SitesBLAST
Comparing AO353_24475 AO353_24475 aldehyde dehydrogenase 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)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
54% identity, 98% coverage: 6:473/477 of query aligns to 7:474/476 of 5x5uA
- active site: N151 (= N150), K174 (= K173), E249 (= E248), C283 (= C282), E380 (= E379), E457 (= E456)
- binding glycerol: D15 (≠ N14), A16 (≠ T15), A17 (≠ H16), G19 (≠ D18)
- binding nicotinamide-adenine-dinucleotide: P149 (= P148), P207 (≠ S206), A208 (≠ G207), S211 (= S210), G227 (= G226), S228 (= S227), V231 (= V230), R329 (≠ G328), R330 (= R329), E380 (= E379), F382 (= F381)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
54% identity, 98% coverage: 6:473/477 of query aligns to 7:474/476 of 5x5tA
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
37% identity, 98% coverage: 7:473/477 of query aligns to 14:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
37% identity, 98% coverage: 7:473/477 of query aligns to 13:479/481 of 3jz4A
- active site: N156 (= N150), K179 (= K173), E254 (= E248), C288 (= C282), E385 (= E379), E462 (= E456)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P148), W155 (= W149), K179 (= K173), A181 (= A175), S182 (≠ T176), A212 (≠ S206), G216 (≠ S210), G232 (= G226), S233 (= S227), I236 (≠ V230), C288 (= C282), K338 (≠ A332), E385 (= E379), F387 (= F381)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
37% identity, 99% coverage: 7:476/477 of query aligns to 13:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ F146), T153 (≠ A147), P154 (= P148), K179 (= K173), A212 (≠ S206), K213 (≠ G207), F230 (= F224), T231 (= T225), G232 (= G226), S233 (= S227), V236 (= V230), W239 (≠ K233), G256 (= G250)
P51649 Succinate-semialdehyde dehydrogenase, mitochondrial; Aldehyde dehydrogenase family 5 member A1; NAD(+)-dependent succinic semialdehyde dehydrogenase; EC 1.2.1.24 from Homo sapiens (Human) (see 5 papers)
37% identity, 98% coverage: 7:472/477 of query aligns to 64:531/535 of P51649
- C93 (≠ A38) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G121) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P125) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ R127) to L: 48% of activity; dbSNP:rs3765310
- R213 (≠ K158) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C168) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KGAT 173:176) binding
- T233 (≠ A178) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A182) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N200) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ S210) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTPVG 226:231) binding
- R334 (= R276) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N277) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C282) modified: Disulfide link with 342, In inhibited form
- C342 (≠ S284) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D313) natural variant: N -> S
- P382 (= P323) to L: in SSADHD; 2% of activity
- V406 (≠ L347) to I: in dbSNP:rs143741652
- G409 (= G350) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ A439) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
36% identity, 98% coverage: 7:472/477 of query aligns to 14:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
36% identity, 98% coverage: 7:472/477 of query aligns to 14:481/485 of 2w8qA
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
35% identity, 98% coverage: 6:472/477 of query aligns to 12:488/505 of O24174
- N164 (= N150) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
- W172 (≠ K158) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
36% identity, 99% coverage: 3:475/477 of query aligns to 4:477/477 of 2opxA
- active site: N151 (= N150), K174 (= K173), E249 (= E248), C283 (= C282), E381 (= E379), A458 (≠ E456)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ A104), F152 (= F151), N284 (≠ V283), F312 (≠ V311), G313 (= G312), R318 (≠ P317), D320 (vs. gap), I321 (≠ V319), A322 (≠ T320), Y362 (≠ F360), F440 (≠ V438), F440 (≠ V438), E441 (≠ A439)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
35% identity, 98% coverage: 3:469/477 of query aligns to 1:471/477 of 6j76A
- active site: N148 (= N150), E246 (= E248), C280 (= C282), E458 (= E456)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (≠ F146), T145 (≠ A147), A146 (≠ P148), W147 (= W149), N148 (= N150), K171 (= K173), T173 (≠ A175), S174 (≠ T176), G204 (≠ S206), G208 (≠ S210), T223 (= T225), G224 (= G226), S225 (= S227), A228 (≠ V230), S231 (≠ K233), I232 (≠ L234), E246 (= E248), L247 (= L249), C280 (= C282), E381 (= E379), F383 (= F381), H447 (≠ F445)
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)
33% identity, 98% coverage: 6:472/477 of query aligns to 10:483/497 of P17202
- I28 (= I24) binding
- D96 (≠ E90) binding
- SPW 156:158 (≠ APW 147:149) binding
- Y160 (≠ F151) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ K158) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KGAT 173:176) binding
- L186 (≠ E177) binding
- SSAT 236:239 (≠ STPV 227:230) binding
- V251 (≠ M242) binding in other chain
- L258 (= L249) binding
- W285 (≠ R276) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E379) binding
- A441 (= A430) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ A439) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F445) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K449) binding
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
36% identity, 99% coverage: 3:475/477 of query aligns to 4:477/477 of 2impA
- active site: N151 (= N150), K174 (= K173), E249 (= E248), C283 (= C282), E381 (= E379), A458 (≠ E456)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (≠ F146), L148 (≠ A147), P149 (= P148), W150 (= W149), K174 (= K173), E177 (≠ T176), F178 (≠ E177), G207 (≠ S206), G211 (≠ S210), Q212 (≠ E211), S228 (= S227), A231 (≠ V230), K234 (= K233), R334 (≠ A332)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
36% identity, 99% coverage: 3:475/477 of query aligns to 4:477/477 of 2iluA
- active site: N151 (= N150), K174 (= K173), E249 (= E248), C283 (= C282), E381 (= E379), A458 (≠ E456)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (≠ F146), L148 (≠ A147), P149 (= P148), W150 (= W149), K174 (= K173), S176 (≠ A175), E177 (≠ T176), R206 (≠ D205), G207 (≠ S206), G211 (≠ S210), Q212 (≠ E211), S228 (= S227), A231 (≠ V230), K234 (= K233), I235 (≠ L234), N328 (≠ H326), R334 (≠ A332), F383 (= F381)
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 99% coverage: 3:475/477 of query aligns to 6:479/479 of P25553
- L150 (≠ A147) binding
- R161 (≠ K158) binding
- KPSE 176:179 (≠ KGAT 173:176) binding
- F180 (≠ E177) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ E211) binding
- S230 (= S227) binding
- E251 (= E248) binding
- N286 (≠ V283) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (≠ A332) binding
- E443 (≠ A439) binding
- H449 (≠ F445) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
36% identity, 98% coverage: 6:473/477 of query aligns to 15:486/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (≠ F146), T159 (≠ A147), P160 (= P148), W161 (= W149), K185 (= K173), E188 (≠ T176), G218 (≠ S206), G222 (≠ S210), F236 (= F224), S239 (= S227), V242 (= V230)
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
36% identity, 98% coverage: 6:473/477 of query aligns to 16:487/489 of 7a6qB
- active site: N163 (= N150), E262 (= E248), C296 (= C282), E470 (= E456)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ F146), W162 (= W149), K186 (= K173), E189 (≠ T176), G219 (≠ S206), G223 (≠ S210), S240 (= S227), V243 (= V230), K342 (≠ G328)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (≠ P22), T33 (≠ V23), C34 (≠ I24), P36 (= P26), D103 (≠ E90), E189 (≠ T176), Q190 (≠ E177), F218 (≠ D205), I339 (≠ A325), D340 (≠ H326)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ A104), D141 (≠ R127), N143 (≠ G130), N451 (≠ S437), L453 (≠ A439), A455 (≠ P441)
7a6qA Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
36% identity, 98% coverage: 6:473/477 of query aligns to 16:487/489 of 7a6qA
- active site: N163 (= N150), E262 (= E248), C296 (= C282), E470 (= E456)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ F146), T160 (≠ A147), W162 (= W149), K186 (= K173), A188 (= A175), E189 (≠ T176), G219 (≠ S206), G223 (≠ S210), S240 (= S227), V243 (= V230), K342 (≠ G328), K346 (≠ A332)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ A104), D141 (≠ R127), N143 (≠ G130), N451 (≠ S437), L453 (≠ A439), Y454 (≠ L440)
5fhzA Human aldehyde dehydrogenase 1a3 complexed with NAD(+) and retinoic acid (see paper)
36% identity, 98% coverage: 6:473/477 of query aligns to 16:487/489 of 5fhzA
- active site: N163 (= N150), K186 (= K173), E262 (= E248), C296 (= C282), E393 (= E379), E470 (= E456)
- binding nicotinamide-adenine-dinucleotide: I159 (≠ F146), T160 (≠ A147), W162 (= W149), K186 (= K173), E189 (≠ T176), G219 (≠ S206), G223 (≠ S210), F237 (= F224), G239 (= G226), S240 (= S227), T241 (= T228), V243 (= V230), G264 (= G250), Q343 (≠ R329), E393 (= E379)
- binding retinoic acid: G118 (≠ A104), R121 (≠ D107), F164 (= F151), M168 (≠ Q155), W171 (≠ K158), C295 (≠ V281), C296 (= C282), L453 (≠ A439)
P47895 Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; Aldehyde dehydrogenase 6; Aldehyde dehydrogenase family 1 member A3; ALDH1A3; EC 1.2.1.36 from Homo sapiens (Human) (see 2 papers)
36% identity, 98% coverage: 6:473/477 of query aligns to 34:505/512 of P47895
- R89 (≠ K58) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K173) binding
- E207 (≠ T176) binding
- GSTEVG 257:262 (≠ GSTPVG 226:231) binding
- Q361 (≠ R329) binding
- E411 (= E379) binding
- A493 (= A461) to P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
Query Sequence
>AO353_24475 AO353_24475 aldehyde dehydrogenase
MEQIPLFIGGVWRNTHPDESIPVINPATEEQIGLIAKASLADIEDAAIAAEKGFATWKQV
SALERATIMHKAASLIRERAENIALILTTEHGKPLGEAMGEVAATADTIDWHAEEGRRAY
GRVIPSRALGVHQFTVMEPIGPVVGFAPWNFPLIQAVKKVAGALAAGCSIILKGATEAPT
CAVELVKAFADAGVSPGAVNLLFGDSGQISEHLIAHPSIRKVTFTGSTPVGKKLASLAGL
HMKRSTMELGGHAPVIVMDDADIATAVKISVAAKYRNAGQVCVSPTRFLVHSKVFDEFVS
RFVEGARAVMVGDGLDPNVTMGPMAHAGRLKATEELVADAVSHGAKLETGGNRIGHKGYF
FEPTVLTNVPVTARAMIDEPFGPIALINSFDDIDEAIKEANRLPYGLSAYAYTRSLSSAN
KLFNGIESGAISINHHSVALPEHPFGGVKDSGYGTEGGPGALDAFMTTKFVSLASVL
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