SitesBLAST
Comparing AO353_28230 AO353_28230 succinate-semialdehyde 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)
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)
61% identity, 99% coverage: 5:483/485 of query aligns to 2:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
61% identity, 99% coverage: 5:483/485 of query aligns to 1:480/481 of 3jz4A
- active site: N156 (= N160), K179 (= K183), E254 (= E258), C288 (= C292), E385 (= E388), E462 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P158), W155 (= W159), K179 (= K183), A181 (≠ S185), S182 (≠ D186), A212 (≠ P216), G216 (= G220), G232 (= G236), S233 (= S237), I236 (≠ V240), C288 (= C292), K338 (= K342), E385 (= E388), F387 (= F390)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
56% identity, 99% coverage: 6:485/485 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I156), T153 (= T157), P154 (= P158), K179 (= K183), A212 (≠ P216), K213 (≠ A217), F230 (= F234), T231 (= T235), G232 (= G236), S233 (= S237), V236 (= V240), W239 (≠ L243), G256 (= G260)
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)
54% identity, 98% coverage: 10:485/485 of query aligns to 57:535/535 of P51649
- C93 (≠ M48) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G131) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P135) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P137) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R168) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C178) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPSD 183:186) binding
- T233 (= T188) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A192) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N210) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G220) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTAVG 236:241) binding
- R334 (= R286) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N287) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C292) modified: Disulfide link with 342, In inhibited form
- C342 (= C294) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (= N323) natural variant: N -> S
- P382 (= P333) to L: in SSADHD; 2% of activity
- V406 (≠ L357) to I: in dbSNP:rs143741652
- G409 (= G360) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S448) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G483) 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)
53% identity, 98% coverage: 10:485/485 of query aligns to 7:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
53% identity, 98% coverage: 10:485/485 of query aligns to 7:485/485 of 2w8qA
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
40% identity, 96% coverage: 17:482/485 of query aligns to 8:475/477 of 2opxA
- active site: N151 (= N160), K174 (= K183), E249 (= E258), C283 (= C292), E381 (= E388), A458 (≠ E465)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y114), F152 (= F161), N284 (≠ V293), F312 (≠ V321), G313 (= G322), R318 (vs. gap), D320 (= D328), I321 (≠ V329), A322 (≠ T330), Y362 (≠ F369), F440 (≠ I447), F440 (≠ I447), E441 (≠ S448)
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)
39% identity, 96% coverage: 17:482/485 of query aligns to 10:477/479 of P25553
- L150 (≠ T157) binding
- R161 (= R168) binding
- KPSE 176:179 (≠ KPSD 183:186) binding
- F180 (≠ L187) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ E221) binding
- S230 (= S237) binding
- E251 (= E258) binding
- N286 (≠ V293) 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 (≠ K342) binding
- E443 (≠ S448) binding
- H449 (≠ F454) 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)
39% identity, 96% coverage: 17:482/485 of query aligns to 8:475/477 of 2impA
- active site: N151 (= N160), K174 (= K183), E249 (= E258), C283 (= C292), E381 (= E388), A458 (≠ E465)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I156), L148 (≠ T157), P149 (= P158), W150 (= W159), K174 (= K183), E177 (≠ D186), F178 (≠ L187), G207 (≠ P216), G211 (= G220), Q212 (≠ E221), S228 (= S237), A231 (≠ V240), K234 (≠ L243), R334 (≠ K342)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
39% identity, 96% coverage: 17:482/485 of query aligns to 8:475/477 of 2iluA
- active site: N151 (= N160), K174 (= K183), E249 (= E258), C283 (= C292), E381 (= E388), A458 (≠ E465)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I156), L148 (≠ T157), P149 (= P158), W150 (= W159), K174 (= K183), S176 (= S185), E177 (≠ D186), R206 (≠ M215), G207 (≠ P216), G211 (= G220), Q212 (≠ E221), S228 (= S237), A231 (≠ V240), K234 (≠ L243), I235 (≠ L244), N328 (= N336), R334 (≠ K342), F383 (= F390)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% identity, 96% coverage: 18:482/485 of query aligns to 9:474/476 of 5x5uA
- active site: N151 (= N160), K174 (= K183), E249 (= E258), C283 (= C292), E380 (= E388), E457 (= E465)
- binding glycerol: D15 (≠ G24), A16 (= A25), A17 (≠ D26), G19 (≠ A28)
- binding nicotinamide-adenine-dinucleotide: P149 (= P158), P207 (= P216), A208 (= A217), S211 (≠ G220), G227 (= G236), S228 (= S237), V231 (= V240), R329 (≠ A338), R330 (≠ A339), E380 (= E388), F382 (= F390)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
41% identity, 96% coverage: 18:482/485 of query aligns to 9:474/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 96% coverage: 17:482/485 of query aligns to 5:475/477 of 6j76A
- active site: N148 (= N160), E246 (= E258), C280 (= C292), E458 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I156), T145 (= T157), A146 (≠ P158), W147 (= W159), N148 (= N160), K171 (= K183), T173 (≠ S185), S174 (≠ D186), G204 (≠ P216), G208 (= G220), T223 (= T235), G224 (= G236), S225 (= S237), A228 (≠ V240), S231 (≠ L243), I232 (≠ L244), E246 (= E258), L247 (= L259), C280 (= C292), E381 (= E388), F383 (= F390), H447 (≠ F454)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
37% identity, 95% coverage: 17:479/485 of query aligns to 7:474/489 of 4o6rA
- active site: N150 (= N160), K173 (= K183), E248 (= E258), C282 (= C292), E383 (= E388), E460 (= E465)
- binding adenosine monophosphate: I146 (= I156), V147 (≠ T157), K173 (= K183), G206 (≠ P216), G210 (= G220), Q211 (≠ E221), F224 (= F234), G226 (= G236), S227 (= S237), T230 (≠ V240), R233 (≠ L243)
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
37% identity, 97% coverage: 12:482/485 of query aligns to 16:491/505 of 4neaA
- active site: N166 (= N160), K189 (= K183), E264 (= E258), C298 (= C292), E399 (= E388), E476 (= E465)
- binding nicotinamide-adenine-dinucleotide: P164 (= P158), K189 (= K183), E192 (≠ D186), G222 (≠ P216), G226 (= G220), G242 (= G236), G243 (≠ S237), T246 (≠ V240), H249 (≠ L243), I250 (≠ L244), C298 (= C292), E399 (= E388), F401 (= F390)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
36% identity, 96% coverage: 17:482/485 of query aligns to 6:475/494 of 5izdA
- active site: N149 (= N160), K172 (= K183), E247 (= E258), C281 (= C292), E381 (= E388), E458 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I156), T146 (= T157), W148 (= W159), K172 (= K183), P173 (= P184), S174 (= S185), S175 (≠ D186), R204 (≠ M215), G205 (≠ P216), G209 (= G220), D210 (≠ E221), G225 (= G236), S226 (= S237), T229 (≠ V240)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
38% identity, 95% coverage: 17:479/485 of query aligns to 21:493/498 of 4go2A
- active site: N170 (= N160), K193 (= K183), E269 (= E258), C303 (= C292), E400 (= E388), D479 (≠ E465)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I156), I167 (≠ T157), P168 (= P158), W169 (= W159), K193 (= K183), A195 (≠ S185), Q196 (≠ D186), S225 (≠ M215), G226 (≠ P216), G230 (= G220), Q231 (≠ E221), F244 (= F234), G246 (= G236), S247 (= S237), V250 (= V240), I254 (≠ L244), E269 (= E258), G271 (= G260), C303 (= C292), E400 (= E388), F402 (= F390)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
38% identity, 95% coverage: 17:479/485 of query aligns to 21:493/498 of 2o2rA
- active site: N170 (= N160), K193 (= K183), E269 (= E258), C303 (= C292), E400 (= E388), D479 (≠ E465)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I156), I167 (≠ T157), W169 (= W159), K193 (= K183), A195 (≠ S185), Q196 (≠ D186), S225 (≠ M215), G226 (≠ P216), G230 (= G220), Q231 (≠ E221), F244 (= F234), S247 (= S237), V250 (= V240), I254 (≠ L244)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
38% identity, 95% coverage: 17:479/485 of query aligns to 106:578/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K183), S310 (≠ M215), G311 (≠ P216), G315 (= G220), G331 (= G236), S332 (= S237), V335 (= V240)
- binding 4'-phosphopantetheine: K201 (= K109), F382 (≠ R286), N387 (≠ T291), C388 (= C292), N545 (≠ I446)
P28037 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; FBP-CI; EC 1.5.1.6 from Rattus norvegicus (Rat) (see 5 papers)
38% identity, 95% coverage: 17:479/485 of query aligns to 425:897/902 of P28037
- IPW 571:573 (≠ TPW 157:159) binding
- KPAQ 597:600 (≠ KPSD 183:186) binding
- GSLVGQ 630:635 (≠ PAGIGE 216:221) binding
- GS 650:651 (= GS 236:237) binding
- E673 (= E258) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 258:259) binding
- C707 (= C292) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K342) binding
- ESF 804:806 (≠ ETF 388:390) binding
Sites not aligning to the query:
- 142 Essential for catalytic activity; D→A: Loss of formyltetrahydrofolate dehydrogenase activity. Loss of formyltetrahydrofolate hydrolase activity. No effect on aldehyde dehydrogenase activity.
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation. Loss of formyltetrahydrofolate dehydrogenase activity. No effect on hydrolase and aldehyde dehydrogenase activities in vitro.
Query Sequence
>AO353_28230 AO353_28230 succinate-semialdehyde dehydrogenase
MLKNRLKDPSLLAELAYIDGQWIGADNAATLDVIDPANGQLLARVPAMQGTETRRAIDAA
EKAWPAWRARPAAERAALLERWYQAMIDNLDDLALIMTCEQGKPLNEAKGEIRYGAGFVK
WFAEEARRVYGETIPAPSGDRRLLTLKQPVGVCAAITPWNFPNAMITRKCAPALAAGCPI
IVKPSDLTPLSALALAVLAERVGIPAGVFNVLTGMPAGIGEELTGNPSVRKISFTGSTAV
GRLLMRQSAEHIKRLSLELGGNAPFIVFDDADLEQAVAGIMLSKFRNAGQTCVCANRILV
QDGIYERFAQRLVEEVGKLKVGNGLDADVTIGPLINPAAVSKVARHIDDALSQGARLLCG
GIPEGDSQFVQPTVLGDAHAGMLLANEETFGPVAPLMRFTEEAEALALANATPYGLGAYY
FTQDLRRSWRFGEALEFGMVGLNTGIISMEVAPFGGIKQSGLGREGSKYGLDEYLEVKAF
HIGGL
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