SitesBLAST
Comparing SMa1848 SMa1848 GabD5 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)
58% identity, 99% coverage: 1:481/484 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
58% identity, 99% coverage: 2:481/484 of query aligns to 1:480/481 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 (≠ S182), S182 (≠ E183), A212 (≠ P213), 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
55% identity, 99% coverage: 3:483/484 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ V153), T153 (= T154), P154 (= P155), K179 (= K180), A212 (≠ P213), K213 (≠ T214), F230 (= F231), T231 (= T232), G232 (= G233), S233 (= S234), V236 (= V237), W239 (≠ L240), 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)
54% identity, 98% coverage: 8:483/484 of query aligns to 58:535/535 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 (= P134) 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 (≠ KPSE 180:183) binding
- T233 (= T185) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A189) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N207) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G217) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTRVG 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 (≠ P320) natural variant: N -> S
- P382 (= P330) to L: in SSADHD; 2% of activity
- V406 (≠ L354) to I: in dbSNP:rs143741652
- G409 (≠ R357) 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)
53% identity, 98% coverage: 8:483/484 of query aligns to 8:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
53% identity, 98% coverage: 8:483/484 of query aligns to 8:485/485 of 2w8qA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 96% coverage: 15:480/484 of query aligns to 6:475/477 of 6j76A
- active site: N148 (= N157), E246 (= E255), C280 (= C289), E458 (= E463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (≠ V153), T145 (= T154), A146 (≠ P155), W147 (= W156), N148 (= N157), K171 (= K180), T173 (≠ S182), S174 (≠ E183), G204 (≠ P213), G208 (= G217), T223 (= T232), G224 (= G233), S225 (= S234), A228 (≠ V237), S231 (≠ L240), I232 (≠ L241), E246 (= E255), L247 (= L256), C280 (= C289), E381 (= E386), F383 (= F388), H447 (≠ F452)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
37% identity, 96% coverage: 15:480/484 of query aligns to 9:475/477 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 (≠ E323), D320 (≠ G325), I321 (= I326), A322 (= A327), Y362 (= Y367), F440 (≠ I445), F440 (≠ I445), E441 (≠ S446)
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, 96% coverage: 15:480/484 of query aligns to 9:475/477 of 2impA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E381 (= E386), A458 (≠ E463)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (≠ V153), L148 (≠ T154), P149 (= P155), W150 (= W156), K174 (= K180), E177 (= E183), F178 (= F184), G207 (≠ P213), G211 (= G217), Q212 (≠ N218), S228 (= S234), A231 (≠ V237), K234 (≠ L240), R334 (≠ K339)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
37% identity, 96% coverage: 15:480/484 of query aligns to 9:475/477 of 2iluA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E381 (= E386), A458 (≠ E463)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (≠ V153), L148 (≠ T154), P149 (= P155), W150 (= W156), K174 (= K180), S176 (= S182), E177 (= E183), R206 (≠ M212), G207 (≠ P213), G211 (= G217), Q212 (≠ N218), S228 (= S234), A231 (≠ V237), K234 (≠ L240), I235 (≠ L241), N328 (= N333), R334 (≠ K339), F383 (= F388)
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, 96% coverage: 15:480/484 of query aligns to 11:477/479 of P25553
- L150 (≠ T154) binding
- R161 (= R165) binding
- KPSE 176:179 (= KPSE 180:183) binding
- F180 (= F184) 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
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
40% identity, 96% coverage: 14:480/484 of query aligns to 8:474/476 of 5x5uA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E380 (= E386), E457 (= E463)
- binding glycerol: D15 (≠ A21), A16 (≠ G22), A17 (= A23), G19 (= G25)
- binding nicotinamide-adenine-dinucleotide: P149 (= P155), P207 (= P213), A208 (≠ T214), S211 (≠ G217), G227 (= G233), S228 (= S234), V231 (= V237), R329 (≠ A335), R330 (≠ A336), E380 (= E386), F382 (= F388)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
40% identity, 96% coverage: 14:480/484 of query aligns to 8:474/476 of 5x5tA
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
39% identity, 96% coverage: 14:477/484 of query aligns to 14:483/494 of 4pz2B
- active site: N159 (= N157), K182 (= K180), E258 (= E255), C292 (= C289), E392 (= E386), D469 (≠ E463)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ V153), I156 (≠ T154), P157 (= P155), W158 (= W156), N159 (= N157), M164 (= M162), K182 (= K180), A184 (≠ S182), E185 (= E183), G215 (≠ P213), G219 (= G217), F233 (= F231), T234 (= T232), G235 (= G233), S236 (= S234), V239 (= V237), E258 (= E255), L259 (= L256), C292 (= C289), E392 (= E386), F394 (= 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)
37% identity, 98% coverage: 7:480/484 of query aligns to 11:491/505 of 4neaA
- active site: N166 (= N157), K189 (= K180), E264 (= E255), C298 (= C289), E399 (= E386), E476 (= E463)
- binding nicotinamide-adenine-dinucleotide: P164 (= P155), K189 (= K180), E192 (= E183), G222 (≠ P213), G226 (= G217), G242 (= G233), G243 (≠ S234), T246 (≠ V237), H249 (≠ L240), I250 (≠ L241), C298 (= C289), E399 (= E386), F401 (= F388)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
38% identity, 96% coverage: 14:477/484 of query aligns to 9:475/486 of 4pxlA
- active site: N154 (= N157), K177 (= K180), E253 (= E255), C287 (= C289), E384 (= E386), D461 (≠ E463)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ V153), V151 (≠ T154), P152 (= P155), W153 (= W156), K177 (= K180), E180 (= E183), G210 (≠ P213), G214 (= G217), A215 (≠ N218), F228 (= F231), G230 (= G233), S231 (= S234), V234 (= V237), E253 (= E255), G255 (= G257), C287 (= C289), Q334 (≠ A336), K337 (= K339), E384 (= E386), F386 (= F388)
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
37% identity, 96% coverage: 14:477/484 of query aligns to 13:486/505 of O24174
- N164 (= N157) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
- W172 (≠ R165) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.
3u4jA Crystal structure of NAD-dependent aldehyde dehydrogenase from sinorhizobium meliloti
39% identity, 99% coverage: 1:480/484 of query aligns to 16:495/505 of 3u4jA
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, 96% coverage: 14:477/484 of query aligns to 23:490/501 of Q56YU0
- G152 (≠ I140) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A403) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
35% identity, 97% coverage: 14:484/484 of query aligns to 26:500/503 of O14293
- S248 (= S234) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
Query Sequence
>SMa1848 SMa1848 GabD5 succinate semialdehyde dehdyrogenase
MRLKDRELFRQLGLIGGEWIAGASGVVVDVIDPANQAVLGTVPDMGTAETRAAIEAANAA
FGPWKKKTHAERAAVLERWHALMIENLEDLAVLVTMEQGKPLEEARGEIRYGAAFVKWFA
EESRRIGGHTIPSPTSDRRIVVLKEAVGVCAIVTPWNFPNAMITRKVAPALAAGCTVVIK
PSEFTPFSALALGVLAERAGIPAGVVNIVTGMPTAIGNEFMTNETVRKISFTGSTRVGSL
LMRGAADSVKRLSLELGGNAPFIVFDDANLDLAVEGAIASKFRNGGQTCVCANRILVQAG
VYDAFAEKLGARVNAMKVGPGTEPGIAIGPMINEAAIDKIDRHVEDAIAKGAKLAARGRS
VPEGRQYTAPIVLTGATTDMLLASEETFGPVAPLFRFETEDEAIAIANGTPFGLAAYFYT
EGLKRSWRVAEALEFGMIGLNTGAISTEVAPFGGVKQSGLGREGAQVGIEEYLEMKSFHI
GGLD
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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