SitesBLAST
Comparing CCNA_02480 CCNA_02480 NAD-dependent benzaldehyde dehydrogenase II 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)
Q8NMB0 Vanillin dehydrogenase; Aromatic aldehyde dehydrogenase; EC 1.2.1.67; EC 1.2.1.64; EC 1.2.1.96 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
42% identity, 96% coverage: 12:479/487 of query aligns to 11:482/484 of Q8NMB0
- N157 (= N156) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 2.3-fold decreased affinity for vanillin compared to the wild type.
- K180 (= K179) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 5-fold decreased affinity for vanillin compared to the wild type.
- E199 (≠ A198) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 78% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 5-fold decreased affinity for NAD(+), 2.5-fold decreased affinity for NADP(+) and 1.5-fold decreased affinity for vanillin compared to the wild type.
- E258 (= E254) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 24% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 3.5-fold decreased affinity for NAD(+), 5-fold decreased affinity for NADP(+) and 3.7-fold decreased affinity for vanillin compared to the wild type.
- C292 (= C288) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 7-fold decreased affinity for NADP(+) and 8-fold decreased affinity for vanillin compared to the wild type.
4jz6A Crystal structure of a salicylaldehyde dehydrogenase from pseudomonas putida g7 complexed with salicylaldehyde (see paper)
36% identity, 98% coverage: 12:487/487 of query aligns to 4:484/484 of 4jz6A
- active site: N150 (= N156), K173 (= K179), E251 (= E254), C285 (= C288), E380 (= E382), F458 (≠ I461)
- binding salicylaldehyde: W97 (≠ K104), G151 (≠ F157), V154 (= V160), R247 (≠ K250), C248 (≠ V251), I284 (≠ V287), C285 (= C288), M286 (= M289), Y447 (≠ F449), Y455 (≠ N457)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
36% identity, 95% coverage: 22:486/487 of query aligns to 18:484/490 of 5ekcE
- active site: N154 (= N156), K177 (= K179), E252 (= E254), C286 (= C288), E381 (= E382), E459 (≠ I461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (= I152), T151 (≠ S153), P152 (= P154), W153 (≠ F155), K177 (= K179), S180 (≠ P182), G210 (≠ A213), G214 (= G216), F228 (= F230), G230 (= G232), E231 (≠ S233), T234 (≠ A236), N331 (≠ S332), R333 (≠ G334), Q334 (= Q335)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
36% identity, 95% coverage: 22:486/487 of query aligns to 11:477/482 of 5ek6A
- active site: N147 (= N156), K170 (= K179), E245 (= E254), C279 (= C288), E374 (= E382), E452 (≠ I461)
- binding 2-methylpropanal: I152 (≠ L161), K155 (≠ R164), T222 (= T231), E245 (= E254), F441 (= F449)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (= I152), T144 (≠ S153), W146 (≠ F155), N147 (= N156), I152 (≠ L161), K170 (= K179), A172 (≠ D181), S173 (≠ P182), P202 (≠ D212), G203 (≠ A213), G207 (= G216), F221 (= F230), T222 (= T231), G223 (= G232), E224 (≠ S233), T227 (≠ A236), I231 (≠ V240), E245 (= E254), L246 (= L255), C279 (= C288), E374 (= E382)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
36% identity, 95% coverage: 22:486/487 of query aligns to 11:477/482 of 4h73A
- active site: N147 (= N156), K170 (= K179), E245 (= E254), C279 (= C288), E374 (= E382), E452 (≠ I461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (= I152), T144 (≠ S153), P145 (= P154), W146 (≠ F155), K170 (= K179), A172 (≠ D181), S173 (≠ P182), G203 (≠ A213), G207 (= G216), F221 (= F230), G223 (= G232), E224 (≠ S233), T227 (≠ A236)
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
36% identity, 91% coverage: 30:474/487 of query aligns to 40:490/503 of 1bpwA
- active site: N166 (= N156), K189 (= K179), E263 (= E254), C297 (= C288), E400 (= E382), E477 (≠ I461)
- binding nicotinamide-adenine-dinucleotide: I162 (= I152), L163 (≠ S153), W165 (≠ F155), N166 (= N156), K189 (= K179), G221 (≠ D212), G225 (= G216), T240 (= T231), G241 (= G232), S242 (= S233), T245 (≠ A236), E263 (= E254), L264 (= L255), C297 (= C288), E400 (= E382), F402 (= F384), F466 (= F449)
P56533 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABADH; Aldehyde dehydrogenase family 9 member A1; Betaine aldehyde dehydrogenase; BADH; EC 1.2.1.47; EC 1.2.1.3 from Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias) (see paper)
36% identity, 91% coverage: 30:474/487 of query aligns to 40:490/503 of P56533
7jwwA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
35% identity, 98% coverage: 4:481/487 of query aligns to 3:490/494 of 7jwwA
- active site: N163 (= N156), K186 (= K179), E262 (= E254), C296 (= C288), E393 (= E382), E470 (≠ R460)
- 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 (≠ H111), T122 (≠ F115), F164 (= F157), M168 (≠ L161), Y290 (≠ L282), C295 (≠ V287), C296 (= C288), I297 (≠ M289), V453 (≠ A443), F459 (= F449)
7jwvA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
35% identity, 98% coverage: 4:481/487 of query aligns to 3:490/494 of 7jwvA
- active site: N163 (= N156), K186 (= K179), E262 (= E254), C296 (= C288), E393 (= E382), E470 (≠ R460)
- binding 5-[4-(hydroxymethyl)phenyl]-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ H111), T122 (≠ F115), F164 (= F157), M168 (≠ L161), Y290 (≠ L282), C295 (≠ V287), I297 (≠ M289), V453 (≠ A443), F459 (= F449)
7jwuA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
35% identity, 98% coverage: 4:481/487 of query aligns to 3:490/494 of 7jwuA
- active site: N163 (= N156), K186 (= K179), E262 (= E254), C296 (= C288), E393 (= E382), E470 (≠ R460)
- binding nicotinamide-adenine-dinucleotide: I159 (= I152), I160 (≠ S153), P161 (= P154), W162 (≠ F155), N163 (= N156), K186 (= K179), E189 (≠ P182), G219 (≠ A213), G223 (= G216), A224 (≠ D217), F237 (= F230), T238 (= T231), G239 (= G232), S240 (= S233), V243 (≠ A236), L263 (= L255), C296 (= C288), Q343 (= Q335), K346 (≠ R338), E393 (= E382), F395 (= F384)
- 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 (≠ F115), F164 (= F157), W171 (≠ R164), Y290 (≠ L282), C295 (≠ V287), I297 (≠ M289), V453 (≠ A443), F459 (= F449)
7jwtA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
35% identity, 98% coverage: 4:481/487 of query aligns to 3:490/494 of 7jwtA
- active site: N163 (= N156), K186 (= K179), E262 (= E254), C296 (= C288), E393 (= E382), E470 (≠ R460)
- binding 6-{[(1R)-1-(3-hydroxyphenyl)ethyl]sulfanyl}-1-methyl-5-phenyl-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ H111), T122 (≠ F115), F164 (= F157), M168 (≠ L161), W171 (≠ R164), Y290 (≠ L282), C295 (≠ V287), V453 (≠ A443), F459 (= F449)
7jwsA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
35% identity, 98% coverage: 4:481/487 of query aligns to 3:490/494 of 7jwsA
- active site: N163 (= N156), K186 (= K179), E262 (= E254), C296 (= C288), E393 (= E382), E470 (≠ R460)
- binding 1-methyl-5-phenyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ H111), T122 (≠ F115), F164 (= F157), M168 (≠ L161), W171 (≠ R164), Y290 (≠ L282), C295 (≠ V287), I297 (≠ M289), V453 (≠ A443), F459 (= F449)
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)
35% identity, 98% coverage: 4:481/487 of query aligns to 3:490/494 of 6dumA
- active site: N163 (= N156), K186 (= K179), E262 (= E254), C296 (= C288), E393 (= E382), E470 (≠ R460)
- binding 6-{[(3-fluorophenyl)methyl]sulfanyl}-2-(oxetan-3-yl)-5-phenyl-2,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ H111), T122 (≠ F115), F164 (= F157), M168 (≠ L161), W171 (≠ R164), H286 (≠ W278), Y290 (≠ L282), C295 (≠ V287), C296 (= C288), I297 (≠ M289), G451 (≠ T440), V453 (≠ A443), F459 (= F449)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I159 (= I152), I160 (≠ S153), P161 (= P154), W162 (≠ F155), N163 (= N156), K186 (= K179), E189 (≠ P182), G219 (≠ A213), P220 (vs. gap), G223 (= G216), A224 (≠ D217), F237 (= F230), T238 (= T231), G239 (= G232), S240 (= S233), V243 (≠ A236), L263 (= L255), C296 (= C288), Q343 (= Q335), K346 (≠ R338), E393 (= E382), F395 (= F384)
4wp7A Structure of human aldh1a1 with inhibitor cm026 (see paper)
35% identity, 98% coverage: 4:481/487 of query aligns to 3:490/494 of 4wp7A
- active site: N163 (= N156), K186 (= K179), E262 (= E254), C296 (= C288), E393 (= E382), E470 (≠ R460)
- binding 8-{[4-(furan-2-ylcarbonyl)piperazin-1-yl]methyl}-1,3-dimethyl-7-(3-methylbutyl)-3,7-dihydro-1H-purine-2,6-dione: G118 (≠ H111), T122 (≠ F115), F164 (= F157), G287 (= G279), Y290 (≠ L282), C295 (≠ V287), I297 (≠ M289), G451 (≠ T440), V453 (≠ A443), A455 (≠ P445)
7um9A Human aldh1a1 with bound compound cm38 (see paper)
35% identity, 98% coverage: 4:481/487 of query aligns to 3:490/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I152), I160 (≠ S153), P161 (= P154), W162 (≠ F155), N163 (= N156), K186 (= K179), E189 (≠ P182), G219 (≠ A213), G223 (= G216), F237 (= F230), T238 (= T231), G239 (= G232), S240 (= S233), V243 (≠ A236), E262 (= E254), G264 (= G256), Q343 (= Q335), K346 (≠ R338), E393 (= E382), F395 (= F384)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (≠ R164), H286 (≠ W278), Y290 (≠ L282), I297 (≠ M289), G451 (≠ T440)
5l2oA Crystal structure of aldh1a1 in complex with buc22 (see paper)
35% identity, 98% coverage: 4:481/487 of query aligns to 3:490/494 of 5l2oA
5l2nA Structure of aldh1a1 in complex with buc25 (see paper)
35% identity, 98% coverage: 4:481/487 of query aligns to 3:490/494 of 5l2nA
- active site: N163 (= N156), K186 (= K179), E262 (= E254), C296 (= C288), E393 (= E382), E470 (≠ R460)
- binding 3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate: F164 (= F157), M168 (≠ L161), W171 (≠ R164), H286 (≠ W278), G287 (= G279), Y290 (≠ L282), C295 (≠ V287), C296 (= C288), I297 (≠ M289), Y450 (≠ Q439), G451 (≠ T440), V453 (≠ A443), F459 (= F449)
5l2mA Structure of aldh1a1 in complex with buc11 (see paper)
35% identity, 98% coverage: 4:481/487 of query aligns to 3:490/494 of 5l2mA
- active site: N163 (= N156), K186 (= K179), E262 (= E254), C296 (= C288), E393 (= E382), E470 (≠ R460)
- binding 2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F157), F283 (≠ N275), H286 (≠ W278), Y290 (≠ L282)
4wpnA Structure of human aldh1a1 with inhibitor cm053 (see paper)
35% identity, 98% coverage: 4:481/487 of query aligns to 3:490/494 of 4wpnA
- active site: N163 (= N156), K186 (= K179), E262 (= E254), C296 (= C288), E393 (= E382), E470 (≠ R460)
- binding 1-{[1,3-dimethyl-7-(3-methylbutyl)-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]methyl}piperidine-4-carboxamide: F164 (= F157), H286 (≠ W278), G287 (= G279), Y290 (≠ L282), C295 (≠ V287), I297 (≠ M289), G451 (≠ T440), V453 (≠ A443)
5teiA Structure of human aldh1a1 with inhibitor cm039
35% identity, 98% coverage: 4:481/487 of query aligns to 2:489/493 of 5teiA
- active site: N162 (= N156), K185 (= K179), E261 (= E254), C295 (= C288), E392 (= E382), E469 (≠ R460)
- binding 6-{[(3-fluorophenyl)methyl]sulfanyl}-5-(2-methylphenyl)-2,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: S113 (vs. gap), F163 (= F157), H285 (≠ W278), G286 (= G279), Y289 (≠ L282), C295 (= C288), G450 (≠ T440), V452 (≠ A443), F458 (= F449)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I158 (= I152), I159 (≠ S153), P160 (= P154), W161 (≠ F155), N162 (= N156), K185 (= K179), E188 (≠ P182), G218 (≠ A213), G222 (= G216), A223 (≠ D217), F236 (= F230), T237 (= T231), G238 (= G232), S239 (= S233), V242 (≠ A236), C295 (= C288), Q342 (= Q335), K345 (≠ R338), E392 (= E382), F394 (= F384)
Query Sequence
>CCNA_02480 CCNA_02480 NAD-dependent benzaldehyde dehydrogenase II
MSEPLLSADAWTDRLFSDGWVKPSGGVIAVQEPATETVLTQVGRADRSDVARAAASAKAA
QPAWAALTADARQAILLRAADLLVEHAPDLAPWIMRESGSVAAKAAVELEHAAGFVRQAG
AMATEAAGLVLPSSPGKTSIARRVPLGVVAVISPFNFPLVLSIRAVAPALATGNAVVLKP
DPRTPISGGFLIARVFEAAGLPAGLLHVLPGDAEAGDALCRDPNIAMVAFTGSTGAGRKV
GEVAGAHLKKVALELGGKNPLIILDDADPDVAASNAAWGAWLHQGQVCMTAGRLLVQRGI
HDAVVERLAAKAGHLPVGDPMRGDVALGPLISRGQLDRVHAIVSDTVADGARLVAGGTHK
GLCYAPTVLTGVAPGMRAFEEEIFGPIAAVTVFDDLDEAARLANDGPYGLSAGIISGSVG
RAMTLGAKLEVGHLHINDQTVDAGPHSPFGGMKASGNGTRISGPANLDEFTTWRWETVKA
AATAYPF
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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