SitesBLAST
Comparing WP_011383257.1 AMB_RS04160 NAD-dependent 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)
63% identity, 96% coverage: 19:496/499 of query aligns to 5:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
63% identity, 96% coverage: 19:496/499 of query aligns to 4:480/481 of 3jz4A
- active site: N156 (= N171), K179 (= K194), E254 (= E270), C288 (= C304), E385 (= E401), E462 (= E478)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P169), W155 (= W170), K179 (= K194), A181 (= A196), S182 (≠ E197), A212 (≠ P228), G216 (= G232), G232 (= G248), S233 (= S249), I236 (≠ V252), C288 (= C304), K338 (= K354), E385 (= E401), F387 (= F403)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
56% identity, 96% coverage: 19:498/499 of query aligns to 4:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ V167), T153 (= T168), P154 (= P169), K179 (= K194), A212 (≠ P228), K213 (≠ A229), F230 (= F246), T231 (= T247), G232 (= G248), S233 (= S249), V236 (= V252), W239 (≠ L255), G256 (= G272)
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, 96% coverage: 18:498/499 of query aligns to 54:535/535 of P51649
- C93 (≠ L59) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G142) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P146) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ T148) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R179) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C189) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 194:197) binding
- T233 (= T199) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A203) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N221) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G232) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTRVG 248:253) binding
- R334 (= R298) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N299) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C304) modified: Disulfide link with 342, In inhibited form
- C342 (= C306) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ H335) natural variant: N -> S
- P382 (= P345) to L: in SSADHD; 2% of activity
- V406 (= V369) to I: in dbSNP:rs143741652
- G409 (= G372) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S461) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G496) 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, 96% coverage: 18:498/499 of query aligns to 4:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
56% identity, 96% coverage: 18:498/499 of query aligns to 4:485/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
40% identity, 94% coverage: 29:495/499 of query aligns to 9:474/476 of 5x5uA
- active site: N151 (= N171), K174 (= K194), E249 (= E270), C283 (= C304), E380 (= E401), E457 (= E478)
- binding glycerol: D15 (≠ G35), A16 (= A36), A17 (≠ D37), G19 (= G39)
- binding nicotinamide-adenine-dinucleotide: P149 (= P169), P207 (= P228), A208 (= A229), S211 (≠ G232), G227 (= G248), S228 (= S249), V231 (= V252), R329 (≠ A350), R330 (≠ A351), E380 (= E401), F382 (= F403)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
40% identity, 94% coverage: 29:495/499 of query aligns to 9:474/476 of 5x5tA
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
38% identity, 95% coverage: 23:495/499 of query aligns to 3:475/477 of 2opxA
- active site: N151 (= N171), K174 (= K194), E249 (= E270), C283 (= C304), E381 (= E401), A458 (≠ E478)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y125), F152 (= F172), N284 (≠ I305), F312 (≠ V333), G313 (= G334), R318 (≠ S338), D320 (≠ V340), I321 (≠ V341), A322 (≠ Q342), Y362 (≠ F382), F440 (≠ I460), F440 (≠ I460), E441 (≠ S461)
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, 95% coverage: 23:495/499 of query aligns to 5:477/479 of P25553
- L150 (≠ T168) binding
- R161 (= R179) binding
- KPSE 176:179 (≠ KPAE 194:197) binding
- F180 (≠ D198) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ G233) binding
- S230 (= S249) binding
- E251 (= E270) binding
- N286 (≠ I305) 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 (≠ K354) binding
- E443 (≠ S461) binding
- H449 (≠ F467) 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, 95% coverage: 23:495/499 of query aligns to 3:475/477 of 2impA
- active site: N151 (= N171), K174 (= K194), E249 (= E270), C283 (= C304), E381 (= E401), A458 (≠ E478)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (≠ V167), L148 (≠ T168), P149 (= P169), W150 (= W170), K174 (= K194), E177 (= E197), F178 (≠ D198), G207 (≠ Q227), G211 (= G232), Q212 (≠ G233), S228 (= S249), A231 (≠ V252), K234 (≠ L255), R334 (≠ K354)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
38% identity, 95% coverage: 23:495/499 of query aligns to 3:475/477 of 2iluA
- active site: N151 (= N171), K174 (= K194), E249 (= E270), C283 (= C304), E381 (= E401), A458 (≠ E478)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (≠ V167), L148 (≠ T168), P149 (= P169), W150 (= W170), K174 (= K194), S176 (≠ A196), E177 (= E197), R206 (= R226), G207 (≠ Q227), G211 (= G232), Q212 (≠ G233), S228 (= S249), A231 (≠ V252), K234 (≠ L255), I235 (≠ L256), N328 (= N348), R334 (≠ K354), F383 (= F403)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
37% identity, 95% coverage: 24:495/499 of query aligns to 1:475/477 of 6j76A
- active site: N148 (= N171), E246 (= E270), C280 (= C304), E458 (= E478)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (≠ V167), T145 (= T168), A146 (≠ P169), W147 (= W170), N148 (= N171), K171 (= K194), T173 (≠ A196), S174 (≠ E197), G204 (≠ P228), G208 (= G232), T223 (= T247), G224 (= G248), S225 (= S249), A228 (≠ V252), S231 (≠ L255), I232 (≠ L256), E246 (= E270), L247 (= L271), C280 (= C304), E381 (= E401), F383 (= F403), H447 (≠ F467)
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 95% coverage: 20:495/499 of query aligns to 15:493/501 of Q56YU0
- G152 (≠ L154) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A418) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
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)
36% identity, 94% coverage: 23:493/499 of query aligns to 16:491/505 of 4neaA
- active site: N166 (= N171), K189 (= K194), E264 (= E270), C298 (= C304), E399 (= E401), E476 (= E478)
- binding nicotinamide-adenine-dinucleotide: P164 (= P169), K189 (= K194), E192 (= E197), G222 (≠ P228), G226 (= G232), G242 (= G248), G243 (≠ S249), T246 (≠ V252), H249 (≠ L255), I250 (≠ L256), C298 (= C304), E399 (= E401), F401 (= F403)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
39% identity, 95% coverage: 20:493/499 of query aligns to 6:484/494 of 4pz2B
- active site: N159 (= N171), K182 (= K194), E258 (= E270), C292 (= C304), E392 (= E401), D469 (≠ E478)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ V167), I156 (≠ T168), P157 (= P169), W158 (= W170), N159 (= N171), M164 (= M176), K182 (= K194), A184 (= A196), E185 (= E197), G215 (≠ Q227), G219 (= G232), F233 (= F246), T234 (= T247), G235 (= G248), S236 (= S249), V239 (= V252), E258 (= E270), L259 (= L271), C292 (= C304), E392 (= E401), F394 (= F403)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
38% identity, 94% coverage: 28:494/499 of query aligns to 9:477/486 of 4pxlA
- active site: N154 (= N171), K177 (= K194), E253 (= E270), C287 (= C304), E384 (= E401), D461 (≠ E478)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ V167), V151 (≠ T168), P152 (= P169), W153 (= W170), K177 (= K194), E180 (= E197), G210 (≠ Q227), G214 (= G232), A215 (≠ G233), F228 (= F246), G230 (= G248), S231 (= S249), V234 (= V252), E253 (= E270), G255 (= G272), C287 (= C304), Q334 (≠ A351), K337 (= K354), E384 (= E401), F386 (= F403)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
36% identity, 94% coverage: 28:496/499 of query aligns to 20:489/491 of 5gtlA
- active site: N165 (= N171), K188 (= K194), E263 (= E270), C297 (= C304), E394 (= E401), E471 (= E478)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (≠ V167), P163 (= P169), K188 (= K194), A190 (= A196), E191 (= E197), Q192 (≠ D198), G221 (≠ Q227), G225 (= G232), G241 (= G248), S242 (= S249), T245 (≠ V252), L264 (= L271), C297 (= C304), E394 (= E401), F396 (= F403)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
36% identity, 94% coverage: 28:496/499 of query aligns to 20:489/491 of 5gtkA
- active site: N165 (= N171), K188 (= K194), E263 (= E270), C297 (= C304), E394 (= E401), E471 (= E478)
- binding nicotinamide-adenine-dinucleotide: I161 (≠ V167), I162 (≠ T168), P163 (= P169), W164 (= W170), K188 (= K194), E191 (= E197), G221 (≠ Q227), G225 (= G232), A226 (≠ G233), F239 (= F246), G241 (= G248), S242 (= S249), T245 (≠ V252), Y248 (≠ L255), L264 (= L271), C297 (= C304), Q344 (≠ A351), R347 (≠ K354), E394 (= E401), F396 (= F403)
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, 93% coverage: 28:493/499 of query aligns to 11:482/497 of P17202
- I28 (≠ L45) binding
- D96 (≠ E111) binding
- SPW 156:158 (≠ TPW 168:170) binding
- Y160 (≠ F172) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R179) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAE 194:197) binding
- L186 (≠ D198) binding
- SSAT 236:239 (≠ STRV 249:252) binding
- V251 (= V264) binding in other chain
- L258 (= L271) binding
- W285 (≠ R298) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E401) binding
- A441 (≠ M452) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S461) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F467) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K471) binding
Query Sequence
>WP_011383257.1 AMB_RS04160 NAD-dependent succinate-semialdehyde dehydrogenase
MLVFNVLTLSGRAAVTDLDPSLIKSHAYVDGVWVGADDGRRFDVLDPATGGLIASVPDLG
ATETRRAIDAAEAAWNPWRQRTAKDRAAVMMAWHDLIMAHQDALARLLSAEQGKPLAEAM
GEISYGASFISWFAEEGKRAYGDLIPTTASDRRLLVMKQPIGVVAAVTPWNFPMAMITRK
CAPALAAGCPVVVKPAEDTPLSALALAELAHRAGLPKGLFNIVTTRQPAAVGGEMTGNAK
VRKLSFTGSTRVGKLLMAQCAETVKKVSLELGGNAPFIVFDDCDLDAAVAGALASKYRNS
GQTCICTNRFLVQAGIYEDFAVKLAEKAAAMAVGHALSGVVQQGPLINAAAVAKVAAHVA
DAVSKGARVLTGGRPHALGGGFWQPTVLADVTPAMLCFREETFGPVAPLLRFETEAEAIA
LANASEFGLAGYFYSRDVARVFRVAEALECGMVGVNESLISNEVAPFGGIKESGLGREGS
KYGLDDFMETKYVCIGGLS
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