SitesBLAST
Comparing CCNA_03242 FitnessBrowser__Caulo:CCNA_03242 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)
61% identity, 98% coverage: 8:481/485 of query aligns to 7:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
61% identity, 98% coverage: 8:481/485 of query aligns to 6:480/481 of 3jz4A
- active site: N156 (= N156), K179 (= K179), E254 (= E255), C288 (= C289), E385 (= E386), E462 (= E463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P154), W155 (= W155), K179 (= K179), A181 (= A181), S182 (≠ A182), A212 (≠ S213), G216 (= G217), G232 (= G233), S233 (= S234), I236 (= I237), C288 (= C289), K338 (= K339), 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)
55% identity, 98% coverage: 9:483/485 of query aligns to 58:535/535 of P51649
- C93 (≠ L44) 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 (≠ KPAA 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 (≠ GSTPIG 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 (= V354) 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)
55% 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)
55% identity, 98% coverage: 9:483/485 of query aligns to 8:485/485 of 2w8qA
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
55% identity, 98% coverage: 9:483/485 of query aligns to 7:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I152), T153 (≠ A153), P154 (= P154), K179 (= K179), A212 (≠ S213), K213 (≠ S214), F230 (= F231), T231 (= T232), G232 (= G233), S233 (= S234), V236 (≠ I237), W239 (≠ V240), G256 (= G257)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
42% identity, 97% coverage: 11:479/485 of query aligns to 4:473/476 of 5x5uA
- active site: N151 (= N156), K174 (= K179), E249 (= E255), C283 (= C289), E380 (= E386), E457 (= E463)
- binding glycerol: D15 (≠ R22), A16 (≠ G23), A17 (≠ E24), G19 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: P149 (= P154), P207 (≠ S213), A208 (≠ S214), S211 (≠ G217), G227 (= G233), S228 (= S234), V231 (≠ I237), R329 (≠ K335), R330 (≠ A336), E380 (= E386), F382 (= F388)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
42% identity, 97% coverage: 11:479/485 of query aligns to 4:473/476 of 5x5tA
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, 99% coverage: 2:479/485 of query aligns to 8:492/505 of 4neaA
- active site: N166 (= N156), K189 (= K179), E264 (= E255), C298 (= C289), E399 (= E386), E476 (= E463)
- binding nicotinamide-adenine-dinucleotide: P164 (= P154), K189 (= K179), E192 (≠ A182), G222 (≠ S213), G226 (= G217), G242 (= G233), G243 (≠ S234), T246 (≠ I237), H249 (≠ V240), I250 (≠ L241), C298 (= C289), E399 (= E386), F401 (= F388)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
40% identity, 96% coverage: 10:476/485 of query aligns to 3:471/477 of 2opxA
- active site: N151 (= N156), K174 (= K179), E249 (= E255), C283 (= C289), E381 (= E386), A458 (≠ E463)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y110), F152 (= F157), N284 (≠ V290), F312 (≠ V318), G313 (= G319), R318 (≠ G323), D320 (≠ G325), I321 (≠ V326), A322 (≠ Q327), Y362 (≠ F367), F440 (≠ I445), F440 (≠ I445), E441 (≠ S446)
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)
40% identity, 96% coverage: 10:476/485 of query aligns to 5:473/479 of P25553
- L150 (≠ A153) binding
- R161 (= R164) binding
- KPSE 176:179 (≠ KPAA 179:182) binding
- F180 (≠ E183) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ K218) 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)
40% identity, 96% coverage: 10:476/485 of query aligns to 3:471/477 of 2impA
- active site: N151 (= N156), K174 (= K179), E249 (= E255), C283 (= C289), E381 (= E386), A458 (≠ E463)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I152), L148 (≠ A153), P149 (= P154), W150 (= W155), K174 (= K179), E177 (≠ A182), F178 (≠ E183), G207 (≠ S213), G211 (= G217), Q212 (≠ K218), S228 (= S234), A231 (≠ I237), K234 (≠ V240), R334 (≠ K339)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
40% identity, 96% coverage: 10:476/485 of query aligns to 3:471/477 of 2iluA
- active site: N151 (= N156), K174 (= K179), E249 (= E255), C283 (= C289), E381 (= E386), A458 (≠ E463)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I152), L148 (≠ A153), P149 (= P154), W150 (= W155), K174 (= K179), S176 (≠ A181), E177 (≠ A182), R206 (= R212), G207 (≠ S213), G211 (= G217), Q212 (≠ K218), S228 (= S234), A231 (≠ I237), K234 (≠ V240), I235 (≠ L241), N328 (= N333), R334 (≠ K339), F383 (= F388)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
40% identity, 96% coverage: 12:476/485 of query aligns to 6:474/486 of 4pxlA
- active site: N154 (= N156), K177 (= K179), E253 (= E255), C287 (= C289), E384 (= E386), D461 (≠ E463)
- binding nicotinamide-adenine-dinucleotide: I150 (= I152), V151 (≠ A153), P152 (= P154), W153 (= W155), K177 (= K179), E180 (≠ A182), G210 (≠ R212), G214 (= G217), A215 (≠ K218), F228 (= F231), G230 (= G233), S231 (= S234), V234 (≠ I237), E253 (= E255), G255 (= G257), C287 (= C289), Q334 (≠ A336), K337 (= K339), E384 (= E386), F386 (= F388)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
39% identity, 96% coverage: 10:476/485 of query aligns to 2:473/489 of 4o6rA
- active site: N150 (= N156), K173 (= K179), E248 (= E255), C282 (= C289), E383 (= E386), E460 (= E463)
- binding adenosine monophosphate: I146 (= I152), V147 (≠ A153), K173 (= K179), G206 (≠ S213), G210 (= G217), Q211 (≠ K218), F224 (= F231), G226 (= G233), S227 (= S234), T230 (≠ I237), R233 (≠ V240)
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)
38% identity, 96% coverage: 12:476/485 of query aligns to 20:489/501 of Q56YU0
- G152 (≠ L139) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ A403) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
37% identity, 98% coverage: 10:482/485 of query aligns to 1:479/494 of 5izdA
- active site: N149 (= N156), K172 (= K179), E247 (= E255), C281 (= C289), E381 (= E386), E458 (= E463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I152), T146 (≠ A153), W148 (= W155), K172 (= K179), P173 (= P180), S174 (≠ A181), S175 (≠ A182), R204 (= R212), G205 (≠ S213), G209 (= G217), D210 (≠ K218), G225 (= G233), S226 (= S234), T229 (≠ I237)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
38% identity, 96% coverage: 15:480/485 of query aligns to 106:581/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K179), S310 (≠ T211), G311 (≠ S213), G315 (= G217), G331 (= G233), S332 (= S234), V335 (≠ I237)
- binding 4'-phosphopantetheine: K201 (= K105), F382 (≠ R283), N387 (≠ T288), C388 (= C289), N545 (≠ L444)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
38% identity, 96% coverage: 15:480/485 of query aligns to 21:496/498 of 4go2A
- active site: N170 (= N156), K193 (= K179), E269 (= E255), C303 (= C289), E400 (= E386), D479 (≠ E463)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I152), I167 (≠ A153), P168 (= P154), W169 (= W155), K193 (= K179), A195 (= A181), Q196 (≠ A182), S225 (≠ T211), G226 (≠ S213), G230 (= G217), Q231 (≠ K218), F244 (= F231), G246 (= G233), S247 (= S234), V250 (≠ I237), 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: 15:480/485 of query aligns to 21:496/498 of 2o2rA
- active site: N170 (= N156), K193 (= K179), E269 (= E255), C303 (= C289), E400 (= E386), D479 (≠ E463)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I152), I167 (≠ A153), W169 (= W155), K193 (= K179), A195 (= A181), Q196 (≠ A182), S225 (≠ T211), G226 (≠ S213), G230 (= G217), Q231 (≠ K218), F244 (= F231), S247 (= S234), V250 (≠ I237), I254 (≠ L241)
Query Sequence
>CCNA_03242 FitnessBrowser__Caulo:CCNA_03242
MTCMTALNLVETAALIDGQWVRGEASFDVLNPADGTLIAAVADLGAAETTLAIDAAHRAL
PAWAARTAKERGAILRRWSDLILAHADDLARLMTDEQGKPLAEAKGEVVYGASFIDWFAE
EAKRAYGHTIPTPMPGKRLASIKQPVGVCAAIAPWNFPIAMITRKVGPALAAGCTVVVKP
AAETPLSALAIARLATEAGVPAGVLNIVTTTRSSEVGKVLCDDSRVRKLSFTGSTPIGKV
LYQQCAGTMKKLSLELGGNAPFIVFDDADLEAAVDGAIASKYRNAGQTCVCANRLIVQSG
IHDAFAARLAEKVAALKVGPGTGEGVQIGPLINEKALTKVVGLVSGAVQAGAEVLTGGDV
HGLGGHFYQPTVLVGATPEMRIFQEEIFGPVAPIVKFETEAEAVELANATPFGLAAYFYS
RDVGRCWRVAEQIEAGMVGINEGLISTEVAPFGGVKESGLGREGASEGLDEYLETKYLCF
GGVAG
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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