SitesBLAST
Comparing Echvi_0535 Echvi_0535 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)
6dbbA Crystal structure of a putative aldehyde dehydrogenase family protein burkholderia cenocepacia j2315 in complex with partially reduced nadh
55% identity, 95% coverage: 27:514/514 of query aligns to 13:504/504 of 6dbbA
- active site: N152 (= N166), E259 (= E267), C293 (= C301), E471 (= E481)
- binding nicotinamide-adenine-dinucleotide: I148 (= I162), S149 (= S163), A150 (= A164), F151 (= F165), N152 (= N166), K175 (= K189), S177 (= S191), R218 (≠ A226), T236 (= T244), G237 (= G245), S238 (= S246), M241 (= M249), E259 (= E267), L260 (= L268), G261 (= G269), C293 (= C301), E391 (= E401), F393 (= F403)
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: I148 (= I162), S149 (= S163), A150 (= A164), F151 (= F165), N152 (= N166), K175 (= K189), S177 (= S191), R218 (≠ A226), T236 (= T244), G237 (= G245), S238 (= S246), M241 (= M249), E259 (= E267), L260 (= L268), G261 (= G269), C293 (= C301), E391 (= E401), F393 (= F403)
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
53% identity, 98% coverage: 11:512/514 of query aligns to 13:509/509 of 2jg7A
- active site: N166 (= N166), K189 (= K189), E267 (= E267), C301 (= C301), E398 (= E401), E478 (= E481)
- binding nicotinamide-adenine-dinucleotide: I162 (= I162), T163 (≠ S163), A164 (= A164), F165 (= F165), N166 (= N166), K189 (= K189), P192 (≠ E192), A226 (= A226), G229 (= G229), T230 (≠ A230), F243 (≠ A243), T244 (= T244), G245 (= G245), S246 (= S246), V249 (≠ M249), E267 (= E267), L268 (= L268), C301 (= C301), E398 (= E401), F400 (= F403)
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
53% identity, 98% coverage: 11:512/514 of query aligns to 12:508/509 of 4zulA
- active site: N165 (= N166), K188 (= K189), E266 (= E267), C300 (= C301), E397 (= E401), E477 (= E481)
- binding 2-aminohexanedioic acid: E119 (= E120), F166 (= F167), R299 (= R300), C300 (= C301), T301 (= T302), G459 (= G463), A460 (= A464), F466 (= F470)
4x0tA Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+ (see paper)
53% identity, 98% coverage: 11:512/514 of query aligns to 12:508/509 of 4x0tA
- active site: N165 (= N166), K188 (= K189), E266 (= E267), C300 (= C301), E397 (= E401), E477 (= E481)
- binding 4-(diethylamino)benzaldehyde: F166 (= F167), V170 (= V171), W173 (= W174), C300 (= C301), F466 (= F470)
- binding nicotinamide-adenine-dinucleotide: T162 (≠ S163), A163 (= A164), F164 (= F165), N165 (= N166), K188 (= K189), G189 (≠ P190), A190 (≠ S191), A225 (= A226), G228 (= G229), T229 (≠ A230), F242 (≠ A243), T243 (= T244), G244 (= G245), S245 (= S246), V248 (≠ M249), E266 (= E267), L267 (= L268), C300 (= C301), E397 (= E401), F399 (= F403)
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)
53% identity, 98% coverage: 11:512/514 of query aligns to 42:538/539 of P49419
- TAF 192:194 (≠ SAF 163:165) binding
- A199 (= A170) to V: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912709
- K218 (= K189) binding
- GT 258:259 (≠ GA 229:230) binding
- GS 274:275 (= GS 245:246) binding
- EL 296:297 (= EL 267:268) binding
- C330 (= C301) active site, Nucleophile
- E427 (= E401) binding ; to Q: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (≠ S413) to Q: in dbSNP:rs12514417
Sites not aligning to the query:
- 110:539 natural variant: Missing (in PDE; loss of alpha-AASA dehydrogenase activity)
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
53% identity, 98% coverage: 11:512/514 of query aligns to 13:509/510 of 6o4dB
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
54% identity, 95% coverage: 23:512/514 of query aligns to 19:508/509 of 6rtsA
- active site: N162 (= N166), E263 (= E267), C297 (= C301), E477 (= E481)
- binding nicotinamide-adenine-dinucleotide: I158 (= I162), S159 (= S163), A160 (= A164), F161 (= F165), N162 (= N166), K185 (= K189), S187 (= S191), E188 (= E192), A222 (= A226), G225 (= G229), T240 (= T244), G241 (= G245), S242 (= S246), M245 (= M249), E263 (= E267), L264 (= L268), C297 (= C301), E397 (= E401), F399 (= F403)
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
54% identity, 95% coverage: 23:512/514 of query aligns to 18:507/508 of 6rttA
- active site: N161 (= N166), E262 (= E267), C296 (= C301), E476 (= E481)
- binding pyridine-2-carboxylic acid: A159 (= A164), F162 (= F167), V166 (= V171), W169 (= W174), G240 (= G245), S241 (= S246), R295 (= R300), C296 (= C301), T297 (= T302), E396 (= E401), F398 (= F403), P421 (= P426), K469 (= K474), E470 (= E475)
6rtuA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with alpha-aminoadipic acid (see paper)
54% identity, 95% coverage: 23:512/514 of query aligns to 18:504/505 of 6rtuA
- active site: N161 (= N166), E259 (= E267), C293 (= C301), E473 (= E481)
- binding 2-aminohexanedioic acid: E115 (= E120), F162 (= F167), R292 (= R300), C293 (= C301), T294 (= T302), S454 (= S462), G455 (= G463), A456 (= A464), F462 (= F470)
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
52% identity, 96% coverage: 11:501/514 of query aligns to 12:497/497 of 2j6lA
- active site: N165 (= N166), K188 (= K189), E266 (= E267), C300 (= C301), E397 (= E401), E477 (= E481)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I161 (= I162), T162 (≠ S163), A163 (= A164), F164 (= F165), N165 (= N166), K188 (= K189), A225 (= A226), G228 (= G229), T229 (≠ A230), F242 (≠ A243), T243 (= T244), G244 (= G245), S245 (= S246), V248 (≠ M249), E266 (= E267), L267 (= L268), C300 (= C301), E397 (= E401), F399 (= F403)
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
49% identity, 97% coverage: 10:507/514 of query aligns to 6:498/498 of 4pxnA
- active site: N161 (= N166), K184 (= K189), E262 (= E267), C296 (= C301), E392 (= E401), E472 (= E481)
- binding nicotinamide-adenine-dinucleotide: I157 (= I162), T158 (≠ S163), A159 (= A164), F160 (= F165), N161 (= N166), K184 (= K189), T221 (≠ A226), G224 (= G229), Q225 (≠ A230), F238 (≠ A243), T239 (= T244), G240 (= G245), S241 (= S246), A244 (≠ M249), V248 (= V253), E262 (= E267), L263 (= L268), S264 (≠ G269), C296 (= C301), E392 (= E401), F394 (= F403), F461 (= F470)
4x0uD Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde (see paper)
50% identity, 96% coverage: 11:501/514 of query aligns to 12:487/487 of 4x0uD
- active site: N165 (= N166), K188 (= K189), E266 (= E267), C300 (= C301), E397 (= E401), E467 (= E481)
- binding 4-(diethylamino)benzaldehyde: F166 (= F167), A169 (= A170), V170 (= V171), C300 (= C301), F456 (= F470), H461 (≠ E475)
- binding magnesium ion: E119 (= E120), D122 (= D123)
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)
34% identity, 93% coverage: 32:508/514 of query aligns to 24:510/511 of 6fkuA
- active site: N159 (= N166), E261 (= E267), C295 (= C301), E483 (= E481)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I162), T156 (≠ S163), N159 (= N166), K182 (= K189), S184 (= S191), E185 (= E192), G214 (= G225), G215 (vs. gap), K216 (vs. gap), G220 (= G229), Q221 (≠ A230), F237 (≠ A243), T238 (= T244), G239 (= G245), S240 (= S246), V243 (≠ M249), E261 (= E267), L262 (= L268), C295 (= C301), R342 (≠ D347), F343 (≠ A348), E404 (= E401), F406 (= F403)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
31% identity, 90% coverage: 41:505/514 of query aligns to 25:484/489 of 4o6rA
- active site: N150 (= N166), K173 (= K189), E248 (= E267), C282 (= C301), E383 (= E401), E460 (= E481)
- binding adenosine monophosphate: I146 (= I162), V147 (≠ S163), K173 (= K189), G206 (= G225), G210 (= G229), Q211 (≠ A230), F224 (≠ A243), G226 (= G245), S227 (= S246), T230 (≠ M249), R233 (≠ S252)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
31% identity, 89% coverage: 34:492/514 of query aligns to 20:473/489 of 6wsbA
- active site: N152 (= N166), E250 (= E267), C284 (= C301), E462 (= E481)
- binding nicotinamide-adenine-dinucleotide: I148 (= I162), G149 (≠ S163), A150 (= A164), W151 (≠ F165), N152 (= N166), K175 (= K189), E178 (= E192), G208 (≠ A226), G211 (= G229), A212 (= A230), F225 (≠ A243), T226 (= T244), G227 (= G245), G228 (≠ S246), T231 (≠ M249), V235 (= V253), E250 (= E267), L251 (= L268), G252 (= G269), C284 (= C301), E385 (= E401), F387 (= F403)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
31% identity, 93% coverage: 24:500/514 of query aligns to 5:477/477 of 6j76A
- active site: N148 (= N166), E246 (= E267), C280 (= C301), E458 (= E481)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I162), T145 (≠ S163), A146 (= A164), W147 (≠ F165), N148 (= N166), K171 (= K189), T173 (≠ S191), S174 (≠ E192), G204 (≠ A226), G208 (= G229), T223 (= T244), G224 (= G245), S225 (= S246), A228 (≠ M249), S231 (= S252), I232 (≠ V253), E246 (= E267), L247 (= L268), C280 (= C301), E381 (= E401), F383 (= F403), H447 (≠ F470)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
31% identity, 89% coverage: 34:492/514 of query aligns to 20:474/489 of 4cazA
- active site: N152 (= N166), K175 (= K189), E251 (= E267), C285 (= C301), E386 (= E401), E463 (= E481)
- 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 (= I162), G149 (≠ S163), W151 (≠ F165), N152 (= N166), K175 (= K189), E178 (= E192), G208 (= G225), G212 (= G229), F226 (≠ A243), T227 (= T244), G228 (= G245), G229 (≠ S246), T232 (≠ M249), V236 (= V253), E251 (= E267), L252 (= L268), C285 (= C301), E386 (= E401), F388 (= F403)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
31% identity, 89% coverage: 34:492/514 of query aligns to 20:474/489 of 2woxA
- active site: N152 (= N166), K175 (= K189), E251 (= E267), C285 (= C301), E386 (= E401), E463 (= E481)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I162), G149 (≠ S163), W151 (≠ F165), N152 (= N166), K175 (= K189), S177 (= S191), E178 (= E192), G208 (= G225), G212 (= G229), F226 (≠ A243), T227 (= T244), G228 (= G245), G229 (≠ S246), T232 (≠ M249), V236 (= V253), E251 (= E267), L252 (= L268), C285 (= C301), E386 (= E401), F388 (= F403)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
31% identity, 89% coverage: 34:492/514 of query aligns to 20:474/489 of 2wmeA
- active site: N152 (= N166), K175 (= K189), E251 (= E267), C285 (= C301), E386 (= E401), E463 (= E481)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ S163), W151 (≠ F165), K175 (= K189), S177 (= S191), E178 (= E192), G208 (= G225), G212 (= G229), F226 (≠ A243), G228 (= G245), G229 (≠ S246), T232 (≠ M249), V236 (= V253)
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, 89% coverage: 34:492/514 of query aligns to 21:475/490 of Q9HTJ1
- GAWN 150:153 (≠ SAFN 163:166) binding
- K162 (≠ N175) active site, Charge relay system
- KPSE 176:179 (= KPSE 189:192) binding
- G209 (= G225) binding
- GTST 230:233 (≠ STQM 246:249) binding
- E252 (= E267) active site, Proton acceptor
- C286 (= C301) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E401) binding
- E464 (= E481) active site, Charge relay system
Query Sequence
>Echvi_0535 Echvi_0535 NAD-dependent aldehyde dehydrogenases
MAGTFDTKTLLQDLGLNEVNKGTWTGVEFIDIKGEWLSSYSPVDGKELGKVQMTTRESYE
KVLDQAEKAFKAWRKVPAPQRGEVVRQIGIELRNKKSLLGKLVSYEMGKSYQEGLGEVQE
MIDICDFAVGLSRQLYGLTMHSERPSHRMYEQWHPLGIVGVISAFNFPVAVWSWNTMIAW
VCGDVCVWKPSEKTPLTSVACQLIAADVFNRNGFPEGITSLLIGGANVGAFLTQDPRVAL
ISATGSTQMGKSVGETVGGRLGKVLLELGGNNAIIITEHADLDIAIRGALFGAVGTAGQR
CTSTRRLIIHESVFEEVKERMVAAYSKLTIGNPLDEDNIVGPLIDKDAVQNYLTAIERVK
AEGGKEVVAGGLLEGEEYVSGCYVRPSVFEAENHFQIVQKETFGPILYLMKYSEFDEAIA
MQNNVPQGLSSAIMTTNMREAERYLSSEGSDCGISNVNIGTSGAEIGGAFGGEKETGGGR
ESGSDAWKAYMRRQTNTINYSTDLPLAQGIKFDI
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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