SitesBLAST
Comparing Pf6N2E2_2191 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) 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)
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
73% identity, 98% coverage: 6:385/387 of query aligns to 6:377/377 of 4ktoA
- active site: M130 (= M130), S131 (= S131), E239 (= E247), A360 (= A368), R372 (= R380)
- binding flavin-adenine dinucleotide: L128 (= L128), A129 (= A129), M130 (= M130), S131 (= S131), M155 (≠ T160), W156 (= W161), I157 (= I162), T158 (= T163), R265 (= R273), Q267 (= Q275), F268 (= F276), I272 (= I280), F275 (= F283), M278 (≠ I286), Q333 (= Q341), A334 (≠ I342), G337 (= G345), L355 (= L363), I358 (= I366), G359 (= G367), A360 (= A368), G361 (= G369), T362 (= T370), E364 (= E372), I365 (= I373)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
66% identity, 96% coverage: 10:380/387 of query aligns to 8:382/387 of 1ivhA
- active site: M130 (= M130), S131 (= S131), E249 (= E247), A370 (= A368), R382 (= R380)
- binding coenzyme a persulfide: M130 (= M130), G136 (= G136), S137 (= S137), V139 (= V139), V140 (= V140), S185 (vs. gap), R186 (≠ H184), V239 (= V237), Y240 (≠ K238), M243 (= M241), L246 (= L244), D247 (= D245), E249 (= E247), R250 (= R248), G369 (= G367), A370 (= A368), G371 (= G369), V375 (≠ I373), R382 (= R380)
- binding flavin-adenine dinucleotide: L128 (= L128), A129 (= A129), M130 (= M130), S131 (= S131), G136 (= G136), S137 (= S137), W161 (= W161), I162 (= I162), T163 (= T163), T216 (= T214), R275 (= R273), A277 (≠ Q275), F278 (= F276), I282 (= I280), F285 (= F283), L287 (= L285), M288 (≠ I286), Q343 (= Q341), C344 (≠ I342), G346 (= G344), G347 (= G345), L365 (= L363), I368 (= I366), T372 (= T370), E374 (= E372), L378 (≠ M376)
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)
66% identity, 96% coverage: 10:380/387 of query aligns to 45:419/426 of P26440
- 165:174 (vs. 128:137, 100% identical) binding
- S174 (= S137) binding
- WIT 198:200 (= WIT 161:163) binding
- SR 222:223 (≠ -H 184) binding
- G250 (= G211) to A: in IVA; unknown pathological significance
- Y277 (≠ K238) binding
- DLER 284:287 (≠ DYER 245:248) binding
- E286 (= E247) 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 (≠ S252) to V: in IVA; unknown pathological significance; dbSNP:rs886042098
- R312 (= R273) binding
- Q323 (= Q284) binding
- I379 (= I340) to T: in IVA; unknown pathological significance
- QCFGG 380:384 (≠ QILGG 341:345) binding
- R398 (= R359) to Q: in IVA; unknown pathological significance; dbSNP:rs1477527791
- Y403 (= Y364) to N: in IVA; unknown pathological significance
- A407 (= A368) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (= AG 368:369) binding
- TSE 409:411 (= TSE 370:372) 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, 95% coverage: 16:383/387 of query aligns to 8:373/374 of 5lnxD
- active site: L122 (≠ M130), T123 (≠ S131), G239 (≠ E247), E358 (≠ A368), K370 (≠ R380)
- binding flavin-adenine dinucleotide: F120 (≠ L128), L122 (≠ M130), T123 (≠ S131), G128 (= G136), S129 (= S137), F153 (≠ W161), I154 (= I162), T155 (= T163), R265 (= R273), Q267 (= Q275), F268 (= F276), I272 (= I280), N275 (≠ F283), I278 (= I286), Q331 (= Q341), I332 (= I342), G334 (= G344), G335 (= G345), Y336 (≠ N346), Y357 (≠ G367), T360 (= T370), E362 (= E372)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
42% identity, 98% coverage: 10:387/387 of query aligns to 34:411/412 of P16219
- G90 (= G66) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E80) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 128:137, 60% identical) binding in other chain
- R171 (≠ D147) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 161:163) binding in other chain
- A192 (= A168) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G185) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R273) binding
- Q308 (= Q284) binding in other chain
- R325 (= R301) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ A329) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (= QILGG 341:345) binding
- R380 (= R356) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (= TSE 370:372) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
41% identity, 98% coverage: 10:387/387 of query aligns to 34:411/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
41% identity, 98% coverage: 10:387/387 of query aligns to 7:384/384 of 1jqiA
- active site: G377 (≠ R380)
- binding acetoacetyl-coenzyme a: L95 (= L98), F125 (≠ L128), L127 (≠ M130), G133 (= G136), S134 (= S137), A136 (≠ V139), K181 (≠ H184), F234 (≠ V237), K235 (= K238), M238 (= M241), Q239 (≠ S242), L241 (= L244), D242 (= D245), R245 (= R248), T315 (≠ R318), Y364 (≠ G367), E365 (≠ A368), G366 (= G369), I370 (= I373)
- binding flavin-adenine dinucleotide: F125 (≠ L128), A126 (= A129), L127 (≠ M130), S128 (= S131), G133 (= G136), S134 (= S137), W158 (= W161), I159 (= I162), T160 (= T163), K203 (= K206), T211 (= T214), R270 (= R273), F273 (= F276), L277 (≠ I280), L280 (≠ F283), I283 (= I286), Q338 (= Q341), I339 (= I342), G341 (= G344), G342 (= G345), Y345 (= Y348), I360 (≠ L363), Y364 (≠ G367), T367 (= T370), E369 (= E372), I370 (= I373), L373 (≠ M376)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
42% identity, 98% coverage: 10:387/387 of query aligns to 1:371/371 of 2vigB
- active site: L121 (≠ M130), S122 (= S131), G231 (≠ E247), E352 (≠ A368), G364 (≠ R380)
- binding coenzyme a persulfide: F119 (≠ L128), G127 (= G136), S128 (= S137), F221 (≠ V237), K222 (= K238), M225 (= M241), Q226 (≠ S242), L228 (= L244), D229 (= D245), R232 (= R248), I302 (≠ R318), E352 (≠ A368), G353 (= G369), I357 (= I373)
- binding flavin-adenine dinucleotide: F119 (≠ L128), A120 (= A129), L121 (≠ M130), S122 (= S131), G127 (= G136), S128 (= S137), A151 (≠ T160), W152 (= W161), I153 (= I162), T154 (= T163), K190 (= K206), T198 (= T214), R257 (= R273), F260 (= F276), L264 (≠ I280), L267 (≠ F283), I270 (= I286), Q325 (= Q341), I326 (= I342), G328 (= G344), G329 (= G345), I347 (≠ L363), I350 (= I366), Y351 (≠ G367), T354 (= T370), E356 (= E372), I357 (= I373), L360 (≠ M376)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
38% identity, 98% coverage: 6:385/387 of query aligns to 1:380/380 of 4l1fA
- active site: L125 (≠ M130), T126 (≠ S131), G242 (≠ E247), E363 (≠ A368), R375 (= R380)
- binding coenzyme a persulfide: F123 (≠ L128), T132 (≠ S137), A134 (≠ V139), V178 (≠ P183), H179 (= H184), F232 (≠ V237), M236 (= M241), E237 (≠ S242), L239 (= L244), D240 (= D245), R243 (= R248), S313 (≠ R318), Y362 (≠ G367), E363 (≠ A368), G364 (= G369), V368 (≠ I373), R375 (= R380)
- binding flavin-adenine dinucleotide: F123 (≠ L128), L125 (≠ M130), T126 (≠ S131), G131 (= G136), T132 (≠ S137), F156 (≠ W161), I157 (= I162), T158 (= T163), T209 (= T214), R268 (= R273), Q270 (= Q275), F271 (= F276), I275 (= I280), F278 (= F283), L281 (≠ I286), Q336 (= Q341), I337 (= I342), G339 (= G344), G340 (= G345), Y341 (≠ N346), I358 (≠ L363), Y362 (≠ G367), T365 (= T370), Q367 (≠ E372), I371 (≠ M376)
- binding 1,3-propandiol: L5 (= L10), T6 (≠ G11), Q10 (≠ D15)
5ol2C The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
40% identity, 95% coverage: 16:384/387 of query aligns to 10:378/378 of 5ol2C
- active site: L124 (≠ M130), T125 (≠ S131), G241 (≠ E247), G374 (≠ R380)
- binding calcium ion: E29 (≠ Q35), E33 (≠ D39)
- binding coenzyme a persulfide: T125 (≠ S131), T131 (≠ S137), S134 (≠ V140), F231 (≠ V237), M235 (= M241), L238 (= L244), R242 (= R248), E362 (≠ A368), G363 (= G369), V367 (≠ I373)
- binding flavin-adenine dinucleotide: F122 (≠ L128), L124 (≠ M130), T125 (≠ S131), P127 (= P133), G130 (= G136), T131 (≠ S137), F155 (≠ W161), F155 (≠ W161), I156 (= I162), T157 (= T163), T208 (= T214), R267 (= R273), Q269 (= Q275), F270 (= F276), L274 (≠ I280), F277 (= F283), T280 (≠ I286), Q335 (= Q341), L336 (≠ I342), H337 (≠ L343), G338 (= G344), G339 (= G345), Y340 (≠ N346), Y340 (≠ N346), T343 (≠ I349), D345 (≠ E351), Y346 (≠ F352), I357 (≠ L363), I360 (= I366), Y361 (≠ G367), G363 (= G369), T364 (= T370), E366 (= E372)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
39% identity, 95% coverage: 16:382/387 of query aligns to 12:378/378 of 4n5fA