SitesBLAST
Comparing GFF3587 Psest_3654 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)
69% identity, 99% coverage: 3:486/488 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
69% identity, 99% coverage: 4:486/488 of query aligns to 1:480/481 of 3jz4A
- active site: N156 (= N159), K179 (= K182), E254 (= E260), C288 (= C294), E385 (= E391), E462 (= E468)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P157), W155 (= W158), K179 (= K182), A181 (= A184), S182 (≠ P185), A212 (= A215), G216 (= G222), G232 (= G238), S233 (= S239), I236 (≠ V242), C288 (= C294), K338 (= K344), E385 (= E391), F387 (= F393)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
61% identity, 99% coverage: 5:488/488 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I155), T153 (= T156), P154 (= P157), K179 (= K182), A212 (= A215), K213 (≠ R219), F230 (= F236), T231 (= T237), G232 (= G238), S233 (= S239), V236 (= V242), W239 (≠ K245), G256 (= G262)
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: 10:488/488 of query aligns to 58:535/535 of P51649
- C93 (≠ M47) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G130) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P134) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ H136) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R167) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C177) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAP 182:185) binding
- T233 (= T187) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A191) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S209) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G222) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTAVG 238:243) binding
- R334 (= R288) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N289) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C294) modified: Disulfide link with 342, In inhibited form
- C342 (= C296) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (= N325) natural variant: N -> S
- P382 (= P335) to L: in SSADHD; 2% of activity
- V406 (≠ L359) to I: in dbSNP:rs143741652
- G409 (= G362) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S451) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G486) 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)
56% identity, 98% coverage: 10:488/488 of query aligns to 8:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
56% identity, 98% coverage: 10:488/488 of query aligns to 8:485/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% identity, 96% coverage: 17:485/488 of query aligns to 9:474/476 of 5x5uA
- active site: N151 (= N159), K174 (= K182), E249 (= E260), C283 (= C294), E380 (= E391), E457 (= E468)
- binding glycerol: D15 (≠ E23), A16 (= A24), A17 (≠ D25), G19 (= G27)
- binding nicotinamide-adenine-dinucleotide: P149 (= P157), P207 (≠ A215), A208 (= A216), S211 (≠ G222), G227 (= G238), S228 (= S239), V231 (= V242), R329 (≠ A340), R330 (≠ A341), E380 (= E391), F382 (= F393)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
41% identity, 96% coverage: 17:485/488 of query aligns to 9:474/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
37% identity, 95% coverage: 16:481/488 of query aligns to 5:471/477 of 6j76A
- active site: N148 (= N159), E246 (= E260), C280 (= C294), E458 (= E468)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I155), T145 (= T156), A146 (≠ P157), W147 (= W158), N148 (= N159), K171 (= K182), T173 (≠ A184), S174 (≠ P185), G204 (≠ A215), G208 (= G222), T223 (= T237), G224 (= G238), S225 (= S239), A228 (≠ V242), S231 (≠ K245), I232 (≠ L246), E246 (= E260), L247 (= L261), C280 (= C294), E381 (= E391), F383 (= F393), H447 (≠ F457)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
37% identity, 97% coverage: 11:485/488 of query aligns to 3:475/477 of 2opxA
- active site: N151 (= N159), K174 (= K182), E249 (= E260), C283 (= C294), E381 (= E391), A458 (≠ E468)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y113), F152 (= F160), N284 (≠ V295), F312 (≠ V323), G313 (= G324), R318 (≠ E329), D320 (vs. gap), I321 (≠ V331), A322 (≠ T332), Y362 (≠ F372), F440 (≠ I450), F440 (≠ I450), E441 (≠ S451)
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, 97% coverage: 11:485/488 of query aligns to 5:477/479 of P25553
- L150 (≠ T156) binding
- R161 (= R167) binding
- KPSE 176:179 (≠ KPAP 182:185) binding
- F180 (≠ Q186) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ A223) binding
- S230 (= S239) binding
- E251 (= E260) binding
- N286 (≠ V295) 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 (≠ K344) binding
- E443 (≠ S451) binding
- H449 (≠ F457) 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, 97% coverage: 11:485/488 of query aligns to 3:475/477 of 2impA
- active site: N151 (= N159), K174 (= K182), E249 (= E260), C283 (= C294), E381 (= E391), A458 (≠ E468)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I155), L148 (≠ T156), P149 (= P157), W150 (= W158), K174 (= K182), E177 (≠ P185), F178 (≠ Q186), G207 (≠ A215), G211 (= G222), Q212 (≠ A223), S228 (= S239), A231 (≠ V242), K234 (= K245), R334 (≠ K344)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
37% identity, 97% coverage: 11:485/488 of query aligns to 3:475/477 of 2iluA
- active site: N151 (= N159), K174 (= K182), E249 (= E260), C283 (= C294), E381 (= E391), A458 (≠ E468)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I155), L148 (≠ T156), P149 (= P157), W150 (= W158), K174 (= K182), S176 (≠ A184), E177 (≠ P185), R206 (≠ D214), G207 (≠ A215), G211 (= G222), Q212 (≠ A223), S228 (= S239), A231 (≠ V242), K234 (= K245), I235 (≠ L246), N328 (≠ D338), R334 (≠ K344), F383 (= F393)
7radA Crystal structure analysis of aldh1b1
39% identity, 98% coverage: 7:485/488 of query aligns to 7:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I155), I159 (≠ T156), P160 (= P157), W161 (= W158), N162 (= N159), M167 (= M164), K185 (= K182), E188 (≠ P185), G218 (≠ A215), G222 (= G222), A223 (= A223), T237 (= T237), G238 (= G238), S239 (= S239), V242 (= V242), E261 (= E260), L262 (= L261), C295 (= C294), E392 (= E391), F394 (= F393)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ Y113), F163 (= F160), E285 (≠ I284), F289 (≠ R288), N450 (≠ V449), V452 (≠ S451)
7mjdA Crystal structure analysis of aldh1b1
39% identity, 98% coverage: 7:485/488 of query aligns to 7:486/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I155), I159 (≠ T156), P160 (= P157), W161 (= W158), N162 (= N159), M167 (= M164), K185 (= K182), E188 (≠ P185), G218 (≠ A215), G222 (= G222), F236 (= F236), T237 (= T237), G238 (= G238), S239 (= S239), V242 (= V242), E261 (= E260), L262 (= L261), C295 (= C294), E392 (= E391), F394 (= F393)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ Y113), E285 (≠ I284), F289 (≠ R288), N450 (≠ V449), V452 (≠ S451)
7mjcA Crystal structure analysis of aldh1b1
39% identity, 98% coverage: 7:485/488 of query aligns to 7:486/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I155), I159 (≠ T156), P160 (= P157), W161 (= W158), N162 (= N159), K185 (= K182), E188 (≠ P185), G218 (≠ A215), G222 (= G222), T237 (= T237), G238 (= G238), S239 (= S239), V242 (= V242), E261 (= E260), L262 (= L261), C295 (= C294), E392 (= E391), F394 (= F393)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 95% coverage: 16:481/488 of query aligns to 9:474/486 of 4pxlA
- active site: N154 (= N159), K177 (= K182), E253 (= E260), C287 (= C294), E384 (= E391), D461 (≠ E468)
- binding nicotinamide-adenine-dinucleotide: I150 (= I155), V151 (≠ T156), P152 (= P157), W153 (= W158), K177 (= K182), E180 (≠ P185), G210 (≠ A215), G214 (= G222), A215 (= A223), F228 (= F236), G230 (= G238), S231 (= S239), V234 (= V242), E253 (= E260), G255 (= G262), C287 (= C294), Q334 (≠ A341), K337 (= K344), E384 (= E391), F386 (= F393)
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)
38% identity, 96% coverage: 13:481/488 of query aligns to 7:477/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 156:159) binding
- K162 (= K168) active site, Charge relay system
- KPSE 176:179 (≠ KPAP 182:185) binding
- G209 (≠ S218) binding
- GTST 230:233 (≠ STAV 239:242) binding
- E252 (= E260) active site, Proton acceptor
- C286 (= C294) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E391) binding
- E464 (= E468) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
38% identity, 96% coverage: 13:481/488 of query aligns to 6:476/489 of 4cazA
- active site: N152 (= N159), K175 (= K182), E251 (= E260), C285 (= C294), E386 (= E391), E463 (= E468)
- 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 (= I155), G149 (≠ T156), W151 (= W158), N152 (= N159), K175 (= K182), E178 (≠ P185), G208 (≠ S218), G212 (= G222), F226 (= F236), T227 (= T237), G228 (= G238), G229 (≠ S239), T232 (≠ V242), V236 (≠ L246), E251 (= E260), L252 (= L261), C285 (= C294), E386 (= E391), F388 (= F393)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
38% identity, 96% coverage: 13:481/488 of query aligns to 6:476/489 of 2woxA
- active site: N152 (= N159), K175 (= K182), E251 (= E260), C285 (= C294), E386 (= E391), E463 (= E468)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I155), G149 (≠ T156), W151 (= W158), N152 (= N159), K175 (= K182), S177 (≠ A184), E178 (≠ P185), G208 (≠ S218), G212 (= G222), F226 (= F236), T227 (= T237), G228 (= G238), G229 (≠ S239), T232 (≠ V242), V236 (≠ L246), E251 (= E260), L252 (= L261), C285 (= C294), E386 (= E391), F388 (= F393)
Query Sequence
>GFF3587 Psest_3654 succinate-semialdehyde dehydrogenase
MTLQLGQPDLLRQTAYLNGEWCEADSGARTEIFNPATGELIGAVPNMGRGETRRAIEAAQ
AAQPAWRALTAKERAARLRRWYELMLENQEDLARIMTAEQGKPLAEARGEVAYAASFLEW
FAEEGKRLYGDVIPAHAGDKRILVQKEPVGVTAAITPWNFPSAMITRKAGPALAAGCAMV
LKPAPQTPFSALALAALAERAGIPAGLLSVITADAATSREVGAELCENPIVRKLSFTGST
AVGIKLMQQCAPTLKKLSLELGGNAPFIVFDDADLDAAVEGAMISKYRNAGQTCVCANRI
YVQDGIYDAFVDKLSAAVARLKVGNGAEEGVTTGPLIDAAAVAKVQRHLQDALDKGATLL
AGGKPHALGGNFFEPTLVGGVTSEMAVAREETFGPLAPLFRFRDEDEVIRQANDTEFGLA
AYFYARDLSRVFRVAEALEYGMVGINTGVISTEVAPFGGMKASGLGREGSKYGLDEYVEI
KYLCLGGI
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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