SitesBLAST
Comparing 3609638 FitnessBrowser__Dino:3609638 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
65% identity, 97% coverage: 17:485/485 of query aligns to 4:476/476 of 4yweA
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
44% identity, 94% coverage: 28:482/485 of query aligns to 27:486/494 of 4pz2B
- active site: N159 (= N158), K182 (= K181), E258 (= E256), C292 (= C290), E392 (= E387), D469 (≠ E465)
- binding nicotinamide-adenine-dinucleotide: I155 (= I154), I156 (≠ V155), P157 (= P156), W158 (= W157), N159 (= N158), M164 (≠ I163), K182 (= K181), A184 (= A183), E185 (= E184), G215 (= G214), G219 (= G218), F233 (= F232), T234 (= T233), G235 (= G234), S236 (= S235), V239 (= V238), E258 (= E256), L259 (= L257), C292 (= C290), E392 (= E387), F394 (= F389)
7radA Crystal structure analysis of aldh1b1
39% identity, 99% coverage: 2:481/485 of query aligns to 1:485/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I154), I159 (≠ V155), P160 (= P156), W161 (= W157), N162 (= N158), M167 (≠ I163), K185 (= K181), E188 (= E184), G218 (= G214), G222 (= G218), A223 (= A219), T237 (= T233), G238 (= G234), S239 (= S235), V242 (= V238), E261 (= E256), L262 (= L257), C295 (= C290), E392 (= E387), F394 (= F389)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ A113), F163 (≠ Y159), E285 (≠ K280), F289 (≠ Q284), N450 (≠ G445), V452 (≠ G448)
7mjdA Crystal structure analysis of aldh1b1
39% identity, 99% coverage: 2:481/485 of query aligns to 1:485/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I154), I159 (≠ V155), P160 (= P156), W161 (= W157), N162 (= N158), M167 (≠ I163), K185 (= K181), E188 (= E184), G218 (= G214), G222 (= G218), F236 (= F232), T237 (= T233), G238 (= G234), S239 (= S235), V242 (= V238), E261 (= E256), L262 (= L257), C295 (= C290), E392 (= E387), F394 (= F389)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ A113), E285 (≠ K280), F289 (≠ Q284), N450 (≠ G445), V452 (≠ G448)
7mjcA Crystal structure analysis of aldh1b1
39% identity, 99% coverage: 2:481/485 of query aligns to 1:485/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I154), I159 (≠ V155), P160 (= P156), W161 (= W157), N162 (= N158), K185 (= K181), E188 (= E184), G218 (= G214), G222 (= G218), T237 (= T233), G238 (= G234), S239 (= S235), V242 (= V238), E261 (= E256), L262 (= L257), C295 (= C290), E392 (= E387), F394 (= F389)
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)
38% identity, 100% coverage: 1:483/485 of query aligns to 25:512/518 of O94788
- E50 (≠ A26) to G: in dbSNP:rs34266719
- A110 (≠ G82) to V: in dbSNP:rs35365164
- Q182 (≠ H153) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ VPW 155:157) binding
- KPAE 210:213 (= KPAE 181:184) binding
- STE 264:266 (≠ SVP 235:237) binding
- C320 (= C290) active site, Nucleophile
- R347 (≠ L317) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ T318) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ KQKAR 335:339) binding
- A383 (≠ H357) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E387) binding
- E436 (≠ A406) to K: in dbSNP:rs34744827
- S461 (≠ P431) to Y: in DIH4; decreased retinoic acid biosynthetic process
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)
38% identity, 100% coverage: 1:483/485 of query aligns to 25:512/518 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)
39% identity, 93% coverage: 28:480/485 of query aligns to 36:491/501 of Q56YU0
- G152 (≠ T140) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A404) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
38% identity, 99% coverage: 5:483/485 of query aligns to 3:486/492 of 6b5hA
- active site: N161 (= N158), E260 (= E256), C294 (= C290), E468 (= E465)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ A109), G116 (≠ A113), F162 (≠ Y159), W169 (≠ R166), Q284 (≠ K280), F288 (≠ Q284), T295 (≠ S291), N449 (≠ G445), L451 (≠ G447), N452 (≠ G448), F457 (= F454)
- binding nicotinamide-adenine-dinucleotide: I157 (= I154), I158 (≠ V155), W160 (= W157), N161 (= N158), K184 (= K181), G217 (= G214), G221 (= G218), F235 (= F232), T236 (= T233), G237 (= G234), S238 (= S235), V241 (= V238), E260 (= E256), L261 (= L257), C294 (= C290), F393 (= F389)
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)
38% identity, 99% coverage: 5:483/485 of query aligns to 3:486/492 of 6b5gA
- active site: N161 (= N158), E260 (= E256), C294 (= C290), E468 (= E465)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ Y159), L165 (≠ Q162), W169 (≠ R166), F288 (≠ Q284), C293 (≠ T289), C294 (= C290), T295 (≠ S291), N449 (≠ G445), L451 (≠ G447)
- binding nicotinamide-adenine-dinucleotide: I157 (= I154), I158 (≠ V155), P159 (= P156), W160 (= W157), N161 (= N158), M166 (≠ I163), K184 (= K181), E187 (= E184), G217 (= G214), G221 (= G218), F235 (= F232), T236 (= T233), G237 (= G234), S238 (= S235), V241 (= V238), E260 (= E256), L261 (= L257), C294 (= C290), E391 (= E387), F393 (= F389)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
38% identity, 99% coverage: 5:483/485 of query aligns to 3:486/492 of 6aljA
- active site: N161 (= N158), E260 (= E256), C294 (= C290), E468 (= E465)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ A113), F162 (≠ Y159), L165 (≠ Q162), M166 (≠ I163), W169 (≠ R166), E260 (= E256), C293 (≠ T289), C294 (= C290), L451 (≠ G447), N452 (≠ G448), A453 (≠ G449)
- binding nicotinamide-adenine-dinucleotide: I157 (= I154), I158 (≠ V155), P159 (= P156), W160 (= W157), N161 (= N158), K184 (= K181), E187 (= E184), G217 (= G214), G221 (= G218), F235 (= F232), G237 (= G234), S238 (= S235), V241 (= V238), Q341 (= Q336), K344 (≠ R339), E391 (= E387), F393 (= F389)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
43% identity, 94% coverage: 28:482/485 of query aligns to 22:478/486 of 4pxlA
- active site: N154 (= N158), K177 (= K181), E253 (= E256), C287 (= C290), E384 (= E387), D461 (≠ E465)
- binding nicotinamide-adenine-dinucleotide: I150 (= I154), V151 (= V155), P152 (= P156), W153 (= W157), K177 (= K181), E180 (= E184), G210 (= G214), G214 (= G218), A215 (= A219), F228 (= F232), G230 (= G234), S231 (= S235), V234 (= V238), E253 (= E256), G255 (= G258), C287 (= C290), Q334 (= Q336), K337 (≠ R339), E384 (= E387), F386 (= F389)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
37% identity, 98% coverage: 5:480/485 of query aligns to 7:487/496 of 4fr8C
- active site: N165 (= N158), K188 (= K181), Q264 (≠ E256), C298 (= C290), E395 (= E387), E472 (= E465)
- binding nicotinamide-adenine-dinucleotide: I161 (= I154), I162 (≠ V155), W164 (= W157), K188 (= K181), G221 (= G214), G225 (= G218), A226 (= A219), F239 (= F232), G241 (= G234), S242 (= S235), I245 (≠ V238), Q345 (= Q336), E395 (= E387), F397 (= F389)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 93% coverage: 28:480/485 of query aligns to 33:486/491 of 5gtlA
- active site: N165 (= N158), K188 (= K181), E263 (= E256), C297 (= C290), E394 (= E387), E471 (= E465)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I154), P163 (= P156), K188 (= K181), A190 (= A183), E191 (= E184), Q192 (≠ D185), G221 (= G214), G225 (= G218), G241 (= G234), S242 (= S235), T245 (≠ V238), L264 (= L257), C297 (= C290), E394 (= E387), F396 (= F389)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 93% coverage: 28:480/485 of query aligns to 33:486/491 of 5gtkA
- active site: N165 (= N158), K188 (= K181), E263 (= E256), C297 (= C290), E394 (= E387), E471 (= E465)
- binding nicotinamide-adenine-dinucleotide: I161 (= I154), I162 (≠ V155), P163 (= P156), W164 (= W157), K188 (= K181), E191 (= E184), G221 (= G214), G225 (= G218), A226 (= A219), F239 (= F232), G241 (= G234), S242 (= S235), T245 (≠ V238), Y248 (≠ E241), L264 (= L257), C297 (= C290), Q344 (= Q336), R347 (= R339), E394 (= E387), F396 (= F389)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
37% identity, 98% coverage: 5:480/485 of query aligns to 4:484/493 of 4fr8A
- active site: N162 (= N158), K185 (= K181), Q261 (≠ E256), C295 (= C290), E392 (= E387), E469 (= E465)
- binding nicotinamide-adenine-dinucleotide: I158 (= I154), I159 (≠ V155), W161 (= W157), K185 (= K181), G218 (= G214), G222 (= G218), A223 (= A219), F236 (= F232), G238 (= G234), S239 (= S235), I242 (≠ V238), Q342 (= Q336), K345 (≠ R339), E392 (= E387), F394 (= F389)
- binding propane-1,2,3-triyl trinitrate: F163 (≠ Y159), L166 (≠ Q162), W170 (≠ R166), F289 (≠ Q284), S294 (≠ T289), C295 (= C290), D450 (≠ G445), F452 (≠ G447)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
38% identity, 99% coverage: 5:483/485 of query aligns to 31:514/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
5l13A Structure of aldh2 in complex with 2p3 (see paper)
37% identity, 99% coverage: 5:483/485 of query aligns to 5:488/494 of 5l13A
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E465)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (≠ Y159), M168 (≠ I163), W171 (≠ R166), F290 (≠ Q284), C295 (≠ T289), C296 (= C290), C297 (≠ S291), D451 (≠ G445), F453 (≠ G447)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
37% identity, 99% coverage: 5:483/485 of query aligns to 5:488/494 of 4kwgA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E465)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (≠ Y159), M168 (≠ I163), C295 (≠ T289), C296 (= C290), C297 (≠ S291), D451 (≠ G445), F453 (≠ G447)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
37% identity, 99% coverage: 5:483/485 of query aligns to 5:488/494 of 4kwfA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E465)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (≠ Y159), M168 (≠ I163), W171 (≠ R166), E262 (= E256), C295 (≠ T289), C296 (= C290), C297 (≠ S291), D451 (≠ G445), F453 (≠ G447), F459 (= F454)
Query Sequence
>3609638 FitnessBrowser__Dino:3609638
MLDRPTYDPGFPGDEILIGGVWQRCADTLEVIDPSDGTPLAQIARGGAAEIDRAVAAARA
ALDGDWGRMSATERGRCLTRLGALVAGEVDRLAEMEARDVGKPLSQARADALALARYLEF
YGGAADKVMGETIPYQSGYTVYTLREPHGVTGHIVPWNYPMQIIGRSVGAALAMGNACVL
KPAEDACLTALAFARLAEAAGLPPGALNVVTGLGAEAGAALSDHPGVDHLSFTGSVPVGA
EVQATAARHITPVTLELGGKSPQIVFADADLDAALPFLVKGGVQNAGQTCSAAARILVQT
DVFDAVADRMAEAYRALTVGPALSDPAVGPLISPKQKARVSAMLAQAQPDQILATGHLLP
EAPEGGCYVLPHLLGGIAADHPLAQQEIFGPVQILMRFETEQEAIALANGTEFGLVAGIW
TRDGARQMRMPKRLRAGQVFVNTYGAGGGVELPFGGVGKSGHGREKGFEALFGFSQLKTV
ATHHG
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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