SitesBLAST
Comparing WP_011382620.1 NCBI__GCF_000009985.1:WP_011382620.1 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)
2vroA Crystal structure of aldehyde dehydrogenase from burkholderia xenovorans lb400 (see paper)
50% identity, 95% coverage: 4:493/515 of query aligns to 6:508/521 of 2vroA
- active site: N160 (= N158), K183 (= K181), E258 (= E256), C297 (= C295), E401 (= E392), L496 (= L481)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I156 (= I154), K183 (= K181), S217 (≠ G215), S235 (= S233), T238 (= T236), L242 (= L240), F403 (= F394)
2y53A Crystal structure of e257q mutant of the box pathway encoded aldh from burkholderia xenovorans lb400 (see paper)
50% identity, 98% coverage: 4:508/515 of query aligns to 6:522/529 of 2y53A
- active site: N160 (= N158), K183 (= K181), Q258 (≠ E256), C297 (= C295), E401 (= E392), L495 (= L481)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I156 (= I154), N157 (= N155), F159 (= F157), N160 (= N158), K183 (= K181), A185 (= A183), T186 (= T184), S217 (≠ G215), F232 (= F230), G234 (= G232), S235 (= S233), A236 (= A234), T238 (= T236), A259 (= A257), D260 (= D258), C297 (= C295), F403 (= F394)
P77455 Bifunctional protein PaaZ; EC 3.3.2.12; EC 1.2.1.91 from Escherichia coli (strain K12) (see paper)
48% identity, 99% coverage: 1:508/515 of query aligns to 1:511/681 of P77455
- E256 (= E256) mutation to Q: Catalyzes the formation of 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde instead of 3-oxo-5,6-dehydrosuberyl-CoA.
6jqoA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ccoa (see paper)
48% identity, 98% coverage: 3:508/515 of query aligns to 2:510/678 of 6jqoA
- active site: N157 (= N158), E255 (= E256), C294 (= C295), L483 (= L481)
- binding crotonyl coenzyme a: V97 (≠ L99), F107 (≠ K109), S111 (= S113), F158 (= F159), W161 (= W162)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N154 (= N155), F156 (= F157), N157 (= N158), T183 (= T184), T230 (= T231), G231 (= G232), S232 (= S233), T235 (= T236), A256 (= A257), D257 (= D258), C294 (= C295)
Sites not aligning to the query:
6jqnA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ocoa (see paper)
48% identity, 98% coverage: 3:508/515 of query aligns to 2:510/678 of 6jqnA
- active site: N157 (= N158), E255 (= E256), C294 (= C295), L483 (= L481)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R19 (≠ A20), I153 (= I154), N154 (= N155), A155 (= A156), F156 (= F157), K180 (= K181), A182 (= A183), T183 (= T184), T230 (= T231), G231 (= G232), S232 (= S233), T235 (= T236), L239 (= L240), E255 (= E256), A256 (= A257), D257 (= D258), C294 (= C295), F396 (= F394), H471 (= H469)
Sites not aligning to the query:
6jqmA Structure of paaz with NADPH (see paper)
48% identity, 98% coverage: 3:508/515 of query aligns to 2:510/678 of 6jqmA
- active site: N157 (= N158), E255 (= E256), C294 (= C295), L483 (= L481)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R19 (≠ A20), I153 (= I154), N154 (= N155), A155 (= A156), F156 (= F157), N157 (= N158), K180 (= K181), A182 (= A183), T183 (= T184), G231 (= G232), S232 (= S233), T235 (= T236), A256 (= A257), D257 (= D258), C294 (= C295), E394 (= E392), F396 (= F394)
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
26% identity, 82% coverage: 5:428/515 of query aligns to 19:435/505 of 4neaA
- active site: N166 (= N158), K189 (= K181), E264 (≠ N261), C298 (= C295), E399 (= E392)
- binding nicotinamide-adenine-dinucleotide: P164 (≠ A156), K189 (= K181), E192 (≠ T184), G222 (= G215), G226 (vs. gap), G242 (= G232), G243 (≠ S233), T246 (= T236), H249 (≠ Q239), I250 (≠ L240), C298 (= C295), E399 (= E392), F401 (= F394)
Sites not aligning to the query:
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)
28% identity, 95% coverage: 7:496/515 of query aligns to 23:491/501 of Q56YU0
- G152 (≠ R139) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A409) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
7jwwA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
27% identity, 92% coverage: 7:482/515 of query aligns to 17:472/494 of 7jwwA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C295), E393 (= E392), E470 (= E480)
- binding 5-{4-[(Z)-2-hydroxyethenyl]phenyl}-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (= G103), T122 (= T107), F164 (= F159), M168 (≠ G163), Y290 (≠ V289), C295 (≠ K294), C296 (= C295), I297 (≠ T296), V453 (= V463), F459 (≠ H469)
7jwvA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
27% identity, 92% coverage: 7:482/515 of query aligns to 17:472/494 of 7jwvA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C295), E393 (= E392), E470 (= E480)
- binding 5-[4-(hydroxymethyl)phenyl]-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (= G103), T122 (= T107), F164 (= F159), M168 (≠ G163), Y290 (≠ V289), C295 (≠ K294), I297 (≠ T296), V453 (= V463), F459 (≠ H469)
7jwuA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
27% identity, 92% coverage: 7:482/515 of query aligns to 17:472/494 of 7jwuA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C295), E393 (= E392), E470 (= E480)
- binding nicotinamide-adenine-dinucleotide: I159 (= I154), I160 (≠ N155), P161 (≠ A156), W162 (≠ F157), N163 (= N158), K186 (= K181), E189 (≠ T184), G219 (= G215), G223 (vs. gap), A224 (vs. gap), F237 (= F230), T238 (= T231), G239 (= G232), S240 (= S233), V243 (≠ T236), L263 (≠ A257), C296 (= C295), Q343 (= Q342), K346 (≠ A345), E393 (= E392), F395 (= F394)
- binding 1-methyl-5-phenyl-6-{[(1R)-1-(pyridin-2-yl)ethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: T122 (= T107), F164 (= F159), W171 (≠ E166), Y290 (≠ V289), C295 (≠ K294), I297 (≠ T296), V453 (= V463), F459 (≠ H469)
7jwtA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
27% identity, 92% coverage: 7:482/515 of query aligns to 17:472/494 of 7jwtA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C295), E393 (= E392), E470 (= E480)
- binding 6-{[(1R)-1-(3-hydroxyphenyl)ethyl]sulfanyl}-1-methyl-5-phenyl-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (= G103), T122 (= T107), F164 (= F159), M168 (≠ G163), W171 (≠ E166), Y290 (≠ V289), C295 (≠ K294), V453 (= V463), F459 (≠ H469)
7jwsA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
27% identity, 92% coverage: 7:482/515 of query aligns to 17:472/494 of 7jwsA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C295), E393 (= E392), E470 (= E480)
- binding 1-methyl-5-phenyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (= G103), T122 (= T107), F164 (= F159), M168 (≠ G163), W171 (≠ E166), Y290 (≠ V289), C295 (≠ K294), I297 (≠ T296), V453 (= V463), F459 (≠ H469)
6dumA Aldh1a1 n121s in complex with 6-{[(3-fluorophenyl)methyl]sulfanyl}-2- (oxetan-3-yl)-5-phenyl-2,5-dihydro-4h-pyrazolo[3,4-d]pyrimidin-4-one (compound 13g) (see paper)
27% identity, 92% coverage: 7:482/515 of query aligns to 17:472/494 of 6dumA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C295), E393 (= E392), E470 (= E480)
- binding 6-{[(3-fluorophenyl)methyl]sulfanyl}-2-(oxetan-3-yl)-5-phenyl-2,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (= G103), T122 (= T107), F164 (= F159), M168 (≠ G163), W171 (≠ E166), H286 (≠ R285), Y290 (≠ V289), C295 (≠ K294), C296 (= C295), I297 (≠ T296), G451 (= G461), V453 (= V463), F459 (≠ H469)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I159 (= I154), I160 (≠ N155), P161 (≠ A156), W162 (≠ F157), N163 (= N158), K186 (= K181), E189 (≠ T184), G219 (= G215), P220 (≠ R216), G223 (vs. gap), A224 (vs. gap), F237 (= F230), T238 (= T231), G239 (= G232), S240 (= S233), V243 (≠ T236), L263 (≠ A257), C296 (= C295), Q343 (= Q342), K346 (≠ A345), E393 (= E392), F395 (= F394)
7um9A Human aldh1a1 with bound compound cm38 (see paper)
27% identity, 92% coverage: 7:482/515 of query aligns to 17:472/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I154), I160 (≠ N155), P161 (≠ A156), W162 (≠ F157), N163 (= N158), K186 (= K181), E189 (≠ T184), G219 (= G215), G223 (vs. gap), F237 (= F230), T238 (= T231), G239 (= G232), S240 (= S233), V243 (≠ T236), E262 (= E256), G264 (≠ D258), Q343 (= Q342), K346 (≠ A345), E393 (= E392), F395 (= F394)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (≠ E166), H286 (≠ R285), Y290 (≠ V289), I297 (≠ T296), G451 (= G461)
5l2oA Crystal structure of aldh1a1 in complex with buc22 (see paper)
27% identity, 92% coverage: 7:482/515 of query aligns to 17:472/494 of 5l2oA
5l2nA Structure of aldh1a1 in complex with buc25 (see paper)
27% identity, 92% coverage: 7:482/515 of query aligns to 17:472/494 of 5l2nA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C295), E393 (= E392), E470 (= E480)
- binding 3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate: F164 (= F159), M168 (≠ G163), W171 (≠ E166), H286 (≠ R285), G287 (≠ E286), Y290 (≠ V289), C295 (≠ K294), C296 (= C295), I297 (≠ T296), Y450 (≠ H460), G451 (= G461), V453 (= V463), F459 (≠ H469)
5l2mA Structure of aldh1a1 in complex with buc11 (see paper)
27% identity, 92% coverage: 7:482/515 of query aligns to 17:472/494 of 5l2mA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C295), E393 (= E392), E470 (= E480)
- binding 2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F159), F283 (= F276), H286 (≠ R285), Y290 (≠ V289)
5ac0A Ovis aries aldehyde dehydrogenase 1a1 in complex with a duocarmycin analog (see paper)
26% identity, 92% coverage: 7:482/515 of query aligns to 17:472/494 of 5ac0A
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C295), E393 (= E392), E470 (= E480)
- binding 1-[(1S)-1-methyl-5-oxidanyl-1,2-dihydrobenzo[e]indol-3-yl]hexan-1-one: M114 (vs. gap), F164 (= F159), W171 (≠ E166), Y290 (≠ V289), C295 (≠ K294), C296 (= C295)
- binding nicotinamide-adenine-dinucleotide: I159 (= I154), I160 (≠ N155), P161 (≠ A156), W162 (≠ F157), K186 (= K181), E189 (≠ T184), G219 (= G215), G223 (vs. gap), A224 (vs. gap), F237 (= F230), G239 (= G232), S240 (= S233), V243 (≠ T236), G264 (≠ D258), C296 (= C295), Q343 (= Q342), K346 (≠ A345), E393 (= E392)
5abmA Sheep aldehyde dehydrogenase 1a1 (see paper)
26% identity, 92% coverage: 7:482/515 of query aligns to 17:472/494 of 5abmA
- active site: N163 (= N158), K186 (= K181), E262 (= E256), C296 (= C295), E393 (= E392), E470 (= E480)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I159 (= I154), I160 (≠ N155), P161 (≠ A156), W162 (≠ F157), K186 (= K181), E189 (≠ T184), G219 (= G215), G223 (vs. gap), F237 (= F230), G239 (= G232), S240 (= S233), V243 (≠ T236), G264 (≠ D258), Q343 (= Q342), K346 (≠ A345), E393 (= E392), F395 (= F394)
Query Sequence
>WP_011382620.1 NCBI__GCF_000009985.1:WP_011382620.1
MIRLQSYLAGRWQDGAGSGAQLKDPVSGEVLATASGDGLDIAEALAFARDRGGPALRALS
FAGRAGLINALAGVLAENRERYNTVALANSGNTAVDAGLDVDGGIGTLKYYASIGRKLGE
ARLLAEATDDQLTKDEAFRGRHIWTSNRGVAVHINAFNFPSWGLWEKAAVSLLAGVPFLA
KPATATSWLAYEMVKDVVAAGVLPEGAMSLLCGGGRDLMDHLKPGDVVAFTGSAETAAQL
RSNPNVIAANVRFAVEADSLNLCALGPDAAPDAPEFAAFIKEVSREMTVKAGQKCTAIRR
VLVPRSRVDDVVAALKPALAKALMGDPRTEGVRMGPLVSRAQTVAAWAGLEALKAETQVV
AGGGNDDGGCFVPATLLLCNDPLAARAVHEIEVFGPVATLMPYDSVEQAVDLAHKGGGSL
AASVFSGDAAFLAGFVPAIATSHGRVLVVDSSVAASHSGHGVVMPHCIHGGPGRAGGGEE
LGGLRGLRFYMQRSAIQGSRSMLDAMTQGAAVVAL
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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