SitesBLAST
Comparing WP_012173167.1 NCBI__GCF_000010525.1:WP_012173167.1 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)
6es9A Methylsuccinyl-coa dehydrogenase of paracoccus denitrificans with bound flavin adenine dinucleotide (see paper)
67% identity, 95% coverage: 26:560/564 of query aligns to 18:545/545 of 6es9A
- active site: F281 (= F296), T282 (= T297), A408 (= A423), R541 (= R556)
- binding coenzyme a: R75 (= R83), F467 (= F482), W470 (≠ R485)
- binding flavin-adenine dinucleotide: Q50 (= Q58), A279 (= A294), F281 (= F296), T282 (= T297), G287 (= G302), S288 (= S303), W312 (= W327), I313 (= I328), T314 (= T329), E374 (= E389), R434 (= R449), Q436 (= Q451), F437 (= F452), L441 (= L456), F444 (= F459), Q502 (= Q517), I503 (= I518), G505 (= G520), G506 (= G521), F528 (= F543), A531 (= A546), E533 (= E548), I534 (= I549)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
41% identity, 68% coverage: 181:562/564 of query aligns to 7:379/383 of 4iv6B
- active site: L121 (≠ F296), T122 (= T297), G240 (≠ A423), E361 (= E544), K373 (≠ R556)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ F296), T122 (= T297), G126 (≠ T301), G127 (= G302), S128 (= S303), W152 (= W327), I153 (= I328), S154 (≠ T329), R266 (= R449), S268 (≠ Q451), F269 (= F452), I273 (≠ L456), H276 (≠ F459), V279 (= V462), R334 (≠ Q517), V335 (≠ I518), G338 (= G521), L356 (≠ I539), G360 (≠ F543), T363 (≠ A546), E365 (= E548), I366 (= I549)
8ciwA Methylsuccinyl-coa dehydrogenase from pseudomonas migulae with bound fad and (2s)-methylsuccinyl-coa (see paper)
37% identity, 93% coverage: 35:560/564 of query aligns to 24:548/555 of 8ciwA
- binding flavin-adenine dinucleotide: Q47 (= Q58), I275 (≠ A294), I277 (≠ F296), T278 (= T297), G283 (= G302), S284 (= S303), W308 (= W327), T310 (= T329), R437 (= R449), V439 (≠ Q451), F440 (= F452), L444 (= L456), Q504 (= Q517), I505 (= I518), G508 (= G521), F530 (= F543), E535 (= E548), T536 (≠ I549)
- binding (2S)-Methylsuccinyl-CoA: R242 (= R261), S284 (= S303), V286 (≠ L305), H332 (≠ Y350), Y370 (= Y384), F401 (= F413), Y402 (≠ K414), M405 (= M417), M408 (≠ F420), R412 (= R424), R418 (= R430), F530 (= F543), E531 (= E544), G532 (= G545), R544 (= R556)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
36% identity, 69% coverage: 173:559/564 of query aligns to 2:377/379 of 1ukwB
- active site: L124 (≠ F296), S125 (≠ T297), T241 (≠ A423), E362 (= E544), R374 (= R556)
- binding cobalt (ii) ion: D145 (= D317), H146 (≠ V318)
- binding flavin-adenine dinucleotide: F122 (≠ A294), L124 (≠ F296), S125 (≠ T297), G130 (= G302), S131 (= S303), W155 (= W327), S157 (≠ T329), K200 (≠ G377), L357 (≠ I539), Y361 (≠ F543), E362 (= E544), T364 (≠ A546), E366 (= E548), L370 (≠ Q552)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
36% identity, 69% coverage: 173:559/564 of query aligns to 2:377/379 of 1ukwA
- active site: L124 (≠ F296), S125 (≠ T297), T241 (≠ A423), E362 (= E544), R374 (= R556)
- binding flavin-adenine dinucleotide: F122 (≠ A294), L124 (≠ F296), S125 (≠ T297), G130 (= G302), S131 (= S303), W155 (= W327), S157 (≠ T329), L357 (≠ I539), Y361 (≠ F543), E362 (= E544), T364 (≠ A546), E366 (= E548), L370 (≠ Q552)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
38% identity, 66% coverage: 190:560/564 of query aligns to 18:378/378 of 5ol2F
- active site: L124 (≠ F296), T125 (= T297), G241 (≠ A423), G374 (≠ R556)
- binding calcium ion: E29 (= E201), E33 (≠ K205), R35 (≠ A207)
- binding coenzyme a persulfide: L238 (≠ F420), R242 (= R424), E362 (= E544), G363 (= G545)
- binding flavin-adenine dinucleotide: F122 (≠ A294), L124 (≠ F296), T125 (= T297), P127 (= P299), T131 (≠ S303), F155 (≠ W327), I156 (= I328), T157 (= T329), E198 (≠ G373), R267 (= R449), F270 (= F452), L274 (= L456), F277 (= F459), Q335 (= Q517), L336 (≠ I518), G338 (= G520), G339 (= G521), Y361 (≠ F543), T364 (≠ A546), E366 (= E548)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
37% identity, 67% coverage: 183:559/564 of query aligns to 9:373/374 of 5lnxD
- active site: L122 (≠ F296), T123 (= T297), G239 (≠ A423), E358 (= E544), K370 (≠ R556)
- binding flavin-adenine dinucleotide: L122 (≠ F296), T123 (= T297), G128 (= G302), S129 (= S303), F153 (≠ W327), T155 (= T329), R265 (= R449), Q267 (= Q451), F268 (= F452), I272 (≠ L456), N275 (≠ F459), I278 (≠ V462), Q331 (= Q517), I332 (= I518), G335 (= G521), Y357 (≠ F543), T360 (≠ A546), E362 (= E548)
P11310 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; Medium chain acyl-CoA dehydrogenase; MCADH; EC 1.3.8.7 from Homo sapiens (Human) (see 16 papers)
34% identity, 69% coverage: 176:564/564 of query aligns to 41:421/421 of P11310
- Y67 (≠ W202) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (≠ V222) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (= L234) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (= L236) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (≠ V244) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (≠ L268) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 294:303, 50% identical) binding in other chain
- S167 (= S303) binding octanoyl-CoA
- W191 (= W327) mutation to A: Loss of electron transfer to ETF.; mutation to F: Reduces rate of electron transfer to ETF about six-fold.
- WIT 191:193 (= WIT 327:329) binding in other chain
- T193 (= T329) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (= E380) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (≠ E421) binding octanoyl-CoA
- T280 (≠ A423) mutation to E: Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410.
- R281 (= R424) binding octanoyl-CoA; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ RIQ 449:451) binding FAD
- HQ 316:317 (≠ FP 459:460) binding in other chain
- K329 (≠ E472) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ QIHGG 517:521) binding FAD
- E384 (= E527) mutation to A: Reduces rate of electron transfer to ETF three-fold.; mutation to Q: Reduces rate of electron transfer to ETF two-fold.
- E401 (= E544) active site, Proton acceptor; binding octanoyl-CoA; mutation to G: Changed substrate specificity towards longer acyl chains; when associated with E-280.; mutation to Q: Loss of acyl-CoA dehydrogenase activity.; mutation to T: Loss of acyl-CoA dehydrogenase activity; when associated with E-280.
- EGTSQ 401:405 (≠ EGAAE 544:548) binding in other chain
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
34% identity, 69% coverage: 176:564/564 of query aligns to 8:388/388 of 2a1tC
- active site: V127 (≠ F296), T128 (= T297), T247 (≠ A423), E368 (= E544), R380 (= R556)
- binding flavin-adenine dinucleotide: Y125 (≠ A294), V127 (≠ F296), T128 (= T297), G133 (= G302), S134 (= S303), Q155 (≠ N324), W158 (= W327), W158 (= W327), I159 (= I328), T160 (= T329), R273 (= R449), T275 (≠ Q451), F276 (= F452), L280 (= L456), H283 (≠ F459), I286 (≠ V462), Q341 (= Q517), I342 (= I518), G345 (= G521), I363 (= I539), T370 (≠ A546), Q372 (≠ E548)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
35% identity, 69% coverage: 176:564/564 of query aligns to 41:421/421 of P41367
- 158:167 (vs. 294:303, 50% identical) binding in other chain
- S167 (= S303) binding octanoyl-CoA
- WIT 191:193 (= WIT 327:329) binding in other chain
- S216 (≠ Y350) binding octanoyl-CoA
- D278 (≠ E421) binding octanoyl-CoA
- R281 (= R424) binding octanoyl-CoA
- RKT 306:308 (≠ RIQ 449:451) binding FAD
- HQ 316:317 (≠ FP 459:460) binding in other chain
- R349 (= R492) binding octanoyl-CoA
- T351 (≠ D494) binding octanoyl-CoA
- QVFGG 374:378 (≠ QIHGG 517:521) binding FAD
- E401 (= E544) active site, Proton acceptor; binding octanoyl-CoA
- GTAQ 402:405 (≠ GAAE 545:548) binding in other chain
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
36% identity, 68% coverage: 176:556/564 of query aligns to 6:378/385 of 3mdeA