SitesBLAST
Comparing Pf6N2E2_368 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_368 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)
61% identity, 99% coverage: 5:483/485 of query aligns to 2:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
61% identity, 99% coverage: 5:483/485 of query aligns to 1:480/481 of 3jz4A
- active site: N156 (= N160), K179 (= K183), E254 (= E258), C288 (= C292), E385 (= E388), E462 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P158), W155 (= W159), K179 (= K183), A181 (≠ S185), S182 (≠ D186), A212 (≠ P216), G216 (= G220), G232 (= G236), S233 (= S237), I236 (≠ V240), C288 (= C292), K338 (= K342), E385 (= E388), F387 (= F390)
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
55% identity, 99% coverage: 5:485/485 of query aligns to 19:500/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (= I156), A171 (≠ T157), P172 (= P158), W173 (= W159), K197 (= K183), A230 (≠ P216), F248 (= F234), G250 (= G236), S251 (= S237), V254 (= V240), M257 (≠ L243), L273 (= L259), C306 (= C292), K356 (= K342), E403 (= E388), F405 (= F390)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565 (see paper)
56% identity, 99% coverage: 6:485/485 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I156), T153 (= T157), P154 (= P158), K179 (= K183), A212 (≠ P216), K213 (≠ A217), F230 (= F234), T231 (= T235), G232 (= G236), S233 (= S237), V236 (= V240), W239 (≠ L243), G256 (= G260)
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)
54% identity, 98% coverage: 10:485/485 of query aligns to 57:535/535 of P51649
- C93 (≠ M48) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G131) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P135) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P137) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R168) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C178) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPSD 183:186) binding NAD(+)
- T233 (= T188) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A192) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N210) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G220) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTAVG 236:241) binding NAD(+)
- R334 (= R286) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N287) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C292) modified: Disulfide link with 342, In inhibited form
- C342 (= C294) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (= N323) natural variant: N -> S
- P382 (= P333) to L: in SSADHD; 2% of activity
- V406 (≠ L357) to I: in dbSNP:rs143741652
- G409 (= G360) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S448) binding substrate; 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)
54% identity, 98% coverage: 10:485/485 of query aligns to 7:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
54% identity, 98% coverage: 10:485/485 of query aligns to 7:485/485 of 2w8qA
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
40% identity, 96% coverage: 17:482/485 of query aligns to 8:475/477 of 2opxA
- active site: N151 (= N160), K174 (= K183), E249 (= E258), C283 (= C292), E381 (= E388), A458 (≠ E465)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y114), F152 (= F161), N284 (≠ V293), F312 (≠ V321), G313 (= G322), R318 (≠ A327), D320 (vs. gap), I321 (≠ V329), A322 (≠ M330), Y362 (≠ F369), F440 (≠ I447), F440 (≠ I447), E441 (≠ S448)
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: 17:482/485 of query aligns to 10:477/479 of P25553
- L150 (≠ T157) binding NAD(+)
- R161 (= R168) binding (S)-lactate
- KPSE 176:179 (≠ KPSD 183:186) binding NAD(+)
- F180 (≠ L187) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ E221) binding NAD(+)
- S230 (= S237) binding NAD(+)
- E251 (= E258) binding (S)-lactate
- N286 (≠ V293) binding (S)-lactate; 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 (≠ K342) binding NAD(+)
- E443 (≠ S448) binding (S)-lactate
- H449 (≠ F454) binding (S)-lactate
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)
40% identity, 96% coverage: 17:482/485 of query aligns to 8:475/477 of 2impA