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: I152 (= I162), P154 (= P164), W155 (= W165), N156 (= N166), K179 (= K189), A181 (= A191), S182 (≠ E192), S211 (≠ D221), A212 (≠ P222), G213 (≠ R223), G216 (= G226), F230 (= F240), T231 (= T241), G232 (= G242), S233 (= S243), I236 (≠ V246), E254 (= E264), L255 (= L265), C288 (= C298), K338 (= K348), E385 (= E395), F387 (= F397)
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
- active site: N155 (= N166), K178 (= K189), E256 (= E264), A290 (≠ C298), E388 (= E395), E465 (= E472)
- binding adenosine-5'-diphosphate: I151 (= I162), T152 (= T163), P153 (= P164), W154 (= W165), K178 (= K189), P179 (= P190), A180 (= A191), E181 (= E192), A214 (≠ P222), K215 (≠ R223), F232 (= F240), S235 (= S243), T238 (≠ V246)
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
- active site: N155 (= N166), K178 (= K189), E256 (= E264), A290 (≠ C298), E388 (= E395), E465 (= E472)
- binding succinic acid: Y109 (= Y120), F156 (= F167), R163 (= R174), E256 (= E264), R284 (= R292), A290 (≠ C298), V291 (= V299), S448 (= S455), F454 (= F461)
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), P172 (= P190), T173 (≠ A191), S174 (≠ E192), G203 (≠ D221), G204 (≠ P222), R205 (= R223), G208 (= G226), N209 (≠ A227), T223 (= T241), G224 (= G242), S225 (= S243), A228 (≠ V246), S231 (≠ M249), I232 (≠ L250), E246 (= E264), L247 (= L265), G248 (= G266), 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), W150 (= W165), N151 (= N166), P207 (= P222), A208 (≠ R223), 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 (= 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), P176 (= P190), S177 (≠ A191), E178 (= E192), D207 (= D221), G208 (≠ P222), G211 (= G226), A212 (= A227), F225 (= F240), T226 (= T241), G227 (= G242), G228 (≠ S243), T231 (≠ V246), K234 (≠ M249), 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