SitesBLAST
Comparing AZOBR_RS09720 FitnessBrowser__azobra:AZOBR_RS09720 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)
71% identity, 97% coverage: 12:493/497 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
71% identity, 97% coverage: 14:493/497 of query aligns to 2:480/481 of 3jz4A
- active site: N156 (= N168), K179 (= K191), E254 (= E266), C288 (= C300), E385 (= E398), E462 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (= I164), P154 (= P166), W155 (= W167), N156 (= N168), K179 (= K191), A181 (= A193), S182 (≠ T194), S211 (= S223), A212 (= A224), G213 (≠ R225), G216 (= G228), F230 (= F242), T231 (= T243), G232 (= G244), S233 (= S245), I236 (= I248), E254 (= E266), L255 (= L267), C288 (= C300), K338 (= K351), E385 (= E398), F387 (= F400)
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, 98% coverage: 9:495/497 of query aligns to 48:535/535 of P51649
- C93 (≠ M56) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G139) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P143) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ H145) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R176) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C186) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAT 191:194) binding
- T233 (= T196) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A200) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S218) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G228) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEIG 244:249) binding
- R334 (= R294) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N295) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C300) modified: Disulfide link with 342, In inhibited form
- C342 (= C302) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ P331) natural variant: N -> S
- P382 (= P342) to L: in SSADHD; 2% of activity
- V406 (= V366) to I: in dbSNP:rs143741652
- G409 (= G369) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S458) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G493) 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, 97% coverage: 16:495/497 of query aligns to 5:485/485 of 2w8rA
- active site: N155 (= N168), K178 (= K191), E256 (= E266), A290 (≠ C300), E388 (= E398), E465 (= E475)
- binding adenosine-5'-diphosphate: I151 (= I164), T152 (= T165), P153 (= P166), W154 (= W167), K178 (= K191), P179 (= P192), A180 (= A193), E181 (≠ T194), A214 (= A224), K215 (≠ R225), F232 (= F242), S235 (= S245), T238 (≠ I248)
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
57% identity, 97% coverage: 16:495/497 of query aligns to 5:485/485 of 2w8qA
- active site: N155 (= N168), K178 (= K191), E256 (= E266), A290 (≠ C300), E388 (= E398), E465 (= E475)
- binding succinic acid: Y109 (= Y122), F156 (= F169), R163 (= R176), E256 (= E266), R284 (= R294), A290 (≠ C300), V291 (= V301), S448 (= S458), F454 (= F464)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
39% identity, 94% coverage: 25:492/497 of query aligns to 8:475/477 of 2opxA
- active site: N151 (= N168), K174 (= K191), E249 (= E266), C283 (= C300), E381 (= E398), A458 (≠ E475)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: Q97 (≠ A114), L98 (≠ E115), V101 (≠ G118), F105 (≠ Y122), F152 (= F169), F155 (≠ A172), D273 (≠ A290), I277 (≠ R294), N284 (≠ V301), F312 (≠ V329), G313 (= G330), R318 (≠ T335), D320 (≠ G337), I321 (≠ A338), A322 (≠ Q339), K359 (≠ G376), Y362 (≠ F379), F440 (≠ I457), F440 (≠ I457), E441 (≠ S458)
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)
39% identity, 94% coverage: 25:492/497 of query aligns to 10:477/479 of P25553
- L150 (≠ T165) binding
- R161 (= R176) binding
- KPSE 176:179 (≠ KPAT 191:194) binding
- F180 (≠ A195) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ G229) binding
- S230 (= S245) binding
- E251 (= E266) binding
- N286 (≠ V301) 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 (≠ K351) binding
- E443 (≠ S458) binding
- H449 (≠ F464) 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)
39% identity, 94% coverage: 25:492/497 of query aligns to 8:475/477 of 2impA
- active site: N151 (= N168), K174 (= K191), E249 (= E266), C283 (= C300), E381 (= E398), A458 (≠ E475)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I164), L148 (≠ T165), P149 (= P166), W150 (= W167), K174 (= K191), P175 (= P192), S176 (≠ A193), E177 (≠ T194), F178 (≠ A195), G207 (≠ A224), E208 (≠ R225), G211 (= G228), Q212 (≠ G229), M225 (≠ F242), G227 (= G244), S228 (= S245), A231 (≠ I248), K234 (≠ E251), I235 (≠ L252), N328 (≠ D345), A330 (= A347), R334 (≠ K351)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
39% identity, 94% coverage: 25:492/497 of query aligns to 8:475/477 of 2iluA
- active site: N151 (= N168), K174 (= K191), E249 (= E266), C283 (= C300), E381 (= E398), A458 (≠ E475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I164), L148 (≠ T165), P149 (= P166), W150 (= W167), K174 (= K191), S176 (≠ A193), E177 (≠ T194), F178 (≠ A195), R206 (≠ S223), G207 (≠ A224), E208 (≠ R225), G211 (= G228), Q212 (≠ G229), M225 (≠ F242), G227 (= G244), S228 (= S245), A231 (≠ I248), K234 (≠ E251), I235 (≠ L252), N328 (≠ D345), R334 (≠ K351), F383 (= F400)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
42% identity, 95% coverage: 23:492/497 of query aligns to 6:474/476 of 5x5uA