SitesBLAST
Comparing 6938534 Sama_2637 succinate-semialdehyde dehydrogenase (NAD(P)(+)) (RefSeq) 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)
70% identity, 100% coverage: 1:480/480 of query aligns to 1:482/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
70% identity, 100% coverage: 2:480/480 of query aligns to 1:481/481 of 3jz4A
- active site: N156 (= N157), K179 (= K180), E254 (= E255), C288 (= C289), E385 (= E384), E462 (= E461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P155), W155 (= W156), K179 (= K180), A181 (= A182), S182 (≠ P183), A212 (= A213), G216 (= G217), G232 (= G233), S233 (= S234), I236 (≠ V237), C288 (= C289), K338 (= K339), E385 (= E384), F387 (= F386)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
61% identity, 99% coverage: 3:478/480 of query aligns to 2:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I153), T153 (= T154), P154 (= P155), K179 (= K180), A212 (= A213), K213 (≠ V214), F230 (= F231), T231 (= T232), G232 (= G233), S233 (= S234), V236 (= V237), W239 (≠ K240), 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, 98% coverage: 7:477/480 of query aligns to 57:531/535 of P51649
- C93 (≠ M45) 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 (≠ KPAP 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 (≠ GSTGVG 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 (≠ L354) to I: in dbSNP:rs143741652
- G409 (= G357) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S444) 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)
55% identity, 98% coverage: 7:477/480 of query aligns to 7:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
55% identity, 98% coverage: 7:477/480 of query aligns to 7:481/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% identity, 98% coverage: 11:478/480 of query aligns to 5:474/476 of 5x5uA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E380 (= E384), E457 (= E461)
- binding glycerol: D15 (= D21), A16 (= A22), A17 (≠ L23), G19 (= G25)
- binding nicotinamide-adenine-dinucleotide: P149 (= P155), P207 (≠ A213), A208 (≠ V214), S211 (≠ G217), G227 (= G233), S228 (= S234), V231 (= V237), R329 (≠ A335), R330 (≠ A336), E380 (= E384), F382 (= F386)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
41% identity, 98% coverage: 11:478/480 of query aligns to 5:474/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 98% coverage: 10:479/480 of query aligns to 1:476/477 of 6j76A
- active site: N148 (= N157), E246 (= E255), C280 (= C289), E458 (= E461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I153), T145 (= T154), A146 (≠ P155), W147 (= W156), N148 (= N157), K171 (= K180), T173 (≠ A182), S174 (≠ P183), G204 (≠ A213), G208 (= G217), T223 (= T232), G224 (= G233), S225 (= S234), A228 (≠ V237), S231 (≠ K240), I232 (≠ L241), E246 (= E255), L247 (= L256), C280 (= C289), E381 (= E384), F383 (= F386), H447 (≠ F450)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 97% coverage: 11:477/480 of query aligns to 6:477/486 of 4pxlA
- active site: N154 (= N157), K177 (= K180), E253 (= E255), C287 (= C289), E384 (= E384), D461 (≠ E461)
- binding nicotinamide-adenine-dinucleotide: I150 (= I153), V151 (≠ T154), P152 (= P155), W153 (= W156), K177 (= K180), E180 (≠ P183), G210 (≠ A213), G214 (= G217), A215 (≠ N218), F228 (= F231), G230 (= G233), S231 (= S234), V234 (= V237), E253 (= E255), G255 (= G257), C287 (= C289), Q334 (≠ A336), K337 (= K339), E384 (= E384), F386 (= F386)
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)
37% identity, 98% coverage: 9:479/480 of query aligns to 5:478/479 of P25553
- L150 (≠ T154) binding
- R161 (= R165) binding
- KPSE 176:179 (≠ KPAP 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 (≠ N218) 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 (≠ S444) binding
- H449 (≠ F450) 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)
37% identity, 98% coverage: 9:479/480 of query aligns to 3:476/477 of 2impA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E381 (= E384), A458 (≠ E461)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I153), L148 (≠ T154), P149 (= P155), W150 (= W156), K174 (= K180), E177 (≠ P183), F178 (≠ Q184), G207 (≠ A213), G211 (= G217), Q212 (≠ N218), S228 (= S234), A231 (≠ V237), K234 (= K240), R334 (≠ K339)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
37% identity, 98% coverage: 9:479/480 of query aligns to 3:476/477 of 2iluA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E381 (= E384), A458 (≠ E461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I153), L148 (≠ T154), P149 (= P155), W150 (= W156), K174 (= K180), S176 (≠ A182), E177 (≠ P183), R206 (≠ D212), G207 (≠ A213), G211 (= G217), Q212 (≠ N218), S228 (= S234), A231 (≠ V237), K234 (= K240), I235 (≠ L241), N328 (= N333), R334 (≠ K339), F383 (= F386)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
37% identity, 98% coverage: 9:479/480 of query aligns to 3:476/477 of 2opxA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E381 (= E384), A458 (≠ E461)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y111), F152 (= F158), N284 (≠ V290), F312 (≠ V318), G313 (= G319), R318 (≠ P324), D320 (vs. gap), I321 (≠ V326), A322 (≠ T327), Y362 (≠ F365), F440 (≠ I443), F440 (≠ I443), E441 (≠ S444)
Q28399 Aldehyde dehydrogenase, cytosolic 1; ALDH class 1; ETA-crystallin; EC 1.2.1.3 from Elephantulus edwardii (Cape long-eared elephant shrew) (see paper)
39% identity, 100% coverage: 3:480/480 of query aligns to 13:496/501 of Q28399
1o9jA The x-ray crystal structure of eta-crystallin (see paper)
39% identity, 100% coverage: 3:480/480 of query aligns to 6:489/494 of 1o9jA
- active site: N163 (= N157), K186 (= K180), E262 (= E255), C296 (= C289), E393 (= E384), E470 (= E461)
- binding nicotinamide-adenine-dinucleotide: I159 (= I153), F160 (≠ T154), P161 (= P155), W162 (= W156), N163 (= N157), K186 (= K180), E189 (≠ P183), G219 (≠ A213), G223 (= G217), F237 (= F231), T238 (= T232), G239 (= G233), S240 (= S234), V243 (= V237), E262 (= E255), L263 (= L256), C296 (= C289), E393 (= E384), F395 (= F386), L421 (= L412)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
36% identity, 98% coverage: 9:478/480 of query aligns to 1:475/494 of 5izdA
- active site: N149 (= N157), K172 (= K180), E247 (= E255), C281 (= C289), E381 (= E384), E458 (= E461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I153), T146 (= T154), W148 (= W156), K172 (= K180), P173 (= P181), S174 (≠ A182), S175 (≠ P183), R204 (≠ D212), G205 (≠ A213), G209 (= G217), D210 (≠ N218), G225 (= G233), S226 (= S234), T229 (≠ V237)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 98% coverage: 6:476/480 of query aligns to 6:484/494 of 4pz2B
- active site: N159 (= N157), K182 (= K180), E258 (= E255), C292 (= C289), E392 (= E384), D469 (≠ E461)
- binding nicotinamide-adenine-dinucleotide: I155 (= I153), I156 (≠ T154), P157 (= P155), W158 (= W156), N159 (= N157), M164 (= M162), K182 (= K180), A184 (= A182), E185 (≠ P183), G215 (≠ A213), G219 (= G217), F233 (= F231), T234 (= T232), G235 (= G233), S236 (= S234), V239 (= V237), E258 (= E255), L259 (= L256), C292 (= C289), E392 (= E384), F394 (= F386)
P00352 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Homo sapiens (Human) (see 7 papers)
38% identity, 98% coverage: 11:480/480 of query aligns to 21:496/501 of P00352
- N121 (≠ G107) to S: in dbSNP:rs1049981
- IPWN 167:170 (≠ TPWN 154:157) binding
- I177 (≠ T164) to F: in dbSNP:rs8187929
- KPAE 193:196 (≠ KPAP 180:183) binding
- GP 226:227 (≠ AV 213:214) binding
- GS 246:247 (= GS 233:234) binding
- E269 (= E255) active site, Proton acceptor
- ELG 269:271 (= ELG 255:257) binding
- C302 (≠ T288) mutation C->A,S: Does not prevent inhibition by duocarmycin analogs.
- C303 (= C289) active site, Nucleophile
- EQYDK 349:353 (≠ AALEK 335:339) binding
- EIF 400:402 (≠ ETF 384:386) binding
- G458 (≠ L442) mutation to N: No significant effect on aldehyde dehydrogenase activity. Prevents the inhibition by ALDH1A1-specific inhibitors.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
- 336:501 Mediates interaction with PRMT3
7um9A Human aldh1a1 with bound compound cm38 (see paper)
38% identity, 98% coverage: 11:480/480 of query aligns to 14:489/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I153), I160 (≠ T154), P161 (= P155), W162 (= W156), N163 (= N157), K186 (= K180), E189 (≠ P183), G219 (≠ A213), G223 (= G217), F237 (= F231), T238 (= T232), G239 (= G233), S240 (= S234), V243 (= V237), E262 (= E255), G264 (= G257), Q343 (≠ A336), K346 (= K339), E393 (= E384), F395 (= F386)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (≠ R165), H286 (≠ I279), Y290 (≠ R283), I297 (≠ V290), G451 (≠ L442)
Query Sequence
>6938534 Sama_2637 succinate-semialdehyde dehydrogenase (NAD(P)(+)) (RefSeq)
MQLKRPSLLKTKCYINGEWRDALSGETVTIANPATNEAIASVPVMGRDETREAIAAAEAA
LPAWRALTAKERGAKLRRWYELMLENADDLALMMTTEQGKPLAEAKGEVVYAASFIEWFA
EEAKRLYGDTIPGHQGDKRIMVIKQGVGVTAAITPWNFPAAMITRKAGPALAAGCTMIVK
PAPQTPFTALALAELAAEAGIPPGVFSVVTGDAVAIGNELCENPVVRKLSFTGSTGVGIK
LMQQCAPTLKKVSLELGGNAPFIVFNDADLDAAVEGAMISKYRNAGQTCVCANRLYVQDG
VYDAFAQKLAAAVAKLKVGNGAEPGVTTGPLINAAALEKVQSHLQDALDKGATLVAGGKP
LGGNFMEPAIVTNVDASMKVAREETFGPLAPLFRFSDVDDVIRQANDTEFGLAAYFYGRD
ISLIWKVAEALEYGMVGVNTGLISTEVAPFGGMKSSGLGREGSKYGIDEYVEIKYICLSV
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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