SitesBLAST
Comparing RR42_RS13660 FitnessBrowser__Cup4G11:RR42_RS13660 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)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
42% identity, 92% coverage: 27:478/490 of query aligns to 26:476/489 of 4o6rA
- active site: N150 (= N152), K173 (= K175), E248 (= E250), C282 (= C284), E383 (= E385), E460 (= E462)
- binding adenosine monophosphate: I146 (= I148), V147 (≠ T149), K173 (= K175), G206 (= G208), G210 (= G212), Q211 (≠ D213), F224 (= F226), G226 (= G228), S227 (≠ G229), T230 (= T232), R233 (≠ H235)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 94% coverage: 18:478/490 of query aligns to 30:487/491 of 5gtlA
- active site: N165 (= N152), K188 (= K175), E263 (= E250), C297 (= C284), E394 (= E385), E471 (= E462)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I148), P163 (= P150), K188 (= K175), A190 (= A177), E191 (= E178), Q192 (≠ I179), G221 (= G208), G225 (= G212), G241 (= G228), S242 (≠ G229), T245 (= T232), L264 (= L251), C297 (= C284), E394 (= E385), F396 (= F387)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 94% coverage: 18:478/490 of query aligns to 30:487/491 of 5gtkA
- active site: N165 (= N152), K188 (= K175), E263 (= E250), C297 (= C284), E394 (= E385), E471 (= E462)
- binding nicotinamide-adenine-dinucleotide: I161 (= I148), I162 (≠ T149), P163 (= P150), W164 (= W151), K188 (= K175), E191 (= E178), G221 (= G208), G225 (= G212), A226 (≠ D213), F239 (= F226), G241 (= G228), S242 (≠ G229), T245 (= T232), Y248 (≠ H235), L264 (= L251), C297 (= C284), Q344 (≠ H331), R347 (≠ S334), E394 (= E385), F396 (= F387)
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)
41% identity, 94% coverage: 19:477/490 of query aligns to 21:479/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 149:152) binding
- K162 (= K161) active site, Charge relay system
- KPSE 176:179 (≠ KPAE 175:178) binding
- G209 (= G208) binding
- GTST 230:233 (≠ GTTT 229:232) binding
- E252 (= E250) active site, Proton acceptor
- C286 (= C284) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E385) binding
- E464 (= E462) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
41% identity, 94% coverage: 19:477/490 of query aligns to 20:478/489 of 4cazA
- active site: N152 (= N152), K175 (= K175), E251 (= E250), C285 (= C284), E386 (= E385), E463 (= E462)
- 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 (= I148), G149 (≠ T149), W151 (= W151), N152 (= N152), K175 (= K175), E178 (= E178), G208 (= G208), G212 (= G212), F226 (= F226), T227 (= T227), G228 (= G228), G229 (= G229), T232 (= T232), V236 (≠ I236), E251 (= E250), L252 (= L251), C285 (= C284), E386 (= E385), F388 (= F387)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
41% identity, 94% coverage: 19:477/490 of query aligns to 20:478/489 of 2woxA
- active site: N152 (= N152), K175 (= K175), E251 (= E250), C285 (= C284), E386 (= E385), E463 (= E462)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I148), G149 (≠ T149), W151 (= W151), N152 (= N152), K175 (= K175), S177 (≠ A177), E178 (= E178), G208 (= G208), G212 (= G212), F226 (= F226), T227 (= T227), G228 (= G228), G229 (= G229), T232 (= T232), V236 (≠ I236), E251 (= E250), L252 (= L251), C285 (= C284), E386 (= E385), F388 (= F387)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
41% identity, 94% coverage: 19:477/490 of query aligns to 20:478/489 of 2wmeA
- active site: N152 (= N152), K175 (= K175), E251 (= E250), C285 (= C284), E386 (= E385), E463 (= E462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T149), W151 (= W151), K175 (= K175), S177 (≠ A177), E178 (= E178), G208 (= G208), G212 (= G212), F226 (= F226), G228 (= G228), G229 (= G229), T232 (= T232), V236 (≠ I236)
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, 94% coverage: 27:488/490 of query aligns to 40:502/505 of 4neaA
- active site: N166 (= N152), K189 (= K175), E264 (= E250), C298 (= C284), E399 (= E385), E476 (= E462)
- binding nicotinamide-adenine-dinucleotide: P164 (= P150), K189 (= K175), E192 (= E178), G222 (= G208), G226 (= G212), G242 (= G228), G243 (= G229), T246 (= T232), H249 (= H235), I250 (= I236), C298 (= C284), E399 (= E385), F401 (= F387)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
40% identity, 94% coverage: 27:487/490 of query aligns to 25:483/487 of 4go4A
- active site: N149 (= N152), K172 (= K175), E247 (= E250), C281 (= C284), E381 (= E385), E458 (= E462)
- binding nicotinamide-adenine-dinucleotide: I145 (= I148), V146 (≠ T149), W148 (= W151), N149 (= N152), F154 (≠ S157), K172 (= K175), G205 (= G208), G209 (= G212), Q210 (≠ D213), F223 (= F226), T224 (= T227), G225 (= G228), S226 (≠ G229), T229 (= T232), E247 (= E250), G249 (= G252), C281 (= C284), E381 (= E385), F383 (= F387)
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, 96% coverage: 8:477/490 of query aligns to 40:509/518 of O94788
- E50 (vs. gap) to G: in dbSNP:rs34266719
- A110 (= A76) to V: in dbSNP:rs35365164
- Q182 (≠ A147) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPW 149:151) binding
- KPAE 210:213 (= KPAE 175:178) binding
- STE 264:266 (≠ GTT 229:231) binding
- C320 (= C284) active site, Nucleophile
- R347 (≠ L311) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ R312) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ RHRDS 330:334) binding
- A383 (≠ G347) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E385) binding
- E436 (≠ A404) to K: in dbSNP:rs34744827
- S461 (≠ A429) 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, 96% coverage: 8:477/490 of query aligns to 14:483/492 of 6b5hA
- active site: N161 (= N152), E260 (= E250), C294 (= C284), E468 (= E462)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ L104), G116 (≠ S107), F162 (≠ S153), W169 (≠ Q160), Q284 (≠ Y274), F288 (≠ S278), T295 (≠ I285), N449 (≠ K443), L451 (≠ F445), N452 (≠ S446), F457 (= F451)
- binding nicotinamide-adenine-dinucleotide: I157 (= I148), I158 (≠ T149), W160 (= W151), N161 (= N152), K184 (= K175), G217 (= G208), G221 (= G212), F235 (= F226), T236 (= T227), G237 (= G228), S238 (≠ G229), V241 (≠ T232), E260 (= E250), L261 (= L251), C294 (= C284), F393 (= F387)
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, 96% coverage: 8:477/490 of query aligns to 14:483/492 of 6b5gA
- active site: N161 (= N152), E260 (= E250), C294 (= C284), E468 (= E462)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ S153), L165 (≠ A156), W169 (≠ Q160), F288 (≠ S278), C293 (≠ S283), C294 (= C284), T295 (≠ I285), N449 (≠ K443), L451 (≠ F445)
- binding nicotinamide-adenine-dinucleotide: I157 (= I148), I158 (≠ T149), P159 (= P150), W160 (= W151), N161 (= N152), M166 (≠ S157), K184 (= K175), E187 (= E178), G217 (= G208), G221 (= G212), F235 (= F226), T236 (= T227), G237 (= G228), S238 (≠ G229), V241 (≠ T232), E260 (= E250), L261 (= L251), C294 (= C284), E391 (= E385), F393 (= F387)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
40% identity, 96% coverage: 8:477/490 of query aligns to 14:483/492 of 6aljA
- active site: N161 (= N152), E260 (= E250), C294 (= C284), E468 (= E462)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ S107), F162 (≠ S153), L165 (≠ A156), M166 (≠ S157), W169 (≠ Q160), E260 (= E250), C293 (≠ S283), C294 (= C284), L451 (≠ F445), N452 (≠ S446), A453 (≠ I447)
- binding nicotinamide-adenine-dinucleotide: I157 (= I148), I158 (≠ T149), P159 (= P150), W160 (= W151), N161 (= N152), K184 (= K175), E187 (= E178), G217 (= G208), G221 (= G212), F235 (= F226), G237 (= G228), S238 (≠ G229), V241 (≠ T232), Q341 (≠ H331), K344 (≠ S334), E391 (= E385), F393 (= F387)
7radA Crystal structure analysis of aldh1b1
40% identity, 96% coverage: 8:477/490 of query aligns to 15:484/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I148), I159 (≠ T149), P160 (= P150), W161 (= W151), N162 (= N152), M167 (≠ S157), K185 (= K175), E188 (= E178), G218 (= G208), G222 (= G212), A223 (≠ D213), T237 (= T227), G238 (= G228), S239 (≠ G229), V242 (≠ T232), E261 (= E250), L262 (= L251), C295 (= C284), E392 (= E385), F394 (= F387)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (= L104), E117 (≠ S107), F163 (≠ S153), E285 (≠ Y274), F289 (≠ S278), N450 (≠ K443), V452 (≠ F445)
7mjdA Crystal structure analysis of aldh1b1
40% identity, 96% coverage: 8:477/490 of query aligns to 15:484/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I148), I159 (≠ T149), P160 (= P150), W161 (= W151), N162 (= N152), M167 (≠ S157), K185 (= K175), E188 (= E178), G218 (= G208), G222 (= G212), F236 (= F226), T237 (= T227), G238 (= G228), S239 (≠ G229), V242 (≠ T232), E261 (= E250), L262 (= L251), C295 (= C284), E392 (= E385), F394 (= F387)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ S107), E285 (≠ Y274), F289 (≠ S278), N450 (≠ K443), V452 (≠ F445)
7mjcA Crystal structure analysis of aldh1b1
40% identity, 96% coverage: 8:477/490 of query aligns to 15:484/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I148), I159 (≠ T149), P160 (= P150), W161 (= W151), N162 (= N152), K185 (= K175), E188 (= E178), G218 (= G208), G222 (= G212), T237 (= T227), G238 (= G228), S239 (≠ G229), V242 (≠ T232), E261 (= E250), L262 (= L251), C295 (= C284), E392 (= E385), F394 (= F387)
Q63639 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 Rattus norvegicus (Rat) (see paper)
40% identity, 96% coverage: 8:477/490 of query aligns to 40:509/518 of Q63639
8skfA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (lattice translocation disorder)
40% identity, 94% coverage: 19:477/490 of query aligns to 28:486/497 of 8skfA
- binding calcium ion: T33 (= T24), I34 (≠ R25), D100 (= D93), V187 (≠ I179)
- binding nicotinamide-adenine-dinucleotide: I156 (= I148), G157 (≠ T149), A158 (≠ P150), W159 (= W151), K183 (= K175), E186 (= E178), G216 (= G208), G220 (= G212), T235 (= T227), G236 (= G228), G237 (= G229), S240 (≠ T232), K243 (≠ H235), E259 (= E250), C293 (= C284), F396 (= F387)
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
40% identity, 94% coverage: 19:477/490 of query aligns to 19:477/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
40% identity, 94% coverage: 19:477/490 of query aligns to 19:477/488 of 8vr0A
Query Sequence
>RR42_RS13660 FitnessBrowser__Cup4G11:RR42_RS13660
MKQEILPICIAGQWRLGGGERYATRYPATGEVVAELNAASLDDVEEAVQGAHRAFLTSGW
AQRKPHERAAVLHRVADLIRARAEPLAQRQRLDNGKPISETRALVASAAGTFQFFAAACE
TLEEALTPARGDFLTMSVHEAMGVVAAITPWNSPIASEAQKLAPALAAGNAVVIKPAEIT
PLMALELAAICEEAGVPKGLISVLPGKGSVIGDAITKHPLVRRVSFTGGTTTGRHIAHIA
ADKMMPVSLELGGKSPTMVFDDADLDHAVNGVLYGIFSSSGESCIAGSRLFVARSLYEPF
MDRLAEGAARLRVGDPADERTQMGPLISDRHRDSIESYVALGVSEGGQLRTGGIRPAVAG
CENGYFYTPTIIEGLDNSARVCQEEIFGPVLVAMAFDDEDDLIAQANDSVYALAAGVWTR
DYKRAWRFARAVQAGNVWINTYKQFSISTPFGGWRDSGLGREKGRLGILQYMEQKSVYWG
MHEQPLPWAN
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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