SitesBLAST
Comparing GFF3161 FitnessBrowser__Phaeo:GFF3161 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)
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
66% identity, 97% coverage: 15:485/485 of query aligns to 4:476/476 of 4yweA
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
45% identity, 96% coverage: 15:480/485 of query aligns to 9:476/486 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 (≠ T238), E253 (= E256), G255 (= G258), C287 (= C290), Q334 (= Q336), K337 (≠ I339), E384 (= E387), F386 (= F389)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
41% identity, 96% coverage: 15:480/485 of query aligns to 20:486/491 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 (≠ E185), G221 (= G214), G225 (= G218), G241 (= G234), S242 (= S235), T245 (= T238), L264 (= L257), C297 (= C290), E394 (= E387), F396 (= F389)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
41% identity, 96% coverage: 15:480/485 of query aligns to 20:486/491 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 (= T238), Y248 (≠ L241), L264 (= L257), C297 (= C290), Q344 (= Q336), R347 (≠ I339), E394 (= E387), F396 (= F389)
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)
41% identity, 96% coverage: 15:480/485 of query aligns to 23:491/501 of Q56YU0
- G152 (≠ V141) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A404) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
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)
40% identity, 96% coverage: 15:481/485 of query aligns to 41:510/518 of Q63639
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)
40% identity, 96% coverage: 15:481/485 of query aligns to 41:510/518 of O94788
- E50 (≠ A24) 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 (≠ SVR 235:237) binding
- C320 (= C290) active site, Nucleophile
- R347 (≠ Q316) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ L317) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ RQK-- 335:337) binding
- A383 (= A348) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E387) binding
- E436 (≠ R406) to K: in dbSNP:rs34744827
- S461 (≠ A431) 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)
40% identity, 96% coverage: 15:481/485 of query aligns to 15:484/492 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 (≠ N280), 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 (≠ T238), 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)
40% identity, 96% coverage: 15:481/485 of query aligns to 15:484/492 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 (≠ T238), E260 (= E256), L261 (= L257), C294 (= C290), E391 (= E387), F393 (= F389)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
40% identity, 96% coverage: 15:481/485 of query aligns to 15:484/492 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 (≠ T238), Q341 (= Q336), K344 (vs. gap), E391 (= E387), F393 (= F389)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
42% identity, 96% coverage: 15:481/485 of query aligns to 16:485/493 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 (≠ T238), Q342 (= Q336), K345 (≠ I339), 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)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
42% identity, 96% coverage: 15:480/485 of query aligns to 19:487/496 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 (≠ T238), Q345 (= Q336), E395 (= E387), F397 (= F389)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
42% identity, 96% coverage: 15:480/485 of query aligns to 17:485/494 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)
42% identity, 96% coverage: 15:480/485 of query aligns to 17:485/494 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)
42% identity, 96% coverage: 15:480/485 of query aligns to 17:485/494 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)
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)
42% identity, 96% coverage: 15:480/485 of query aligns to 17:485/494 of 3sz9A
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E465)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (≠ Y159), C295 (≠ T289), C296 (= C290), D451 (≠ G445), F453 (≠ G447), F459 (= F454)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
42% identity, 96% coverage: 15:480/485 of query aligns to 17:485/494 of 3injA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E465)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ A113), F164 (≠ Y159), L167 (≠ Q162), F286 (≠ N280), F290 (≠ Q284), D451 (≠ G445), F453 (≠ G447)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
42% identity, 96% coverage: 15:480/485 of query aligns to 17:485/494 of 2vleA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E465)
- binding daidzin: M118 (≠ A113), F164 (≠ Y159), M168 (≠ I163), W171 (≠ R166), F286 (≠ N280), F290 (≠ Q284), C295 (≠ T289), C296 (= C290), D451 (≠ G445), V452 (≠ A446), F453 (≠ G447)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
42% identity, 96% coverage: 15:480/485 of query aligns to 17:485/494 of 1o01B
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E465)
- binding (2e)-but-2-enal: C296 (= C290), C297 (≠ S291), F453 (≠ G447)
- binding nicotinamide-adenine-dinucleotide: I159 (= I154), I160 (≠ V155), P161 (= P156), W162 (= W157), K186 (= K181), E189 (= E184), G219 (= G214), G223 (= G218), A224 (= A219), F237 (= F232), G239 (= G234), S240 (= S235), I243 (≠ T238), L263 (= L257), G264 (= G258), C296 (= C290), Q343 (= Q336), E393 (= E387), F395 (= F389)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
42% identity, 96% coverage: 15:480/485 of query aligns to 17:485/494 of 1cw3A
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C290), E393 (= E387), E470 (= E465)
- binding magnesium ion: V34 (≠ T32), D103 (= D99), Q190 (≠ E185)
- binding nicotinamide-adenine-dinucleotide: I159 (= I154), I160 (≠ V155), P161 (= P156), W162 (= W157), K186 (= K181), G219 (= G214), G223 (= G218), A224 (= A219), F237 (= F232), G239 (= G234), S240 (= S235), I243 (≠ T238), L263 (= L257), G264 (= G258), C296 (= C290), Q343 (= Q336), K346 (≠ I339), E393 (= E387), F395 (= F389)
Query Sequence
>GFF3161 FitnessBrowser__Phaeo:GFF3161
MTDAAPLWFDPALCLIDGSWQAPAGGGTLPLTNPSDGSPLCQIARGDARDIDAAVAAARA
ALDGPWGGMTATERGRLLTRMGQMVLERVDTLAQLEAMDVGKPLTQARADAVALARYLEF
YGGAADKLHGETIPYQAGYTVYTLREPHGVTGHIVPWNYPMQIIGRSVGAALAMGNACVL
KPAEEACLTALAFAHIAVEAGLPAGALNVVPGIGAEAGAALAGHPGVDHISFTGSVRTGA
LVQQAAGANVVPVTLELGGKSPQLVFDDADLEAALPFLVNAGIQNAGQTCSAASRILVQR
GVYDQVRAAMAAAYSQLTVGPALSDLRLGPLISTRQKEIVEGYLAKGADLAIAAQGVLSE
EASDKGAYVRPTLFADVGADHPLAQEEIFGPVQVLIPFEDEAEAVRIANSTDYGLVAGIW
TRDGARQMRLAKRLRAGQVFLNNYGAGGGVELPFGGVGKSGHGREKGFEALYGFSQLKTV
AAYHG
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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