SitesBLAST
Comparing SMc02780 SMc02780 succinate-semialdehyde dehydrogenase [NADP+] protein 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)
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)
69% identity, 99% coverage: 1:481/484 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
69% identity, 99% coverage: 3:481/484 of query aligns to 2:480/481 of 3jz4A
- active site: N156 (= N157), K179 (= K180), E254 (= E255), C288 (= C289), E385 (= E386), E462 (= E463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P155), W155 (= W156), K179 (= K180), A181 (= A182), S182 (≠ A183), A212 (= A213), G216 (= G217), G232 (= G233), S233 (= S234), I236 (≠ V237), C288 (= C289), K338 (= K339), E385 (= E386), F387 (= F388)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
64% identity, 99% coverage: 3:483/484 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I153), T153 (= T154), P154 (= P155), K179 (= K180), A212 (= A213), K213 (≠ R214), F230 (= F231), T231 (= T232), G232 (= G233), S233 (= S234), V236 (= V237), W239 (≠ E240), G256 (= G257)
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)
55% identity, 99% coverage: 7:483/484 of query aligns to 57:535/535 of P51649
- C93 (≠ L45) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G128) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P132) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ H134) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R165) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C175) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAA 180:183) binding
- T233 (= T185) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A189) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S207) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G217) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 233:238) binding
- R334 (= R283) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N284) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C289) modified: Disulfide link with 342, In inhibited form
- C342 (= C291) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (= N320) natural variant: N -> S
- P382 (= P330) to L: in SSADHD; 2% of activity
- V406 (= V354) to I: in dbSNP:rs143741652
- G409 (= G357) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S446) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G481) to R: in SSADHD; <1% of activity; dbSNP:rs72552284
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
55% identity, 99% coverage: 7:483/484 of query aligns to 7:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
55% identity, 99% coverage: 7:483/484 of query aligns to 7:485/485 of 2w8qA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 95% coverage: 15:476/484 of query aligns to 6:471/477 of 6j76A
- active site: N148 (= N157), E246 (= E255), C280 (= C289), E458 (= E463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I153), T145 (= T154), A146 (≠ P155), W147 (= W156), N148 (= N157), K171 (= K180), T173 (≠ A182), S174 (≠ A183), G204 (≠ A213), G208 (= G217), T223 (= T232), G224 (= G233), S225 (= S234), A228 (≠ V237), S231 (≠ E240), I232 (≠ L241), E246 (= E255), L247 (= L256), C280 (= C289), E381 (= E386), F383 (= F388), H447 (≠ F452)
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)
38% identity, 94% coverage: 28:480/484 of query aligns to 24:477/479 of P25553
- L150 (≠ T154) binding
- R161 (= R165) binding
- KPSE 176:179 (≠ KPAA 180:183) binding
- F180 (≠ Q184) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ A218) binding
- S230 (= S234) binding
- E251 (= E255) binding
- N286 (≠ V290) 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 (≠ K339) binding
- E443 (≠ S446) binding
- H449 (≠ F452) 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)
38% identity, 94% coverage: 28:480/484 of query aligns to 22:475/477 of 2impA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E381 (= E386), A458 (≠ E463)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I153), L148 (≠ T154), P149 (= P155), W150 (= W156), K174 (= K180), E177 (≠ A183), F178 (≠ Q184), G207 (≠ A213), G211 (= G217), Q212 (≠ A218), S228 (= S234), A231 (≠ V237), K234 (≠ E240), R334 (≠ K339)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
38% identity, 94% coverage: 28:480/484 of query aligns to 22:475/477 of 2iluA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E381 (= E386), A458 (≠ E463)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I153), L148 (≠ T154), P149 (= P155), W150 (= W156), K174 (= K180), S176 (≠ A182), E177 (≠ A183), R206 (≠ S212), G207 (≠ A213), G211 (= G217), Q212 (≠ A218), S228 (= S234), A231 (≠ V237), K234 (≠ E240), I235 (≠ L241), N328 (≠ D333), R334 (≠ K339), F383 (= F388)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
38% identity, 94% coverage: 28:480/484 of query aligns to 22:475/477 of 2opxA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E381 (= E386), A458 (≠ E463)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y111), F152 (= F158), N284 (≠ V290), F312 (≠ T318), G313 (= G319), R318 (vs. gap), D320 (≠ G325), I321 (≠ V326), A322 (≠ I327), Y362 (≠ F367), F440 (≠ I445), F440 (≠ I445), E441 (≠ S446)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
37% identity, 97% coverage: 11:478/484 of query aligns to 6:478/489 of 4cazA
- active site: N152 (= N157), K175 (= K180), E251 (= E255), C285 (= C289), E386 (= E386), E463 (= E463)
- 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 (= I153), G149 (≠ T154), W151 (= W156), N152 (= N157), K175 (= K180), E178 (≠ A183), G208 (≠ A213), G212 (= G217), F226 (= F231), T227 (= T232), G228 (= G233), G229 (≠ S234), T232 (≠ V237), V236 (≠ L241), E251 (= E255), L252 (= L256), C285 (= C289), E386 (= E386), F388 (= F388)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
37% identity, 97% coverage: 11:478/484 of query aligns to 6:478/489 of 2woxA
- active site: N152 (= N157), K175 (= K180), E251 (= E255), C285 (= C289), E386 (= E386), E463 (= E463)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I153), G149 (≠ T154), W151 (= W156), N152 (= N157), K175 (= K180), S177 (≠ A182), E178 (≠ A183), G208 (≠ A213), G212 (= G217), F226 (= F231), T227 (= T232), G228 (= G233), G229 (≠ S234), T232 (≠ V237), V236 (≠ L241), E251 (= E255), L252 (= L256), C285 (= C289), E386 (= E386), F388 (= F388)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
37% identity, 97% coverage: 11:478/484 of query aligns to 6:478/489 of 2wmeA
- active site: N152 (= N157), K175 (= K180), E251 (= E255), C285 (= C289), E386 (= E386), E463 (= E463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T154), W151 (= W156), K175 (= K180), S177 (≠ A182), E178 (≠ A183), G208 (≠ A213), G212 (= G217), F226 (= F231), G228 (= G233), G229 (≠ S234), T232 (≠ V237), V236 (≠ L241)
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)
37% identity, 97% coverage: 11:478/484 of query aligns to 7:479/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 154:157) binding
- K162 (= K166) active site, Charge relay system
- KPSE 176:179 (≠ KPAA 180:183) binding
- G209 (≠ A213) binding
- GTST 230:233 (≠ STEV 234:237) binding
- E252 (= E255) active site, Proton acceptor
- C286 (= C289) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E386) binding
- E464 (= E463) active site, Charge relay system
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)
37% identity, 97% coverage: 10:478/484 of query aligns to 8:482/497 of P17202
- I28 (≠ N31) binding
- D96 (≠ E97) binding
- SPW 156:158 (≠ TPW 154:156) binding
- Y160 (≠ F158) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R165) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAA 180:183) binding
- L186 (≠ Q184) binding
- SSAT 236:239 (≠ STEV 234:237) binding
- V251 (≠ I249) binding in other chain
- L258 (= L256) binding
- W285 (≠ R283) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E386) binding
- A441 (≠ M437) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S446) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F452) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K456) binding
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
40% identity, 96% coverage: 14:480/484 of query aligns to 8:474/476 of 5x5uA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E380 (= E386), E457 (= E463)
- binding glycerol: D15 (≠ E21), A16 (= A22), A17 (≠ D23), G19 (≠ K25)
- binding nicotinamide-adenine-dinucleotide: P149 (= P155), P207 (≠ A213), A208 (≠ R214), S211 (≠ G217), G227 (= G233), S228 (= S234), V231 (= V237), R329 (≠ P335), R330 (≠ A336), E380 (= E386), F382 (= F388)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
40% identity, 96% coverage: 14:480/484 of query aligns to 8:474/476 of 5x5tA
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
37% identity, 97% coverage: 10:478/484 of query aligns to 6:480/495 of 4v37A
- active site: N157 (= N157), K180 (= K180), E255 (= E255), A289 (≠ C289), E388 (= E386), E465 (= E463)
- binding 3-aminopropan-1-ol: C448 (≠ S446), W454 (≠ F452)
- binding nicotinamide-adenine-dinucleotide: I153 (= I153), S154 (≠ T154), P155 (= P155), W156 (= W156), N157 (= N157), M162 (= M162), K180 (= K180), S182 (≠ A182), E183 (≠ A183), G213 (≠ A213), G217 (= G217), A218 (= A218), T232 (= T232), G233 (= G233), S234 (= S234), T237 (≠ V237), E255 (= E255), L256 (= L256), A289 (≠ C289), E388 (= E386), F390 (= F388)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
36% identity, 96% coverage: 19:482/484 of query aligns to 11:479/494 of 5izdA
- active site: N149 (= N157), K172 (= K180), E247 (= E255), C281 (= C289), E381 (= E386), E458 (= E463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I153), T146 (= T154), W148 (= W156), K172 (= K180), P173 (= P181), S174 (≠ A182), S175 (≠ A183), R204 (≠ S212), G205 (≠ A213), G209 (= G217), D210 (≠ A218), G225 (= G233), S226 (= S234), T229 (≠ V237)
Query Sequence
>SMc02780 SMc02780 succinate-semialdehyde dehydrogenase [NADP+] protein
MNLKDPSLFRQAALVGETWIEADPKNAIEVNNPATGEIIGRVPKLGAADTRTAIEAAARV
QKEWAARTAKERSAVLRRWFELMIENKDDLGRILTMEQGKPLAEATGEIVYGASFIEWFA
EEARRVYGDLVPGHQKDKRILVMKQPIGVVAAITPWNFPNAMITRKAGPALAAGCAMVLK
PAAQTPFSAIAIAVLAERAGMPKGLFSVITGSAREIGAEMTSNPTVRKLTFTGSTEVGAE
LYRQSAATIKKLGLELGGNAPFIVFDDADLDAAVEGALIAKFRNNGQTCVCANRIYVQDG
VYEAFSDKLAQAVAKLKTGNGMEDGVILGPLIDQPALKKVEEHVADALAKGARVVQGGRR
HSLGGTFYEATVLADVTQAMAVAREETFGPVAPLFRFKDESDVIAQANDTEFGLASYFYA
KDLARVFRVAEALEYGMVGVNTGLISTAEAPFGGVKLSGLGREGSKYGIEEFMEIKYVCL
GGIA
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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