SitesBLAST
Comparing WP_026607193.1 NCBI__GCF_000427445.1:WP_026607193.1 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)
57% identity, 100% coverage: 1:482/484 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
57% identity, 99% coverage: 4:482/484 of query aligns to 3:480/481 of 3jz4A
- active site: N156 (= N157), K179 (= K180), E254 (= E256), C288 (= C290), E385 (= E387), E462 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P155), W155 (= W156), K179 (= K180), A181 (= A182), S182 (≠ E183), A212 (= A214), G216 (= G218), G232 (= G234), S233 (= S235), I236 (≠ V238), C288 (= C290), K338 (= K340), E385 (= E387), F387 (= F389)
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)
56% identity, 99% coverage: 8:484/484 of query aligns to 58:535/535 of P51649
- C93 (= C45) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G128) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ D132) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P134) 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 (= KPAE 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 (= N207) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G218) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 234:239) binding NAD(+)
- R334 (= R284) binding substrate; 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 (≠ A321) natural variant: N -> S
- P382 (= P331) to L: in SSADHD; 2% of activity
- V406 (≠ L355) to I: in dbSNP:rs143741652
- G409 (= G358) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S447) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G482) 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)
56% identity, 99% coverage: 8:484/484 of query aligns to 8:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
56% identity, 99% coverage: 8:484/484 of query aligns to 8:485/485 of 2w8qA
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
54% identity, 99% coverage: 4:484/484 of query aligns to 21:500/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (= I153), A171 (≠ T154), P172 (= P155), W173 (= W156), K197 (= K180), A230 (= A214), F248 (= F232), G250 (= G234), S251 (= S235), V254 (= V238), M257 (≠ T241), L273 (= L257), C306 (= C290), K356 (= K340), E403 (= E387), F405 (= F389)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565 (see paper)
54% identity, 99% coverage: 4:484/484 of query aligns to 3:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I153), T153 (= T154), P154 (= P155), K179 (= K180), A212 (= A214), K213 (≠ A215), F230 (= F232), T231 (= T233), G232 (= G234), S233 (= S235), V236 (= V238), W239 (≠ T241), G256 (= G258)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
42% identity, 99% coverage: 5:481/484 of query aligns to 4:474/476 of 5x5uA
- active site: N151 (= N157), K174 (= K180), E249 (= E256), C283 (= C290), E380 (= E387), E457 (= E464)
- binding glycerol: D15 (≠ E21), A16 (= A22), A17 (= A23), G19 (= G25)
- binding nicotinamide-adenine-dinucleotide: P149 (= P155), P207 (≠ A214), A208 (= A215), S211 (≠ G218), G227 (= G234), S228 (= S235), V231 (= V238), R329 (≠ E336), R330 (≠ A337), E380 (= E387), F382 (= F389)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
42% identity, 99% coverage: 5:481/484 of query aligns to 4:474/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
39% identity, 98% coverage: 10:481/484 of query aligns to 1:475/477 of 6j76A
- active site: N148 (= N157), E246 (= E256), C280 (= C290), E458 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I153), T145 (= T154), A146 (≠ P155), W147 (= W156), N148 (= N157), K171 (= K180), T173 (≠ A182), S174 (≠ E183), G204 (≠ A214), G208 (= G218), T223 (= T233), G224 (= G234), S225 (= S235), A228 (≠ V238), S231 (≠ T241), I232 (= I242), E246 (= E256), L247 (= L257), C280 (= C290), E381 (= E387), F383 (= F389), H447 (≠ F453)
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)
40% identity, 98% coverage: 7:479/484 of query aligns to 14:491/505 of 4neaA
- active site: N166 (= N157), K189 (= K180), E264 (= E256), C298 (= C290), E399 (= E387), E476 (= E464)
- binding nicotinamide-adenine-dinucleotide: P164 (= P155), K189 (= K180), E192 (= E183), G222 (≠ A214), G226 (= G218), G242 (= G234), G243 (≠ S235), T246 (≠ V238), H249 (≠ T241), I250 (= I242), C298 (= C290), E399 (= E387), F401 (= F389)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
43% identity, 97% coverage: 12:479/484 of query aligns to 12:484/494 of 4pz2B
- active site: N159 (= N157), K182 (= K180), E258 (= E256), C292 (= C290), E392 (= E387), D469 (≠ E464)
- binding nicotinamide-adenine-dinucleotide: I155 (= I153), I156 (≠ T154), P157 (= P155), W158 (= W156), N159 (= N157), M164 (= M162), K182 (= K180), A184 (= A182), E185 (= E183), G215 (≠ A214), G219 (= G218), F233 (= F232), T234 (= T233), G235 (= G234), S236 (= S235), V239 (= V238), E258 (= E256), L259 (= L257), C292 (= C290), E392 (= E387), F394 (= F389)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
43% identity, 97% coverage: 12:479/484 of query aligns to 7:476/486 of 4pxlA
- active site: N154 (= N157), K177 (= K180), E253 (= E256), C287 (= C290), E384 (= E387), D461 (≠ E464)
- binding nicotinamide-adenine-dinucleotide: I150 (= I153), V151 (≠ T154), P152 (= P155), W153 (= W156), K177 (= K180), E180 (= E183), G210 (≠ A214), G214 (= G218), A215 (≠ R219), F228 (= F232), G230 (= G234), S231 (= S235), V234 (= V238), E253 (= E256), G255 (= G258), C287 (= C290), Q334 (≠ A337), K337 (= K340), E384 (= E387), F386 (= F389)
Q63639 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Rattus norvegicus (Rat) (see paper)
41% identity, 97% coverage: 12:481/484 of query aligns to 39:511/518 of Q63639
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
40% identity, 97% coverage: 12:481/484 of query aligns to 13:485/492 of 6b5hA
- active site: N161 (= N157), E260 (= E256), C294 (= C290), E468 (= E464)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ E108), G116 (= G112), F162 (= F158), W169 (≠ R165), Q284 (≠ A280), F288 (≠ R284), T295 (≠ V291), N449 (≠ V445), L451 (≠ S447), N452 (≠ T448), F457 (= F453)
- binding nicotinamide-adenine-dinucleotide: I157 (= I153), I158 (≠ T154), W160 (= W156), N161 (= N157), K184 (= K180), G217 (≠ A214), G221 (= G218), F235 (= F232), T236 (= T233), G237 (= G234), S238 (= S235), V241 (= V238), E260 (= E256), L261 (= L257), C294 (= C290), F393 (= F389)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
40% identity, 97% coverage: 12:481/484 of query aligns to 13:485/492 of 6b5gA
- active site: N161 (= N157), E260 (= E256), C294 (= C290), E468 (= E464)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F158), L165 (≠ A161), W169 (≠ R165), F288 (≠ R284), C293 (≠ T289), C294 (= C290), T295 (≠ V291), N449 (≠ V445), L451 (≠ S447)
- binding nicotinamide-adenine-dinucleotide: I157 (= I153), I158 (≠ T154), P159 (= P155), W160 (= W156), N161 (= N157), M166 (= M162), K184 (= K180), E187 (= E183), G217 (≠ A214), G221 (= G218), F235 (= F232), T236 (= T233), G237 (= G234), S238 (= S235), V241 (= V238), E260 (= E256), L261 (= L257), C294 (= C290), E391 (= E387), F393 (= F389)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
40% identity, 97% coverage: 12:481/484 of query aligns to 13:485/492 of 6aljA
- active site: N161 (= N157), E260 (= E256), C294 (= C290), E468 (= E464)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (= G112), F162 (= F158), L165 (≠ A161), M166 (= M162), W169 (≠ R165), E260 (= E256), C293 (≠ T289), C294 (= C290), L451 (≠ S447), N452 (≠ T448), A453 (≠ V449)
- binding nicotinamide-adenine-dinucleotide: I157 (= I153), I158 (≠ T154), P159 (= P155), W160 (= W156), N161 (= N157), K184 (= K180), E187 (= E183), G217 (≠ A214), G221 (= G218), F235 (= F232), G237 (= G234), S238 (= S235), V241 (= V238), Q341 (≠ A337), K344 (= K340), E391 (= E387), F393 (= F389)
O94788 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Homo sapiens (Human) (see 6 papers)
40% identity, 97% coverage: 12:481/484 of query aligns to 39:511/518 of O94788
- E50 (≠ A23) to G: in dbSNP:rs34266719
- A110 (≠ H80) to V: in dbSNP:rs35365164
- Q182 (≠ A152) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPW 154:156) binding NAD(+)
- KPAE 210:213 (= KPAE 180:183) binding NAD(+)
- STE 264:266 (= STE 235:237) binding NAD(+)
- C320 (= C290) active site, Nucleophile
- R347 (≠ L317) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K318) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ EAVAK 336:340) binding NAD(+)
- A383 (= A353) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E387) binding NAD(+)
- E436 (≠ G406) to K: in dbSNP:rs34744827
- S461 (≠ A431) to Y: in DIH4; decreased retinoic acid biosynthetic process
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
39% identity, 97% coverage: 14:481/484 of query aligns to 26:495/503 of O14293
- S248 (= S235) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
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)
39% identity, 97% coverage: 12:479/484 of query aligns to 21:491/501 of Q56YU0
- G152 (≠ I140) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ V404) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
Query Sequence
>WP_026607193.1 NCBI__GCF_000427445.1:WP_026607193.1
MNARDSKLLRHKAFIGGEWVEAARGGSFEVLDPATGLAIAHVADCSAEDAERAIEAAQAS
FVVWRATLARERARLLRRWHELIMEHKDDLGDLLAREQGKPLAEARAEIVYGAAFVEWFA
EEARRVYGDLIDAPAPGREILVMKQPVGVVAAITPWNFPNAMITRKIAPALAAGCAAIVK
PAEETPLSALALGALAQEAGFPRGLVNILPTTRAAEVGRVLTSHPLVRKVSFTGSTEVGR
TIMRQSAETIKSLSLELGGNAPFIVFDDADLDAVVAGAVASKYRNSGQTCVCANRFYVQA
GIYEAFAEKLAAAVRALKVGAAFEPGTQQGPLITPEAVAKVESLVNDAVDKGAKLRLGGA
RHARGGNFFEPTVLADVPADARLLTEEIFGPVAALVRFETETEVIGLANASEAGLAAYFY
TKDLARAFRVARAIEAGIVGVNQAVISTVEAPFGGVKQSGLGREGARHGIDEYLEVKAVH
IGGL
Or try a new SitesBLAST search
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