SitesBLAST
Comparing BWI76_RS12820 BWI76_RS12820 NAD-dependent phenylacetaldehyde 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)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 99% coverage: 4:498/499 of query aligns to 1:489/491 of 5gtlA
- active site: N165 (= N174), K188 (= K197), E263 (= E272), C297 (= C306), E394 (= E403), E471 (≠ D480)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I170), P163 (= P172), K188 (= K197), A190 (≠ S199), E191 (= E200), Q192 (≠ T201), G221 (= G230), G225 (= G234), G241 (= G250), S242 (= S251), T245 (= T254), L264 (= L273), C297 (= C306), E394 (= E403), F396 (= F405)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 99% coverage: 4:498/499 of query aligns to 1:489/491 of 5gtkA
- active site: N165 (= N174), K188 (= K197), E263 (= E272), C297 (= C306), E394 (= E403), E471 (≠ D480)
- binding nicotinamide-adenine-dinucleotide: I161 (= I170), I162 (≠ V171), P163 (= P172), W164 (= W173), K188 (= K197), E191 (= E200), G221 (= G230), G225 (= G234), A226 (= A235), F239 (= F248), G241 (= G250), S242 (= S251), T245 (= T254), Y248 (≠ Q257), L264 (= L273), C297 (= C306), Q344 (≠ H353), R347 (≠ K356), E394 (= E403), F396 (= F405)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
42% identity, 95% coverage: 22:495/499 of query aligns to 13:484/494 of 4pz2B
- active site: N159 (= N174), K182 (= K197), E258 (= E272), C292 (= C306), E392 (= E403), D469 (= D480)
- binding nicotinamide-adenine-dinucleotide: I155 (= I170), I156 (≠ V171), P157 (= P172), W158 (= W173), N159 (= N174), M164 (≠ I179), K182 (= K197), A184 (≠ S199), E185 (= E200), G215 (= G230), G219 (= G234), F233 (= F248), T234 (= T249), G235 (= G250), S236 (= S251), V239 (≠ T254), E258 (= E272), L259 (= L273), C292 (= C306), E392 (= E403), F394 (= F405)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
41% identity, 96% coverage: 19:497/499 of query aligns to 3:477/489 of 4o6rA
- active site: N150 (= N174), K173 (= K197), E248 (= E272), C282 (= C306), E383 (= E403), E460 (≠ D480)
- binding adenosine monophosphate: I146 (= I170), V147 (= V171), K173 (= K197), G206 (= G230), G210 (= G234), Q211 (≠ A235), F224 (= F248), G226 (= G250), S227 (= S251), T230 (= T254), R233 (≠ Q257)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 96% coverage: 18:496/499 of query aligns to 4:477/486 of 4pxlA
- active site: N154 (= N174), K177 (= K197), E253 (= E272), C287 (= C306), E384 (= E403), D461 (= D480)
- binding nicotinamide-adenine-dinucleotide: I150 (= I170), V151 (= V171), P152 (= P172), W153 (= W173), K177 (= K197), E180 (= E200), G210 (= G230), G214 (= G234), A215 (= A235), F228 (= F248), G230 (= G250), S231 (= S251), V234 (≠ T254), E253 (= E272), G255 (= G274), C287 (= C306), Q334 (≠ H353), K337 (= K356), E384 (= E403), F386 (= F405)
7radA Crystal structure analysis of aldh1b1
40% identity, 96% coverage: 22:498/499 of query aligns to 15:487/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I170), I159 (≠ V171), P160 (= P172), W161 (= W173), N162 (= N174), M167 (≠ I179), K185 (= K197), E188 (= E200), G218 (= G230), G222 (= G234), A223 (= A235), T237 (= T249), G238 (= G250), S239 (= S251), V242 (≠ T254), E261 (= E272), L262 (= L273), C295 (= C306), E392 (= E403), F394 (= F405)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ F119), E117 (≠ C123), F163 (= F175), E285 (≠ T296), F289 (≠ L300), N450 (≠ T461), V452 (≠ I463)
7mjdA Crystal structure analysis of aldh1b1
40% identity, 96% coverage: 22:498/499 of query aligns to 15:487/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I170), I159 (≠ V171), P160 (= P172), W161 (= W173), N162 (= N174), M167 (≠ I179), K185 (= K197), E188 (= E200), G218 (= G230), G222 (= G234), F236 (= F248), T237 (= T249), G238 (= G250), S239 (= S251), V242 (≠ T254), E261 (= E272), L262 (= L273), C295 (= C306), E392 (= E403), F394 (= F405)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ C123), E285 (≠ T296), F289 (≠ L300), N450 (≠ T461), V452 (≠ I463)
7mjcA Crystal structure analysis of aldh1b1
40% identity, 96% coverage: 22:498/499 of query aligns to 15:487/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I170), I159 (≠ V171), P160 (= P172), W161 (= W173), N162 (= N174), K185 (= K197), E188 (= E200), G218 (= G230), G222 (= G234), T237 (= T249), G238 (= G250), S239 (= S251), V242 (≠ T254), E261 (= E272), L262 (= L273), C295 (= C306), E392 (= E403), F394 (= F405)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
41% identity, 96% coverage: 22:498/499 of query aligns to 42:514/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
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)
38% identity, 99% coverage: 4:495/499 of query aligns to 8:491/505 of 4neaA
- active site: N166 (= N174), K189 (= K197), E264 (= E272), C298 (= C306), E399 (= E403), E476 (≠ D480)
- binding nicotinamide-adenine-dinucleotide: P164 (= P172), K189 (= K197), E192 (= E200), G222 (= G230), G226 (= G234), G242 (= G250), G243 (≠ S251), T246 (= T254), H249 (≠ Q257), I250 (= I258), C298 (= C306), E399 (= E403), F401 (= F405)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
40% identity, 96% coverage: 22:498/499 of query aligns to 16:488/494 of 5l13A
- active site: N163 (= N174), K186 (= K197), E262 (= E272), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F175), M168 (≠ I179), W171 (= W182), F290 (≠ L300), C295 (≠ V305), C296 (= C306), C297 (≠ A307), D451 (≠ T461), F453 (≠ I463)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
40% identity, 96% coverage: 22:498/499 of query aligns to 16:488/494 of 4kwgA
- active site: N163 (= N174), K186 (= K197), E262 (= E272), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F175), M168 (≠ I179), C295 (≠ V305), C296 (= C306), C297 (≠ A307), D451 (≠ T461), F453 (≠ I463)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
40% identity, 96% coverage: 22:498/499 of query aligns to 16:488/494 of 4kwfA
- active site: N163 (= N174), K186 (= K197), E262 (= E272), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F175), M168 (≠ I179), W171 (= W182), E262 (= E272), C295 (≠ V305), C296 (= C306), C297 (≠ A307), D451 (≠ T461), F453 (≠ I463), F459 (= F469)
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)
40% identity, 96% coverage: 22:498/499 of query aligns to 16:488/494 of 3sz9A
- active site: N163 (= N174), K186 (= K197), E262 (= E272), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F175), C295 (≠ V305), C296 (= C306), D451 (≠ T461), F453 (≠ I463), F459 (= F469)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
40% identity, 96% coverage: 22:498/499 of query aligns to 16:488/494 of 3injA
- active site: N163 (= N174), K186 (= K197), E262 (= E272), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ C123), F164 (= F175), L167 (≠ M178), F286 (≠ T296), F290 (≠ L300), D451 (≠ T461), F453 (≠ I463)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
40% identity, 96% coverage: 22:498/499 of query aligns to 16:488/494 of 2vleA
- active site: N163 (= N174), K186 (= K197), E262 (= E272), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding daidzin: M118 (≠ C123), F164 (= F175), M168 (≠ I179), W171 (= W182), F286 (≠ T296), F290 (≠ L300), C295 (≠ V305), C296 (= C306), D451 (≠ T461), V452 (≠ L462), F453 (≠ I463)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
40% identity, 96% coverage: 22:498/499 of query aligns to 16:488/494 of 1o01B
- active site: N163 (= N174), K186 (= K197), E262 (= E272), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding (2e)-but-2-enal: C296 (= C306), C297 (≠ A307), F453 (≠ I463)
- binding nicotinamide-adenine-dinucleotide: I159 (= I170), I160 (≠ V171), P161 (= P172), W162 (= W173), K186 (= K197), E189 (= E200), G219 (= G230), G223 (= G234), A224 (= A235), F237 (= F248), G239 (= G250), S240 (= S251), I243 (≠ T254), L263 (= L273), G264 (= G274), C296 (= C306), Q343 (≠ H353), E393 (= E403), F395 (= F405)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
40% identity, 96% coverage: 22:498/499 of query aligns to 16:488/494 of 1cw3A
- active site: N163 (= N174), K186 (= K197), E262 (= E272), C296 (= C306), E393 (= E403), E470 (≠ D480)
- binding magnesium ion: V34 (≠ W40), D103 (≠ E108), Q190 (≠ T201)
- binding nicotinamide-adenine-dinucleotide: I159 (= I170), I160 (≠ V171), P161 (= P172), W162 (= W173), K186 (= K197), G219 (= G230), G223 (= G234), A224 (= A235), F237 (= F248), G239 (= G250), S240 (= S251), I243 (≠ T254), L263 (= L273), G264 (= G274), C296 (= C306), Q343 (≠ H353), K346 (= K356), E393 (= E403), F395 (= F405)
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
38% identity, 96% coverage: 22:498/499 of query aligns to 14:486/492 of 6b5hA
- active site: N161 (= N174), E260 (= E272), C294 (= C306), E468 (≠ D480)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ F119), G116 (≠ C123), F162 (= F175), W169 (= W182), Q284 (≠ T296), F288 (≠ L300), T295 (≠ A307), N449 (≠ T461), L451 (≠ I463), N452 (≠ D464), F457 (= F469)
- binding nicotinamide-adenine-dinucleotide: I157 (= I170), I158 (≠ V171), W160 (= W173), N161 (= N174), K184 (= K197), G217 (= G230), G221 (= G234), F235 (= F248), T236 (= T249), G237 (= G250), S238 (= S251), V241 (≠ T254), E260 (= E272), L261 (= L273), C294 (= C306), F393 (= F405)
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)
38% identity, 96% coverage: 22:498/499 of query aligns to 14:486/492 of 6b5gA
- active site: N161 (= N174), E260 (= E272), C294 (= C306), E468 (≠ D480)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F175), L165 (≠ M178), W169 (= W182), F288 (≠ L300), C293 (≠ V305), C294 (= C306), T295 (≠ A307), N449 (≠ T461), L451 (≠ I463)
- binding nicotinamide-adenine-dinucleotide: I157 (= I170), I158 (≠ V171), P159 (= P172), W160 (= W173), N161 (= N174), M166 (≠ I179), K184 (= K197), E187 (= E200), G217 (= G230), G221 (= G234), F235 (= F248), T236 (= T249), G237 (= G250), S238 (= S251), V241 (≠ T254), E260 (= E272), L261 (= L273), C294 (= C306), E391 (= E403), F393 (= F405)
Query Sequence
>BWI76_RS12820 BWI76_RS12820 NAD-dependent phenylacetaldehyde dehydrogenase
MSTSQVALLASVQQFLDRQHGLYLDGTQQAAESEQRLTVWNPATGQAIASTADANAADVD
RAVMSAWRAFVSRSWAGRTPADRERILLRFADLVEQHGEELAQLETLEQGKSINISRAFE
VGCTLNWMRYTAGLTTKISGRTLDVSIPFPAGGRYQAWTKKEPVGVVAGIVPWNFPLMIG
MWKVMPALAAGCSIVIKPSETTPLTLLRVAELATEAGVPDGVFNVVTGSGAGCGAALTSH
PLVAKVSFTGSTATGKQIARVAADRLTRVTLELGGKNPAIVLKDADPQWVIEGLMTGSFL
NQGQVCAASSRIYIEAPLFDTLVSGFEQAVKSLQVGPGMLESSQINPVVSQAHCAKVAAY
LDEARQQKAELISGHAGPDAQGYYIAPTLVINPDAGLRLCREEVFGPVVNLVRVADGEEA
LLLANDSDFGLTASVWTRDLTQALSYTDRLQAGTVWVNSHTLIDANLPFGGMKQSGTGRD
FGPDWLDDWCETKSVCVRY
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