SitesBLAST
Comparing AZOBR_RS09720 AZOBR_RS09720 succinate-semialdehyde dehdyrogenase 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)
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: P154 (= P166), W155 (= W167), K179 (= K191), A181 (= A193), S182 (≠ T194), A212 (= A224), G216 (= G228), G232 (= G244), S233 (= S245), I236 (= I248), C288 (= C300), K338 (= K351), E385 (= E398), F387 (= F400)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
59% identity, 97% coverage: 14:495/497 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I164), T153 (= T165), P154 (= P166), K179 (= K191), A212 (= A224), K213 (≠ R225), F230 (= F242), T231 (= T243), G232 (= G244), S233 (= S245), V236 (≠ I248), W239 (≠ E251), G256 (= G268)
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
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
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: F105 (≠ Y122), F152 (= F169), N284 (≠ V301), F312 (≠ V329), G313 (= G330), R318 (≠ T335), D320 (≠ G337), I321 (≠ A338), A322 (≠ Q339), 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), E177 (≠ T194), F178 (≠ A195), G207 (≠ A224), G211 (= G228), Q212 (≠ G229), S228 (= S245), A231 (≠ I248), K234 (≠ E251), 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), R206 (≠ S223), G207 (≠ A224), G211 (= G228), Q212 (≠ G229), 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
- active site: N151 (= N168), K174 (= K191), E249 (= E266), C283 (= C300), E380 (= E398), E457 (= E475)
- binding glycerol: D15 (= D32), A16 (= A33), A17 (≠ D34), G19 (= G36)
- binding nicotinamide-adenine-dinucleotide: P149 (= P166), P207 (≠ A224), A208 (≠ R225), S211 (≠ G228), G227 (= G244), S228 (= S245), V231 (≠ I248), R329 (vs. gap), R330 (vs. gap), E380 (= E398), F382 (= F400)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
42% identity, 95% coverage: 23:492/497 of query aligns to 6:474/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 94% coverage: 21:488/497 of query aligns to 1:471/477 of 6j76A
- active site: N148 (= N168), E246 (= E266), C280 (= C300), E458 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I164), T145 (= T165), A146 (≠ P166), W147 (= W167), N148 (= N168), K171 (= K191), T173 (≠ A193), S174 (≠ T194), G204 (≠ A224), G208 (= G228), T223 (= T243), G224 (= G244), S225 (= S245), A228 (≠ I248), S231 (≠ E251), I232 (≠ L252), E246 (= E266), L247 (= L267), C280 (= C300), E381 (= E398), F383 (= F400), H447 (≠ F464)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
38% identity, 94% coverage: 22:488/497 of query aligns to 18:492/498 of 4go2A
- active site: N170 (= N168), K193 (= K191), E269 (= E266), C303 (= C300), E400 (= E398), D479 (≠ E475)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I164), I167 (≠ T165), P168 (= P166), W169 (= W167), K193 (= K191), A195 (= A193), Q196 (≠ T194), S225 (= S223), G226 (≠ A224), G230 (= G228), Q231 (≠ G229), F244 (= F242), G246 (= G244), S247 (= S245), V250 (≠ I248), I254 (≠ L252), E269 (= E266), G271 (= G268), C303 (= C300), E400 (= E398), F402 (= F400)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
38% identity, 94% coverage: 22:488/497 of query aligns to 18:492/498 of 2o2rA
- active site: N170 (= N168), K193 (= K191), E269 (= E266), C303 (= C300), E400 (= E398), D479 (≠ E475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I164), I167 (≠ T165), W169 (= W167), K193 (= K191), A195 (= A193), Q196 (≠ T194), S225 (= S223), G226 (≠ A224), G230 (= G228), Q231 (≠ G229), F244 (= F242), S247 (= S245), V250 (≠ I248), I254 (≠ L252)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
38% identity, 94% coverage: 22:488/497 of query aligns to 103:577/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K191), S310 (= S223), G311 (≠ A224), G315 (= G228), G331 (= G244), S332 (= S245), V335 (≠ I248)
- binding 4'-phosphopantetheine: K201 (≠ R117), F382 (≠ R294), N387 (≠ T299), C388 (= C300), N545 (≠ I456)
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)
38% identity, 94% coverage: 22:488/497 of query aligns to 422:896/902 of P28037
- IPW 571:573 (≠ TPW 165:167) binding
- KPAQ 597:600 (≠ KPAT 191:194) binding
- GSLVGQ 630:635 (≠ ARAIGG 224:229) binding
- GS 650:651 (= GS 244:245) binding
- E673 (= E266) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 266:267) binding
- C707 (= C300) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K351) binding
- ESF 804:806 (≠ ETF 398:400) 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.
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)
39% identity, 94% coverage: 25:492/497 of query aligns to 23:493/501 of Q56YU0
- G152 (= G148) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A415) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
36% identity, 95% coverage: 18:491/497 of query aligns to 11:492/505 of 4neaA
- active site: N166 (= N168), K189 (= K191), E264 (= E266), C298 (= C300), E399 (= E398), E476 (= E475)
- binding nicotinamide-adenine-dinucleotide: P164 (= P166), K189 (= K191), E192 (≠ T194), G222 (≠ A224), G226 (= G228), G242 (= G244), G243 (≠ S245), T246 (≠ I248), H249 (≠ E251), I250 (≠ L252), C298 (= C300), E399 (= E398), F401 (= F400)
Q3SY69 Mitochondrial 10-formyltetrahydrofolate dehydrogenase; Mitochondrial 10-FTHFDH; mtFDH; Aldehyde dehydrogenase family 1 member L2; EC 1.5.1.6 from Homo sapiens (Human) (see paper)
37% identity, 95% coverage: 22:492/497 of query aligns to 443:921/923 of Q3SY69
Sites not aligning to the query:
- 374 S→A: No effect on phosphopantetheinylation.
- 375 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation.
Query Sequence
>AZOBR_RS09720 AZOBR_RS09720 succinate-semialdehyde dehdyrogenase
MPYDSVDTARRLGLKDAELLRFQGFVDGRWIDADSGKTVEVTNPADGSVLGSVPMMGADE
TRRAIEAAERAWPAWRALTAKERAKTLRTWFDLMMANQEDIARIMTAEQGKPLAEARGEV
AYAASFIEWFAEEGKRVYGDTIPQHLPGRRIVVTKEPIGVTAAITPWNFPAAMITRKAGP
ALAAGCPMVIKPATATPLTALAMAVLAERAGIPAGILSVVTGSARAIGGEMTGNPTVRKL
TFTGSTEIGKELMAQCAGTVKKVSLELGGNAPFLVFNDADLDEAVKGAIASKYRNTGQTC
VCANRLLVQSGVYDAFAAKLAEAVKALKVGPGLTTEGAQQGPLIDMAAVEKVEDHIRDAT
EKGARVVLGGKRHELGGSFFEPTILADVTPAMKVAREETFGPVAPLFRFETEEEAVRMAN
ATEFGLAAYFYSRDIGRVWRVAEALEYGIVGINEGIISTEVAPFGGMKESGIGREGSKYG
IEDYLEIKYLCMGGIGG
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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