SitesBLAST
Comparing WP_055435174.1 NCBI__GCF_001418085.1:WP_055435174.1 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)
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
42% identity, 96% coverage: 3:378/390 of query aligns to 2:378/380 of 2pg0A
- active site: M124 (≠ V127), T125 (= T128), E243 (= E243), A364 (≠ G364), R376 (≠ K376)
- binding flavin-adenine dinucleotide: I122 (≠ M125), M124 (≠ V127), T125 (= T128), G130 (= G133), S131 (= S134), F155 (= F158), I156 (= I159), T157 (= T160), R269 (= R269), F272 (= F272), F279 (= F279), Q337 (= Q337), L338 (≠ M338), G340 (= G340), G341 (= G341), V359 (≠ L359), I362 (= I362), Y363 (≠ G363), T366 (= T366), E368 (= E368), M369 (≠ I369)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
38% identity, 97% coverage: 4:380/390 of query aligns to 51:428/430 of P51174
- K318 (≠ Q270) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (= K274) modified: N6-acetyllysine; alternate; mutation to R: Reduces activity by 23%; reduces activity by 80% when associated with R-318.
Sites not aligning to the query:
- 42 modified: N6-acetyllysine; K→R: Reduces activity by 90% when associated with R-318 and R-322.
8w0uA Human lcad complexed with acetoacetyl coenzyme a (see paper)
39% identity, 97% coverage: 4:381/390 of query aligns to 19:398/398 of 8w0uA
- binding acetoacetyl-coenzyme a: M140 (≠ V127), S147 (= S134), Q150 (≠ A137), S193 (≠ N180), H196 (vs. gap), Y250 (≠ P234), E259 (= E243), R260 (= R244), Y379 (≠ G363), G380 (= G364), G381 (= G365), I385 (= I369), L389 (≠ I373), R392 (≠ K376)
- binding flavin-adenine dinucleotide: I138 (≠ M125), M140 (≠ V127), T141 (= T128), G146 (= G133), S147 (= S134), F171 (= F158), S173 (≠ T160), R285 (= R269), F288 (= F272), L295 (≠ F279), Q353 (= Q337), L354 (≠ M338), G357 (= G341), V375 (≠ L359), Y379 (≠ G363), T382 (= T366), E384 (= E368)
8w0tA Human lcad (see paper)
39% identity, 97% coverage: 4:381/390 of query aligns to 19:398/398 of 8w0tA
- binding flavin-adenine dinucleotide: I138 (≠ M125), M140 (≠ V127), T141 (= T128), G146 (= G133), S147 (= S134), F171 (= F158), I172 (= I159), S173 (≠ T160), R285 (= R269), F288 (= F272), L295 (≠ F279), Q353 (= Q337), L354 (≠ M338), G356 (= G340), G357 (= G341), V375 (≠ L359), T382 (= T366), E384 (= E368), I385 (= I369)
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
39% identity, 97% coverage: 4:381/390 of query aligns to 51:430/430 of P28330
- E291 (= E243) active site, Proton acceptor; mutation to Q: Loss of long-chain-acyl-CoA dehydrogenase activity. No effect on protein abundance. No effect on solubility. No effect on substrate binding.
- S303 (≠ A255) to T: in dbSNP:rs1801204
- K333 (≠ T285) to Q: in dbSNP:rs2286963
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
38% identity, 96% coverage: 5:378/390 of query aligns to 4:377/378 of 3r7kA
- active site: V126 (= V127), T127 (= T128), E242 (= E243), G363 (= G364), K375 (= K376)
- binding dihydroflavine-adenine dinucleotide: V126 (= V127), T127 (= T128), G132 (= G133), S133 (= S134), F157 (= F158), I158 (= I159), T159 (= T160), R268 (= R269), T270 (≠ A271), F271 (= F272), L275 (≠ I276), R278 (≠ F279), I281 (≠ L282), Q336 (= Q337), I337 (≠ M338), G340 (= G341), I358 (≠ L359), T365 (= T366), E367 (= E368)
8sgrA Human liver mitochondrial isovaleryl-coa dehydrogenase (see paper)
37% identity, 95% coverage: 6:376/390 of query aligns to 12:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T128), G140 (= G133), S141 (= S134), W165 (≠ F158), T167 (= T160), R279 (= R269), F282 (= F272), I286 (= I276), F289 (= F279), Q347 (= Q337), C348 (≠ M338), G351 (= G341), L369 (= L359), G375 (= G365), T376 (= T366), L382 (≠ E372)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
37% identity, 95% coverage: 6:376/390 of query aligns to 8:382/387 of 1ivhA
- active site: M130 (≠ V127), S131 (≠ T128), E249 (= E243), A370 (≠ G364), R382 (≠ K376)
- binding coenzyme a persulfide: S137 (= S134), S185 (≠ N180), R186 (≠ K181), V239 (≠ F233), Y240 (≠ P234), M243 (= M237), E249 (= E243), R250 (= R244), G369 (= G363), A370 (≠ G364), G371 (= G365), V375 (≠ I369)
- binding flavin-adenine dinucleotide: L128 (≠ M125), M130 (≠ V127), S131 (≠ T128), G136 (= G133), S137 (= S134), W161 (≠ F158), T163 (= T160), R275 (= R269), F278 (= F272), F285 (= F279), M288 (≠ L282), Q343 (= Q337), C344 (≠ M338), G347 (= G341), T372 (= T366), E374 (= E368)
P26440 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Butyryl-CoA dehydrogenase; EC 1.3.8.4; EC 1.3.8.1 from Homo sapiens (Human) (see 5 papers)
37% identity, 95% coverage: 6:376/390 of query aligns to 45:419/426 of P26440
- 165:174 (vs. 125:134, 50% identical) binding FAD
- S174 (= S134) binding substrate
- WIT 198:200 (≠ FIT 158:160) binding FAD
- SR 222:223 (≠ NK 180:181) binding substrate
- G250 (≠ A207) to A: in IVA; uncertain significance
- Y277 (≠ P234) binding substrate
- DLER 284:287 (≠ AFER 241:244) binding substrate
- E286 (= E243) active site, Proton acceptor; mutation to D: Residual isovaleryl-CoA dehydrogenase activity.; mutation to G: Loss of isovaleryl-CoA dehydrogenase activity. Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 407-E.; mutation to Q: Loss of isovaleryl-CoA dehydrogenase activity.
- A291 (≠ G248) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R269) binding FAD
- Q323 (= Q280) binding FAD
- I379 (≠ L336) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QMLGG 337:341) binding FAD
- R398 (= R355) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ G360) to N: in IVA; uncertain significance
- A407 (≠ G364) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ GG 364:365) binding substrate
- TSE 409:411 (= TSE 366:368) binding FAD
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
3p4tA Crystal structure of a putative acyl-coa dehydrogenase from mycobacterium smegmatis (see paper)
37% identity, 96% coverage: 3:378/390 of query aligns to 1:377/381 of 3p4tA
- active site: I125 (≠ V127), T126 (= T128), E241 (= E243), G363 (= G364), K375 (= K376)
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-[(4aS,10aR)-7,8-dimethyl-2,4-dioxo-1,3,4,4a,5,10a-hexahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate: L123 (≠ M125), I125 (≠ V127), T126 (= T128), G130 (= G132), G131 (= G133), S132 (= S134), Y156 (≠ F158), I157 (= I159), T158 (= T160), K200 (= K202), R267 (= R269), T269 (≠ A271), L274 (≠ I276), R277 (≠ F279), Q336 (= Q337), L337 (≠ M338), G340 (= G341), I358 (≠ L359), T365 (= T366)
3oibA Crystal structure of a putative acyl-coa dehydrogenase from mycobacterium smegmatis, iodide soak (see paper)
37% identity, 96% coverage: 3:378/390 of query aligns to 1:377/381 of 3oibA
- active site: I125 (≠ V127), T126 (= T128), E241 (= E243), G363 (= G364), K375 (= K376)
- binding dihydroflavine-adenine dinucleotide: L123 (≠ M125), I125 (≠ V127), T126 (= T128), G131 (= G133), S132 (= S134), Y156 (≠ F158), I157 (= I159), T158 (= T160), K200 (= K202), R267 (= R269), T269 (≠ A271), L274 (≠ I276), R277 (≠ F279), Q336 (= Q337), L337 (≠ M338), G340 (= G341), I358 (≠ L359), T365 (= T366), E367 (= E368)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
37% identity, 96% coverage: 6:379/390 of query aligns to 5:378/380 of 4l1fA