SitesBLAST
Comparing H281DRAFT_02680 H281DRAFT_02680 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)
67% identity, 98% coverage: 11:490/492 of query aligns to 2:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
67% identity, 98% coverage: 11:490/492 of query aligns to 1:480/481 of 3jz4A
- active site: N156 (= N166), K179 (= K189), E254 (= E264), C288 (= C298), E385 (= E395), E462 (= E472)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P164), W155 (= W165), K179 (= K189), A181 (= A191), S182 (≠ E192), A212 (≠ P222), G216 (= G226), G232 (= G242), S233 (= S243), I236 (≠ V246), C288 (= C298), K338 (= K348), E385 (= E395), F387 (= F397)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
62% identity, 98% coverage: 12:492/492 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I162), T153 (= T163), P154 (= P164), K179 (= K189), A212 (≠ P222), K213 (≠ R223), F230 (= F240), T231 (= T241), G232 (= G242), S233 (= S243), V236 (= V246), W239 (≠ M249), G256 (= G266)
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)
58% identity, 97% coverage: 16:492/492 of query aligns to 57:535/535 of P51649
- C93 (≠ M54) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G137) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ A141) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P143) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R174) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C184) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 189:192) binding
- T233 (= T194) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A198) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S216) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G226) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTPVG 242:247) binding
- R334 (= R292) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N293) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C298) modified: Disulfide link with 342, In inhibited form
- C342 (= C300) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (= N329) natural variant: N -> S
- P382 (= P339) to L: in SSADHD; 2% of activity
- V406 (= V363) to I: in dbSNP:rs143741652
- G409 (= G366) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S455) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G490) 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)
58% identity, 97% coverage: 16:492/492 of query aligns to 7:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
58% identity, 97% coverage: 16:492/492 of query aligns to 7:485/485 of 2w8qA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
39% identity, 94% coverage: 23:485/492 of query aligns to 5:471/477 of 6j76A
- active site: N148 (= N166), E246 (= E264), C280 (= C298), E458 (= E472)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I162), T145 (= T163), A146 (≠ P164), W147 (= W165), N148 (= N166), K171 (= K189), T173 (≠ A191), S174 (≠ E192), G204 (≠ P222), G208 (= G226), T223 (= T241), G224 (= G242), S225 (= S243), A228 (≠ V246), S231 (≠ M249), I232 (≠ L250), E246 (= E264), L247 (= L265), C280 (= C298), E381 (= E395), F383 (= F397), H447 (≠ F461)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
40% identity, 96% coverage: 20:489/492 of query aligns to 5:474/476 of 5x5uA
- active site: N151 (= N166), K174 (= K189), E249 (= E264), C283 (= C298), E380 (= E395), E457 (= E472)
- binding glycerol: D15 (≠ G30), A16 (= A31), A17 (≠ D32), G19 (≠ A34)
- binding nicotinamide-adenine-dinucleotide: P149 (= P164), P207 (= P222), A208 (≠ R223), S211 (≠ G226), G227 (= G242), S228 (= S243), V231 (= V246), R329 (≠ A344), R330 (≠ A345), E380 (= E395), F382 (= F397)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
40% identity, 96% coverage: 20:489/492 of query aligns to 5:474/476 of 5x5tA
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
44% identity, 94% coverage: 23:485/492 of query aligns to 9:475/489 of 6wsbA
- active site: N152 (= N166), E250 (= E264), C284 (= C298), E462 (= E472)
- binding nicotinamide-adenine-dinucleotide: I148 (= I162), G149 (≠ T163), A150 (≠ P164), W151 (= W165), N152 (= N166), K175 (= K189), E178 (= E192), G208 (≠ P222), G211 (= G226), A212 (= A227), F225 (= F240), T226 (= T241), G227 (= G242), G228 (≠ S243), T231 (≠ V246), V235 (≠ L250), E250 (= E264), L251 (= L265), G252 (= G266), C284 (= C298), E385 (= E395), F387 (= F397)
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, 97% coverage: 12:487/492 of query aligns to 1:482/497 of P17202
- I28 (≠ D40) binding
- D96 (≠ E106) binding
- SPW 156:158 (≠ TPW 163:165) binding
- Y160 (≠ F167) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R174) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAE 189:192) binding
- L186 (≠ A193) binding
- SSAT 236:239 (≠ STPV 243:246) binding
- V251 (= V258) binding in other chain
- L258 (= L265) binding
- W285 (≠ R292) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E395) binding
- A441 (≠ M446) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S455) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F461) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K465) binding
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
37% identity, 95% coverage: 23:489/492 of query aligns to 8:475/477 of 2opxA
- active site: N151 (= N166), K174 (= K189), E249 (= E264), C283 (= C298), E381 (= E395), A458 (≠ E472)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y120), F152 (= F167), N284 (≠ V299), F312 (≠ V327), G313 (= G328), R318 (vs. gap), D320 (≠ G334), I321 (≠ V335), A322 (≠ T336), Y362 (≠ F376), F440 (≠ I454), F440 (≠ I454), E441 (≠ S455)
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, 95% coverage: 23:489/492 of query aligns to 10:477/479 of P25553
- L150 (≠ T163) binding
- R161 (= R174) binding
- KPSE 176:179 (≠ KPAE 189:192) binding
- F180 (≠ A193) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ A227) binding
- S230 (= S243) binding
- E251 (= E264) binding
- N286 (≠ V299) 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 (≠ K348) binding
- E443 (≠ S455) binding
- H449 (≠ F461) 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, 95% coverage: 23:489/492 of query aligns to 8:475/477 of 2impA
- active site: N151 (= N166), K174 (= K189), E249 (= E264), C283 (= C298), E381 (= E395), A458 (≠ E472)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I162), L148 (≠ T163), P149 (= P164), W150 (= W165), K174 (= K189), E177 (= E192), F178 (≠ A193), G207 (≠ P222), G211 (= G226), Q212 (≠ A227), S228 (= S243), A231 (≠ V246), K234 (≠ M249), R334 (≠ K348)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
37% identity, 95% coverage: 23:489/492 of query aligns to 8:475/477 of 2iluA
- active site: N151 (= N166), K174 (= K189), E249 (= E264), C283 (= C298), E381 (= E395), A458 (≠ E472)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I162), L148 (≠ T163), P149 (= P164), W150 (= W165), K174 (= K189), S176 (≠ A191), E177 (= E192), R206 (≠ D221), G207 (≠ P222), G211 (= G226), Q212 (≠ A227), S228 (= S243), A231 (≠ V246), K234 (≠ M249), I235 (≠ L250), N328 (= N342), R334 (≠ K348), F383 (= F397)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
37% identity, 95% coverage: 23:487/492 of query aligns to 9:480/495 of 4v37A
- active site: N157 (= N166), K180 (= K189), E255 (= E264), A289 (≠ C298), E388 (= E395), E465 (= E472)
- binding 3-aminopropan-1-ol: C448 (≠ S455), W454 (≠ F461)
- binding nicotinamide-adenine-dinucleotide: I153 (= I162), S154 (≠ T163), P155 (= P164), W156 (= W165), N157 (= N166), M162 (= M171), K180 (= K189), S182 (≠ A191), E183 (= E192), G213 (≠ P222), G217 (= G226), A218 (= A227), T232 (= T241), G233 (= G242), S234 (= S243), T237 (≠ V246), E255 (= E264), L256 (= L265), A289 (≠ C298), E388 (= E395), F390 (= F397)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 96% coverage: 12:485/492 of query aligns to 1:485/505 of O24174
- N164 (= N166) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
- W172 (≠ R174) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.
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)
37% identity, 97% coverage: 15:489/492 of query aligns to 15:493/501 of Q56YU0
- G152 (≠ M149) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A412) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 95% coverage: 20:485/492 of query aligns to 6:474/486 of 4pxlA
- active site: N154 (= N166), K177 (= K189), E253 (= E264), C287 (= C298), E384 (= E395), D461 (≠ E472)
- binding nicotinamide-adenine-dinucleotide: I150 (= I162), V151 (≠ T163), P152 (= P164), W153 (= W165), K177 (= K189), E180 (= E192), G210 (≠ P222), G214 (= G226), A215 (= A227), F228 (= F240), G230 (= G242), S231 (= S243), V234 (= V246), E253 (= E264), G255 (= G266), C287 (= C298), Q334 (≠ A345), K337 (= K348), E384 (= E395), F386 (= F397)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
41% identity, 96% coverage: 15:485/492 of query aligns to 6:482/494 of 4pz2B
- active site: N159 (= N166), K182 (= K189), E258 (= E264), C292 (= C298), E392 (= E395), D469 (≠ E472)
- binding nicotinamide-adenine-dinucleotide: I155 (= I162), I156 (≠ T163), P157 (= P164), W158 (= W165), N159 (= N166), M164 (= M171), K182 (= K189), A184 (= A191), E185 (= E192), G215 (≠ P222), G219 (= G226), F233 (= F240), T234 (= T241), G235 (= G242), S236 (= S243), V239 (= V246), E258 (= E264), L259 (= L265), C292 (= C298), E392 (= E395), F394 (= F397)
Query Sequence
>H281DRAFT_02680 H281DRAFT_02680 succinate semialdehyde dehydrogenase
MTMTEFNPLSRLADPSLLRTLAYIDGQWCGADDARTFAVDDPATGEKIADVPLMTGAETR
RAIEAGEHAQRGWRKLTAAQRSTILKRWHALMIANTDDLAIIMSAEQGKPLAEAKGEIGY
AASFIEWFAEQAKRVDGDVLASPAADKRMLVTKEPIGVCAAITPWNFPAAMITRKVAPAL
AAGCAMILKPAEATPLSALALAELAHRAGVPAGVFSVVVGDPRSIGAEMTSNPIVRKLSF
TGSTPVGRMLMSQCAPTVKKLSLELGGNAPFIVFDDADLDAAVEGALASKYRNAGQTCVC
TNRVYVQDGVYDAFAEKFAAAVGRIKVGNGFESGVTQGPLINEAAVEKVEAHIADAVAHG
ARVLTGGKRHAAGKLFFEPTVVGDVTARMRFATEETFGPVAPLFRFTNEREAIAAANATE
FGLAAYFYSRDIGRIWRVAEALEYGMVGINTGLISNEVAPFGGVKQSGLGREGSKYGIED
YLEIKYLCMGGL
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