SitesBLAST
Comparing WP_110205192.1 NCBI__GCF_003194585.1:WP_110205192.1 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)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
48% identity, 99% coverage: 3:380/383 of query aligns to 50:427/430 of P51174
- K318 (= K271) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ Q275) 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)
46% identity, 99% coverage: 3:380/383 of query aligns to 18:395/398 of 8w0uA
- binding acetoacetyl-coenzyme a: M140 (= M127), S147 (= S134), Q150 (= Q137), S193 (≠ G179), H196 (≠ R181), Y250 (≠ G235), E259 (= E244), R260 (= R245), Y379 (≠ F364), G380 (= G365), G381 (= G366), I385 (≠ V370), L389 (≠ I374), R392 (= R377)
- binding flavin-adenine dinucleotide: I138 (= I125), M140 (= M127), T141 (= T128), G146 (= G133), S147 (= S134), F171 (= F158), S173 (≠ T160), R285 (= R270), F288 (= F273), L295 (≠ F280), Q353 (= Q338), L354 (= L339), G357 (= G342), V375 (≠ I360), Y379 (≠ F364), T382 (≠ A367), E384 (= E369)
8w0tA Human lcad (see paper)
46% identity, 99% coverage: 3:380/383 of query aligns to 18:395/398 of 8w0tA
- binding flavin-adenine dinucleotide: I138 (= I125), M140 (= M127), T141 (= T128), G146 (= G133), S147 (= S134), F171 (= F158), I172 (= I159), S173 (≠ T160), R285 (= R270), F288 (= F273), L295 (≠ F280), Q353 (= Q338), L354 (= L339), G356 (= G341), G357 (= G342), V375 (≠ I360), T382 (≠ A367), E384 (= E369), I385 (≠ V370)
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
46% identity, 99% coverage: 3:380/383 of query aligns to 50:427/430 of P28330
- E291 (= E244) 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 (≠ A256) to T: in dbSNP:rs1801204
- K333 (≠ E286) to Q: in dbSNP:rs2286963
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
46% identity, 97% coverage: 8:379/383 of query aligns to 7:378/380 of 2pg0A
- active site: M124 (= M127), T125 (= T128), E243 (= E244), A364 (≠ G365), R376 (= R377)
- binding flavin-adenine dinucleotide: I122 (= I125), M124 (= M127), T125 (= T128), G130 (= G133), S131 (= S134), F155 (= F158), I156 (= I159), T157 (= T160), R269 (= R270), F272 (= F273), F279 (= F280), Q337 (= Q338), L338 (= L339), G340 (= G341), G341 (= G342), V359 (≠ I360), I362 (= I363), Y363 (≠ F364), T366 (≠ A367), E368 (= E369), M369 (≠ V370)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
37% identity, 98% coverage: 5:380/383 of query aligns to 3:377/378 of 5ol2F
- active site: L124 (≠ M127), T125 (= T128), G241 (≠ E244), G374 (≠ R377)
- binding calcium ion: E29 (≠ R31), E33 (= E35), R35 (≠ I37)
- binding coenzyme a persulfide: L238 (= L241), R242 (= R245), E362 (≠ G365), G363 (= G366)
- binding flavin-adenine dinucleotide: F122 (≠ I125), L124 (≠ M127), T125 (= T128), P127 (= P130), T131 (≠ S134), F155 (= F158), I156 (= I159), T157 (= T160), E198 (≠ L201), R267 (= R270), F270 (= F273), L274 (≠ I277), F277 (= F280), Q335 (= Q338), L336 (= L339), G338 (= G341), G339 (= G342), Y361 (≠ F364), T364 (≠ A367), E366 (= E369)
8sgrA Human liver mitochondrial isovaleryl-coa dehydrogenase (see paper)
36% identity, 97% coverage: 7:377/383 of query aligns to 13:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T128), G140 (= G133), S141 (= S134), W165 (≠ F158), T167 (= T160), R279 (= R270), F282 (= F273), I286 (= I277), F289 (= F280), Q347 (= Q338), C348 (≠ L339), G351 (= G342), L369 (≠ I360), G375 (= G366), T376 (≠ A367), L382 (= L373)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
36% identity, 97% coverage: 7:377/383 of query aligns to 9:382/387 of 1ivhA
- active site: M130 (= M127), S131 (≠ T128), E249 (= E244), A370 (≠ G365), R382 (= R377)
- binding coenzyme a persulfide: S137 (= S134), S185 (vs. gap), R186 (= R181), V239 (≠ F234), Y240 (≠ G235), M243 (≠ K238), E249 (= E244), R250 (= R245), G369 (≠ F364), A370 (≠ G365), G371 (= G366), V375 (= V370)
- binding flavin-adenine dinucleotide: L128 (≠ I125), M130 (= M127), S131 (≠ T128), G136 (= G133), S137 (= S134), W161 (≠ F158), T163 (= T160), R275 (= R270), F278 (= F273), F285 (= F280), M288 (≠ T283), Q343 (= Q338), C344 (≠ L339), G347 (= G342), T372 (≠ A367), E374 (= E369)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
36% identity, 98% coverage: 5:379/383 of query aligns to 5:378/378 of 4n5fA
- active site: L126 (≠ M127), T127 (= T128), G243 (≠ E244), E364 (≠ G365), R376 (= R377)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M127), T127 (= T128), G132 (= G133), S133 (= S134), F157 (= F158), T159 (= T160), T210 (= T211), Y363 (≠ F364), T366 (≠ A367), E368 (= E369), M372 (≠ L373)
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)
36% identity, 97% coverage: 7:377/383 of query aligns to 46:419/426 of P26440
- 165:174 (vs. 125:134, 60% identical) binding FAD
- S174 (= S134) binding substrate
- WIT 198:200 (≠ FIT 158:160) binding FAD
- SR 222:223 (≠ -R 181) binding substrate
- G250 (≠ A208) to A: in IVA; uncertain significance
- Y277 (≠ G235) binding substrate
- DLER 284:287 (≠ PLER 242:245) binding substrate
- E286 (= E244) 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 (= A249) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R270) binding FAD
- Q323 (= Q281) binding FAD
- I379 (≠ L337) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QLHGG 338:342) binding FAD
- R398 (≠ Q356) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ Q361) to N: in IVA; uncertain significance
- A407 (≠ G365) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ GG 365:366) binding substrate
- TSE 409:411 (≠ ANE 367:369) binding FAD
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
37% identity, 98% coverage: 7:380/383 of query aligns to 6:378/380 of 4l1fA
- active site: L125 (≠ M127), T126 (= T128), G242 (≠ E244), E363 (≠ G365), R375 (= R377)
- binding coenzyme a persulfide: T132 (≠ S134), H179 (≠ R181), F232 (= F234), M236 (≠ K238), E237 (≠ N239), L239 (= L241), D240 (≠ P242), R243 (= R245), Y362 (≠ F364), E363 (≠ G365), G364 (= G366), R375 (= R377)
- binding flavin-adenine dinucleotide: F123 (≠ I125), L125 (≠ M127), T126 (= T128), G131 (= G133), T132 (≠ S134), F156 (= F158), I157 (= I159), T158 (= T160), R268 (= R270), Q270 (≠ A272), F271 (= F273), I275 (= I277), F278 (= F280), L281 (≠ T283), Q336 (= Q338), I337 (≠ L339), G340 (= G342), I358 (= I360), Y362 (≠ F364), T365 (≠ A367), Q367 (≠ E369)
- binding 1,3-propandiol: Q10 (≠ E11)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
36% identity, 98% coverage: 5:381/383 of query aligns to 1:374/374 of 5lnxD