SitesBLAST
Comparing AO356_29070 AO356_29070 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)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
59% identity, 98% coverage: 5:482/489 of query aligns to 2:478/481 of 3jz4A
- active site: N156 (= N159), K179 (= K182), E254 (= E258), C288 (= C292), E385 (= E389), E462 (= E466)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P157), W155 (= W158), K179 (= K182), A181 (= A184), S182 (= S185), A212 (≠ T216), G216 (≠ A220), G232 (= G236), S233 (= S237), I236 (≠ V240), C288 (= C292), K338 (= K342), E385 (= E389), F387 (= F391)
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, 98% coverage: 5:482/489 of query aligns to 3:479/482 of P25526
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
56% identity, 99% coverage: 5:486/489 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I155), T153 (= T156), P154 (= P157), K179 (= K182), A212 (≠ T216), K213 (≠ R217), 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)
52% identity, 98% coverage: 10:486/489 of query aligns to 58:535/535 of P51649
- C93 (= C47) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G130) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P134) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ V136) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R167) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C177) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAS 182:185) binding
- T233 (= T187) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A191) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S209) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ A220) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 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 (≠ G294) 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 (= S449) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (≠ D484) 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)
52% identity, 98% coverage: 10:486/489 of query aligns to 8:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
52% identity, 98% coverage: 10:486/489 of query aligns to 8:485/485 of 2w8qA
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
39% identity, 96% coverage: 13:479/489 of query aligns to 6:474/486 of 4pxlA
- active site: N154 (= N159), K177 (= K182), E253 (= E258), C287 (= C292), E384 (= E389), D461 (≠ E466)
- binding nicotinamide-adenine-dinucleotide: I150 (= I155), V151 (≠ T156), P152 (= P157), W153 (= W158), K177 (= K182), E180 (≠ S185), G210 (≠ D215), G214 (≠ I219), A215 (= A220), 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)
37% identity, 97% coverage: 5:479/489 of query aligns to 12:489/501 of Q56YU0
- G152 (≠ I142) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A406) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
37% identity, 96% coverage: 16:484/489 of query aligns to 21:497/498 of 4go2A
- active site: N170 (= N159), K193 (= K182), E269 (= E258), C303 (= C292), E400 (= E389), D479 (≠ E466)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I155), I167 (≠ T156), P168 (= P157), W169 (= W158), K193 (= K182), A195 (= A184), Q196 (≠ S185), S225 (≠ N214), G226 (≠ D215), G230 (≠ A220), Q231 (≠ G221), F244 (= F234), G246 (= G236), S247 (= S237), V250 (= V240), I254 (≠ L244), E269 (= E258), G271 (= G260), C303 (= C292), E400 (= E389), F402 (= F391)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
37% identity, 96% coverage: 16:484/489 of query aligns to 21:497/498 of 2o2rA
- active site: N170 (= N159), K193 (= K182), E269 (= E258), C303 (= C292), E400 (= E389), D479 (≠ E466)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I155), I167 (≠ T156), W169 (= W158), K193 (= K182), A195 (= A184), Q196 (≠ S185), S225 (≠ N214), G226 (≠ D215), G230 (≠ A220), Q231 (≠ G221), F244 (= F234), S247 (= S237), V250 (= V240), I254 (≠ L244)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
37% identity, 96% coverage: 16:484/489 of query aligns to 106:582/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K182), S310 (≠ N214), G311 (≠ D215), G315 (≠ A220), G331 (= G236), S332 (= S237), V335 (= V240)
- binding 4'-phosphopantetheine: K201 (≠ R108), F382 (≠ R286), N387 (≠ S291), C388 (= C292), N545 (≠ L447)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 97% coverage: 4:479/489 of query aligns to 2:482/494 of 4pz2B
- active site: N159 (= N159), K182 (= K182), E258 (= E258), C292 (= C292), E392 (= E389), D469 (≠ E466)
- binding nicotinamide-adenine-dinucleotide: I155 (= I155), I156 (≠ T156), P157 (= P157), W158 (= W158), N159 (= N159), M164 (= M164), K182 (= K182), A184 (= A184), E185 (≠ S185), G215 (≠ D215), G219 (= G221), F233 (= F234), T234 (= T235), G235 (= G236), S236 (= S237), V239 (= V240), E258 (= E258), L259 (= L259), C292 (= C292), E392 (= E389), F394 (= F391)
P28037 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; FBP-CI; EC 1.5.1.6 from Rattus norvegicus (Rat) (see 5 papers)
37% identity, 96% coverage: 16:484/489 of query aligns to 425:901/902 of P28037
- IPW 571:573 (≠ TPW 156:158) binding
- KPAQ 597:600 (≠ KPAS 182:185) binding
- GSL-VGQ 630:635 (≠ DTRDIAG 215:221) binding
- GS 650:651 (= GS 236:237) binding
- E673 (= E258) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 258:259) binding
- C707 (= C292) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K342) binding
- ESF 804:806 (≠ EIF 389:391) binding
Sites not aligning to the query:
- 142 Essential for catalytic activity; D→A: Loss of formyltetrahydrofolate dehydrogenase activity. Loss of formyltetrahydrofolate hydrolase activity. No effect on aldehyde dehydrogenase activity.
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation. Loss of formyltetrahydrofolate dehydrogenase activity. No effect on hydrolase and aldehyde dehydrogenase activities in vitro.
Q28399 Aldehyde dehydrogenase, cytosolic 1; ALDH class 1; ETA-crystallin; EC 1.2.1.3 from Elephantulus edwardii (Cape long-eared elephant shrew) (see paper)
38% identity, 97% coverage: 5:479/489 of query aligns to 13:490/501 of Q28399
1o9jA The x-ray crystal structure of eta-crystallin (see paper)
38% identity, 97% coverage: 5:479/489 of query aligns to 6:483/494 of 1o9jA
- active site: N163 (= N159), K186 (= K182), E262 (= E258), C296 (= C292), E393 (= E389), E470 (= E466)
- binding nicotinamide-adenine-dinucleotide: I159 (= I155), F160 (≠ T156), P161 (= P157), W162 (= W158), N163 (= N159), K186 (= K182), E189 (≠ S185), G219 (≠ D215), G223 (≠ I219), F237 (= F234), T238 (= T235), G239 (= G236), S240 (= S237), V243 (= V240), E262 (= E258), L263 (= L259), C296 (= C292), E393 (= E389), F395 (= F391), L421 (= L417)
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)
38% identity, 95% coverage: 16:479/489 of query aligns to 10:477/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 156:159) binding
- K162 (= K168) active site, Charge relay system
- KPSE 176:179 (≠ KPAS 182:185) binding
- G209 (≠ D215) binding
- GTST 230:233 (≠ STEV 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
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
38% identity, 95% coverage: 16:479/489 of query aligns to 9:476/489 of 4cazA
- active site: N152 (= N159), K175 (= K182), 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 (= I155), G149 (≠ T156), W151 (= W158), N152 (= N159), K175 (= K182), E178 (≠ S185), G208 (≠ D215), G212 (≠ A220), 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)
38% identity, 95% coverage: 16:479/489 of query aligns to 9:476/489 of 2woxA
- active site: N152 (= N159), K175 (= K182), E251 (= E258), C285 (= C292), E386 (= E389), E463 (= E466)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I155), G149 (≠ T156), W151 (= W158), N152 (= N159), K175 (= K182), S177 (≠ A184), E178 (≠ S185), G208 (≠ D215), G212 (≠ A220), 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)
38% identity, 95% coverage: 16:479/489 of query aligns to 9:476/489 of 2wmeA
- active site: N152 (= N159), K175 (= K182), E251 (= E258), C285 (= C292), E386 (= E389), E463 (= E466)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T156), W151 (= W158), K175 (= K182), S177 (≠ A184), E178 (≠ S185), G208 (≠ D215), G212 (≠ A220), F226 (= F234), G228 (= G236), G229 (≠ S237), T232 (≠ V240), V236 (≠ L244)
7a6qB Crystal structure of human aldehyde dehydrogenase 1a3 in complex with selective nr6 inhibitor compound (see paper)
39% identity, 96% coverage: 13:479/489 of query aligns to 14:483/489 of 7a6qB
- active site: N163 (= N159), E262 (= E258), C296 (= C292), E470 (= E466)
- binding nicotinamide-adenine-dinucleotide: I159 (= I155), W162 (= W158), K186 (= K182), E189 (≠ S185), G219 (≠ D215), G223 (≠ A220), S240 (= S237), V243 (= V240), K342 (≠ A338)
- binding (3-oxidanylidene-3-sodiooxy-propanoyl)oxysodium: A32 (≠ T31), T33 (≠ L32), C34 (≠ R33), P36 (= P35), D103 (≠ E99), E189 (≠ S185), Q190 (= Q186), F218 (≠ N214), I339 (= I335), D340 (= D336)
- binding 3-(2-phenylimidazo[1,2-a]pyridin-6-yl)benzenecarbonitrile: G118 (≠ Y113), D141 (≠ K137), N143 (≠ T139), N451 (≠ L447), L453 (≠ S449), A455 (≠ E451)
Query Sequence
>AO356_29070 AO356_29070 succinate-semialdehyde dehydrogenase
VKHLLKDPTLWRTGAYIAGEWLTETPNGQYTLRNPVDQSVLAELPRCGEAEVRHAIDAAH
EAFGPWRRLTAKRRGEVLRRWYELMVEHREDIATLITLEEGKPLEEARGEVDYAASFVRW
FGEEATRVRGDLIPGVKDTQRIVVLREPIGVCAAITPWNFPAAMITRKAAPALAAGCTMV
VKPASQTPLTALALAELALRAGVPAGVFSVITGNDTRDIAGELTANPLVRKLTFTGSTEV
GRLLLAQAAQTVKKCSMELGGNAPFIVFDDADLDAAADGVMLAKFRNGGQSCIGANRVLV
QSGVYDALAERIVERMARLKVGNGLEPGVQVGPLIDDAAVRKSQALVDDALAQGARLLSG
GKPHALGGCFFQPTLLADVTHGMRVAREEIFGPVMPLVRFDRDDEAIAMANDSEFGLAAY
LFSRDAARIWRNAARIESGMVGINCGLISNEVAPFGGVKQSGLGREGSHLGIDEFLEVKY
LCWDGLENV
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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