SitesBLAST
Comparing WP_005453549.1 NCBI__GCF_000244975.1:WP_005453549.1 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)
6mvtA Structure of a bacterial aldh16 complexed with nadh (see paper)
56% identity, 97% coverage: 9:474/479 of query aligns to 1:459/751 of 6mvtA
- active site: N151 (= N160), E247 (= E257), C281 (= C291), E450 (= E465)
- binding 1,4-dihydronicotinamide adenine dinucleotide: V147 (= V156), I148 (= I157), K174 (= K183), E177 (= E186), G207 (= G216), G210 (= G219), E211 (≠ A220), F223 (= F233), S226 (= S236), V229 (= V239), D327 (≠ E337), R331 (≠ K341)
6mvsA Structure of a bacterial aldh16 complexed with NAD (see paper)
56% identity, 97% coverage: 9:474/479 of query aligns to 1:459/751 of 6mvsA
- active site: N151 (= N160), E247 (= E257), C281 (= C291), E450 (= E465)
- binding nicotinamide-adenine-dinucleotide: V147 (= V156), I148 (= I157), W150 (= W159), K174 (= K183), E177 (= E186), G207 (= G216), G210 (= G219), E211 (≠ A220), F223 (= F233), S226 (= S236), V229 (= V239)
6mvuA Structure of a bacterial aldh16 active site mutant c295a complexed with p-nitrophenylacetate (see paper)
56% identity, 97% coverage: 9:474/479 of query aligns to 1:459/752 of 6mvuA
- active site: N151 (= N160), E247 (= E257), A281 (≠ C291), E450 (= E465)
- binding 4-nitrophenyl acetate: G207 (= G216), G210 (= G219), E211 (≠ A220), V214 (= V223), V229 (= V239), R232 (≠ Q242), I233 (= I243), A236 (≠ T246)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
45% identity, 97% coverage: 16:478/479 of query aligns to 11:484/491 of 5gtlA
- active site: N165 (= N160), K188 (= K183), E263 (= E257), C297 (= C291), E394 (= E388), E471 (= E465)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (≠ V156), P163 (= P158), K188 (= K183), A190 (= A185), E191 (= E186), Q192 (≠ T187), G221 (= G216), G225 (= G219), G241 (= G235), S242 (= S236), T245 (≠ V239), L264 (= L258), C297 (= C291), E394 (= E388), F396 (= F390)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
45% identity, 97% coverage: 16:478/479 of query aligns to 11:484/491 of 5gtkA
- active site: N165 (= N160), K188 (= K183), E263 (= E257), C297 (= C291), E394 (= E388), E471 (= E465)
- binding nicotinamide-adenine-dinucleotide: I161 (≠ V156), I162 (= I157), P163 (= P158), W164 (= W159), K188 (= K183), E191 (= E186), G221 (= G216), G225 (= G219), A226 (= A220), F239 (= F233), G241 (= G235), S242 (= S236), T245 (≠ V239), Y248 (≠ Q242), L264 (= L258), C297 (= C291), Q344 (= Q338), R347 (≠ K341), E394 (= E388), F396 (= F390)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
47% identity, 95% coverage: 25:478/479 of query aligns to 17:483/494 of 5l13A
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C291), E393 (= E388), E470 (= E465)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F161), M168 (= M165), W171 (= W168), F290 (= F285), C295 (≠ V290), C296 (= C291), C297 (= C292), D451 (≠ N446), F453 (= F448)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
47% identity, 95% coverage: 25:478/479 of query aligns to 17:483/494 of 4kwgA
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C291), E393 (= E388), E470 (= E465)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F161), M168 (= M165), C295 (≠ V290), C296 (= C291), C297 (= C292), D451 (≠ N446), F453 (= F448)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
47% identity, 95% coverage: 25:478/479 of query aligns to 17:483/494 of 4kwfA
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C291), E393 (= E388), E470 (= E465)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F161), M168 (= M165), W171 (= W168), E262 (= E257), C295 (≠ V290), C296 (= C291), C297 (= C292), D451 (≠ N446), F453 (= F448), 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)
47% identity, 95% coverage: 25:478/479 of query aligns to 17:483/494 of 3sz9A
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C291), E393 (= E388), E470 (= E465)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F161), C295 (≠ V290), C296 (= C291), D451 (≠ N446), F453 (= F448), F459 (= F454)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
47% identity, 95% coverage: 25:478/479 of query aligns to 17:483/494 of 3injA
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C291), E393 (= E388), E470 (= E465)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ T123), F164 (= F161), L167 (= L164), F286 (≠ N281), F290 (= F285), D451 (≠ N446), F453 (= F448)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
47% identity, 95% coverage: 25:478/479 of query aligns to 17:483/494 of 2vleA
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C291), E393 (= E388), E470 (= E465)
- binding daidzin: M118 (≠ T123), F164 (= F161), M168 (= M165), W171 (= W168), F286 (≠ N281), F290 (= F285), C295 (≠ V290), C296 (= C291), D451 (≠ N446), V452 (≠ R447), F453 (= F448)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
47% identity, 95% coverage: 25:478/479 of query aligns to 17:483/494 of 1o01B
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C291), E393 (= E388), E470 (= E465)
- binding (2e)-but-2-enal: C296 (= C291), C297 (= C292), F453 (= F448)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ V156), I160 (= I157), P161 (= P158), W162 (= W159), K186 (= K183), E189 (= E186), G219 (= G216), G223 (= G219), A224 (= A220), F237 (= F233), G239 (= G235), S240 (= S236), I243 (≠ V239), L263 (= L258), G264 (= G259), C296 (= C291), Q343 (= Q338), E393 (= E388), F395 (= F390)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
47% identity, 95% coverage: 25:478/479 of query aligns to 17:483/494 of 1cw3A
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C291), E393 (= E388), E470 (= E465)
- binding magnesium ion: V34 (= V41), D103 (= D108), Q190 (≠ T187)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ V156), I160 (= I157), P161 (= P158), W162 (= W159), K186 (= K183), G219 (= G216), G223 (= G219), A224 (= A220), F237 (= F233), G239 (= G235), S240 (= S236), I243 (≠ V239), L263 (= L258), G264 (= G259), C296 (= C291), Q343 (= Q338), K346 (= K341), E393 (= E388), F395 (= F390)
2onmA Human mitochondrial aldehyde dehydrogenase asian variant, aldh2 2, Complexed with NAD+ (see paper)
47% identity, 94% coverage: 25:474/479 of query aligns to 17:479/494 of 2onmA
- active site: N163 (= N160), K186 (= K183), E262 (= E257), C296 (= C291), E393 (= E388), E470 (= E465)
- binding adenosine-5'-diphosphate: E189 (= E186), G219 (= G216), G223 (= G219), A224 (= A220), F237 (= F233), G239 (= G235), S240 (= S236), I243 (≠ V239)
7radA Crystal structure analysis of aldh1b1
46% identity, 96% coverage: 20:478/479 of query aligns to 11:482/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (≠ V156), I159 (= I157), P160 (= P158), W161 (= W159), N162 (= N160), M167 (= M165), K185 (= K183), E188 (= E186), G218 (= G216), G222 (= G219), A223 (= A220), T237 (= T234), G238 (= G235), S239 (= S236), V242 (= V239), E261 (= E257), L262 (= L258), C295 (= C291), E392 (= E388), F394 (= F390)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ T119), E117 (≠ T123), F163 (= F161), E285 (≠ N281), F289 (= F285), N450 (= N446), V452 (≠ F448)
7mjdA Crystal structure analysis of aldh1b1
46% identity, 96% coverage: 20:478/479 of query aligns to 11:482/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (≠ V156), I159 (= I157), P160 (= P158), W161 (= W159), N162 (= N160), M167 (= M165), K185 (= K183), E188 (= E186), G218 (= G216), G222 (= G219), F236 (= F233), T237 (= T234), G238 (= G235), S239 (= S236), V242 (= V239), E261 (= E257), L262 (= L258), C295 (= C291), E392 (= E388), F394 (= F390)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ T123), E285 (≠ N281), F289 (= F285), N450 (= N446), V452 (≠ F448)
7mjcA Crystal structure analysis of aldh1b1
46% identity, 96% coverage: 20:478/479 of query aligns to 11:482/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (≠ V156), I159 (= I157), P160 (= P158), W161 (= W159), N162 (= N160), K185 (= K183), E188 (= E186), G218 (= G216), G222 (= G219), T237 (= T234), G238 (= G235), S239 (= S236), V242 (= V239), E261 (= E257), L262 (= L258), C295 (= C291), E392 (= E388), F394 (= F390)
1nzwA Cys302ser mutant of human mitochondrial aldehyde dehydrogenase complexed with nadh and mg2+ (see paper)
46% identity, 95% coverage: 25:478/479 of query aligns to 17:483/494 of 1nzwA
- active site: N163 (= N160), K186 (= K183), E262 (= E257), S296 (≠ C291), E393 (= E388), E470 (= E465)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I159 (≠ V156), I160 (= I157), P161 (= P158), K186 (= K183), E189 (= E186), G219 (= G216), P220 (vs. gap), G223 (= G219), A224 (= A220), F237 (= F233), G239 (= G235), S240 (= S236), I243 (≠ V239), E262 (= E257), G264 (= G259), S296 (≠ C291), Q343 (= Q338), E393 (= E388), F395 (= F390)
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)
45% identity, 100% coverage: 1:478/479 of query aligns to 20:507/518 of O94788
- E50 (vs. gap) to G: in dbSNP:rs34266719
- A110 (= A91) to V: in dbSNP:rs35365164
- Q182 (= Q155) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (= IPW 157:159) binding NAD(+)
- KPAE 210:213 (= KPAE 183:186) binding NAD(+)
- STE 264:266 (= STE 236:238) binding NAD(+)
- C320 (= C291) active site, Nucleophile
- R347 (≠ L318) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ R319) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ EQLAK 337:341) binding NAD(+)
- A383 (= A354) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E388) binding NAD(+)
- E436 (≠ A407) to K: in dbSNP:rs34744827
- S461 (≠ A432) 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)
46% identity, 96% coverage: 17:478/479 of query aligns to 6:481/492 of 6b5hA
- active site: N161 (= N160), E260 (= E257), C294 (= C291), E468 (= E465)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ T119), G116 (≠ T123), F162 (= F161), W169 (= W168), Q284 (≠ N281), F288 (= F285), T295 (≠ C292), N449 (= N446), L451 (≠ F448), N452 (≠ D449), F457 (= F454)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V156), I158 (= I157), W160 (= W159), N161 (= N160), K184 (= K183), G217 (= G216), G221 (= G219), F235 (= F233), T236 (= T234), G237 (= G235), S238 (= S236), V241 (= V239), E260 (= E257), L261 (= L258), C294 (= C291), F393 (= F390)
Query Sequence
>WP_005453549.1 NCBI__GCF_000244975.1:WP_005453549.1
MSQWEYAPAPESREIANLKPKYRPFIGGEFVDGSGEPLKTVNPATEEVLAEVGTASTSDV
DTAVKAARKAYDRVWGPMPGTERAKYVFRIARLLQERARELAVLETLDNGKPIKESRDTD
IPTAAAHFFYHAGWADKLDHAGLGPDPRPLGVAGQVIPWNFPLLMLAWKVAPALATGNTV
VLKPAETTPLTALVFAEICQQADLPPGVVNIVPGAGDIGAAVVEHPDVDKVAFTGSTEVG
KQIQRTLAGTRKRLTLELGGKAANIVFDDAPLDQAVEGIVNGIFFNQGHVCCAGSRLLVQ
ESVADELLDKLRARVSTLRLGDPLDKNTDVGAINSPEQLAKIKELVASGERDGAQRWSSP
CPVPEKGFFFAPTVFSGVEQSMRIAREEIFGPVLSVLTFRTPDEAVAKANNTPYGLSAGV
WTEKGSRILWMADRLRAGVVWANTFNRFDPAAPFGGYKESGFGREGGRTGLEAYLHVQG
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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