SitesBLAST
Comparing WP_011383730.1 AMB_RS06710 NAD-dependent 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)
68% identity, 99% coverage: 2:483/485 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
68% identity, 99% coverage: 4:483/485 of query aligns to 2:480/481 of 3jz4A
- active site: N156 (= N158), K179 (= K181), E254 (= E257), C288 (= C291), E385 (= E388), E462 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P156), W155 (= W157), K179 (= K181), A181 (= A183), S182 (≠ E184), A212 (≠ P215), G216 (= G219), G232 (= G235), S233 (= S236), I236 (≠ V239), C288 (= C291), K338 (= K341), E385 (= E388), F387 (= F390)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
60% identity, 99% coverage: 4:485/485 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I154), T153 (= T155), P154 (= P156), K179 (= K181), A212 (≠ P215), K213 (= K216), F230 (= F233), T231 (= T234), G232 (= G235), S233 (= S236), V236 (= V239), W239 (≠ L242), G256 (= G259)
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, 99% coverage: 6:485/485 of query aligns to 55:535/535 of P51649
- C93 (≠ M46) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G129) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P133) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ H135) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R166) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C176) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 181:184) binding
- T233 (= T186) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A190) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N208) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G219) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 235:240) binding
- R334 (= R285) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N286) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C291) modified: Disulfide link with 342, In inhibited form
- C342 (= C293) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ P322) natural variant: N -> S
- P382 (= P332) to L: in SSADHD; 2% of activity
- V406 (= V356) to I: in dbSNP:rs143741652
- G409 (= G359) 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)
57% identity, 99% coverage: 6:485/485 of query aligns to 5:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
57% identity, 99% coverage: 6:485/485 of query aligns to 5:485/485 of 2w8qA
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
40% identity, 96% coverage: 15:482/485 of query aligns to 8:475/477 of 2opxA
- active site: N151 (= N158), K174 (= K181), E249 (= E257), C283 (= C291), E381 (= E388), A458 (≠ E465)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y112), F152 (= F159), N284 (≠ V292), F312 (≠ V320), G313 (= G321), R318 (≠ E325), D320 (= D327), I321 (≠ F328), A322 (≠ Q329), Y362 (≠ F369), F440 (≠ I447), F440 (≠ I447), E441 (≠ S448)
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)
40% identity, 96% coverage: 15:482/485 of query aligns to 8:475/477 of 2impA
- active site: N151 (= N158), K174 (= K181), E249 (= E257), C283 (= C291), E381 (= E388), A458 (≠ E465)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I154), L148 (≠ T155), P149 (= P156), W150 (= W157), K174 (= K181), E177 (= E184), F178 (≠ D185), G207 (≠ P215), G211 (= G219), Q212 (≠ F220), S228 (= S236), A231 (≠ V239), K234 (≠ L242), R334 (≠ K341)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
40% identity, 96% coverage: 15:482/485 of query aligns to 8:475/477 of 2iluA
- active site: N151 (= N158), K174 (= K181), E249 (= E257), C283 (= C291), E381 (= E388), A458 (≠ E465)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I154), L148 (≠ T155), P149 (= P156), W150 (= W157), K174 (= K181), S176 (≠ A183), E177 (= E184), R206 (≠ D214), G207 (≠ P215), G211 (= G219), Q212 (≠ F220), S228 (= S236), A231 (≠ V239), K234 (≠ L242), I235 (≠ L243), N328 (= N335), R334 (≠ K341), F383 (= F390)
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)
40% identity, 96% coverage: 15:482/485 of query aligns to 10:477/479 of P25553
- L150 (≠ T155) binding
- R161 (= R166) binding
- KPSE 176:179 (≠ KPAE 181:184) binding
- F180 (≠ D185) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ F220) binding
- S230 (= S236) binding
- E251 (= E257) binding
- N286 (≠ V292) 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 (≠ K341) binding
- E443 (≠ S448) binding
- H449 (≠ F454) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% identity, 99% coverage: 5:482/485 of query aligns to 3:474/476 of 5x5uA
- active site: N151 (= N158), K174 (= K181), E249 (= E257), C283 (= C291), E380 (= E388), E457 (= E465)
- binding glycerol: D15 (≠ A22), A16 (= A23), A17 (≠ Q24), G19 (= G26)
- binding nicotinamide-adenine-dinucleotide: P149 (= P156), P207 (= P215), A208 (≠ K216), S211 (≠ G219), G227 (= G235), S228 (= S236), V231 (= V239), R329 (≠ E337), R330 (≠ A338), E380 (= E388), F382 (= F390)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
41% identity, 99% coverage: 5:482/485 of query aligns to 3:474/476 of 5x5tA
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)
38% identity, 97% coverage: 10:481/485 of query aligns to 16:492/505 of 4neaA
- active site: N166 (= N158), K189 (= K181), E264 (= E257), C298 (= C291), E399 (= E388), E476 (= E465)
- binding nicotinamide-adenine-dinucleotide: P164 (= P156), K189 (= K181), E192 (= E184), G222 (≠ P215), G226 (= G219), G242 (= G235), G243 (≠ S236), T246 (≠ V239), H249 (≠ L242), I250 (≠ L243), C298 (= C291), E399 (= E388), F401 (= F390)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
41% identity, 97% coverage: 7:478/485 of query aligns to 5:485/505 of O24174
- N164 (= N158) 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 (≠ R166) 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.
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
38% identity, 96% coverage: 15:478/485 of query aligns to 26:491/503 of O14293
- S248 (= S236) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
41% identity, 96% coverage: 15:478/485 of query aligns to 9:474/486 of 4pxlA
- active site: N154 (= N158), K177 (= K181), E253 (= E257), C287 (= C291), E384 (= E388), D461 (≠ E465)
- binding nicotinamide-adenine-dinucleotide: I150 (= I154), V151 (≠ T155), P152 (= P156), W153 (= W157), K177 (= K181), E180 (= E184), G210 (≠ D214), G214 (= G219), A215 (≠ F220), F228 (= F233), G230 (= G235), S231 (= S236), V234 (= V239), E253 (= E257), G255 (= G259), C287 (= C291), Q334 (≠ A338), K337 (= K341), E384 (= E388), F386 (= F390)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 96% coverage: 15:478/485 of query aligns to 5:471/477 of 6j76A
- active site: N148 (= N158), E246 (= E257), C280 (= C291), E458 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I154), T145 (= T155), A146 (≠ P156), W147 (= W157), N148 (= N158), K171 (= K181), T173 (≠ A183), S174 (≠ E184), G204 (≠ D214), G208 (= G219), T223 (= T234), G224 (= G235), S225 (= S236), A228 (≠ V239), S231 (≠ L242), I232 (≠ L243), E246 (= E257), L247 (= L258), C280 (= C291), E381 (= E388), F383 (= F390), H447 (≠ F454)
7radA Crystal structure analysis of aldh1b1
40% identity, 97% coverage: 12:482/485 of query aligns to 13:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I154), I159 (≠ T155), P160 (= P156), W161 (= W157), N162 (= N158), M167 (= M163), K185 (= K181), E188 (= E184), G218 (≠ D214), G222 (= G219), A223 (≠ F220), T237 (= T234), G238 (= G235), S239 (= S236), V242 (= V239), E261 (= E257), L262 (= L258), C295 (= C291), E392 (= E388), F394 (= F390)
- 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 (≠ Y112), F163 (= F159), E285 (≠ A281), F289 (≠ R285), N450 (≠ L446), V452 (≠ S448)
7mjdA Crystal structure analysis of aldh1b1
40% identity, 97% coverage: 12:482/485 of query aligns to 13:486/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I154), I159 (≠ T155), P160 (= P156), W161 (= W157), N162 (= N158), M167 (= M163), K185 (= K181), E188 (= E184), G218 (≠ D214), G222 (= G219), F236 (= F233), T237 (= T234), G238 (= G235), S239 (= S236), V242 (= V239), E261 (= E257), L262 (= L258), C295 (= C291), E392 (= E388), F394 (= F390)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ Y112), E285 (≠ A281), F289 (≠ R285), N450 (≠ L446), V452 (≠ S448)
7mjcA Crystal structure analysis of aldh1b1
40% identity, 97% coverage: 12:482/485 of query aligns to 13:486/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I154), I159 (≠ T155), P160 (= P156), W161 (= W157), N162 (= N158), K185 (= K181), E188 (= E184), G218 (≠ D214), G222 (= G219), T237 (= T234), G238 (= G235), S239 (= S236), V242 (= V239), E261 (= E257), L262 (= L258), C295 (= C291), E392 (= E388), F394 (= F390)
Query Sequence
>WP_011383730.1 AMB_RS06710 NAD-dependent succinate-semialdehyde dehydrogenase
MLDLSDSALLRDHAYINGSWVAAQSGERLAVTNPADGSLIIRVPAMGAAETRQAIEAADR
AWGPWKAKTAKERSAVLRRWFELIMAAQNDLAKLMTAEQGKPLAEAKGEVAYGASFVEWF
AEEAKRVYGDTIPEHMPGRRIVVVKEPIGVVAAITPWNFPLAMITRKCAPALAAGCPVVV
KPAEDTPLSALALAELAERAGFPPGVFNVITAGDPKAVGFELTANPKVRKLSFTGSTEVG
KLLMAQCAATVKKLSLELGGNAPFMVFDDADLDAAVAGAMASKYRNTGQTCVCANRLLVQ
DGIYDAFTARLAEAVAALKVGPGLEGDFQQGPLINEEAVRKVERHIADAVAKGARVVMGG
KRHARGGTFFEPTILADVTPDMAPAREETFGPVAPLFRFKTEEEAVRMANDTEFGLAAYF
YSRDVGRVWRVSRALEYGIVGINEGLISTEVAPFGGVKESGLGREGSKYGIEDFLEVKYL
CMGGI
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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