SitesBLAST
Comparing CA265_RS14635 CA265_RS14635 aldehyde dehydrogenase 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)
P37685 Aldehyde dehydrogenase B; Acetaldehyde dehydrogenase; EC 1.2.1.4 from Escherichia coli (strain K12) (see paper)
63% identity, 98% coverage: 10:501/501 of query aligns to 21:512/512 of P37685
- R197 (≠ E186) mutation to E: Less than 10% of wild-type acetaldehyde dehydrogenase activity.
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
42% identity, 97% coverage: 13:496/501 of query aligns to 3:482/489 of 4o6rA
- active site: N150 (= N160), K173 (= K183), E248 (= E257), C282 (= C296), E383 (= E397), E460 (= E474)
- binding adenosine monophosphate: I146 (= I156), V147 (≠ I157), K173 (= K183), G206 (= G215), G210 (= G219), Q211 (≠ R220), F224 (= F233), G226 (= G235), S227 (= S236), T230 (= T239), R233 (≠ L242)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
44% identity, 95% coverage: 17:492/501 of query aligns to 26:496/503 of O14293
- S248 (= S236) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
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)
43% identity, 95% coverage: 17:491/501 of query aligns to 23:493/501 of Q56YU0
- G152 (≠ S143) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A414) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
5l13A Structure of aldh2 in complex with 2p3 (see paper)
43% identity, 95% coverage: 17:491/501 of query aligns to 17:487/494 of 5l13A
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C296), E393 (= E397), E470 (= E474)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F161), M168 (= M165), W171 (= W168), F290 (vs. gap), C295 (≠ I295), C296 (= C296), C297 (≠ T297), D451 (≠ H455), F453 (≠ Y457)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
43% identity, 95% coverage: 17:491/501 of query aligns to 17:487/494 of 4kwgA
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C296), E393 (= E397), E470 (= E474)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F161), M168 (= M165), C295 (≠ I295), C296 (= C296), C297 (≠ T297), D451 (≠ H455), F453 (≠ Y457)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
43% identity, 95% coverage: 17:491/501 of query aligns to 17:487/494 of 4kwfA
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C296), E393 (= E397), E470 (= E474)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F161), M168 (= M165), W171 (= W168), E262 (= E257), C295 (≠ I295), C296 (= C296), C297 (≠ T297), D451 (≠ H455), F453 (≠ Y457), F459 (= F463)
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)
43% identity, 95% coverage: 17:491/501 of query aligns to 17:487/494 of 3sz9A
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C296), E393 (= E397), E470 (= E474)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F161), C295 (≠ I295), C296 (= C296), D451 (≠ H455), F453 (≠ Y457), F459 (= F463)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
43% identity, 95% coverage: 17:491/501 of query aligns to 17:487/494 of 3injA
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C296), E393 (= E397), E470 (= E474)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ L115), F164 (= F161), L167 (= L164), F286 (= F288), F290 (vs. gap), D451 (≠ H455), F453 (≠ Y457)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
43% identity, 95% coverage: 17:491/501 of query aligns to 17:487/494 of 2vleA
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C296), E393 (= E397), E470 (= E474)
- binding daidzin: M118 (≠ L115), F164 (= F161), M168 (= M165), W171 (= W168), F286 (= F288), F290 (vs. gap), C295 (≠ I295), C296 (= C296), D451 (≠ H455), V452 (≠ A456), F453 (≠ Y457)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
43% identity, 95% coverage: 17:491/501 of query aligns to 17:487/494 of 1o01B
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C296), E393 (= E397), E470 (= E474)
- binding (2e)-but-2-enal: C296 (= C296), C297 (≠ T297), F453 (≠ Y457)
- binding nicotinamide-adenine-dinucleotide: I159 (= I156), I160 (= I157), P161 (= P158), W162 (= W159), K186 (= K183), E189 (= E186), G219 (= G215), G223 (= G219), A224 (≠ R220), F237 (= F233), G239 (= G235), S240 (= S236), I243 (≠ T239), L263 (= L258), G264 (= G259), C296 (= C296), Q343 (= Q343), E393 (= E397), F395 (= F399)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
43% identity, 95% coverage: 17:491/501 of query aligns to 17:487/494 of 1cw3A
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C296), E393 (= E397), E470 (= E474)
- binding magnesium ion: V34 (≠ I34), D103 (= D100), Q190 (≠ S187)
- binding nicotinamide-adenine-dinucleotide: I159 (= I156), I160 (= I157), P161 (= P158), W162 (= W159), K186 (= K183), G219 (= G215), G223 (= G219), A224 (≠ R220), F237 (= F233), G239 (= G235), S240 (= S236), I243 (≠ T239), L263 (= L258), G264 (= G259), C296 (= C296), Q343 (= Q343), K346 (= K346), E393 (= E397), F395 (= F399)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
43% identity, 95% coverage: 17:491/501 of query aligns to 19:489/496 of 4fr8C
- active site: N165 (= N160), K188 (= K183), Q264 (≠ E257), C298 (= C296), E395 (= E397), E472 (= E474)
- binding nicotinamide-adenine-dinucleotide: I161 (= I156), I162 (= I157), W164 (= W159), K188 (= K183), G221 (= G215), G225 (= G219), A226 (≠ R220), F239 (= F233), G241 (= G235), S242 (= S236), I245 (≠ T239), Q345 (= Q343), E395 (= E397), F397 (= F399)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
43% identity, 95% coverage: 17:491/501 of query aligns to 16:486/493 of 4fr8A
- active site: N162 (= N160), K185 (= K183), Q261 (≠ E257), C295 (= C296), E392 (= E397), E469 (= E474)
- binding nicotinamide-adenine-dinucleotide: I158 (= I156), I159 (= I157), W161 (= W159), K185 (= K183), G218 (= G215), G222 (= G219), A223 (≠ R220), F236 (= F233), G238 (= G235), S239 (= S236), I242 (≠ T239), Q342 (= Q343), K345 (= K346), E392 (= E397), F394 (= F399)
- binding propane-1,2,3-triyl trinitrate: F163 (= F161), L166 (= L164), W170 (= W168), F289 (vs. gap), S294 (≠ I295), C295 (= C296), D450 (≠ H455), F452 (≠ Y457)
2onmA Human mitochondrial aldehyde dehydrogenase asian variant, aldh2 2, Complexed with NAD+ (see paper)
44% identity, 93% coverage: 17:483/501 of query aligns to 17:474/494 of 2onmA
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C296), E393 (= E397), E470 (= E474)
- binding adenosine-5'-diphosphate: E189 (= E186), G219 (= G215), G223 (= G219), A224 (≠ R220), F237 (= F233), G239 (= G235), S240 (= S236), I243 (≠ T239)
1nzwA Cys302ser mutant of human mitochondrial aldehyde dehydrogenase complexed with nadh and mg2+ (see paper)
43% identity, 95% coverage: 17:491/501 of query aligns to 17:487/494 of 1nzwA
- active site: N163 (= N160), K186 (= K183), E262 (= E257), S296 (≠ T297), E393 (= E397), E470 (= E474)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I159 (= I156), I160 (= I157), P161 (= P158), K186 (= K183), E189 (= E186), G219 (= G215), P220 (≠ S216), G223 (= G219), A224 (≠ R220), F237 (= F233), G239 (= G235), S240 (= S236), I243 (≠ T239), E262 (= E257), G264 (= G259), S296 (≠ T297), Q343 (= Q343), E393 (= E397), F395 (= F399)
7radA Crystal structure analysis of aldh1b1
43% identity, 95% coverage: 17:491/501 of query aligns to 16:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I156), I159 (= I157), P160 (= P158), W161 (= W159), N162 (= N160), M167 (= M165), K185 (= K183), E188 (= E186), G218 (= G215), G222 (= G219), A223 (≠ R220), T237 (= T234), G238 (= G235), S239 (= S236), V242 (≠ T239), E261 (= E257), L262 (= L258), C295 (= C296), E392 (= E397), F394 (= F399)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ A111), E117 (≠ L115), F163 (= F161), E285 (vs. gap), F289 (≠ L290), N450 (≠ H455), V452 (≠ Y457)
7mjdA Crystal structure analysis of aldh1b1
43% identity, 95% coverage: 17:491/501 of query aligns to 16:486/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I156), I159 (= I157), P160 (= P158), W161 (= W159), N162 (= N160), M167 (= M165), K185 (= K183), E188 (= E186), G218 (= G215), G222 (= G219), F236 (= F233), T237 (= T234), G238 (= G235), S239 (= S236), V242 (≠ T239), E261 (= E257), L262 (= L258), C295 (= C296), E392 (= E397), F394 (= F399)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ L115), E285 (vs. gap), F289 (≠ L290), N450 (≠ H455), V452 (≠ Y457)
7mjcA Crystal structure analysis of aldh1b1
43% identity, 95% coverage: 17:491/501 of query aligns to 16:486/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I156), I159 (= I157), P160 (= P158), W161 (= W159), N162 (= N160), K185 (= K183), E188 (= E186), G218 (= G215), G222 (= G219), T237 (= T234), G238 (= G235), S239 (= S236), V242 (≠ T239), E261 (= E257), L262 (= L258), C295 (= C296), E392 (= E397), F394 (= F399)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
43% identity, 95% coverage: 17:491/501 of query aligns to 43:513/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
Query Sequence
>CA265_RS14635 CA265_RS14635 aldehyde dehydrogenase
MENLIEKPSFKPQYDNYIGGKFVAPVKGAYFDNISPIDGKVFTKAAHSTKEDLELAVDAA
HEAFKTWSKTSSTERSIILNKIAQRMEDNLEYLAAVETIDNGKAVRETLAADLPLGVDHF
RYFAGVIRAEEGSLSELDQNTVSLIVHEPIGVVAQIIPWNFPLLMGIWKLAPALAAGNCV
VLKPAESTPVSIMVLMELIGDLLPPGVVNVVNGFGSELGRALVTNPKVSKAAFTGSTPTG
RLVMQYATENIIPVTLELGGKSPNIFFSSVMAEDDAFLDKAVEGAVMFALNQGEICTCPS
RLLIQEDIYEKFIAKVIERTKAIKIGSPLDRTVMMGAQASKIQFEKIAAYIKLGKEEGAE
VLTGGEINELPGELGGGYYIKPTIFKGHNKMRIFQEEIFGPVLAVTTFKTVEEAIEIAND
TLYGLGAGVWTRDAHELYQVPRAIQAGRVWVNQYHAYPAGAPFGGYKQSGVGRENHKMML
GHYRQTKNMLISYDKNKLGFF
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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