SitesBLAST
Comparing 5210745 Shew_3173 succinic semialdehyde dehydrogenase (RefSeq) 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)
59% identity, 99% coverage: 4:481/485 of query aligns to 3:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
59% identity, 99% coverage: 4:481/485 of query aligns to 2:480/481 of 3jz4A
- active site: N156 (= N156), K179 (≠ R179), E254 (= E255), C288 (= C289), E385 (= E386), E462 (= E463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P154), W155 (= W155), K179 (≠ R179), A181 (≠ S181), S182 (≠ P182), A212 (= A213), G216 (= G217), G232 (= G233), S233 (= S234), I236 (≠ V237), C288 (= C289), K338 (≠ N339), E385 (= E386), F387 (= F388)
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)
54% identity, 98% coverage: 9:483/485 of query aligns to 58:535/535 of P51649
- C93 (≠ A44) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G127) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P131) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P133) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R164) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C174) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ RPSP 179:182) binding
- T233 (= T184) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A188) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N206) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G217) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTAVG 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 (≠ D320) 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
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
54% identity, 99% coverage: 4:483/485 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I152), T153 (= T153), P154 (= P154), K179 (≠ R179), A212 (= A213), K213 (≠ V214), F230 (= F231), T231 (= T232), G232 (= G233), S233 (= S234), V236 (= V237), W239 (≠ I240), G256 (= G257)
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
54% identity, 98% coverage: 9:483/485 of query aligns to 8:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
54% identity, 98% coverage: 9:483/485 of query aligns to 8:485/485 of 2w8qA
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
38% identity, 95% coverage: 15:476/485 of query aligns to 11:480/497 of P17202
- I28 (≠ V30) binding
- D96 (≠ E96) binding
- SPW 156:158 (≠ TPW 153:155) binding
- Y160 (≠ F157) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R164) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ RPSP 179:182) binding
- L186 (= L183) binding
- SSAT 236:239 (≠ STAV 234:237) binding
- V251 (= V249) binding in other chain
- L258 (= L256) binding
- W285 (≠ R283) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E386) binding
- A441 (≠ M437) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S446) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F452) binding ; mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K456) binding
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
40% identity, 98% coverage: 6:480/485 of query aligns to 4:474/476 of 5x5uA
- active site: N151 (= N156), K174 (≠ R179), E249 (= E255), C283 (= C289), E380 (= E386), E457 (= E463)
- binding glycerol: D15 (vs. gap), A16 (vs. gap), A17 (≠ V22), G19 (≠ E24)
- binding nicotinamide-adenine-dinucleotide: P149 (= P154), P207 (≠ A213), A208 (≠ V214), S211 (≠ G217), G227 (= G233), S228 (= S234), V231 (= V237), R329 (≠ D335), R330 (≠ A336), E380 (= E386), F382 (= F388)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
40% identity, 98% coverage: 6:480/485 of query aligns to 4:474/476 of 5x5tA
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
38% identity, 95% coverage: 15:476/485 of query aligns to 9:478/495 of 4v37A
- active site: N157 (= N156), K180 (≠ R179), E255 (= E255), A289 (≠ C289), E388 (= E386), E465 (= E463)
- binding 3-aminopropan-1-ol: C448 (≠ S446), W454 (≠ F452)
- binding nicotinamide-adenine-dinucleotide: I153 (= I152), S154 (≠ T153), P155 (= P154), W156 (= W155), N157 (= N156), M162 (= M161), K180 (≠ R179), S182 (= S181), E183 (≠ P182), G213 (= G210), G217 (= G217), A218 (≠ K218), T232 (= T232), G233 (= G233), S234 (= S234), T237 (≠ V237), E255 (= E255), L256 (= L256), A289 (≠ C289), E388 (= E386), F390 (= F388)
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)
38% identity, 96% coverage: 15:478/485 of query aligns to 21:491/505 of 4neaA
- active site: N166 (= N156), K189 (≠ R179), E264 (= E255), C298 (= C289), E399 (= E386), E476 (= E463)
- binding nicotinamide-adenine-dinucleotide: P164 (= P154), K189 (≠ R179), E192 (≠ P182), G222 (≠ D212), G226 (= G217), G242 (= G233), G243 (≠ S234), T246 (≠ V237), H249 (≠ I240), I250 (≠ L241), C298 (= C289), E399 (= E386), F401 (= F388)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
38% identity, 96% coverage: 11:476/485 of query aligns to 16:484/491 of 5gtlA
- active site: N165 (= N156), K188 (≠ R179), E263 (= E255), C297 (= C289), E394 (= E386), E471 (= E463)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I152), P163 (= P154), K188 (≠ R179), A190 (≠ S181), E191 (≠ P182), Q192 (≠ L183), G221 (= G210), G225 (= G217), G241 (= G233), S242 (= S234), T245 (≠ V237), L264 (= L256), C297 (= C289), E394 (= E386), F396 (= F388)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
38% identity, 96% coverage: 11:476/485 of query aligns to 16:484/491 of 5gtkA
- active site: N165 (= N156), K188 (≠ R179), E263 (= E255), C297 (= C289), E394 (= E386), E471 (= E463)
- binding nicotinamide-adenine-dinucleotide: I161 (= I152), I162 (≠ T153), P163 (= P154), W164 (= W155), K188 (≠ R179), E191 (≠ P182), G221 (= G210), G225 (= G217), A226 (≠ K218), F239 (= F231), G241 (= G233), S242 (= S234), T245 (≠ V237), Y248 (≠ I240), L264 (= L256), C297 (= C289), Q344 (≠ A336), R347 (≠ N339), E394 (= E386), F396 (= F388)
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
38% identity, 96% coverage: 15:478/485 of query aligns to 8:477/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
38% identity, 96% coverage: 15:478/485 of query aligns to 8:477/488 of 8vr0A
8vqzA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (cmp bound)
38% identity, 96% coverage: 15:478/485 of query aligns to 8:477/488 of 8vqzA
8vqwC Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (coa bound)
38% identity, 96% coverage: 15:478/485 of query aligns to 8:477/488 of 8vqwC
- binding coenzyme a: I147 (= I152), W150 (= W155), K174 (≠ R179), S176 (= S181), E177 (≠ P182), G207 (≠ D212), G211 (= G217), F225 (= F231), G227 (= G233), G228 (≠ S234), S231 (≠ V237), H331 (≠ A336), F387 (= F388)
8vj3A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (fad bound)
38% identity, 96% coverage: 15:478/485 of query aligns to 8:477/488 of 8vj3A
8uzoA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (adp bound)
38% identity, 96% coverage: 15:478/485 of query aligns to 8:477/488 of 8uzoA
8uznA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (amp bound)
38% identity, 96% coverage: 15:478/485 of query aligns to 8:477/488 of 8uznA
- binding adenosine monophosphate: I147 (= I152), G148 (≠ T153), K174 (≠ R179), S176 (= S181), E177 (≠ P182), G207 (≠ D212), G211 (= G217), F225 (= F231), G228 (≠ S234), S231 (≠ V237), K234 (≠ I240)
Query Sequence
>5210745 Shew_3173 succinic semialdehyde dehydrogenase (RefSeq)
MQGIKDTQLIKLSSYIDGRWTVGEQRFDVVNPASQEVIAQVVDASLDDTQEAILAAKRAL
PEWSKRSANERAALMRKWFNLMMEHQEDLGRLLTLEQGKPLAEAKGEIAYGAAFIDWFAE
EGKRVYGDTIPAPANDKRILVIKQPVGVVASITPWNFPNAMIARKAAAALAAGCTFVARP
SPLTPLSALAMAELAERAGIPAGVFNIVVGEDAVGMGKVLTQHPDVAKFTFTGSTAVGKI
LLAQCATSVKKVSMELGGNAPFIVFDDADIDAAVQGALISKYRNAGQTCVCTNRIFVQKG
VAAAFTEKFTAAVANLKLGDGLGDGVTVGPMISKDAVQNVLKLVDDTVASGAKLVTGGQP
SELGESFLAPVIVTDVTNEMPLARNEIFGPVTPIISFDSEAEALAMANDTEYGLAAYFYA
RDIGRIFRVAEGLEYGMVGVNEGIISNAAAPFGGVKQSGNGREGSKYGLDDYLEIKYLCL
GGLDK
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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