SitesBLAST
Comparing Ac3H11_4184 Aldehyde dehydrogenase B (EC 1.2.1.22) 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)
59% identity, 97% coverage: 11:492/498 of query aligns to 3:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
59% identity, 97% coverage: 11:492/498 of query aligns to 2:480/481 of 3jz4A
- active site: N156 (= N163), K179 (= K186), E254 (= E264), C288 (= C298), E385 (= E397), E462 (= E474)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (= I159), P154 (= P161), W155 (= W162), N156 (= N163), K179 (= K186), A181 (= A188), S182 (≠ E189), S211 (≠ D218), A212 (≠ S219), G213 (≠ D220), G216 (= G226), F230 (= F240), T231 (= T241), G232 (= G242), S233 (= S243), I236 (≠ V246), E254 (= E264), L255 (= L265), C288 (= C298), K338 (= K348), E385 (= E397), F387 (= F399)
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)
57% identity, 96% coverage: 16:494/498 of query aligns to 58:535/535 of P51649
- C93 (≠ L51) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G134) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P138) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ F140) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R171) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C181) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 186:189) binding
- T233 (= T191) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A195) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N213) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G226) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 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 (≠ A457) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G492) 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, 96% coverage: 16:494/498 of query aligns to 8:485/485 of 2w8rA
- active site: N155 (= N163), K178 (= K186), E256 (= E264), A290 (≠ C298), E388 (= E397), E465 (= E474)
- binding adenosine-5'-diphosphate: I151 (= I159), T152 (= T160), P153 (= P161), W154 (= W162), K178 (= K186), P179 (= P187), A180 (= A188), E181 (= E189), A214 (≠ S222), K215 (≠ I223), F232 (= F240), S235 (= S243), T238 (≠ V246)
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
57% identity, 96% coverage: 16:494/498 of query aligns to 8:485/485 of 2w8qA
- active site: N155 (= N163), K178 (= K186), E256 (= E264), A290 (≠ C298), E388 (= E397), E465 (= E474)
- binding succinic acid: Y109 (= Y117), F156 (= F164), R163 (= R171), E256 (= E264), R284 (= R292), A290 (≠ C298), V291 (= V299), S448 (≠ A457), F454 (= F463)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 96% coverage: 10:487/498 of query aligns to 2:482/494 of 4pz2B
- active site: N159 (= N163), K182 (= K186), E258 (= E264), C292 (= C298), E392 (= E397), D469 (≠ E474)
- binding nicotinamide-adenine-dinucleotide: I155 (= I159), I156 (≠ T160), P157 (= P161), W158 (= W162), N159 (= N163), M164 (= M168), K182 (= K186), P183 (= P187), A184 (= A188), E185 (= E189), G215 (≠ S219), P216 (≠ D220), G219 (= G226), A220 (≠ K227), F233 (= F240), T234 (= T241), G235 (= G242), S236 (= S243), V239 (= V246), L242 (≠ I249), I243 (≠ L250), E258 (= E264), L259 (= L265), G260 (= G266), C292 (= C298), E392 (= E397), F394 (= F399), L420 (= L425), F458 (= F463)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
39% identity, 96% coverage: 15:491/498 of query aligns to 1:474/476 of 5x5uA
- active site: N151 (= N163), K174 (= K186), E249 (= E264), C283 (= C298), E380 (= E397), E457 (= E474)
- binding glycerol: D15 (≠ V29), A16 (≠ G30), A17 (≠ S31), G19 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: P149 (= P161), W150 (= W162), N151 (= N163), P207 (≠ S219), A208 (≠ D220), S211 (≠ G226), F225 (= F240), T226 (= T241), G227 (= G242), S228 (= S243), V231 (= V246), L235 (= L250), E249 (= E264), L250 (= L265), C283 (= C298), R329 (≠ A344), R330 (≠ A345), E380 (= E397), F382 (= F399)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
39% identity, 96% coverage: 15:491/498 of query aligns to 1:474/476 of 5x5tA
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
39% identity, 94% coverage: 22:487/498 of query aligns to 9:474/486 of 4pxlA
- active site: N154 (= N163), K177 (= K186), E253 (= E264), C287 (= C298), E384 (= E397), D461 (≠ E474)
- binding nicotinamide-adenine-dinucleotide: I150 (= I159), V151 (≠ T160), P152 (= P161), W153 (= W162), N154 (= N163), K177 (= K186), P178 (= P187), A179 (= A188), E180 (= E189), G210 (≠ S219), P211 (≠ D220), G214 (= G226), A215 (≠ K227), F228 (= F240), T229 (= T241), G230 (= G242), S231 (= S243), V234 (= V246), E253 (= E264), L254 (= L265), G255 (= G266), C287 (= C298), Q334 (≠ A345), K337 (= K348), E384 (= E397), F386 (= F399)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
37% identity, 95% coverage: 15:487/498 of query aligns to 18:491/503 of O14293