SitesBLAST
Comparing WP_086509800.1 NCBI__GCF_002151265.1:WP_086509800.1 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)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
64% identity, 99% coverage: 4:484/485 of query aligns to 2:481/481 of 3jz4A
- active site: N156 (= N158), K179 (= K181), E254 (= E256), C288 (= C290), E385 (= E388), E462 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P156), W155 (= W157), K179 (= K181), A181 (= A183), S182 (= S184), A212 (= A214), G216 (≠ A218), G232 (= G234), S233 (= S235), I236 (≠ V238), C288 (= C290), K338 (= K341), E385 (= E388), F387 (= F390)
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)
64% identity, 99% coverage: 4:484/485 of query aligns to 3:482/482 of P25526
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565 (see paper)
58% identity, 99% coverage: 3:482/485 of query aligns to 1:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I154), T153 (= T155), P154 (= P156), K179 (= K181), A212 (= A214), K213 (≠ S215), F230 (= F232), T231 (= T233), G232 (= G234), S233 (= S235), V236 (= V238), W239 (≠ E241), G256 (= G258)
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
52% identity, 99% coverage: 1:482/485 of query aligns to 17:497/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (= I154), A171 (≠ T155), P172 (= P156), W173 (= W157), K197 (= K181), A230 (= A214), F248 (= F232), G250 (= G234), S251 (= S235), V254 (= V238), M257 (≠ E241), L273 (= L257), C306 (= C290), K356 (= K341), E403 (= E388), F405 (= F390)
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, 96% coverage: 14:481/485 of query aligns to 63:531/535 of P51649
- C93 (≠ L46) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G129) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P133) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ A135) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R166) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C176) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAS 181:184) binding
- T233 (= T186) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A190) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N208) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ A218) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 234:239) binding
- R334 (= R284) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N285) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C290) modified: Disulfide link with 342, In inhibited form
- C342 (= C292) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D322) natural variant: N -> S
- P382 (= P332) to L: in SSADHD; 2% of activity
- V406 (≠ L356) to I: in dbSNP:rs143741652
- G409 (= G359) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S448) binding ; 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)
54% identity, 96% coverage: 14:481/485 of query aligns to 13:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
54% identity, 96% coverage: 14:481/485 of query aligns to 13:481/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
43% identity, 98% coverage: 6:482/485 of query aligns to 4:474/476 of 5x5uA
- active site: N151 (= N158), K174 (= K181), E249 (= E256), C283 (= C290), E380 (= E388), E457 (= E465)
- binding glycerol: D15 (≠ A22), A16 (= A23), A17 (≠ D24), G19 (= G26)
- binding nicotinamide-adenine-dinucleotide: P149 (= P156), P207 (≠ A214), A208 (≠ S215), S211 (≠ A218), G227 (= G234), S228 (= S235), V231 (= V238), R329 (≠ K337), R330 (≠ A338), E380 (= E388), F382 (= F390)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
43% identity, 98% coverage: 6:482/485 of query aligns to 4:474/476 of 5x5tA
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
39% identity, 98% coverage: 2:478/485 of query aligns to 7:492/498 of 4go2A
- active site: N170 (= N158), K193 (= K181), E269 (= E256), C303 (= C290), E400 (= E388), D479 (≠ E465)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I154), I167 (≠ T155), P168 (= P156), W169 (= W157), K193 (= K181), A195 (= A183), Q196 (≠ S184), S225 (≠ R213), G226 (≠ A214), G230 (≠ A218), Q231 (≠ S219), F244 (= F232), G246 (= G234), S247 (= S235), V250 (= V238), I254 (≠ L242), E269 (= E256), G271 (= G258), C303 (= C290), E400 (= E388), F402 (= F390)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
39% identity, 98% coverage: 2:478/485 of query aligns to 7:492/498 of 2o2rA
- active site: N170 (= N158), K193 (= K181), E269 (= E256), C303 (= C290), E400 (= E388), D479 (≠ E465)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I154), I167 (≠ T155), W169 (= W157), K193 (= K181), A195 (= A183), Q196 (≠ S184), S225 (≠ R213), G226 (≠ A214), G230 (≠ A218), Q231 (≠ S219), F244 (= F232), S247 (= S235), V250 (= V238), I254 (≠ L242)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
38% identity, 99% coverage: 2:483/485 of query aligns to 92:582/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K181), S310 (≠ R213), G311 (≠ A214), G315 (≠ A218), G331 (= G234), S332 (= S235), V335 (= V238)
- binding 4'-phosphopantetheine: K201 (≠ A107), F382 (≠ R284), N387 (≠ T289), C388 (= C290), N545 (≠ L446)
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, 99% coverage: 2:483/485 of query aligns to 411:901/902 of P28037
- IPW 571:573 (≠ TPW 155:157) binding
- KPAQ 597:600 (≠ KPAS 181:184) binding
- GSLVGQ 630:635 (≠ ASEIAS 214:219) binding
- GS 650:651 (= GS 234:235) binding
- E673 (= E256) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 256:257) binding
- C707 (= C290) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K341) binding
- ESF 804:806 (≠ ETF 388:390) 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.
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
36% identity, 97% coverage: 15:483/485 of query aligns to 6:476/494 of 5izdA
- active site: N149 (= N158), K172 (= K181), E247 (= E256), C281 (= C290), E381 (= E388), E458 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I154), T146 (= T155), W148 (= W157), K172 (= K181), P173 (= P182), S174 (≠ A183), S175 (= S184), R204 (= R213), G205 (≠ A214), G209 (≠ A218), D210 (≠ S219), G225 (= G234), S226 (= S235), T229 (≠ V238)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
39% identity, 97% coverage: 15:484/485 of query aligns to 9:480/486 of 4pxlA
- active site: N154 (= N158), K177 (= K181), E253 (= E256), C287 (= C290), E384 (= E388), D461 (≠ E465)
- binding nicotinamide-adenine-dinucleotide: I150 (= I154), V151 (≠ T155), P152 (= P156), W153 (= W157), K177 (= K181), E180 (≠ S184), G210 (≠ A214), G214 (≠ A218), A215 (≠ S219), F228 (= F232), G230 (= G234), S231 (= S235), V234 (= V238), E253 (= E256), G255 (= G258), C287 (= C290), Q334 (≠ A338), K337 (= K341), E384 (= E388), F386 (= F390)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
36% identity, 97% coverage: 15:483/485 of query aligns to 5:476/477 of 6j76A
- active site: N148 (= N158), E246 (= E256), C280 (= C290), E458 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I154), T145 (= T155), A146 (≠ P156), W147 (= W157), N148 (= N158), K171 (= K181), T173 (≠ A183), S174 (= S184), G204 (≠ A214), G208 (≠ A218), T223 (= T233), G224 (= G234), S225 (= S235), A228 (≠ V238), S231 (≠ E241), I232 (≠ L242), E246 (= E256), L247 (= L257), C280 (= C290), E381 (= E388), F383 (= F390), H447 (≠ F454)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 97% coverage: 15:484/485 of query aligns to 20:490/491 of 5gtlA
- active site: N165 (= N158), K188 (= K181), E263 (= E256), C297 (= C290), E394 (= E388), E471 (= E465)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I154), P163 (= P156), K188 (= K181), A190 (= A183), E191 (≠ S184), Q192 (= Q185), G221 (≠ A214), G225 (≠ A218), G241 (= G234), S242 (= S235), T245 (≠ V238), L264 (= L257), C297 (= C290), E394 (= E388), F396 (= F390)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 97% coverage: 15:484/485 of query aligns to 20:490/491 of 5gtkA
- active site: N165 (= N158), K188 (= K181), E263 (= E256), C297 (= C290), E394 (= E388), E471 (= E465)
- binding nicotinamide-adenine-dinucleotide: I161 (= I154), I162 (≠ T155), P163 (= P156), W164 (= W157), K188 (= K181), E191 (≠ S184), G221 (≠ A214), G225 (≠ A218), A226 (≠ S219), F239 (= F232), G241 (= G234), S242 (= S235), T245 (≠ V238), Y248 (≠ E241), L264 (= L257), C297 (= C290), Q344 (≠ A338), R347 (≠ K341), E394 (= E388), F396 (= F390)
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, 96% coverage: 15:482/485 of query aligns to 10:477/479 of P25553
- L150 (≠ T155) binding
- R161 (= R166) binding
- KPSE 176:179 (≠ KPAS 181:184) binding
- F180 (≠ Q185) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ S219) binding
- S230 (= S235) binding
- E251 (= E256) binding
- N286 (≠ I291) 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 (≠ K341) binding
- E443 (≠ S448) binding
- H449 (≠ F454) 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)
38% identity, 96% coverage: 15:482/485 of query aligns to 8:475/477 of 2impA
- active site: N151 (= N158), K174 (= K181), E249 (= E256), C283 (= C290), E381 (= E388), A458 (≠ E465)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I154), L148 (≠ T155), P149 (= P156), W150 (= W157), K174 (= K181), E177 (≠ S184), F178 (≠ Q185), G207 (≠ A214), G211 (≠ A218), Q212 (≠ S219), S228 (= S235), A231 (≠ V238), K234 (≠ E241), R334 (≠ K341)
Query Sequence
>WP_086509800.1 NCBI__GCF_002151265.1:WP_086509800.1
MEALKETQLYCPFAYIDGSWVAADSGEQIEVVNPATGETFGTVPRLGRAETERAIAAADA
ALVGWRALTAQERADILMKWHDLMMEHQDDLAMIMTHEQGKPLKEAAGEIAYAASFLRWF
AEEARRIYGETIPAAKPNQRIVVTKQPVGVVGAITPWNFPAAMITRKAGAALAAGCTIVI
KPASQTPFSATALALLAERAGIPRGVFNVVPGRASEIASAMTESPLVRKITFTGSTEVGR
ELMAQASRHIQKISLELGGNAPFIVFEDADLDAAVEGAMAAKFRNAGQTCICTNRFLVQS
SVINAFCEKLAVAMNSELKVGDGTEPDINIGPLIDEKAVAKVSEHVHDAVDKGAELLLGG
NPHPLGGNFFSPTLISFANADMKVAHEETFGPLAAVFPFEDEEDAVQMANDTQYGLASYF
YSRDLGRVWRVADALEYGMVGINTGLISNTAAPFGGVKASGLGREGGHQGIEEFLETKYL
CIDLG
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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