SitesBLAST
Comparing HSERO_RS19695 HSERO_RS19695 aldehyde dehydrogenase 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)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
48% identity, 98% coverage: 2:473/480 of query aligns to 2:473/476 of 5x5uA
- active site: N151 (= N151), K174 (= K174), E249 (= E249), C283 (= C283), E380 (= E380), E457 (= E457)
- binding glycerol: D15 (≠ G15), A16 (≠ V16), A17 (≠ E17), G19 (≠ R19)
- binding nicotinamide-adenine-dinucleotide: P149 (= P149), P207 (≠ S207), A208 (≠ S208), S211 (= S211), G227 (= G227), S228 (= S228), V231 (= V231), R329 (= R329), R330 (= R330), E380 (= E380), F382 (= F382)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
48% identity, 98% coverage: 2:473/480 of query aligns to 2:473/476 of 5x5tA
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
41% identity, 98% coverage: 6:473/480 of query aligns to 11:478/481 of 3jz4A
- active site: N156 (= N151), K179 (= K174), E254 (= E249), C288 (= C283), E385 (= E380), E462 (= E457)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P149), W155 (= W150), K179 (= K174), A181 (≠ P176), S182 (= S177), A212 (≠ S207), G216 (≠ S211), G232 (= G227), S233 (= S228), I236 (≠ V231), C288 (= C283), K338 (≠ A333), E385 (= E380), F387 (= F382)
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)
41% identity, 98% coverage: 6:473/480 of query aligns to 12:479/482 of P25526
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)
42% identity, 94% coverage: 24:473/480 of query aligns to 78:531/535 of P51649
- C93 (≠ A39) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G122) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ G126) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ R128) to L: 48% of activity; dbSNP:rs3765310
- R213 (≠ K159) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C169) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KGPS 174:177) binding
- T233 (≠ S179) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (≠ I183) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N201) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ S211) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSVPVG 227:232) binding
- R334 (= R277) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N278) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C283) modified: Disulfide link with 342, In inhibited form
- C342 (≠ S285) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ P314) natural variant: N -> S
- P382 (= P324) to L: in SSADHD; 2% of activity
- V406 (≠ L348) to I: in dbSNP:rs143741652
- G409 (= G351) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ A440) 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)
41% identity, 94% coverage: 24:473/480 of query aligns to 28:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
41% identity, 94% coverage: 24:473/480 of query aligns to 28:481/485 of 2w8qA
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
39% identity, 98% coverage: 6:473/480 of query aligns to 11:478/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I147), T153 (≠ S148), P154 (= P149), K179 (= K174), A212 (≠ S207), K213 (≠ S208), F230 (= F225), T231 (= T226), G232 (= G227), S233 (= S228), V236 (= V231), W239 (≠ K234), G256 (= G251)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
37% identity, 97% coverage: 6:472/480 of query aligns to 7:476/486 of 4pxlA
- active site: N154 (= N151), K177 (= K174), E253 (= E249), C287 (= C283), E384 (= E380), D461 (≠ E457)
- binding nicotinamide-adenine-dinucleotide: I150 (= I147), V151 (≠ S148), P152 (= P149), W153 (= W150), K177 (= K174), E180 (≠ S177), G210 (≠ S207), G214 (≠ S211), A215 (≠ Q212), F228 (= F225), G230 (= G227), S231 (= S228), V234 (= V231), E253 (= E249), G255 (= G251), C287 (= C283), Q334 (≠ R330), K337 (≠ A333), E384 (= E380), F386 (= F382)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
36% identity, 97% coverage: 7:472/480 of query aligns to 7:473/477 of 2opxA
- active site: N151 (= N151), K174 (= K174), E249 (= E249), C283 (= C283), E381 (= E380), A458 (≠ E457)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ N105), F152 (= F152), N284 (≠ V284), F312 (≠ V312), G313 (= G313), R318 (≠ E317), D320 (≠ G319), I321 (≠ V320), A322 (≠ Q321), Y362 (≠ F361), F440 (≠ M439), F440 (≠ M439), E441 (≠ A440)
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)
36% identity, 98% coverage: 5:473/480 of query aligns to 10:484/487 of Q9H2A2
- R109 (≠ N105) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N151) mutation to A: Complete loss of activity.
- R451 (≠ A440) mutation to A: Complete loss of activity.
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, 97% coverage: 7:472/480 of query aligns to 9:475/479 of P25553
- L150 (≠ S148) binding
- R161 (≠ K159) binding
- K-PSE 176:179 (≠ KGPSE 174:178) binding
- F180 (vs. gap) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (= Q212) binding
- S230 (= S228) binding
- E251 (= E249) binding
- N286 (≠ V284) 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 (≠ A333) binding
- E443 (≠ A440) binding
- H449 (≠ F446) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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, 97% coverage: 7:472/480 of query aligns to 7:473/477 of 2impA
- active site: N151 (= N151), K174 (= K174), E249 (= E249), C283 (= C283), E381 (= E380), A458 (≠ E457)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I147), L148 (≠ S148), P149 (= P149), W150 (= W150), K174 (= K174), E177 (= E178), F178 (vs. gap), G207 (≠ S207), G211 (≠ S211), Q212 (= Q212), S228 (= S228), A231 (≠ V231), K234 (= K234), R334 (≠ A333)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
36% identity, 97% coverage: 7:472/480 of query aligns to 7:473/477 of 2iluA
- active site: N151 (= N151), K174 (= K174), E249 (= E249), C283 (= C283), E381 (= E380), A458 (≠ E457)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I147), L148 (≠ S148), P149 (= P149), W150 (= W150), K174 (= K174), S176 (= S177), E177 (= E178), R206 (≠ V206), G207 (≠ S207), G211 (≠ S211), Q212 (= Q212), S228 (= S228), A231 (≠ V231), K234 (= K234), I235 (≠ L235), N328 (≠ H327), R334 (≠ A333), F383 (= F382)
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)
35% identity, 98% coverage: 3:474/480 of query aligns to 6:484/497 of P17202
- I28 (≠ R25) binding
- D96 (= D91) binding
- SPW 156:158 (= SPW 148:150) binding
- Y160 (≠ F152) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ K159) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- K-PSE 182:185 (≠ KGPSE 174:178) binding
- L186 (≠ S179) binding
- SSAT 236:239 (≠ SVPV 228:231) binding
- V251 (≠ M243) binding in other chain
- L258 (= L250) binding
- W285 (≠ R277) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E380) binding
- A441 (≠ M431) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ A440) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F446) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G450) binding
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 98% coverage: 6:477/480 of query aligns to 21:496/501 of Q56YU0
- G152 (≠ Q134) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A397) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
36% identity, 90% coverage: 8:438/480 of query aligns to 9:438/454 of 3ty7B
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
34% identity, 98% coverage: 3:474/480 of query aligns to 4:482/495 of 4v37A
- active site: N157 (= N151), K180 (= K174), E255 (= E249), A289 (≠ C283), E388 (= E380), E465 (= E457)
- binding 3-aminopropan-1-ol: C448 (≠ A440), W454 (≠ F446)
- binding nicotinamide-adenine-dinucleotide: I153 (= I147), S154 (= S148), P155 (= P149), W156 (= W150), N157 (= N151), M162 (≠ Q156), K180 (= K174), S182 (= S177), E183 (= E178), G213 (≠ S207), G217 (≠ S211), A218 (≠ Q212), T232 (= T226), G233 (= G227), S234 (= S228), T237 (≠ V231), E255 (= E249), L256 (= L250), A289 (≠ C283), E388 (= E380), F390 (= F382)
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)
34% identity, 98% coverage: 2:472/480 of query aligns to 4:479/490 of Q9HTJ1
- GAWN 150:153 (≠ SPWN 148:151) binding
- K162 (= K160) active site, Charge relay system
- KPSE 176:179 (≠ KGPS 174:177) binding
- G209 (≠ S207) binding
- GTST 230:233 (≠ SVPV 228:231) binding
- E252 (= E249) active site, Proton acceptor
- C286 (= C283) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E380) binding
- E464 (= E457) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
34% identity, 98% coverage: 2:472/480 of query aligns to 3:478/489 of 4cazA
- active site: N152 (= N151), K175 (= K174), E251 (= E249), C285 (= C283), E386 (= E380), E463 (= E457)
- 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 (= I147), G149 (≠ S148), W151 (= W150), N152 (= N151), K175 (= K174), E178 (≠ S177), G208 (≠ S207), G212 (≠ S211), F226 (= F225), T227 (= T226), G228 (= G227), G229 (≠ S228), T232 (≠ V231), V236 (≠ L235), E251 (= E249), L252 (= L250), C285 (= C283), E386 (= E380), F388 (= F382)
Query Sequence
>HSERO_RS19695 HSERO_RS19695 aldehyde dehydrogenase
MYPDLQLYIDGRFHGVEGRRYQEVRDPATGDVLGRLPWAERADIEEAIQAAHRAFQQWRQ
VSPLERSDILRRAAALARERAQAMAPAITMDNGKPLADAVAEIINAAEHLDWHAEEGRRL
YGRVVGARHPEVRQLVVREPVGVCAAISPWNFPFGQAMKKVAAAMAAGCTVVLKGPSESP
AAIVLMAQLFHDAGVPAGVFNIVSGVSSEISQHLIESPLVRNISFTGSVPVGSKLAAQAA
LHMKRMSMELGGHAPVLVFDDAEVEPAARLLARLKTRNAGQVCVSPSRFYVQKGIYARFV
TAFAEALLQIKVGPGHEPGVQMGPLIHGRRFEAVQGLIDDALAQGSELVTGGARLGQRGH
FYAPTLITGVPPSARVMQEEPFGPIAAVTPFSQAEEAIAMANALPLGLASYVFTQSLDTA
HRVSRDLQAGMVNINHSGMAHPELPFGGIGESGFGSEGGVEGFESFLVTKMISQITHVPA
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