SitesBLAST
Comparing Ac3H11_2991 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) 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)
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
70% identity, 97% coverage: 9:394/396 of query aligns to 5:377/377 of 4ktoA
- active site: M130 (= M134), S131 (= S135), E239 (= E251), A360 (= A377), R372 (= R389)
- binding flavin-adenine dinucleotide: L128 (= L132), A129 (= A133), M130 (= M134), S131 (= S135), M155 (= M164), W156 (= W165), I157 (= I166), T158 (= T167), R265 (= R277), Q267 (= Q279), F268 (= F280), I272 (= I284), F275 (= F287), M278 (≠ I290), Q333 (= Q350), A334 (≠ I351), G337 (= G354), L355 (= L372), I358 (= I375), G359 (= G376), A360 (= A377), G361 (= G378), T362 (= T379), E364 (= E381), I365 (= I382)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
62% identity, 96% coverage: 14:394/396 of query aligns to 8:387/387 of 1ivhA
- active site: M130 (= M134), S131 (= S135), E249 (= E251), A370 (= A377), R382 (= R389)
- binding coenzyme a persulfide: M130 (= M134), G136 (= G140), S137 (= S141), V139 (= V143), V140 (≠ I144), S185 (≠ A187), R186 (= R188), V239 (≠ A241), Y240 (≠ K242), M243 (= M245), L246 (= L248), D247 (= D249), E249 (= E251), R250 (= R252), G369 (= G376), A370 (= A377), G371 (= G378), V375 (≠ I382), R382 (= R389)
- binding flavin-adenine dinucleotide: L128 (= L132), A129 (= A133), M130 (= M134), S131 (= S135), G136 (= G140), S137 (= S141), W161 (= W165), I162 (= I166), T163 (= T167), T216 (= T218), R275 (= R277), A277 (≠ Q279), F278 (= F280), I282 (= I284), F285 (= F287), L287 (= L289), M288 (≠ I290), Q343 (= Q350), C344 (≠ I351), G346 (= G353), G347 (= G354), L365 (= L372), I368 (= I375), T372 (= T379), E374 (= E381), L378 (≠ M385)
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)
62% identity, 96% coverage: 14:394/396 of query aligns to 45:424/426 of P26440
- 165:174 (vs. 132:141, 90% identical) binding
- S174 (= S141) binding
- WIT 198:200 (= WIT 165:167) binding
- SR 222:223 (≠ AR 187:188) binding
- G250 (= G215) to A: in IVA; unknown pathological significance
- Y277 (≠ K242) binding
- DLER 284:287 (≠ DYER 249:252) binding
- E286 (= E251) 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 (≠ T256) to V: in IVA; unknown pathological significance; dbSNP:rs886042098
- R312 (= R277) binding
- Q323 (= Q288) binding
- I379 (≠ V349) to T: in IVA; unknown pathological significance
- QCFGG 380:384 (≠ QIYGG 350:354) binding
- R398 (= R368) to Q: in IVA; unknown pathological significance; dbSNP:rs1477527791
- Y403 (= Y373) to N: in IVA; unknown pathological significance
- A407 (= A377) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (= AG 377:378) binding
- TSE 409:411 (= TSE 379:381) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
43% identity, 94% coverage: 21:392/396 of query aligns to 9:373/374 of 5lnxD
- active site: L122 (≠ M134), T123 (≠ S135), G239 (≠ E251), E358 (≠ A377), K370 (≠ R389)
- binding flavin-adenine dinucleotide: F120 (≠ L132), L122 (≠ M134), T123 (≠ S135), G128 (= G140), S129 (= S141), F153 (≠ W165), I154 (= I166), T155 (= T167), R265 (= R277), Q267 (= Q279), F268 (= F280), I272 (= I284), N275 (≠ F287), I278 (= I290), Q331 (= Q350), I332 (= I351), G334 (= G353), G335 (= G354), Y336 (≠ N355), Y357 (≠ G376), T360 (= T379), E362 (= E381)
5ol2C The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
40% identity, 94% coverage: 21:392/396 of query aligns to 11:377/378 of 5ol2C
- active site: L124 (≠ M134), T125 (≠ S135), G241 (≠ E251), G374 (≠ R389)
- binding calcium ion: E29 (≠ D39), E33 (≠ S43)
- binding coenzyme a persulfide: T125 (≠ S135), T131 (≠ S141), S134 (≠ I144), F231 (≠ A241), M235 (= M245), L238 (= L248), R242 (= R252), E362 (≠ A377), G363 (= G378), V367 (≠ I382)
- binding flavin-adenine dinucleotide: F122 (≠ L132), L124 (≠ M134), T125 (≠ S135), P127 (= P137), G130 (= G140), T131 (≠ S141), F155 (≠ W165), F155 (≠ W165), I156 (= I166), T157 (= T167), T208 (= T218), R267 (= R277), Q269 (= Q279), F270 (= F280), L274 (≠ I284), F277 (= F287), T280 (≠ I290), Q335 (= Q350), L336 (≠ I351), H337 (≠ Y352), G338 (= G353), G339 (= G354), Y340 (≠ N355), Y340 (≠ N355), T343 (≠ I358), D345 (≠ E360), Y346 (= Y361), I357 (≠ L372), I360 (= I375), Y361 (≠ G376), G363 (= G378), T364 (= T379), E366 (= E381)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
38% identity, 96% coverage: 11:392/396 of query aligns to 4:380/384 of 1jqiA
- active site: G377 (≠ R389)
- binding acetoacetyl-coenzyme a: L95 (= L102), F125 (≠ L132), L127 (≠ M134), G133 (= G140), S134 (= S141), A136 (≠ V143), K181 (≠ R188), F234 (≠ A241), K235 (= K242), M238 (= M245), Q239 (≠ S246), L241 (= L248), D242 (= D249), R245 (= R252), T315 (≠ R327), Y364 (≠ G376), E365 (≠ A377), G366 (= G378), I370 (= I382)
- binding flavin-adenine dinucleotide: F125 (≠ L132), A126 (= A133), L127 (≠ M134), S128 (= S135), G133 (= G140), S134 (= S141), W158 (= W165), I159 (= I166), T160 (= T167), K203 (= K210), T211 (= T218), R270 (= R277), F273 (= F280), L277 (≠ I284), L280 (≠ F287), I283 (= I290), Q338 (= Q350), I339 (= I351), G341 (= G353), G342 (= G354), Y345 (= Y357), I360 (≠ L372), Y364 (≠ G376), T367 (= T379), E369 (= E381), I370 (= I382), L373 (≠ M385)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
38% identity, 96% coverage: 11:392/396 of query aligns to 31:407/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
39% identity, 96% coverage: 11:392/396 of query aligns to 31:407/412 of P16219
- G90 (= G70) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E84) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 132:141, 70% identical) binding in other chain
- R171 (≠ E151) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 165:167) binding in other chain
- A192 (= A172) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G189) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R277) binding
- Q308 (= Q288) binding in other chain
- R325 (= R305) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ A338) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIYGG 350:354) binding
- R380 (= R365) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (= TSE 379:381) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
38% identity, 97% coverage: 10:392/396 of query aligns to 1:378/380 of 4l1fA
- active site: L125 (≠ M134), T126 (≠ S135), G242 (≠ E251), E363 (≠ A377), R375 (= R389)
- binding coenzyme a persulfide: F123 (≠ L132), T132 (≠ S141), A134 (≠ V143), V178 (≠ A187), H179 (≠ R188), F232 (≠ A241), M236 (= M245), E237 (≠ S246), L239 (= L248), D240 (= D249), R243 (= R252), S313 (≠ R327), Y362 (≠ G376), E363 (≠ A377), G364 (= G378), V368 (≠ I382), R375 (= R389)
- binding flavin-adenine dinucleotide: F123 (≠ L132), L125 (≠ M134), T126 (≠ S135), G131 (= G140), T132 (≠ S141), F156 (≠ W165), I157 (= I166), T158 (= T167), T209 (= T218), R268 (= R277), Q270 (= Q279), F271 (= F280), I275 (= I284), F278 (= F287), L281 (≠ I290), Q336 (= Q350), I337 (= I351), G339 (= G353), G340 (= G354), Y341 (≠ N355), I358 (≠ L372), Y362 (≠ G376), T365 (= T379), Q367 (≠ E381), I371 (≠ M385)
- binding 1,3-propandiol: L5 (= L14), T6 (≠ G15), Q10 (≠ D19)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
39% identity, 96% coverage: 14:392/396 of query aligns to 1:367/371 of 2vigB
- active site: L121 (≠ M134), S122 (= S135), G231 (≠ E251), E352 (≠ A377), G364 (≠ R389)
- binding coenzyme a persulfide: F119 (≠ L132), G127 (= G140), S128 (= S141), F221 (≠ A241), K222 (= K242), M225 (= M245), Q226 (≠ S246), L228 (= L248), D229 (= D249), R232 (= R252), I302 (≠ R327), E352 (≠ A377), G353 (= G378), I357 (= I382)
- binding flavin-adenine dinucleotide: F119 (≠ L132), A120 (= A133), L121 (≠ M134), S122 (= S135), G127 (= G140), S128 (= S141), A151 (≠ M164), W152 (= W165), I153 (= I166), T154 (= T167), K190 (= K210), T198 (= T218), R257 (= R277), F260 (= F280), L264 (≠ I284), L267 (≠ F287), I270 (= I290), Q325 (= Q350), I326 (= I351), G328 (= G353), G329 (= G354), I347 (≠ L372), I350 (= I375), Y351 (≠ G376), T354 (= T379), E356 (= E381), I357 (= I382), L360 (≠ M385)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
36% identity, 97% coverage: 10:393/396 of query aligns to 1:378/379 of 1ukwB