SitesBLAST
Comparing GFF4164 Psest_4237 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)
78% identity, 100% coverage: 1:482/482 of query aligns to 1:482/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
78% identity, 100% coverage: 2:482/482 of query aligns to 1:481/481 of 3jz4A
- active site: N156 (= N157), K179 (= K180), E254 (= E255), C288 (= C289), E385 (= E386), E462 (= E463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P155), W155 (= W156), K179 (= K180), A181 (= A182), S182 (= S183), A212 (= A213), G216 (= G217), G232 (= G233), S233 (= S234), I236 (≠ V237), C288 (= C289), K338 (= K339), E385 (= E386), F387 (= F388)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
62% identity, 99% coverage: 3:481/482 of query aligns to 2:480/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I153), T153 (= T154), P154 (= P155), K179 (= K180), A212 (= A213), K213 (≠ G214), F230 (= F231), T231 (= T232), G232 (= G233), S233 (= S234), V236 (= V237), W239 (≠ K240), G256 (= G257)
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)
56% identity, 99% coverage: 7:481/482 of query aligns to 57:533/535 of P51649
- C93 (≠ M45) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G128) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P132) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ H134) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R165) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C175) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAS 180:183) binding
- T233 (= T185) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A189) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S207) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G217) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 233:238) binding
- R334 (= R283) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N284) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C289) modified: Disulfide link with 342, In inhibited form
- C342 (= C291) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (= N320) natural variant: N -> S
- P382 (= P330) to L: in SSADHD; 2% of activity
- V406 (≠ L354) to I: in dbSNP:rs143741652
- G409 (= G357) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S446) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G481) 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)
56% identity, 99% coverage: 7:481/482 of query aligns to 7:483/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
56% identity, 99% coverage: 7:481/482 of query aligns to 7:483/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
42% identity, 97% coverage: 12:480/482 of query aligns to 6:474/476 of 5x5uA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E380 (= E386), E457 (= E463)
- binding glycerol: D15 (= D21), A16 (= A22), A17 (≠ D23), G19 (= G25)
- binding nicotinamide-adenine-dinucleotide: P149 (= P155), P207 (≠ A213), A208 (≠ G214), S211 (≠ G217), G227 (= G233), S228 (= S234), V231 (= V237), R329 (= R335), R330 (≠ A336), E380 (= E386), F382 (= F388)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
42% identity, 97% coverage: 12:480/482 of query aligns to 6:474/476 of 5x5tA
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
38% identity, 97% coverage: 14:480/482 of query aligns to 6:475/494 of 5izdA
- active site: N149 (= N157), K172 (= K180), E247 (= E255), C281 (= C289), E381 (= E386), E458 (= E463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I153), T146 (= T154), W148 (= W156), K172 (= K180), P173 (= P181), S174 (≠ A182), S175 (= S183), R204 (≠ S212), G205 (≠ A213), G209 (= G217), D210 (≠ N218), G225 (= G233), S226 (= S234), T229 (≠ V237)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 96% coverage: 12:476/482 of query aligns to 3:471/477 of 6j76A
- active site: N148 (= N157), E246 (= E255), C280 (= C289), E458 (= E463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I153), T145 (= T154), A146 (≠ P155), W147 (= W156), N148 (= N157), K171 (= K180), T173 (≠ A182), S174 (= S183), G204 (≠ A213), G208 (= G217), T223 (= T232), G224 (= G233), S225 (= S234), A228 (≠ V237), S231 (≠ K240), I232 (≠ L241), E246 (= E255), L247 (= L256), C280 (= C289), E381 (= E386), F383 (= F388), H447 (≠ F452)
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, 97% coverage: 14:480/482 of query aligns to 10:477/479 of P25553
- L150 (≠ T154) binding
- R161 (= R165) binding
- KPSE 176:179 (≠ KPAS 180:183) binding
- F180 (≠ Q184) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ N218) binding
- S230 (= S234) binding
- E251 (= E255) binding
- N286 (≠ V290) 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 (≠ K339) binding
- E443 (≠ S446) binding
- H449 (≠ F452) 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, 97% coverage: 14:480/482 of query aligns to 8:475/477 of 2impA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E381 (= E386), A458 (≠ E463)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I153), L148 (≠ T154), P149 (= P155), W150 (= W156), K174 (= K180), E177 (≠ S183), F178 (≠ Q184), G207 (≠ A213), G211 (= G217), Q212 (≠ N218), S228 (= S234), A231 (≠ V237), K234 (= K240), R334 (≠ K339)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
39% identity, 97% coverage: 14:480/482 of query aligns to 8:475/477 of 2iluA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E381 (= E386), A458 (≠ E463)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I153), L148 (≠ T154), P149 (= P155), W150 (= W156), K174 (= K180), S176 (≠ A182), E177 (≠ S183), R206 (≠ S212), G207 (≠ A213), G211 (= G217), Q212 (≠ N218), S228 (= S234), A231 (≠ V237), K234 (= K240), I235 (≠ L241), N328 (≠ D333), R334 (≠ K339), F383 (= F388)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
39% identity, 97% coverage: 14:480/482 of query aligns to 8:475/477 of 2opxA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E381 (= E386), A458 (≠ E463)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y111), F152 (= F158), N284 (≠ V290), F312 (≠ V318), G313 (= G319), R318 (≠ E324), D320 (vs. gap), I321 (≠ T326), A322 (≠ D327), Y362 (= Y367), F440 (≠ I445), F440 (≠ I445), E441 (≠ S446)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
38% identity, 96% coverage: 12:476/482 of query aligns to 19:492/498 of 4go2A
- active site: N170 (= N157), K193 (= K180), E269 (= E255), C303 (= C289), E400 (= E386), D479 (≠ E463)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I153), I167 (≠ T154), P168 (= P155), W169 (= W156), K193 (= K180), A195 (= A182), Q196 (≠ S183), S225 (= S212), G226 (≠ A213), G230 (= G217), Q231 (≠ N218), F244 (= F231), G246 (= G233), S247 (= S234), V250 (= V237), I254 (≠ L241), E269 (= E255), G271 (= G257), C303 (= C289), E400 (= E386), F402 (= F388)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
38% identity, 96% coverage: 12:476/482 of query aligns to 19:492/498 of 2o2rA
- active site: N170 (= N157), K193 (= K180), E269 (= E255), C303 (= C289), E400 (= E386), D479 (≠ E463)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I153), I167 (≠ T154), W169 (= W156), K193 (= K180), A195 (= A182), Q196 (≠ S183), S225 (= S212), G226 (≠ A213), G230 (= G217), Q231 (≠ N218), F244 (= F231), S247 (= S234), V250 (= V237), I254 (≠ L241)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
38% identity, 96% coverage: 12:476/482 of query aligns to 104:577/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K180), S310 (= S212), G311 (≠ A213), G315 (= G217), G331 (= G233), S332 (= S234), V335 (= V237)
- binding 4'-phosphopantetheine: K201 (= K106), F382 (≠ R283), N387 (≠ T288), C388 (= C289), N545 (≠ L444)
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, 96% coverage: 12:476/482 of query aligns to 423:896/902 of P28037
- IPW 571:573 (≠ TPW 154:156) binding
- KPAQ 597:600 (≠ KPAS 180:183) binding
- GSLVGQ 630:635 (≠ AGDIGN 213:218) binding
- GS 650:651 (= GS 233:234) binding
- E673 (= E255) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 255:256) binding
- C707 (= C289) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K339) binding
- ESF 804:806 (≠ ETF 386:388) 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.
7yjjC Human cytosolic 10-formyltetrahydrofolate dehydrogenase and gossypol complex
38% identity, 98% coverage: 4:476/482 of query aligns to 11:492/498 of 7yjjC
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, 97% coverage: 11:476/482 of query aligns to 7:477/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 154:157) binding
- K162 (= K166) active site, Charge relay system
- KPSE 176:179 (≠ KPAS 180:183) binding
- G209 (≠ A213) binding
- GTST 230:233 (≠ STEV 234:237) binding
- E252 (= E255) active site, Proton acceptor
- C286 (= C289) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E386) binding
- E464 (= E463) active site, Charge relay system
Query Sequence
>GFF4164 Psest_4237 succinate-semialdehyde dehydrogenase
MQLKDTALFRQQAYIDGAWLDADSGQTISVNNPATGETLGTVPKMGAAETRRAIDAAERA
LPAWRDLTAKERSQKLRRWFELLMENQDDLGRLMTLEQGKPLAEAKGEIAYAASFIEWFA
EEAKRIYGDTIPGHQKDKRIIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVIK
PASQTPFSALAMVELAERAGIPKGVLSVVTGSAGDIGNELTANPKVRKISFTGSTEVGAK
LMEQCAPGIKKVSLELGGNAPFIVFDDADLDEAVKGAVQSKYRNAGQTCVCVNRIYVQDG
VYDTFAEKFQAAVAKLRVGNGLEEGTDLGPLIDDRAAAKVREHIEDAVAQGARLVAGGQA
HALGGSYFEPTVLVNVPDSAKVAKEETFGPLAPLFRFKDEADAIAKANDTEFGLASYFYA
RDLGRVFRVAEALEYGMVGINTGLISTEVAPFGGVKSSGLGREGSKYGIEDYLEIKYLCM
GI
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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