SitesBLAST
Comparing 15565 b1444 medium chain aldehyde dehydrogenase (NCBI) 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)
P77674 Gamma-aminobutyraldehyde dehydrogenase; ABALDH; 1-pyrroline dehydrogenase; 4-aminobutanal dehydrogenase; 5-aminopentanal dehydrogenase; EC 1.2.1.19; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
100% identity, 100% coverage: 1:474/474 of query aligns to 1:474/474 of P77674
1wndA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal structure (see paper)
100% identity, 100% coverage: 1:474/474 of query aligns to 1:474/474 of 1wndA
- active site: N149 (= N149), K172 (= K172), E246 (= E246), C280 (= C280), E378 (= E378), D455 (= D455)
- binding calcium ion: G249 (= G249), K250 (= K250), A251 (= A251), G405 (= G405), L406 (= L406), A407 (= A407), Y427 (= Y427)
1wnbB Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
100% identity, 100% coverage: 1:474/474 of query aligns to 1:474/474 of 1wnbB
- active site: N149 (= N149), K172 (= K172), E246 (= E246), C280 (= C280), E378 (= E378), D455 (= D455)
- binding betaine aldehyde: D279 (= D279), F436 (= F436), L438 (= L438)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (= I145), A146 (= A146), W148 (= W148), K172 (= K172), G204 (= G204), G208 (= G208), D209 (= D209), T223 (= T223), G224 (= G224), S225 (= S225), T228 (= T228), H231 (= H231), G248 (= G248), E378 (= E378)
1wnbA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
100% identity, 100% coverage: 1:474/474 of query aligns to 1:474/474 of 1wnbA
- active site: N149 (= N149), K172 (= K172), E246 (= E246), C280 (= C280), E378 (= E378), D455 (= D455)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (= I145), A146 (= A146), W148 (= W148), K172 (= K172), G204 (= G204), G208 (= G208), D209 (= D209), G224 (= G224), S225 (= S225), T228 (= T228), H231 (= H231), G248 (= G248), F380 (= F380)
4f3xA Crystal structure of putative aldehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD
61% identity, 100% coverage: 1:474/474 of query aligns to 2:475/476 of 4f3xA
- active site: N150 (= N149), K173 (= K172), E247 (= E246), C281 (= C280), E379 (= E378), D456 (= D455)
- binding nicotinamide-adenine-dinucleotide: I146 (= I145), A147 (= A146), P148 (= P147), W149 (= W148), K173 (= K172), E176 (= E175), G205 (= G204), G209 (= G208), I213 (≠ T212), I223 (≠ L222), G225 (= G224), D226 (≠ S225), T229 (= T228), G249 (= G248), C281 (= C280), Q328 (≠ H327), R331 (= R330), E379 (= E378), F381 (= F380)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
41% identity, 99% coverage: 4:472/474 of query aligns to 18:488/491 of 5gtlA
- active site: N165 (= N149), K188 (= K172), E263 (= E246), C297 (= C280), E394 (= E378), E471 (≠ D455)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I145), P163 (= P147), K188 (= K172), A190 (≠ S174), E191 (= E175), Q192 (≠ I176), G221 (= G204), G225 (= G208), G241 (= G224), S242 (= S225), T245 (= T228), L264 (= L247), C297 (= C280), E394 (= E378), F396 (= F380)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
41% identity, 99% coverage: 4:472/474 of query aligns to 18:488/491 of 5gtkA
- active site: N165 (= N149), K188 (= K172), E263 (= E246), C297 (= C280), E394 (= E378), E471 (≠ D455)
- binding nicotinamide-adenine-dinucleotide: I161 (= I145), I162 (≠ A146), P163 (= P147), W164 (= W148), K188 (= K172), E191 (= E175), G221 (= G204), G225 (= G208), A226 (≠ D209), F239 (≠ L222), G241 (= G224), S242 (= S225), T245 (= T228), Y248 (≠ H231), L264 (= L247), C297 (= C280), Q344 (≠ H327), R347 (= R330), E394 (= E378), F396 (= F380)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
41% identity, 100% coverage: 1:473/474 of query aligns to 2:478/489 of 4o6rA
- active site: N150 (= N149), K173 (= K172), E248 (= E246), C282 (= C280), E383 (= E378), E460 (≠ D455)
- binding adenosine monophosphate: I146 (= I145), V147 (≠ A146), K173 (= K172), G206 (= G204), G210 (= G208), Q211 (≠ D209), F224 (≠ L222), G226 (= G224), S227 (= S225), T230 (= T228), R233 (≠ H231)
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)
39% identity, 100% coverage: 1:472/474 of query aligns to 16:493/505 of 4neaA
- active site: N166 (= N149), K189 (= K172), E264 (= E246), C298 (= C280), E399 (= E378), E476 (≠ D455)
- binding nicotinamide-adenine-dinucleotide: P164 (= P147), K189 (= K172), E192 (= E175), G222 (= G204), G226 (= G208), G242 (= G224), G243 (≠ S225), T246 (= T228), H249 (= H231), I250 (= I232), C298 (= C280), E399 (= E378), F401 (= F380)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
40% identity, 100% coverage: 1:473/474 of query aligns to 1:476/487 of 4go4A
- active site: N149 (= N149), K172 (= K172), E247 (= E246), C281 (= C280), E381 (= E378), E458 (≠ D455)
- binding nicotinamide-adenine-dinucleotide: I145 (= I145), V146 (≠ A146), W148 (= W148), N149 (= N149), F154 (≠ M154), K172 (= K172), G205 (= G204), G209 (= G208), Q210 (≠ D209), F223 (≠ L222), T224 (= T223), G225 (= G224), S226 (= S225), T229 (= T228), E247 (= E246), G249 (= G248), C281 (= C280), E381 (= E378), F383 (= F380)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
39% identity, 100% coverage: 2:473/474 of query aligns to 5:481/489 of 4cazA
- active site: N152 (= N149), K175 (= K172), E251 (= E246), C285 (= C280), E386 (= E378), E463 (≠ D455)
- 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 (= I145), G149 (≠ A146), W151 (= W148), N152 (= N149), K175 (= K172), E178 (= E175), G208 (= G204), G212 (= G208), F226 (≠ L222), T227 (= T223), G228 (= G224), G229 (≠ S225), T232 (= T228), V236 (≠ I232), E251 (= E246), L252 (= L247), C285 (= C280), E386 (= E378), F388 (= F380)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
39% identity, 100% coverage: 2:473/474 of query aligns to 5:481/489 of 2woxA
- active site: N152 (= N149), K175 (= K172), E251 (= E246), C285 (= C280), E386 (= E378), E463 (≠ D455)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I145), G149 (≠ A146), W151 (= W148), N152 (= N149), K175 (= K172), S177 (= S174), E178 (= E175), G208 (= G204), G212 (= G208), F226 (≠ L222), T227 (= T223), G228 (= G224), G229 (≠ S225), T232 (= T228), V236 (≠ I232), E251 (= E246), L252 (= L247), C285 (= C280), E386 (= E378), F388 (= F380)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
39% identity, 100% coverage: 2:473/474 of query aligns to 5:481/489 of 2wmeA
- active site: N152 (= N149), K175 (= K172), E251 (= E246), C285 (= C280), E386 (= E378), E463 (≠ D455)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ A146), W151 (= W148), K175 (= K172), S177 (= S174), E178 (= E175), G208 (= G204), G212 (= G208), F226 (≠ L222), G228 (= G224), G229 (≠ S225), T232 (= T228), V236 (≠ I232)
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, 100% coverage: 2:473/474 of query aligns to 6:482/490 of Q9HTJ1
- GAWN 150:153 (≠ APWN 146:149) binding
- K162 (= K158) active site, Charge relay system
- KPSE 176:179 (= KPSE 172:175) binding
- G209 (= G204) binding
- GTST 230:233 (≠ SIAT 225:228) binding
- E252 (= E246) active site, Proton acceptor
- C286 (= C280) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E378) binding
- E464 (≠ D455) active site, Charge relay system
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
41% identity, 97% coverage: 16:473/474 of query aligns to 20:480/489 of 6wsbA
- active site: N152 (= N149), E250 (= E246), C284 (= C280), E462 (≠ D455)
- binding nicotinamide-adenine-dinucleotide: I148 (= I145), G149 (≠ A146), A150 (≠ P147), W151 (= W148), N152 (= N149), K175 (= K172), E178 (= E175), G208 (= G204), G211 (= G208), A212 (≠ D209), F225 (≠ L222), T226 (= T223), G227 (= G224), G228 (≠ S225), T231 (= T228), V235 (≠ I232), E250 (= E246), L251 (= L247), G252 (= G248), C284 (= C280), E385 (= E378), F387 (= F380)
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, 99% coverage: 4:473/474 of query aligns to 13:486/492 of 6b5hA
- active site: N161 (= N149), E260 (= E246), C294 (= C280), E468 (≠ D455)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ D99), G116 (≠ A103), F162 (≠ Y150), W169 (= W157), Q284 (≠ T270), F288 (≠ Y274), T295 (= T281), N449 (≠ F436), L451 (= L438), N452 (≠ V439), F457 (≠ H444)
- binding nicotinamide-adenine-dinucleotide: I157 (= I145), I158 (≠ A146), W160 (= W148), N161 (= N149), K184 (= K172), G217 (= G204), G221 (= G208), F235 (≠ L222), T236 (= T223), G237 (= G224), S238 (= S225), V241 (≠ T228), E260 (= E246), L261 (= L247), C294 (= C280), F393 (= F380)
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, 99% coverage: 4:473/474 of query aligns to 13:486/492 of 6b5gA
- active site: N161 (= N149), E260 (= E246), C294 (= C280), E468 (≠ D455)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ Y150), L165 (≠ M153), W169 (= W157), F288 (≠ Y274), C293 (≠ D279), C294 (= C280), T295 (= T281), N449 (≠ F436), L451 (= L438)
- binding nicotinamide-adenine-dinucleotide: I157 (= I145), I158 (≠ A146), P159 (= P147), W160 (= W148), N161 (= N149), M166 (= M154), K184 (= K172), E187 (= E175), G217 (= G204), G221 (= G208), F235 (≠ L222), T236 (= T223), G237 (= G224), S238 (= S225), V241 (≠ T228), E260 (= E246), L261 (= L247), C294 (= C280), E391 (= E378), F393 (= F380)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
38% identity, 99% coverage: 4:473/474 of query aligns to 13:486/492 of 6aljA
- active site: N161 (= N149), E260 (= E246), C294 (= C280), E468 (≠ D455)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ A103), F162 (≠ Y150), L165 (≠ M153), M166 (= M154), W169 (= W157), E260 (= E246), C293 (≠ D279), C294 (= C280), L451 (= L438), N452 (≠ V439), A453 (≠ S440)
- binding nicotinamide-adenine-dinucleotide: I157 (= I145), I158 (≠ A146), P159 (= P147), W160 (= W148), N161 (= N149), K184 (= K172), E187 (= E175), G217 (= G204), G221 (= G208), F235 (≠ L222), G237 (= G224), S238 (= S225), V241 (≠ T228), Q341 (≠ H327), K344 (≠ R330), E391 (= E378), F393 (= F380)
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
38% identity, 96% coverage: 22:474/474 of query aligns to 28:487/487 of Q9H2A2
- R109 (≠ A103) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N149) mutation to A: Complete loss of activity.
- R451 (≠ L438) mutation to A: Complete loss of activity.
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)
38% identity, 99% coverage: 4:473/474 of query aligns to 39:512/518 of O94788
- E50 (= E15) to G: in dbSNP:rs34266719
- A110 (= A71) to V: in dbSNP:rs35365164
- Q182 (≠ S144) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ APW 146:148) binding
- KPAE 210:213 (≠ KPSE 172:175) binding
- STE 264:266 (≠ SIA 225:227) binding
- C320 (= C280) active site, Nucleophile
- R347 (≠ L307) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K308) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ AHLER 326:330) binding
- A383 (≠ H343) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E378) binding
- E436 (≠ N397) to K: in dbSNP:rs34744827
- S461 (= S422) to Y: in DIH4; decreased retinoic acid biosynthetic process
Query Sequence
>15565 b1444 medium chain aldehyde dehydrogenase (NCBI)
MQHKLLINGELVSGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTP
KVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNG
LAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLT
ALKLAELAKDIFPAGVINILFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSI
KRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKL
GAAVATLKSGAPDDESTELGPLSSLAHLERVGKAVEEAKATGHIKVITGGEKRKGNGYYY
APTLLAGALQDDAIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHR
VSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMVKH
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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