SitesBLAST
Comparing AO353_11505 AO353_11505 succinate-semialdehyde 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)
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)
81% 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)
81% 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 (= S183), A212 (= A213), G216 (= G217), G232 (= G233), S233 (= S234), I236 (= I237), C288 (= C289), K338 (= K339), E385 (= E384), F387 (= F386)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
64% identity, 99% coverage: 3:479/480 of query aligns to 2:480/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I153), T153 (= T154), P154 (= P155), K179 (= K180), A212 (= A213), K213 (≠ G214), F230 (= F231), T231 (= T232), G232 (= G233), S233 (= S234), V236 (≠ I237), W239 (≠ Q240), 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)
56% identity, 98% coverage: 8:479/480 of query aligns to 58:533/535 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 (≠ KPAS 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 (≠ GSTEIG 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.
- G533 (= G479) 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, 98% coverage: 8:479/480 of query aligns to 8:483/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
55% identity, 98% coverage: 8:479/480 of query aligns to 8:483/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
43% identity, 97% coverage: 12:478/480 of query aligns to 6:474/476 of 5x5uA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E380 (= E384), E457 (= E461)
- binding glycerol: D15 (= D21), A16 (= A22), A17 (≠ D23), G19 (= G25)
- binding nicotinamide-adenine-dinucleotide: P149 (= P155), P207 (≠ A213), A208 (≠ G214), S211 (≠ G217), G227 (= G233), S228 (= S234), V231 (≠ I237), R329 (≠ K335), R330 (≠ A336), E380 (= E384), F382 (= F386)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
43% identity, 97% coverage: 12:478/480 of query aligns to 6:474/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
39% identity, 97% coverage: 10:474/480 of query aligns to 1:471/477 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 (= S183), G204 (≠ A213), G208 (= G217), T223 (= T232), G224 (= G233), S225 (= S234), A228 (≠ I237), S231 (≠ Q240), I232 (≠ L241), E246 (= E255), L247 (= L256), C280 (= C289), E381 (= E384), F383 (= F386), H447 (≠ F450)
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)
41% identity, 97% coverage: 11:474/480 of query aligns to 8:480/497 of P17202
- I28 (≠ T31) 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 (≠ KPAS 180:183) binding
- L186 (≠ Q184) binding
- SSAT 236:239 (≠ STEI 234:237) binding
- V251 (≠ I249) binding in other chain
- L258 (= L256) binding
- W285 (≠ R283) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E384) binding
- A441 (≠ M435) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S444) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F450) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K454) binding
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
41% identity, 97% coverage: 11:474/480 of query aligns to 6:478/495 of 4v37A
- active site: N157 (= N157), K180 (= K180), E255 (= E255), A289 (≠ C289), E388 (= E384), E465 (= E461)
- binding 3-aminopropan-1-ol: C448 (≠ S444), W454 (≠ F450)
- binding nicotinamide-adenine-dinucleotide: I153 (= I153), S154 (≠ T154), P155 (= P155), W156 (= W156), N157 (= N157), M162 (= M162), K180 (= K180), S182 (≠ A182), E183 (≠ S183), G213 (≠ A213), G217 (= G217), A218 (≠ S218), T232 (= T232), G233 (= G233), S234 (= S234), T237 (≠ I237), E255 (= E255), L256 (= L256), A289 (≠ C289), E388 (= E384), F390 (= F386)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
38% identity, 98% coverage: 4:474/480 of query aligns to 11:492/498 of 4go2A
- active site: N170 (= N157), K193 (= K180), E269 (= E255), C303 (= C289), E400 (= E384), D479 (≠ E461)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I153), I167 (≠ T154), P168 (= P155), W169 (= W156), K193 (= K180), A195 (= A182), Q196 (≠ S183), S225 (= S212), G226 (≠ A213), G230 (= G217), Q231 (≠ S218), F244 (= F231), G246 (= G233), S247 (= S234), V250 (≠ I237), I254 (≠ L241), E269 (= E255), G271 (= G257), C303 (= C289), E400 (= E384), F402 (= F386)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
38% identity, 98% coverage: 4:474/480 of query aligns to 11:492/498 of 2o2rA
- active site: N170 (= N157), K193 (= K180), E269 (= E255), C303 (= C289), E400 (= E384), D479 (≠ E461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I153), I167 (≠ T154), W169 (= W156), K193 (= K180), A195 (= A182), Q196 (≠ S183), S225 (= S212), G226 (≠ A213), G230 (= G217), Q231 (≠ S218), F244 (= F231), S247 (= S234), V250 (≠ I237), I254 (≠ L241)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
38% identity, 97% coverage: 14:478/480 of query aligns to 8:475/477 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 (≠ I318), G313 (= G319), R318 (≠ E324), D320 (vs. gap), I321 (≠ T326), A322 (≠ T327), Y362 (≠ F365), F440 (≠ I443), F440 (≠ I443), E441 (≠ S444)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
38% identity, 98% coverage: 4:474/480 of query aligns to 96:577/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K180), S310 (= S212), G311 (≠ A213), G315 (= G217), G331 (= G233), S332 (= S234), V335 (≠ I237)
- binding 4'-phosphopantetheine: K201 (= K106), F382 (≠ R283), N387 (≠ T288), C388 (= C289), N545 (≠ L442)
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, 97% coverage: 14:478/480 of query aligns to 10:477/479 of P25553
- L150 (≠ T154) binding
- R161 (= R165) binding
- KPSE 176:179 (≠ KPAS 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 (≠ S218) 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)
38% identity, 97% coverage: 14:478/480 of query aligns to 8:475/477 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 (≠ S183), F178 (≠ Q184), G207 (≠ A213), G211 (= G217), Q212 (≠ S218), S228 (= S234), A231 (≠ I237), K234 (≠ Q240), R334 (≠ K339)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
38% identity, 97% coverage: 14:478/480 of query aligns to 8:475/477 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 (≠ S183), R206 (≠ S212), G207 (≠ A213), G211 (= G217), Q212 (≠ S218), S228 (= S234), A231 (≠ I237), K234 (≠ Q240), I235 (≠ L241), N328 (≠ D333), R334 (≠ K339), F383 (= F386)
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, 98% coverage: 4:474/480 of query aligns to 415:896/902 of P28037
- IPW 571:573 (≠ TPW 154:156) binding
- KPAQ 597:600 (≠ KPAS 180:183) binding
- GSLVGQ 630:635 (≠ AGDIGS 213:218) binding
- GS 650:651 (= GS 233:234) binding
- E673 (= E255) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 255:256) binding
- C707 (= C289) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K339) binding
- ESF 804:806 (≠ ETF 384:386) 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.
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, 98% coverage: 9:476/480 of query aligns to 16:491/505 of 4neaA
- active site: N166 (= N157), K189 (= K180), E264 (= E255), C298 (= C289), E399 (= E384), E476 (= E461)
- binding nicotinamide-adenine-dinucleotide: P164 (= P155), K189 (= K180), E192 (≠ S183), G222 (≠ A213), G226 (= G217), G242 (= G233), G243 (≠ S234), T246 (≠ I237), H249 (≠ Q240), I250 (≠ L241), C298 (= C289), E399 (= E384), F401 (= F386)
Query Sequence
>AO353_11505 AO353_11505 succinate-semialdehyde dehydrogenase
MQLKDTLLFRQQAFIDGAWVDADNGQTINVTNPATGEILGTVPKMGAAETRRAIEAADKA
LPAWRALTAKERANKLRRWFELIIENQDDLARLMTLEQGKPLAEAKGEIVYAASFIEWFA
EEAKRIYGDVIPGHQPDKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLK
PASQTPYSAFALAELAQRAGIPKGVLSVVTGSAGDIGSELTSNPIVRKLSFTGSTEIGRQ
LMAECAKDIKKVSLELGGNAPFIVFDDADLDKAVEGAIISKYRNNGQTCVCANRLYIQDS
VYDAFAEKLKVAVAKLKIGNGLEEGTTTGPLIDGKAVAKVQEHIADALSKGATLLAGGKV
MEGNFFEPTILTNVPKSAAVAKEETFGPLAPLFRFKDEAEVIAMSNDTEFGLASYFYARD
LGRVFRVAEALEYGMVGVNTGLISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYLCLGI
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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