SitesBLAST
Comparing GFF3227 PGA1_c32800 aldehyde dehydrogenase 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)
74% identity, 95% coverage: 39:801/802 of query aligns to 1:751/751 of 6mvtA
- active site: N151 (= N191), E247 (= E287), C281 (= C321), E450 (= E493)
- binding 1,4-dihydronicotinamide adenine dinucleotide: V147 (≠ I187), I148 (= I188), K174 (= K214), E177 (= E217), G207 (= G247), G210 (= G250), E211 (= E251), F223 (= F263), S226 (= S266), V229 (= V269), D327 (≠ V367), R331 (≠ T371)
6mvsA Structure of a bacterial aldh16 complexed with NAD (see paper)
74% identity, 95% coverage: 39:801/802 of query aligns to 1:751/751 of 6mvsA
- active site: N151 (= N191), E247 (= E287), C281 (= C321), E450 (= E493)
- binding nicotinamide-adenine-dinucleotide: V147 (≠ I187), I148 (= I188), W150 (= W190), K174 (= K214), E177 (= E217), G207 (= G247), G210 (= G250), E211 (= E251), F223 (= F263), S226 (= S266), V229 (= V269)
6mvuA Structure of a bacterial aldh16 active site mutant c295a complexed with p-nitrophenylacetate (see paper)
74% identity, 95% coverage: 39:801/802 of query aligns to 1:751/752 of 6mvuA
- active site: N151 (= N191), E247 (= E287), A281 (≠ C321), E450 (= E493)
- binding 4-nitrophenyl acetate: G207 (= G247), G210 (= G250), E211 (= E251), V214 (= V254), V229 (= V269), R232 (= R272), I233 (= I273), A236 (= A276)
P37685 Aldehyde dehydrogenase B; Acetaldehyde dehydrogenase; EC 1.2.1.4 from Escherichia coli (strain K12) (see paper)
44% identity, 56% coverage: 55:506/802 of query aligns to 23:498/512 of P37685
- R197 (≠ E217) mutation to E: Less than 10% of wild-type acetaldehyde dehydrogenase activity.
7radA Crystal structure analysis of aldh1b1
42% identity, 56% coverage: 60:509/802 of query aligns to 16:485/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I187), I159 (= I188), P160 (= P189), W161 (= W190), N162 (= N191), M167 (= M196), K185 (= K214), E188 (= E217), G218 (= G247), G222 (≠ E251), A223 (≠ M252), T237 (= T264), G238 (= G265), S239 (= S266), V242 (= V269), E261 (= E287), L262 (= L288), C295 (= C321), E392 (= E416), F394 (= F418)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ I152), E117 (≠ L156), F163 (= F192), E285 (≠ D311), F289 (= F315), N450 (= N474), V452 (≠ F476)
7mjdA Crystal structure analysis of aldh1b1
42% identity, 56% coverage: 60:509/802 of query aligns to 16:485/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I187), I159 (= I188), P160 (= P189), W161 (= W190), N162 (= N191), M167 (= M196), K185 (= K214), E188 (= E217), G218 (= G247), G222 (≠ E251), F236 (= F263), T237 (= T264), G238 (= G265), S239 (= S266), V242 (= V269), E261 (= E287), L262 (= L288), C295 (= C321), E392 (= E416), F394 (= F418)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ L156), E285 (≠ D311), F289 (= F315), N450 (= N474), V452 (≠ F476)
7mjcA Crystal structure analysis of aldh1b1
42% identity, 56% coverage: 60:509/802 of query aligns to 16:485/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I187), I159 (= I188), P160 (= P189), W161 (= W190), N162 (= N191), K185 (= K214), E188 (= E217), G218 (= G247), G222 (≠ E251), T237 (= T264), G238 (= G265), S239 (= S266), V242 (= V269), E261 (= E287), L262 (= L288), C295 (= C321), E392 (= E416), F394 (= F418)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
41% identity, 56% coverage: 60:506/802 of query aligns to 20:484/491 of 5gtlA
- active site: N165 (= N191), K188 (= K214), E263 (= E287), C297 (= C321), E394 (= E416), E471 (= E493)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I187), P163 (= P189), K188 (= K214), A190 (= A216), E191 (= E217), Q192 (≠ Y218), G221 (= G247), G225 (= G250), G241 (= G265), S242 (= S266), T245 (≠ V269), L264 (= L288), C297 (= C321), E394 (= E416), F396 (= F418)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
41% identity, 56% coverage: 60:506/802 of query aligns to 20:484/491 of 5gtkA
- active site: N165 (= N191), K188 (= K214), E263 (= E287), C297 (= C321), E394 (= E416), E471 (= E493)
- binding nicotinamide-adenine-dinucleotide: I161 (= I187), I162 (= I188), P163 (= P189), W164 (= W190), K188 (= K214), E191 (= E217), G221 (= G247), G225 (= G250), A226 (≠ E251), F239 (= F263), G241 (= G265), S242 (= S266), T245 (≠ V269), Y248 (≠ R272), L264 (= L288), C297 (= C321), Q344 (= Q368), R347 (≠ T371), E394 (= E416), F396 (= F418)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
43% identity, 56% coverage: 60:509/802 of query aligns to 17:486/494 of 5l13A
- active site: N163 (= N191), K186 (= K214), E262 (= E287), C296 (= C321), E393 (= E416), E470 (= E493)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F192), M168 (= M196), W171 (= W199), F290 (= F315), C295 (≠ V320), C296 (= C321), C297 (= C322), D451 (≠ N474), F453 (= F476)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
43% identity, 56% coverage: 60:509/802 of query aligns to 17:486/494 of 4kwgA
- active site: N163 (= N191), K186 (= K214), E262 (= E287), C296 (= C321), E393 (= E416), E470 (= E493)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F192), M168 (= M196), C295 (≠ V320), C296 (= C321), C297 (= C322), D451 (≠ N474), F453 (= F476)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
43% identity, 56% coverage: 60:509/802 of query aligns to 17:486/494 of 4kwfA
- active site: N163 (= N191), K186 (= K214), E262 (= E287), C296 (= C321), E393 (= E416), E470 (= E493)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F192), M168 (= M196), W171 (= W199), E262 (= E287), C295 (≠ V320), C296 (= C321), C297 (= C322), D451 (≠ N474), F453 (= F476), F459 (= F482)
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, 56% coverage: 60:509/802 of query aligns to 17:486/494 of 3sz9A
- active site: N163 (= N191), K186 (= K214), E262 (= E287), C296 (= C321), E393 (= E416), E470 (= E493)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F192), C295 (≠ V320), C296 (= C321), D451 (≠ N474), F453 (= F476), F459 (= F482)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
43% identity, 56% coverage: 60:509/802 of query aligns to 17:486/494 of 3injA
- active site: N163 (= N191), K186 (= K214), E262 (= E287), C296 (= C321), E393 (= E416), E470 (= E493)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ L156), F164 (= F192), L167 (= L195), F286 (≠ D311), F290 (= F315), D451 (≠ N474), F453 (= F476)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
43% identity, 56% coverage: 60:509/802 of query aligns to 17:486/494 of 2vleA
- active site: N163 (= N191), K186 (= K214), E262 (= E287), C296 (= C321), E393 (= E416), E470 (= E493)
- binding daidzin: M118 (≠ L156), F164 (= F192), M168 (= M196), W171 (= W199), F286 (≠ D311), F290 (= F315), C295 (≠ V320), C296 (= C321), D451 (≠ N474), V452 (≠ L475), F453 (= F476)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
43% identity, 56% coverage: 60:509/802 of query aligns to 17:486/494 of 1o01B
- active site: N163 (= N191), K186 (= K214), E262 (= E287), C296 (= C321), E393 (= E416), E470 (= E493)
- binding (2e)-but-2-enal: C296 (= C321), C297 (= C322), F453 (= F476)
- binding nicotinamide-adenine-dinucleotide: I159 (= I187), I160 (= I188), P161 (= P189), W162 (= W190), K186 (= K214), E189 (= E217), G219 (= G247), G223 (≠ E251), A224 (≠ M252), F237 (= F263), G239 (= G265), S240 (= S266), I243 (≠ V269), L263 (= L288), G264 (= G289), C296 (= C321), Q343 (= Q368), E393 (= E416), F395 (= F418)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
43% identity, 56% coverage: 60:509/802 of query aligns to 17:486/494 of 1cw3A
- active site: N163 (= N191), K186 (= K214), E262 (= E287), C296 (= C321), E393 (= E416), E470 (= E493)
- binding magnesium ion: V34 (≠ K75), D103 (= D141), Q190 (≠ Y218)
- binding nicotinamide-adenine-dinucleotide: I159 (= I187), I160 (= I188), P161 (= P189), W162 (= W190), K186 (= K214), G219 (= G247), G223 (≠ E251), A224 (≠ M252), F237 (= F263), G239 (= G265), S240 (= S266), I243 (≠ V269), L263 (= L288), G264 (= G289), C296 (= C321), Q343 (= Q368), K346 (≠ T371), E393 (= E416), F395 (= F418)
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, 56% coverage: 60:509/802 of query aligns to 41:510/518 of O94788
- E50 (≠ A67) to G: in dbSNP:rs34266719
- A110 (= A124) to V: in dbSNP:rs35365164
- Q182 (= Q186) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (= IPW 188:190) binding
- KPAE 210:213 (= KPAE 214:217) binding
- STE 264:266 (≠ STA 266:268) binding
- C320 (= C321) active site, Nucleophile
- R347 (≠ L348) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ R349) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ VQLTT 367:371) binding
- A383 (≠ G382) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E416) binding
- E436 (= E435) to K: in dbSNP:rs34744827
- S461 (≠ A460) 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, 56% coverage: 60:509/802 of query aligns to 15:484/492 of 6b5hA
- active site: N161 (= N191), E260 (= E287), C294 (= C321), E468 (= E493)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ I152), G116 (≠ L156), F162 (= F192), W169 (= W199), Q284 (≠ D311), F288 (= F315), T295 (≠ C322), N449 (= N474), L451 (≠ F476), N452 (≠ D477), F457 (= F482)
- binding nicotinamide-adenine-dinucleotide: I157 (= I187), I158 (= I188), W160 (= W190), N161 (= N191), K184 (= K214), G217 (= G247), G221 (≠ E251), F235 (= F263), T236 (= T264), G237 (= G265), S238 (= S266), V241 (= V269), E260 (= E287), L261 (= L288), C294 (= C321), F393 (= F418)
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, 56% coverage: 60:509/802 of query aligns to 15:484/492 of 6b5gA
- active site: N161 (= N191), E260 (= E287), C294 (= C321), E468 (= E493)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F192), L165 (= L195), W169 (= W199), F288 (= F315), C293 (≠ V320), C294 (= C321), T295 (≠ C322), N449 (= N474), L451 (≠ F476)
- binding nicotinamide-adenine-dinucleotide: I157 (= I187), I158 (= I188), P159 (= P189), W160 (= W190), N161 (= N191), M166 (= M196), K184 (= K214), E187 (= E217), G217 (= G247), G221 (≠ E251), F235 (= F263), T236 (= T264), G237 (= G265), S238 (= S266), V241 (= V269), E260 (= E287), L261 (= L288), C294 (= C321), E391 (= E416), F393 (= F418)
Query Sequence
>GFF3227 PGA1_c32800 aldehyde dehydrogenase
MCVRPGRFPDSGQTATDHKARHMTLTVKEIFETMDYGPAPESAADALAWLVDQGARFGHF
INGEFTAPGDGFDSKNPATGEVLATLSQATQSDVDSAVDAARKAQTKWSAAGGAARARYL
YAIARLMQKHARLFAVLETLDNGKPIRESRDIDVPLAQRHFYYHAGMAQLMESELPDREA
LGVCGQIIPWNFPLLMLAWKVAPAIAMGNTVVLKPAEYTSLTALLFADICRQAGLPKGVV
NIVTGDGAVGEMIVGADVDKIAFTGSTAVGRRIREATAGSGKALTLELGGKSPYIVFDDA
DIDSAIEGLVDAIWFNQGQVCCAGSRLLVQEGIAERFHTKLRVRMDKLRIGNPLDKSIDV
GAIVDPVQLTTISEMVAANTAGRMHQAQVAVPERGCFYPPTLIEGLAPSDALMQEEIFGP
VLVSTTFRTPSEAVELANNTRYGLAATLWTENVNLALDIAPKLVAGVVWVNATNLFDAAA
GFGGTRESGFGREGGWEGLSAYTKPKGKTKALEKVTGFSGDGAPVDAVDRTAKFYVGGKQ
TRPDGGYSKAIHSKSGGLLGHVGLGNRKDVRNAVEAAAGANAWSKTTGHLRAQILYYIGE
NLSARVGEFADRIDRMTGKSQGAQEVEASIQRLFTAAAWADKYDGQAHGVPIRGVALAMK
EPVGVIGALCADEAPLLGLVSVMAPAIAMGNRVVLAASEAYPLSATDFYQVLETSDLPGG
VVNILTGRHAEMASPLASHLNVDAVWSFSSSDLSAMIEEASAGNLKRTWVNNGLAMDWSA
DHSRRFLEAATEVKNIWIPYGE
Or try a new SitesBLAST search
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