SitesBLAST
Comparing N515DRAFT_0465 N515DRAFT_0465 aldehyde dehydrogenase (NAD+) 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)
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
54% identity, 99% coverage: 3:509/511 of query aligns to 10:509/509 of 2jg7A
- active site: N166 (= N163), K189 (= K186), E267 (= E264), C301 (= C298), E398 (= E398), E478 (= E478)
- binding nicotinamide-adenine-dinucleotide: I162 (= I159), T163 (≠ S160), A164 (= A161), F165 (= F162), N166 (= N163), K189 (= K186), P192 (= P189), A226 (≠ T223), G229 (≠ S226), T230 (≠ Q227), F243 (= F240), T244 (= T241), G245 (= G242), S246 (= S243), V249 (= V246), E267 (= E264), L268 (= L265), C301 (= C298), E398 (= E398), F400 (= F400)
P49419 Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Homo sapiens (Human) (see 5 papers)
55% identity, 99% coverage: 6:510/511 of query aligns to 42:539/539 of P49419
- 110:539 (vs. 78:510, 58% identical) natural variant: Missing (in PDE; loss of alpha-AASA dehydrogenase activity)
- TAF 192:194 (≠ SAF 160:162) binding
- A199 (= A167) to V: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912709
- K218 (= K186) binding
- GT 258:259 (≠ SQ 226:227) binding
- GS 274:275 (= GS 242:243) binding
- EL 296:297 (= EL 264:265) binding
- C330 (= C298) active site, Nucleophile
- E427 (= E398) binding ; to Q: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (= K410) to Q: in dbSNP:rs12514417
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
55% identity, 99% coverage: 6:510/511 of query aligns to 12:509/509 of 4zulA
- active site: N165 (= N163), K188 (= K186), E266 (= E264), C300 (= C298), E397 (= E398), E477 (= E478)
- binding 2-aminohexanedioic acid: E119 (= E117), F166 (= F164), R299 (= R297), C300 (= C298), T301 (= T299), G459 (= G460), A460 (= A461), F466 (= F467)
4x0tA Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+ (see paper)
55% identity, 99% coverage: 6:510/511 of query aligns to 12:509/509 of 4x0tA
- active site: N165 (= N163), K188 (= K186), E266 (= E264), C300 (= C298), E397 (= E398), E477 (= E478)
- binding 4-(diethylamino)benzaldehyde: F166 (= F164), V170 (= V168), W173 (= W171), C300 (= C298), F466 (= F467)
- binding nicotinamide-adenine-dinucleotide: T162 (≠ S160), A163 (= A161), F164 (= F162), N165 (= N163), K188 (= K186), G189 (≠ P187), A190 (≠ S188), A225 (≠ T223), G228 (≠ S226), T229 (≠ Q227), F242 (= F240), T243 (= T241), G244 (= G242), S245 (= S243), V248 (= V246), E266 (= E264), L267 (= L265), C300 (= C298), E397 (= E398), F399 (= F400)
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
55% identity, 99% coverage: 6:510/511 of query aligns to 13:510/510 of 6o4dB
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
54% identity, 96% coverage: 6:498/511 of query aligns to 12:497/497 of 2j6lA
- active site: N165 (= N163), K188 (= K186), E266 (= E264), C300 (= C298), E397 (= E398), E477 (= E478)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I161 (= I159), T162 (≠ S160), A163 (= A161), F164 (= F162), N165 (= N163), K188 (= K186), A225 (≠ T223), G228 (≠ S226), T229 (≠ Q227), F242 (= F240), T243 (= T241), G244 (= G242), S245 (= S243), V248 (= V246), E266 (= E264), L267 (= L265), C300 (= C298), E397 (= E398), F399 (= F400)
6dbbA Crystal structure of a putative aldehyde dehydrogenase family protein burkholderia cenocepacia j2315 in complex with partially reduced nadh
54% identity, 94% coverage: 33:511/511 of query aligns to 22:504/504 of 6dbbA
- active site: N152 (= N163), E259 (= E264), C293 (= C298), E471 (= E478)
- binding nicotinamide-adenine-dinucleotide: I148 (= I159), S149 (= S160), A150 (= A161), F151 (= F162), N152 (= N163), K175 (= K186), S177 (= S188), R218 (≠ T223), T236 (= T241), G237 (= G242), S238 (= S243), M241 (≠ V246), E259 (= E264), L260 (= L265), G261 (= G266), C293 (= C298), E391 (= E398), F393 (= F400)
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: I148 (= I159), S149 (= S160), A150 (= A161), F151 (= F162), N152 (= N163), K175 (= K186), S177 (= S188), R218 (≠ T223), T236 (= T241), G237 (= G242), S238 (= S243), M241 (≠ V246), E259 (= E264), L260 (= L265), G261 (= G266), C293 (= C298), E391 (= E398), F393 (= F400)
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
51% identity, 98% coverage: 3:504/511 of query aligns to 4:498/498 of 4pxnA
- active site: N161 (= N163), K184 (= K186), E262 (= E264), C296 (= C298), E392 (= E398), E472 (= E478)
- binding nicotinamide-adenine-dinucleotide: I157 (= I159), T158 (≠ S160), A159 (= A161), F160 (= F162), N161 (= N163), K184 (= K186), T221 (= T223), G224 (≠ S226), Q225 (= Q227), F238 (= F240), T239 (= T241), G240 (= G242), S241 (= S243), A244 (≠ V246), V248 (= V250), E262 (= E264), L263 (= L265), S264 (≠ G266), C296 (= C298), E392 (= E398), F394 (= F400), F461 (= F467)
4x0uD Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde (see paper)
53% identity, 96% coverage: 6:498/511 of query aligns to 12:487/487 of 4x0uD
- active site: N165 (= N163), K188 (= K186), E266 (= E264), C300 (= C298), E397 (= E398), E467 (= E478)
- binding 4-(diethylamino)benzaldehyde: F166 (= F164), A169 (= A167), V170 (= V168), C300 (= C298), F456 (= F467), H461 (≠ E472)
- binding magnesium ion: E119 (= E117), D122 (= D120)
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
55% identity, 93% coverage: 33:509/511 of query aligns to 31:507/508 of 6rttA
- active site: N161 (= N163), E262 (= E264), C296 (= C298), E476 (= E478)
- binding pyridine-2-carboxylic acid: A159 (= A161), F162 (= F164), V166 (= V168), W169 (= W171), G240 (= G242), S241 (= S243), R295 (= R297), C296 (= C298), T297 (= T299), E396 (= E398), F398 (= F400), P421 (= P423), K469 (= K471), E470 (= E472)
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
55% identity, 93% coverage: 33:509/511 of query aligns to 32:508/509 of 6rtsA
- active site: N162 (= N163), E263 (= E264), C297 (= C298), E477 (= E478)
- binding nicotinamide-adenine-dinucleotide: I158 (= I159), S159 (= S160), A160 (= A161), F161 (= F162), N162 (= N163), K185 (= K186), S187 (= S188), E188 (≠ P189), A222 (≠ T223), G225 (≠ S226), T240 (= T241), G241 (= G242), S242 (= S243), M245 (≠ V246), E263 (= E264), L264 (= L265), C297 (= C298), E397 (= E398), F399 (= F400)
6rtuA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with alpha-aminoadipic acid (see paper)
55% identity, 93% coverage: 33:509/511 of query aligns to 31:504/505 of 6rtuA
- active site: N161 (= N163), E259 (= E264), C293 (= C298), E473 (= E478)
- binding 2-aminohexanedioic acid: E115 (= E117), F162 (= F164), R292 (= R297), C293 (= C298), T294 (= T299), S454 (= S459), G455 (= G460), A456 (= A461), F462 (= F467)
6fkuA Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an evolutionarily-distinct c-terminal arm (recombinant protein with shortened c-terminal, in complex with NADP) (see paper)
33% identity, 92% coverage: 34:505/511 of query aligns to 29:510/511 of 6fkuA
- active site: N159 (= N163), E261 (= E264), C295 (= C298), E483 (= E478)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I159), T156 (≠ S160), N159 (= N163), K182 (= K186), S184 (= S188), E185 (≠ P189), G214 (≠ F218), G215 (≠ N219), K216 (≠ D220), G220 (vs. gap), Q221 (≠ D224), F237 (= F240), T238 (= T241), G239 (= G242), S240 (= S243), V243 (= V246), E261 (= E264), L262 (= L265), C295 (= C298), R342 (≠ D346), F343 (≠ A347), E404 (= E398), F406 (= F400)
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
31% identity, 93% coverage: 23:499/511 of query aligns to 14:488/497 of P17202
- I28 (≠ V37) binding
- D96 (≠ E103) binding
- SPW 156:158 (≠ SAF 160:162) binding
- Y160 (≠ F164) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (= W171) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPSP 186:189) binding
- L186 (≠ K190) binding
- SSAT 236:239 (≠ STKV 243:246) binding
- V251 (≠ M258) binding in other chain
- L258 (= L265) binding
- W285 (≠ G292) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E398) binding
- A441 (≠ I451) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ A461) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F467) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K471) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
31% identity, 93% coverage: 23:499/511 of query aligns to 12:486/495 of 4v37A
- active site: N157 (= N163), K180 (= K186), E255 (= E264), A289 (≠ C298), E388 (= E398), E465 (= E478)
- binding 3-aminopropan-1-ol: C448 (≠ A461), W454 (≠ F467)
- binding nicotinamide-adenine-dinucleotide: I153 (= I159), S154 (= S160), P155 (≠ A161), W156 (≠ F162), N157 (= N163), M162 (≠ V168), K180 (= K186), S182 (= S188), E183 (≠ P189), G213 (= G222), G217 (≠ S226), A218 (≠ Q227), T232 (= T241), G233 (= G242), S234 (= S243), T237 (≠ V246), E255 (= E264), L256 (= L265), A289 (≠ C298), E388 (= E398), F390 (= F400)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
31% identity, 93% coverage: 14:489/511 of query aligns to 4:474/489 of 4cazA
- active site: N152 (= N163), K175 (= K186), E251 (= E264), C285 (= C298), E386 (= E398), E463 (= E478)
- 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 (= I159), G149 (≠ S160), W151 (≠ F162), N152 (= N163), K175 (= K186), E178 (≠ P189), G208 (= G222), G212 (≠ S226), F226 (= F240), T227 (= T241), G228 (= G242), G229 (≠ S243), T232 (≠ V246), V236 (= V250), E251 (= E264), L252 (= L265), C285 (= C298), E386 (= E398), F388 (= F400)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
31% identity, 93% coverage: 14:489/511 of query aligns to 4:474/489 of 2woxA
- active site: N152 (= N163), K175 (= K186), E251 (= E264), C285 (= C298), E386 (= E398), E463 (= E478)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I159), G149 (≠ S160), W151 (≠ F162), N152 (= N163), K175 (= K186), S177 (= S188), E178 (≠ P189), G208 (= G222), G212 (≠ S226), F226 (= F240), T227 (= T241), G228 (= G242), G229 (≠ S243), T232 (≠ V246), V236 (= V250), E251 (= E264), L252 (= L265), C285 (= C298), E386 (= E398), F388 (= F400)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
31% identity, 93% coverage: 14:489/511 of query aligns to 4:474/489 of 2wmeA
- active site: N152 (= N163), K175 (= K186), E251 (= E264), C285 (= C298), E386 (= E398), E463 (= E478)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ S160), W151 (≠ F162), K175 (= K186), S177 (= S188), E178 (≠ P189), G208 (= G222), G212 (≠ S226), F226 (= F240), G228 (= G242), G229 (≠ S243), T232 (≠ V246), V236 (= V250)
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)
31% identity, 93% coverage: 14:489/511 of query aligns to 5:475/490 of Q9HTJ1
- GAWN 150:153 (≠ SAFN 160:163) binding
- K162 (≠ N172) active site, Charge relay system
- KPSE 176:179 (≠ KPSP 186:189) binding
- G209 (= G222) binding
- GTST 230:233 (≠ STKV 243:246) binding
- E252 (= E264) active site, Proton acceptor
- C286 (= C298) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E398) binding
- E464 (= E478) active site, Charge relay system
7radA Crystal structure analysis of aldh1b1
32% identity, 92% coverage: 24:494/511 of query aligns to 20:485/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I159), I159 (≠ S160), P160 (≠ A161), W161 (≠ F162), N162 (= N163), M167 (≠ V168), K185 (= K186), E188 (≠ P189), G218 (≠ N219), G222 (= G222), A223 (≠ T223), T237 (= T241), G238 (= G242), S239 (= S243), V242 (= V246), E261 (= E264), L262 (= L265), C295 (= C298), E392 (= E398), F394 (= F400)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (= E117), F163 (= F164), E285 (≠ F288), F289 (≠ G292), N450 (= N455), V452 (≠ G457)
Query Sequence
>N515DRAFT_0465 N515DRAFT_0465 aldehyde dehydrogenase (NAD+)
MSHEILKALGIGAEHSGTYLGQGEWSRTSDAGALQPVNPATGEVIGTVHASSAADYETIV
KRAQEAFKTWRTTPAPRRGEAVRLCGEALRKHKDALGSLVALEMGKIKPEGDGEVQEMID
IADFAVGQSRMLYGYTMHSERPGHRMYEQYHPLGLVGIISAFNFPVAVWAWNAFLAAICG
DICIWKPSPKTPLSAIATMKICNEALKAGGFPDIFFLFNDAGTDLSQGFVDDKRIPLISF
TGSTKVGRMVGERVARRMGRSLLELGGNNAIILDASADLKLAIPAIVFGAVGTAGQRCTT
TRRLFVHESIVGEVTDKLVAAYKQVEGKIGDPTLATTLMGPLNSQDAVQAYLGAVEKAKA
SGGKVLTGGAALSDRKGNFVLPTIVTGVKNSDEVVQTETFAPILYIMPFKSLDEAIELQN
DVPQGLSSAIFTRDLKAAEQYLSSAGSDCGIANVNIGTSGAEIGGAFGGEKETGGGRESG
SDAWKVYMRRQTNTSNYSDSLPLAQGIKFDL
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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