SitesBLAST
Comparing 200453 FitnessBrowser__MR1:200453 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, 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)
71% identity, 100% coverage: 3:482/482 of query aligns to 2:481/481 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 (≠ P183), 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 (see paper)
62% identity, 99% coverage: 3:480/482 of query aligns to 2:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I153), T153 (= T154), P154 (= P155), K179 (= K180), A212 (= A213), K213 (≠ I214), F230 (= F231), T231 (= T232), G232 (= G233), S233 (= S234), V236 (= V237), W239 (≠ K240), G256 (= G257)
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
59% identity, 99% coverage: 3:480/482 of query aligns to 20:497/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (= I153), A171 (≠ T154), P172 (= P155), W173 (= W156), K197 (= K180), A230 (= A213), F248 (= F231), G250 (= G233), S251 (= S234), V254 (= V237), M257 (≠ K240), L273 (= L256), C306 (= C289), K356 (= K339), E403 (= E386), F405 (= 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)
55% identity, 98% coverage: 7:479/482 of query aligns to 57:531/535 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 substrate; 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 (≠ KPAP 180:183) binding NAD(+)
- 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 (≠ GSTNVG 233:238) binding NAD(+)
- R334 (= R283) binding substrate; 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 (≠ E320) natural variant: N -> S
- P382 (= P330) to L: in SSADHD; 2% of activity
- V406 (= V354) to I: in dbSNP:rs143741652
- G409 (= G357) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S446) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
55% identity, 98% coverage: 7:479/482 of query aligns to 7:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
55% identity, 98% coverage: 7:479/482 of query aligns to 7:481/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% 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 (≠ N23), G19 (≠ K25)
- binding nicotinamide-adenine-dinucleotide: P149 (= P155), P207 (≠ A213), A208 (≠ I214), 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)
41% identity, 97% coverage: 12:480/482 of query aligns to 6:474/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
39% 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 (≠ P183), 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)
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)
38% identity, 98% coverage: 9:481/482 of query aligns to 3:476/477 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 (≠ P183), 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)
38% identity, 98% coverage: 9:481/482 of query aligns to 3:476/477 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 (≠ P183), R206 (≠ D212), G207 (≠ A213), G211 (= G217), Q212 (≠ N218), S228 (= S234), A231 (≠ V237), K234 (= K240), 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)
38% identity, 98% coverage: 9:481/482 of query aligns to 5:478/479 of P25553
- L150 (≠ T154) binding NAD(+)
- R161 (= R165) binding (S)-lactate
- KPSE 176:179 (≠ KPAP 180:183) binding NAD(+)
- 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 NAD(+)
- S230 (= S234) binding NAD(+)
- E251 (= E255) binding (S)-lactate
- N286 (≠ V290) binding (S)-lactate; 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 NAD(+)
- E443 (≠ S446) binding (S)-lactate
- H449 (≠ F452) binding (S)-lactate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
37% identity, 98% coverage: 9:481/482 of query aligns to 3:476/477 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 (≠ I323), D320 (≠ G325), I321 (≠ V326), A322 (≠ T327), Y362 (≠ F367), F440 (≠ I445), F440 (≠ I445), E441 (≠ S446)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 99% coverage: 1:478/482 of query aligns to 1:484/494 of 4pz2B
- active site: N159 (= N157), K182 (= K180), E258 (= E255), C292 (= C289), E392 (= E386), D469 (≠ E463)
- binding nicotinamide-adenine-dinucleotide: I155 (= I153), I156 (≠ T154), P157 (= P155), W158 (= W156), N159 (= N157), M164 (= M162), K182 (= K180), A184 (= A182), E185 (≠ P183), G215 (≠ A213), G219 (= G217), F233 (= F231), T234 (= T232), G235 (= G233), S236 (= S234), V239 (= V237), E258 (= E255), L259 (= L256), C292 (= C289), E392 (= E386), F394 (= F388)
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 2 papers)
39% identity, 97% coverage: 12:480/482 of query aligns to 444:921/923 of Q3SY69
Sites not aligning to the query:
- 133 P → H: found in a patient with neurodevelopmental disorder; uncertain significance; loss of formyltetrahydrofolate dehydrogenase activity
- 374 S→A: No effect on phosphopantetheinylation.
- 375 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation.
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
37% identity, 98% coverage: 12:481/482 of query aligns to 4:476/494 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 (≠ P183), R204 (≠ D212), G205 (≠ A213), G209 (= G217), D210 (≠ N218), G225 (= G233), S226 (= S234), T229 (≠ V237)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
39% identity, 97% coverage: 12:479/482 of query aligns to 7:477/486 of 4pxlA
- active site: N154 (= N157), K177 (= K180), E253 (= E255), C287 (= C289), E384 (= E386), D461 (≠ E463)
- binding nicotinamide-adenine-dinucleotide: I150 (= I153), V151 (≠ T154), P152 (= P155), W153 (= W156), K177 (= K180), E180 (≠ P183), G210 (≠ A213), 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)
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, 99% coverage: 6:480/482 of query aligns to 15:493/501 of Q56YU0
- G152 (≠ I140) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ V403) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
37% identity, 97% coverage: 12:478/482 of query aligns to 104:579/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K180), S310 (≠ D212), G311 (≠ A213), G315 (= G217), G331 (= G233), S332 (= S234), V335 (= V237)
- binding 4'-phosphopantetheine: K201 (= K106), F382 (≠ R283), N387 (≠ T288), C388 (= C289), N545 (≠ L444)
Query Sequence
>200453 FitnessBrowser__MR1:200453
MLLNDPSLLRQQCYINGQWCDANSKETVAITNPATGAVIACVPVMGQAETQAAIAAAEAA
LPAWRALTAKERGAKLRRWFELLNENSDDLALLMTSEQGKPLTEAKGEVTYAASFIEWFA
EEAKRIYGDTIPGHQGDKRIMVIKQPVGVTAAITPWNFPAAMITRKAAPALAAGCTMVVK
PAPQTPFTALALAVLAERAGIPAGVFSVITGDAIAIGNEMCTNPIVRKLSFTGSTNVGIK
LMAQCAPTLKKLSLELGGNAPFIVFDDANIDAAVEGAMIAKYRNAGQTCVCANRIYVQAG
VYDEFAEKLSMAVAKLKVGEGIIAGVTTGPLINAAAVEKVQSHLEDAIKKGATVLAGGKV
HELGGNFFEPTVLTNADKSMRVAREETFGPLAPLFKFNDVDDVIKQANDTEFGLAAYFYG
RDISLVWKVAESLEYGMVGVNTGLISTEVAPFGGMKSSGLGREGSKYGIEEYLEIKYICM
SV
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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