SitesBLAST
Comparing BPHYT_RS22430 BPHYT_RS22430 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: 4:484/486 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
68% identity, 99% coverage: 6:484/486 of query aligns to 2:480/481 of 3jz4A
- active site: N156 (= N160), K179 (= K183), E254 (= E258), C288 (= C292), E385 (= E389), E462 (= E466)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P158), W155 (= W159), K179 (= K183), A181 (= A185), S182 (≠ E186), A212 (≠ P216), G216 (= G220), G232 (= G236), S233 (= S237), I236 (≠ V240), C288 (= C292), K338 (= K342), E385 (= E389), F387 (= F391)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
63% identity, 99% coverage: 5:486/486 of query aligns to 1:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I156), T153 (= T157), P154 (= P158), K179 (= K183), A212 (≠ P216), K213 (= K217), 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)
57% identity, 98% coverage: 10:486/486 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 ; 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 (= KPAE 183:186) binding
- 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 (≠ GSTPVG 236:241) binding
- R334 (= R286) binding ; 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 (≠ R323) natural variant: N -> S
- P382 (= P333) to L: in SSADHD; 2% of activity
- V406 (≠ I357) to I: in dbSNP:rs143741652
- G409 (= G360) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S449) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G484) 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, 98% coverage: 10:486/486 of query aligns to 7:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
57% identity, 98% coverage: 10:486/486 of query aligns to 7:485/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
43% identity, 97% coverage: 14:483/486 of query aligns to 5:474/476 of 5x5uA
- active site: N151 (= N160), K174 (= K183), E249 (= E258), C283 (= C292), E380 (= E389), E457 (= E466)
- binding glycerol: D15 (≠ G24), A16 (= A25), A17 (≠ D26), G19 (= G28)
- binding nicotinamide-adenine-dinucleotide: P149 (= P158), P207 (= P216), A208 (≠ K217), S211 (≠ G220), G227 (= G236), S228 (= S237), V231 (= V240), R329 (≠ A338), R330 (≠ A339), E380 (= E389), F382 (= F391)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
43% identity, 97% coverage: 14:483/486 of query aligns to 5:474/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 97% coverage: 13:483/486 of query aligns to 1:475/477 of 6j76A
- active site: N148 (= N160), E246 (= E258), C280 (= C292), E458 (= E466)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I156), T145 (= T157), A146 (≠ P158), W147 (= W159), N148 (= N160), K171 (= K183), T173 (≠ A185), S174 (≠ E186), G204 (≠ P216), G208 (= G220), T223 (= T235), G224 (= G236), S225 (= S237), A228 (≠ V240), S231 (≠ L243), I232 (≠ L244), E246 (= E258), L247 (= L259), C280 (= C292), E381 (= E389), F383 (= F391), H447 (≠ F455)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
39% identity, 96% coverage: 17:483/486 of query aligns to 9:480/489 of 4cazA
- active site: N152 (= N160), K175 (= K183), E251 (= E258), C285 (= C292), E386 (= E389), E463 (= E466)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (= I156), G149 (≠ T157), W151 (= W159), N152 (= N160), K175 (= K183), E178 (= E186), G208 (≠ P216), G212 (= G220), F226 (= F234), T227 (= T235), G228 (= G236), G229 (≠ S237), T232 (≠ V240), V236 (≠ L244), E251 (= E258), L252 (= L259), C285 (= C292), E386 (= E389), F388 (= F391)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
39% identity, 96% coverage: 17:483/486 of query aligns to 9:480/489 of 2woxA
- active site: N152 (= N160), K175 (= K183), E251 (= E258), C285 (= C292), E386 (= E389), E463 (= E466)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I156), G149 (≠ T157), W151 (= W159), N152 (= N160), K175 (= K183), S177 (≠ A185), E178 (= E186), G208 (≠ P216), G212 (= G220), F226 (= F234), T227 (= T235), G228 (= G236), G229 (≠ S237), T232 (≠ V240), V236 (≠ L244), E251 (= E258), L252 (= L259), C285 (= C292), E386 (= E389), F388 (= F391)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
39% identity, 96% coverage: 17:483/486 of query aligns to 9:480/489 of 2wmeA
- active site: N152 (= N160), K175 (= K183), E251 (= E258), C285 (= C292), E386 (= E389), E463 (= E466)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T157), W151 (= W159), K175 (= K183), S177 (≠ A185), E178 (= E186), G208 (≠ P216), G212 (= G220), F226 (= F234), G228 (= G236), G229 (≠ S237), T232 (≠ V240), V236 (≠ L244)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
39% identity, 96% coverage: 17:483/486 of query aligns to 10:481/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 157:160) binding
- K162 (= K169) active site, Charge relay system
- KPSE 176:179 (≠ KPAE 183:186) binding
- G209 (≠ P216) binding
- GTST 230:233 (≠ STPV 237:240) binding
- E252 (= E258) active site, Proton acceptor
- C286 (= C292) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E389) binding
- E464 (= E466) active site, Charge relay system
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
37% identity, 95% coverage: 17:476/486 of query aligns to 8:468/477 of 2opxA
- active site: N151 (= N160), K174 (= K183), E249 (= E258), C283 (= C292), E381 (= E389), A458 (≠ E466)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y114), F152 (= F161), N284 (≠ V293), F312 (≠ V321), G313 (= G322), R318 (vs. gap), D320 (≠ G328), I321 (≠ V329), A322 (≠ T330), Y362 (≠ F370), F440 (≠ I448), F440 (≠ I448), E441 (≠ S449)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
41% identity, 95% coverage: 17:479/486 of query aligns to 9:474/486 of 4pxlA
- active site: N154 (= N160), K177 (= K183), E253 (= E258), C287 (= C292), E384 (= E389), D461 (≠ E466)
- binding nicotinamide-adenine-dinucleotide: I150 (= I156), V151 (≠ T157), P152 (= P158), W153 (= W159), K177 (= K183), E180 (= E186), G210 (≠ P216), G214 (= G220), A215 (= A221), F228 (= F234), G230 (= G236), S231 (= S237), V234 (= V240), E253 (= E258), G255 (= G260), C287 (= C292), Q334 (≠ A339), K337 (= K342), E384 (= E389), F386 (= F391)
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 98% coverage: 5:479/486 of query aligns to 11:489/501 of Q56YU0
- G152 (≠ I143) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ V406) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
39% identity, 97% coverage: 9:479/486 of query aligns to 6:482/494 of 4pz2B
- active site: N159 (= N160), K182 (= K183), E258 (= E258), C292 (= C292), E392 (= E389), D469 (≠ E466)
- binding nicotinamide-adenine-dinucleotide: I155 (= I156), I156 (≠ T157), P157 (= P158), W158 (= W159), N159 (= N160), M164 (= M165), K182 (= K183), A184 (= A185), E185 (= E186), G215 (≠ P216), G219 (= G220), F233 (= F234), T234 (= T235), G235 (= G236), S236 (= S237), V239 (= V240), E258 (= E258), L259 (= L259), C292 (= C292), E392 (= E389), F394 (= F391)
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)
37% identity, 95% coverage: 17:476/486 of query aligns to 10:470/479 of P25553
- L150 (≠ T157) binding
- R161 (= R168) binding
- KPSE 176:179 (≠ KPAE 183:186) binding
- F180 (≠ A187) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ A221) binding
- S230 (= S237) binding
- E251 (= E258) binding
- N286 (≠ V293) 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 (≠ K342) binding
- E443 (≠ S449) binding
- H449 (≠ F455) 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)
37% identity, 95% coverage: 17:476/486 of query aligns to 8:468/477 of 2impA
- active site: N151 (= N160), K174 (= K183), E249 (= E258), C283 (= C292), E381 (= E389), A458 (≠ E466)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I156), L148 (≠ T157), P149 (= P158), W150 (= W159), K174 (= K183), E177 (= E186), F178 (≠ A187), G207 (≠ P216), G211 (= G220), Q212 (≠ A221), S228 (= S237), A231 (≠ V240), K234 (≠ L243), R334 (≠ K342)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
37% identity, 95% coverage: 17:476/486 of query aligns to 8:468/477 of 2iluA
- active site: N151 (= N160), K174 (= K183), E249 (= E258), C283 (= C292), E381 (= E389), A458 (≠ E466)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I156), L148 (≠ T157), P149 (= P158), W150 (= W159), K174 (= K183), S176 (≠ A185), E177 (= E186), R206 (≠ E215), G207 (≠ P216), G211 (= G220), Q212 (≠ A221), S228 (= S237), A231 (≠ V240), K234 (≠ L243), I235 (≠ L244), N328 (= N336), R334 (≠ K342), F383 (= F391)
Query Sequence
>BPHYT_RS22430 BPHYT_RS22430 succinate-semialdehyde dehydrogenase
MTTLSLKDPSLLKSHAYIAGEWQGADDGTTFEVKNPATGETIATVPRMGTAETRRAIDTA
NAAWPAWRATTAKQRAVILRKWHDLMMENADDLAKILTTEQGKPLAEAKGEIQYAASFLE
WFAEEGKRVNGDTIPTPASDKRIVVTKEPIGVCAAITPWNFPAAMITRKVGPALAAGCPI
IVKPAEATPLSALALAVLAERAGVPRGVFNVVTGEPKAIGAEMTGNPIVRKLSFTGSTPV
GRLLMAQCAPTVKKVSLELGGNAPFIVFDDADLDAAVAGAIASKYRNSGQTCVCTNRFYV
HDKVYDAFAEKLRVAVEQLKVGRGTEDGVTQGPLINDAAVLKVESHIEDALAKGARIVTG
GKRHALGHGFFEPTVLADVTPAMKVARDETFGPLAPLFRFSSDEEVIRLANDTEFGLASY
FYSRDIGRVWRVAEALEYGMVGINTGLISNEVAPFGGVKQSGLGREGSHYGIDDYVVIKY
LCVGGI
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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