SitesBLAST
Comparing GFF882 Psest_0905 NAD-dependent aldehyde dehydrogenases 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)
P37685 Aldehyde dehydrogenase B; Acetaldehyde dehydrogenase; EC 1.2.1.4 from Escherichia coli (strain K12) (see paper)
50% identity, 97% coverage: 15:499/499 of query aligns to 23:512/512 of P37685
- R197 (≠ E189) mutation to E: Less than 10% of wild-type acetaldehyde dehydrogenase activity.
7radA Crystal structure analysis of aldh1b1
45% identity, 96% coverage: 13:491/499 of query aligns to 8:488/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (≠ V159), I159 (= I160), P160 (= P161), W161 (= W162), N162 (= N163), M167 (= M168), K185 (= K186), E188 (= E189), G218 (= G218), G222 (= G222), A223 (≠ Q223), T237 (= T237), G238 (= G238), S239 (= S239), V242 (= V242), E261 (= E260), L262 (= L261), C295 (= C294), E392 (= E395), F394 (= F397)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ V114), E117 (≠ L118), F163 (= F164), E285 (≠ L284), F289 (≠ W288), N450 (≠ H453), V452 (≠ I455)
7mjdA Crystal structure analysis of aldh1b1
45% identity, 96% coverage: 13:491/499 of query aligns to 8:488/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (≠ V159), I159 (= I160), P160 (= P161), W161 (= W162), N162 (= N163), M167 (= M168), K185 (= K186), E188 (= E189), G218 (= G218), G222 (= G222), F236 (= F236), T237 (= T237), G238 (= G238), S239 (= S239), V242 (= V242), E261 (= E260), L262 (= L261), C295 (= C294), E392 (= E395), F394 (= F397)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ L118), E285 (≠ L284), F289 (≠ W288), N450 (≠ H453), V452 (≠ I455)
7mjcA Crystal structure analysis of aldh1b1
45% identity, 96% coverage: 13:491/499 of query aligns to 8:488/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (≠ V159), I159 (= I160), P160 (= P161), W161 (= W162), N162 (= N163), K185 (= K186), E188 (= E189), G218 (= G218), G222 (= G222), T237 (= T237), G238 (= G238), S239 (= S239), V242 (= V242), E261 (= E260), L262 (= L261), C295 (= C294), E392 (= E395), F394 (= F397)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
45% identity, 95% coverage: 19:492/499 of query aligns to 6:480/489 of 4o6rA
- active site: N150 (= N163), K173 (= K186), E248 (= E260), C282 (= C294), E383 (= E395), E460 (= E472)
- binding adenosine monophosphate: I146 (≠ V159), V147 (≠ I160), K173 (= K186), G206 (= G218), G210 (= G222), Q211 (= Q223), F224 (= F236), G226 (= G238), S227 (= S239), T230 (≠ V242), R233 (≠ L245)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
44% identity, 97% coverage: 9:491/499 of query aligns to 31:515/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
44% identity, 95% coverage: 18:491/499 of query aligns to 24:497/503 of O14293
- S248 (= S239) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
43% identity, 95% coverage: 19:493/499 of query aligns to 8:484/489 of 4cazA
- active site: N152 (= N163), K175 (= K186), E251 (= E260), C285 (= C294), E386 (= E395), E463 (= E472)
- 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 (≠ V159), G149 (≠ I160), W151 (= W162), N152 (= N163), K175 (= K186), E178 (= E189), G208 (= G218), G212 (= G222), F226 (= F236), T227 (= T237), G228 (= G238), G229 (≠ S239), T232 (≠ V242), V236 (= V246), E251 (= E260), L252 (= L261), C285 (= C294), E386 (= E395), F388 (= F397)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
43% identity, 95% coverage: 19:493/499 of query aligns to 8:484/489 of 2woxA
- active site: N152 (= N163), K175 (= K186), E251 (= E260), C285 (= C294), E386 (= E395), E463 (= E472)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ V159), G149 (≠ I160), W151 (= W162), N152 (= N163), K175 (= K186), S177 (= S188), E178 (= E189), G208 (= G218), G212 (= G222), F226 (= F236), T227 (= T237), G228 (= G238), G229 (≠ S239), T232 (≠ V242), V236 (= V246), E251 (= E260), L252 (= L261), C285 (= C294), E386 (= E395), F388 (= F397)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
43% identity, 95% coverage: 19:493/499 of query aligns to 8:484/489 of 2wmeA
- active site: N152 (= N163), K175 (= K186), E251 (= E260), C285 (= C294), E386 (= E395), E463 (= E472)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ I160), W151 (= W162), K175 (= K186), S177 (= S188), E178 (= E189), G208 (= G218), G212 (= G222), F226 (= F236), G228 (= G238), G229 (≠ S239), T232 (≠ V242), V236 (= V246)
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)
43% identity, 95% coverage: 19:493/499 of query aligns to 9:485/490 of Q9HTJ1
- GAWN 150:153 (≠ IPWN 160:163) binding
- K162 (= K172) active site, Charge relay system
- KPSE 176:179 (= KPSE 186:189) binding
- G209 (= G218) binding
- GTST 230:233 (≠ STRV 239:242) binding
- E252 (= E260) active site, Proton acceptor
- C286 (= C294) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E395) binding
- E464 (= E472) active site, Charge relay system
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)
44% identity, 95% coverage: 19:491/499 of query aligns to 40:513/518 of O94788
- E50 (= E29) to G: in dbSNP:rs34266719
- A110 (= A86) to V: in dbSNP:rs35365164
- Q182 (= Q158) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (= IPW 160:162) binding
- KPAE 210:213 (≠ KPSE 186:189) binding
- STE 264:266 (≠ STR 239:241) binding
- C320 (= C294) active site, Nucleophile
- R347 (≠ V321) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ R322) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ SQMER 340:344) binding
- A383 (= A357) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E395) binding
- E436 (≠ A414) to K: in dbSNP:rs34744827
- S461 (≠ A439) 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)
44% identity, 95% coverage: 19:491/499 of query aligns to 14:487/492 of 6b5hA
- active site: N161 (= N163), E260 (= E260), C294 (= C294), E468 (= E472)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (= V114), G116 (≠ L118), F162 (= F164), W169 (= W171), Q284 (≠ L284), F288 (≠ W288), T295 (≠ E295), N449 (≠ H453), L451 (≠ I455), N452 (≠ P456), F457 (= F461)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V159), I158 (= I160), W160 (= W162), N161 (= N163), K184 (= K186), G217 (= G218), G221 (= G222), F235 (= F236), T236 (= T237), G237 (= G238), S238 (= S239), V241 (= V242), E260 (= E260), L261 (= L261), C294 (= C294), F393 (= F397)
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)
44% identity, 95% coverage: 19:491/499 of query aligns to 14:487/492 of 6b5gA
- active site: N161 (= N163), E260 (= E260), C294 (= C294), E468 (= E472)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F164), L165 (= L167), W169 (= W171), F288 (≠ W288), C293 (≠ V293), C294 (= C294), T295 (≠ E295), N449 (≠ H453), L451 (≠ I455)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V159), I158 (= I160), P159 (= P161), W160 (= W162), N161 (= N163), M166 (= M168), K184 (= K186), E187 (= E189), G217 (= G218), G221 (= G222), F235 (= F236), T236 (= T237), G237 (= G238), S238 (= S239), V241 (= V242), E260 (= E260), L261 (= L261), C294 (= C294), E391 (= E395), F393 (= F397)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
44% identity, 95% coverage: 19:491/499 of query aligns to 14:487/492 of 6aljA
- active site: N161 (= N163), E260 (= E260), C294 (= C294), E468 (= E472)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ L118), F162 (= F164), L165 (= L167), M166 (= M168), W169 (= W171), E260 (= E260), C293 (≠ V293), C294 (= C294), L451 (≠ I455), N452 (≠ P456), A453 (= A457)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ V159), I158 (= I160), P159 (= P161), W160 (= W162), N161 (= N163), K184 (= K186), E187 (= E189), G217 (= G218), G221 (= G222), F235 (= F236), G237 (= G238), S238 (= S239), V241 (= V242), Q341 (= Q341), K344 (≠ R344), E391 (= E395), F393 (= F397)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
43% identity, 97% coverage: 9:491/499 of query aligns to 5:489/494 of 5l13A
- active site: N163 (= N163), K186 (= K186), E262 (= E260), C296 (= C294), E393 (= E395), E470 (= E472)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F164), M168 (= M168), W171 (= W171), F290 (≠ W288), C295 (≠ V293), C296 (= C294), C297 (≠ E295), D451 (≠ H453), F453 (≠ I455)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
43% identity, 97% coverage: 9:491/499 of query aligns to 5:489/494 of 4kwgA
- active site: N163 (= N163), K186 (= K186), E262 (= E260), C296 (= C294), E393 (= E395), E470 (= E472)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F164), M168 (= M168), C295 (≠ V293), C296 (= C294), C297 (≠ E295), D451 (≠ H453), F453 (≠ I455)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
43% identity, 97% coverage: 9:491/499 of query aligns to 5:489/494 of 4kwfA
- active site: N163 (= N163), K186 (= K186), E262 (= E260), C296 (= C294), E393 (= E395), E470 (= E472)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F164), M168 (= M168), W171 (= W171), E262 (= E260), C295 (≠ V293), C296 (= C294), C297 (≠ E295), D451 (≠ H453), F453 (≠ I455), F459 (= F461)
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)
43% identity, 97% coverage: 9:491/499 of query aligns to 5:489/494 of 3sz9A
- active site: N163 (= N163), K186 (= K186), E262 (= E260), C296 (= C294), E393 (= E395), E470 (= E472)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F164), C295 (≠ V293), C296 (= C294), D451 (≠ H453), F453 (≠ I455), F459 (= F461)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
43% identity, 97% coverage: 9:491/499 of query aligns to 5:489/494 of 3injA
- active site: N163 (= N163), K186 (= K186), E262 (= E260), C296 (= C294), E393 (= E395), E470 (= E472)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ L118), F164 (= F164), L167 (= L167), F286 (≠ L284), F290 (≠ W288), D451 (≠ H453), F453 (≠ I455)
Query Sequence
>GFF882 Psest_0905 NAD-dependent aldehyde dehydrogenases
MKDSSDTHPNHLPDSSYGLFIDNQWVSDEYGETLDIINPANGKILTNIPNATAADVDRAV
QAAQRAFMTWRTTSPAERANALLKIADLLEADADRFAVLETLDVGKPIRESRSVDIPLAI
DHFRYFAGVIRSQSDEAVMLDEQTLSIALSEPLGVVGQVIPWNFPLLMAAWKIAPAIAAG
NTVVIKPSELTPVTILELAKIFAKVLPAGVVNIVTGLGTTVGQALLDHPDLRKLAFTGST
RVGELVANAAAKKIIPATLELGGKSANIVFPDANWDKAVEGAVLAILWNQGQVCESGARL
FVHESIYERFLAELKHKFEAVRVGDPLNPDTMMGAQVSKSQMERILGYVDIAKQEGAEVL
IGGGRLTGANYDAGFFIQPTILVGVRNDMRVAYEEIFGPVLCVIPFKDEAEVIAMANDSE
YGLAGAVWTQDINRALRVARAVETGRMWVNTYHEIPAHAPFGGYKKSGLGRETHKSMLEA
YSQKKNIYVSLNEAPLGLF
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