SitesBLAST
Comparing WP_085770042.1 NCBI__GCF_002117405.1:WP_085770042.1 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)
6x9lA Crystal structure of aldehyde dehydrogenasE C (aldc) mutant (c291a) from pseudomonas syringae in complexed with NAD+ and octanal (see paper)
54% identity, 99% coverage: 6:474/474 of query aligns to 13:482/485 of 6x9lA
- active site: N154 (= N147), E252 (= E245), A286 (≠ C279), E462 (= E454)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), T151 (= T144), W153 (= W146), N154 (= N147), Q159 (= Q152), K177 (= K170), E180 (= E173), G210 (= G203), P211 (= P204), G214 (= G207), T229 (= T222), G230 (= G223), S231 (= S224), E252 (= E245), L253 (= L246), A286 (≠ C279), E386 (= E378), F388 (= F380), F451 (= F443)
- binding octanal: W155 (= W148), S285 (= S278)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
49% identity, 99% coverage: 1:471/474 of query aligns to 2:451/454 of 3ty7B
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
39% identity, 99% coverage: 1:469/474 of query aligns to 13:486/491 of 5gtlA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E378), E471 (= E454)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I143), P163 (= P145), K188 (= K170), A190 (≠ S172), E191 (= E173), Q192 (≠ I174), G221 (= G203), G225 (= G207), G241 (= G223), S242 (= S224), T245 (≠ A227), L264 (= L246), C297 (= C279), E394 (= E378), F396 (= F380)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
39% identity, 99% coverage: 1:469/474 of query aligns to 13:486/491 of 5gtkA
- active site: N165 (= N147), K188 (= K170), E263 (= E245), C297 (= C279), E394 (= E378), E471 (= E454)
- binding nicotinamide-adenine-dinucleotide: I161 (= I143), I162 (≠ T144), P163 (= P145), W164 (= W146), K188 (= K170), E191 (= E173), G221 (= G203), G225 (= G207), A226 (= A208), F239 (= F221), G241 (= G223), S242 (= S224), T245 (≠ A227), Y248 (≠ E230), L264 (= L246), C297 (= C279), Q344 (= Q325), R347 (≠ K328), E394 (= E378), F396 (= F380)
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
41% identity, 99% coverage: 3:470/474 of query aligns to 4:476/483 of 3b4wA
- active site: N154 (= N147), K177 (= K170), E251 (= E245), C285 (= C279), E384 (= E378), E460 (= E454)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), V151 (≠ T144), W153 (= W146), N154 (= N147), K177 (= K170), I210 (≠ P204), G213 (= G207), T228 (= T222), G229 (= G223), S230 (= S224), V233 (≠ A227), E236 (= E230), E251 (= E245), L252 (= L246), C285 (= C279), E384 (= E378), F386 (= F380)
7radA Crystal structure analysis of aldh1b1
39% identity, 99% coverage: 4:474/474 of query aligns to 12:489/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I143), I159 (≠ T144), P160 (= P145), W161 (= W146), N162 (= N147), M167 (≠ Q152), K185 (= K170), E188 (= E173), G218 (= G203), G222 (= G207), A223 (= A208), T237 (= T222), G238 (= G223), S239 (= S224), V242 (≠ A227), E261 (= E245), L262 (= L246), C295 (= C279), E392 (= E378), F394 (= F380)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ S112), E117 (= E116), F163 (≠ W148), E285 (≠ N269), F289 (≠ L273), N450 (≠ P436), V452 (vs. gap)
7mjdA Crystal structure analysis of aldh1b1
39% identity, 99% coverage: 4:474/474 of query aligns to 12:489/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I143), I159 (≠ T144), P160 (= P145), W161 (= W146), N162 (= N147), M167 (≠ Q152), K185 (= K170), E188 (= E173), G218 (= G203), G222 (= G207), F236 (= F221), T237 (= T222), G238 (= G223), S239 (= S224), V242 (≠ A227), E261 (= E245), L262 (= L246), C295 (= C279), E392 (= E378), F394 (= F380)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (= E116), E285 (≠ N269), F289 (≠ L273), N450 (≠ P436), V452 (vs. gap)
7mjcA Crystal structure analysis of aldh1b1
39% identity, 99% coverage: 4:474/474 of query aligns to 12:489/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I143), I159 (≠ T144), P160 (= P145), W161 (= W146), N162 (= N147), K185 (= K170), E188 (= E173), G218 (= G203), G222 (= G207), T237 (= T222), G238 (= G223), S239 (= S224), V242 (≠ A227), E261 (= E245), L262 (= L246), C295 (= C279), E392 (= E378), F394 (= F380)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 99% coverage: 4:470/474 of query aligns to 5:477/486 of 4pxlA
- active site: N154 (= N147), K177 (= K170), E253 (= E245), C287 (= C279), E384 (= E378), D461 (≠ E454)
- binding nicotinamide-adenine-dinucleotide: I150 (= I143), V151 (≠ T144), P152 (= P145), W153 (= W146), K177 (= K170), E180 (= E173), G210 (= G203), G214 (= G207), A215 (= A208), F228 (= F221), G230 (= G223), S231 (= S224), V234 (≠ A227), E253 (= E245), G255 (= G247), C287 (= C279), Q334 (= Q325), K337 (= K328), E384 (= E378), F386 (= F380)
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: 4:474/474 of query aligns to 39:516/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
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: 3:469/474 of query aligns to 10:483/492 of 6b5hA
- active site: N161 (= N147), E260 (= E245), C294 (= C279), E468 (= E454)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ S112), G116 (≠ E116), F162 (≠ W148), W169 (≠ C155), Q284 (≠ N269), F288 (≠ L273), T295 (≠ N280), N449 (vs. gap), L451 (≠ M437), N452 (≠ D438), F457 (= F443)
- binding nicotinamide-adenine-dinucleotide: I157 (= I143), I158 (≠ T144), W160 (= W146), N161 (= N147), K184 (= K170), G217 (= G203), G221 (= G207), F235 (= F221), T236 (= T222), G237 (= G223), S238 (= S224), V241 (≠ A227), E260 (= E245), L261 (= L246), C294 (= C279), F393 (= F380)
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: 3:469/474 of query aligns to 10:483/492 of 6b5gA
- active site: N161 (= N147), E260 (= E245), C294 (= C279), E468 (= E454)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ W148), L165 (≠ N151), W169 (≠ C155), F288 (≠ L273), C293 (≠ S278), C294 (= C279), T295 (≠ N280), N449 (vs. gap), L451 (≠ M437)
- binding nicotinamide-adenine-dinucleotide: I157 (= I143), I158 (≠ T144), P159 (= P145), W160 (= W146), N161 (= N147), M166 (≠ Q152), K184 (= K170), E187 (= E173), G217 (= G203), G221 (= G207), F235 (= F221), T236 (= T222), G237 (= G223), S238 (= S224), V241 (≠ A227), E260 (= E245), L261 (= L246), C294 (= C279), E391 (= E378), F393 (= F380)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
38% identity, 99% coverage: 3:469/474 of query aligns to 10:483/492 of 6aljA
- active site: N161 (= N147), E260 (= E245), C294 (= C279), E468 (= E454)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ E116), F162 (≠ W148), L165 (≠ N151), M166 (≠ Q152), W169 (≠ C155), E260 (= E245), C293 (≠ S278), C294 (= C279), L451 (≠ M437), N452 (≠ D438), A453 (≠ L439)
- binding nicotinamide-adenine-dinucleotide: I157 (= I143), I158 (≠ T144), P159 (= P145), W160 (= W146), N161 (= N147), K184 (= K170), E187 (= E173), G217 (= G203), G221 (= G207), F235 (= F221), G237 (= G223), S238 (= S224), V241 (≠ A227), Q341 (= Q325), K344 (= K328), E391 (= E378), F393 (= F380)
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, 99% coverage: 3:469/474 of query aligns to 36:509/518 of O94788
- E50 (≠ A17) to G: in dbSNP:rs34266719
- A110 (≠ V74) to V: in dbSNP:rs35365164
- Q182 (≠ F142) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPW 144:146) binding NAD(+)
- KPAE 210:213 (≠ KPSE 170:173) binding NAD(+)
- STE 264:266 (≠ STR 224:226) binding NAD(+)
- C320 (= C279) active site, Nucleophile
- R347 (≠ T306) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ T307) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ AQWNK 324:328) binding NAD(+)
- A383 (= A341) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E378) binding NAD(+)
- E436 (= E397) to K: in dbSNP:rs34744827
- S461 (≠ A422) 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, 99% coverage: 3:469/474 of query aligns to 36:509/518 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)
38% identity, 99% coverage: 3:470/474 of query aligns to 18:492/501 of Q56YU0
- G152 (vs. gap) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A395) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
37% identity, 99% coverage: 6:474/474 of query aligns to 14:489/493 of 4fr8A
- active site: N162 (= N147), K185 (= K170), Q261 (≠ E245), C295 (= C279), E392 (= E378), E469 (= E454)
- binding nicotinamide-adenine-dinucleotide: I158 (= I143), I159 (≠ T144), W161 (= W146), K185 (= K170), G218 (= G203), G222 (= G207), A223 (= A208), F236 (= F221), G238 (= G223), S239 (= S224), I242 (≠ A227), Q342 (= Q325), K345 (= K328), E392 (= E378), F394 (= F380)
- binding propane-1,2,3-triyl trinitrate: F163 (≠ W148), L166 (≠ N151), W170 (≠ C155), F289 (≠ L273), S294 (= S278), C295 (= C279), D450 (≠ P436), F452 (vs. gap)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
37% identity, 99% coverage: 6:474/474 of query aligns to 17:492/496 of 4fr8C
- active site: N165 (= N147), K188 (= K170), Q264 (≠ E245), C298 (= C279), E395 (= E378), E472 (= E454)
- binding nicotinamide-adenine-dinucleotide: I161 (= I143), I162 (≠ T144), W164 (= W146), K188 (= K170), G221 (= G203), G225 (= G207), A226 (= A208), F239 (= F221), G241 (= G223), S242 (= S224), I245 (≠ A227), Q345 (= Q325), E395 (= E378), F397 (= F380)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
37% identity, 99% coverage: 6:474/474 of query aligns to 15:490/494 of 5l13A
- active site: N163 (= N147), K186 (= K170), E262 (= E245), C296 (= C279), E393 (= E378), E470 (= E454)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (≠ W148), M168 (≠ Q152), W171 (≠ C155), F290 (≠ L273), C295 (≠ S278), C296 (= C279), C297 (≠ N280), D451 (≠ P436), F453 (vs. gap)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
37% identity, 99% coverage: 6:474/474 of query aligns to 15:490/494 of 4kwgA
- active site: N163 (= N147), K186 (= K170), E262 (= E245), C296 (= C279), E393 (= E378), E470 (= E454)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (≠ W148), M168 (≠ Q152), C295 (≠ S278), C296 (= C279), C297 (≠ N280), D451 (≠ P436), F453 (vs. gap)
Query Sequence
>WP_085770042.1 NCBI__GCF_002117405.1:WP_085770042.1
MREYLKFYIDGHWVEPAELRTLEVINPATEAVCGHIALGSATDVDRAVAAAGEAFKSFSR
TSRRERLELLQRIVVELEKRHEDMARAITEEMGAPVWLAQRAQARMGAAHFSTAIEVLKR
YEFEERRGATIIVKEPIGVCGFITPWNWPLNQMACKIAPALATGCAMVLKPSEIAPFSGI
VLAEALEAAGTPPGVFNLVNGDGPTVGAAISSHPGVSMVSFTGSTRAGVEVAKNAAPTVK
RICQELGGKSPNILLEDADMKAAVTAGVNAVMLNSGQSCNAPTRMLAPRKRMEEVIGFAR
SAAEATTVGDPNGNAQMGPVVSEAQWNKVQGLIQKGLEEGASLVAGGLGKPEGLEKGYYV
KPTVFANVTNDMTIAREEIFGPVLSILAYDRVADAIEIANDTEYGLSAYVSGADPARLME
TASRLRAGQVQLNSAPMDLMAPFGGYKMSGNGREWGDHAFAEFLETKAIIGVAP
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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