLKAAENMQPGDPLDPDSFMGAIVDEAQHRRILDY
IRQGVEEGARLRTGGQAIDGPGLFIPPTVFDGVTPQMTIGREEIFGPVLAVLGFDTEEEA
VAMANDTPYGLAAGLWSQDIDRIMRVTRRLQSGQVFVNNWAGGDQTMPFGGVKQSGNGRD
KSHHSLEEYSELKSVWMSLQPS
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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