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Comparing WP_011385953.1 AMB_RS18195 DUF1487 domain-containing protein 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)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 100% coverage: 1:496/496 of query aligns to 3:491/491 of 5gtlA
- active site: N165 (= N164), K188 (= K187), E263 (= E261), C297 (= C296), E394 (= E398), E471 (= E475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I160), P163 (= P162), K188 (= K187), A190 (= A189), E191 (= E190), Q192 (≠ E191), G221 (= G219), G225 (= G223), G241 (= G239), S242 (= S240), T245 (= T243), L264 (= L262), C297 (= C296), E394 (= E398), F396 (= F400)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 100% coverage: 1:496/496 of query aligns to 3:491/491 of 5gtkA
- active site: N165 (= N164), K188 (= K187), E263 (= E261), C297 (= C296), E394 (= E398), E471 (= E475)
- binding nicotinamide-adenine-dinucleotide: I161 (= I160), I162 (= I161), P163 (= P162), W164 (= W163), K188 (= K187), E191 (= E190), G221 (= G219), G225 (= G223), A226 (= A224), F239 (= F237), G241 (= G239), S242 (= S240), T245 (= T243), Y248 (≠ I246), L264 (= L262), C297 (= C296), Q344 (= Q343), R347 (= R346), E394 (= E398), F396 (= F400)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
39% identity, 96% coverage: 21:495/496 of query aligns to 7:479/489 of 4o6rA
- active site: N150 (= N164), K173 (= K187), E248 (= E261), C282 (= C296), E383 (= E398), E460 (= E475)
- binding adenosine monophosphate: I146 (= I160), V147 (≠ I161), K173 (= K187), G206 (= G219), G210 (= G223), Q211 (≠ A224), F224 (= F237), G226 (= G239), S227 (= S240), T230 (= T243), R233 (≠ I246)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
39% identity, 96% coverage: 20:496/496 of query aligns to 29:506/515 of 2d4eC
- active site: N173 (= N164), K196 (= K187), E271 (= E261), C305 (= C296), E409 (= E398), E486 (= E475)
- binding nicotinamide-adenine-dinucleotide: I169 (= I160), T170 (≠ I161), P171 (= P162), W172 (= W163), K196 (= K187), A198 (= A189), G229 (= G219), G233 (= G223), A234 (= A224), T248 (= T238), G249 (= G239), E250 (≠ S240), T253 (= T243), E271 (= E261), L272 (= L262), C305 (= C296), E409 (= E398), F411 (= F400), F475 (≠ Y464)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
39% identity, 95% coverage: 19:491/496 of query aligns to 12:485/494 of 4pz2B
- active site: N159 (= N164), K182 (= K187), E258 (= E261), C292 (= C296), E392 (= E398), D469 (≠ E475)
- binding nicotinamide-adenine-dinucleotide: I155 (= I160), I156 (= I161), P157 (= P162), W158 (= W163), N159 (= N164), M164 (≠ L169), K182 (= K187), A184 (= A189), E185 (= E190), G215 (= G219), G219 (= G223), F233 (= F237), T234 (= T238), G235 (= G239), S236 (= S240), V239 (≠ T243), E258 (= E261), L259 (= L262), C292 (= C296), E392 (= E398), F394 (= F400)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
39% identity, 97% coverage: 9:491/496 of query aligns to 4:484/493 of 4fr8A
- active site: N162 (= N164), K185 (= K187), Q261 (≠ E261), C295 (= C296), E392 (= E398), E469 (= E475)
- binding nicotinamide-adenine-dinucleotide: I158 (= I160), I159 (= I161), W161 (= W163), K185 (= K187), G218 (= G219), G222 (= G223), A223 (= A224), F236 (= F237), G238 (= G239), S239 (= S240), I242 (≠ T243), Q342 (= Q343), K345 (≠ R346), E392 (= E398), F394 (= F400)
- binding propane-1,2,3-triyl trinitrate: F163 (≠ V165), L166 (= L168), W170 (≠ M172), F289 (≠ T290), S294 (= S295), C295 (= C296), D450 (≠ L456), F452 (≠ V458)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
39% identity, 97% coverage: 9:491/496 of query aligns to 7:487/496 of 4fr8C
- active site: N165 (= N164), K188 (= K187), Q264 (≠ E261), C298 (= C296), E395 (= E398), E472 (= E475)
- binding nicotinamide-adenine-dinucleotide: I161 (= I160), I162 (= I161), W164 (= W163), K188 (= K187), G221 (= G219), G225 (= G223), A226 (= A224), F239 (= F237), G241 (= G239), S242 (= S240), I245 (≠ T243), Q345 (= Q343), E395 (= E398), F397 (= F400)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
39% identity, 97% coverage: 12:491/496 of query aligns to 1:479/490 of Q9HTJ1
- GAWN 150:153 (≠ IPWN 161:164) binding
- K162 (= K173) active site, Charge relay system
- KPSE 176:179 (≠ KSAE 187:190) binding
- G209 (= G219) binding
- GTST 230:233 (≠ SVET 240:243) binding
- E252 (= E261) active site, Proton acceptor
- C286 (= C296) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E398) binding
- E464 (= E475) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
39% identity, 95% coverage: 19:491/496 of query aligns to 7:478/489 of 4cazA
- active site: N152 (= N164), K175 (= K187), E251 (= E261), C285 (= C296), E386 (= E398), E463 (= E475)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (= I160), G149 (≠ I161), W151 (= W163), N152 (= N164), K175 (= K187), E178 (= E190), G208 (= G219), G212 (= G223), F226 (= F237), T227 (= T238), G228 (= G239), G229 (≠ S240), T232 (= T243), V236 (≠ I246), E251 (= E261), L252 (= L262), C285 (= C296), E386 (= E398), F388 (= F400)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
39% identity, 95% coverage: 19:491/496 of query aligns to 7:478/489 of 2woxA
- active site: N152 (= N164), K175 (= K187), E251 (= E261), C285 (= C296), E386 (= E398), E463 (= E475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I160), G149 (≠ I161), W151 (= W163), N152 (= N164), K175 (= K187), S177 (≠ A189), E178 (= E190), G208 (= G219), G212 (= G223), F226 (= F237), T227 (= T238), G228 (= G239), G229 (≠ S240), T232 (= T243), V236 (≠ I246), E251 (= E261), L252 (= L262), C285 (= C296), E386 (= E398), F388 (= F400)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
39% identity, 95% coverage: 19:491/496 of query aligns to 7:478/489 of 2wmeA
- active site: N152 (= N164), K175 (= K187), E251 (= E261), C285 (= C296), E386 (= E398), E463 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ I161), W151 (= W163), K175 (= K187), S177 (≠ A189), E178 (= E190), G208 (= G219), G212 (= G223), F226 (= F237), G228 (= G239), G229 (≠ S240), T232 (= T243), V236 (≠ I246)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
39% identity, 97% coverage: 9:491/496 of query aligns to 5:485/494 of 5l13A
- active site: N163 (= N164), K186 (= K187), E262 (= E261), C296 (= C296), E393 (= E398), E470 (= E475)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (≠ V165), M168 (≠ L169), W171 (≠ M172), F290 (≠ T290), C295 (≠ S295), C296 (= C296), C297 (≠ T297), D451 (≠ L456), F453 (≠ V458)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
39% identity, 97% coverage: 9:491/496 of query aligns to 5:485/494 of 4kwgA
- active site: N163 (= N164), K186 (= K187), E262 (= E261), C296 (= C296), E393 (= E398), E470 (= E475)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (≠ V165), M168 (≠ L169), C295 (≠ S295), C296 (= C296), C297 (≠ T297), D451 (≠ L456), F453 (≠ V458)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
39% identity, 97% coverage: 9:491/496 of query aligns to 5:485/494 of 4kwfA
- active site: N163 (= N164), K186 (= K187), E262 (= E261), C296 (= C296), E393 (= E398), E470 (= E475)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (≠ V165), M168 (≠ L169), W171 (≠ M172), E262 (= E261), C295 (≠ S295), C296 (= C296), C297 (≠ T297), D451 (≠ L456), F453 (≠ V458), F459 (≠ Y464)
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)
39% identity, 97% coverage: 9:491/496 of query aligns to 5:485/494 of 3sz9A
- active site: N163 (= N164), K186 (= K187), E262 (= E261), C296 (= C296), E393 (= E398), E470 (= E475)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (≠ V165), C295 (≠ S295), C296 (= C296), D451 (≠ L456), F453 (≠ V458), F459 (≠ Y464)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
39% identity, 97% coverage: 9:491/496 of query aligns to 5:485/494 of 3injA
- active site: N163 (= N164), K186 (= K187), E262 (= E261), C296 (= C296), E393 (= E398), E470 (= E475)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ V119), F164 (≠ V165), L167 (= L168), F286 (≠ A285), F290 (≠ T290), D451 (≠ L456), F453 (≠ V458)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
39% identity, 97% coverage: 9:491/496 of query aligns to 5:485/494 of 2vleA
- active site: N163 (= N164), K186 (= K187), E262 (= E261), C296 (= C296), E393 (= E398), E470 (= E475)
- binding daidzin: M118 (≠ V119), F164 (≠ V165), M168 (≠ L169), W171 (≠ M172), F286 (≠ A285), F290 (≠ T290), C295 (≠ S295), C296 (= C296), D451 (≠ L456), V452 (= V457), F453 (≠ V458)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
39% identity, 97% coverage: 9:491/496 of query aligns to 5:485/494 of 1o01B
- active site: N163 (= N164), K186 (= K187), E262 (= E261), C296 (= C296), E393 (= E398), E470 (= E475)
- binding (2e)-but-2-enal: C296 (= C296), C297 (≠ T297), F453 (≠ V458)
- binding nicotinamide-adenine-dinucleotide: I159 (= I160), I160 (= I161), P161 (= P162), W162 (= W163), K186 (= K187), E189 (= E190), G219 (= G219), G223 (= G223), A224 (= A224), F237 (= F237), G239 (= G239), S240 (= S240), I243 (≠ T243), L263 (= L262), G264 (= G263), C296 (= C296), Q343 (= Q343), E393 (= E398), F395 (= F400)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
39% identity, 97% coverage: 9:491/496 of query aligns to 5:485/494 of 1cw3A
- active site: N163 (= N164), K186 (= K187), E262 (= E261), C296 (= C296), E393 (= E398), E470 (= E475)
- binding magnesium ion: V34 (≠ D38), D103 (≠ E104), Q190 (≠ E191)
- binding nicotinamide-adenine-dinucleotide: I159 (= I160), I160 (= I161), P161 (= P162), W162 (= W163), K186 (= K187), G219 (= G219), G223 (= G223), A224 (= A224), F237 (= F237), G239 (= G239), S240 (= S240), I243 (≠ T243), L263 (= L262), G264 (= G263), C296 (= C296), Q343 (= Q343), K346 (≠ R346), E393 (= E398), F395 (= F400)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
39% identity, 96% coverage: 19:492/496 of query aligns to 7:477/486 of 4pxlA
- active site: N154 (= N164), K177 (= K187), E253 (= E261), C287 (= C296), E384 (= E398), D461 (≠ E475)
- binding nicotinamide-adenine-dinucleotide: I150 (= I160), V151 (≠ I161), P152 (= P162), W153 (= W163), K177 (= K187), E180 (= E190), G210 (= G219), G214 (= G223), A215 (= A224), F228 (= F237), G230 (= G239), S231 (= S240), V234 (≠ T243), E253 (= E261), G255 (= G263), C287 (= C296), Q334 (= Q343), K337 (≠ R346), E384 (= E398), F386 (= F400)
Query Sequence
>WP_011385953.1 AMB_RS18195 DUF1487 domain-containing protein
MTLTPELDPFKLAKALSGKHLIGGKLVPAGCGEVFEVDNPATGEIIGTAAFGTKEDVDIA
VISAKAAQKDWAKQSARARGKLVAECGRVLSAHVEELGRLVALETGKALRTESRVEAGVL
ADMFTFFGGLGSELKGETIPFNPDMLTVTVREPVGVVGCIIPWNVPLLLMAMKAAAALVA
GNSVVVKSAEEAPLTVLRVAEIMNTVLPPGLFNMLSGFGPECGAPLVEHPDVKKVTFTGS
VETGRIVYKAAAEKLIPVTLELGGKSPMIVCADADMDQAVAGALAGMRFTRQGQSCTASS
RLFVHESIHDEFVAKVKAKVDAMVMGDPLDEKTDIGTIVSDGQLERVRSYIKIGEETKGA
TKHVCSALPTDPKLAKGRFVQPVIFTGMKNSDRLCQEEIFGPVCAVIKWSDYEDVLAQAN
DSEYGLAASIWTRDFKLAMDATKRLEAGFVQVNQNLVVQPGLSYGGVKTSGIGKEASLES
MLEHFTHKKTIIFNMK
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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