SitesBLAST
Comparing GFF1190 FitnessBrowser__Phaeo:GFF1190 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
48% identity, 98% coverage: 7:383/383 of query aligns to 2:378/380 of 2pg0A
- active site: M124 (= M129), T125 (= T130), E243 (= E248), A364 (≠ G369), R376 (= R381)
- binding flavin-adenine dinucleotide: I122 (≠ L127), A123 (= A128), M124 (= M129), T125 (= T130), G130 (= G135), S131 (= S136), F155 (= F160), I156 (= I161), T157 (= T162), R269 (= R274), A271 (= A276), F272 (= F277), V276 (≠ L281), F279 (= F284), Q337 (= Q342), L338 (= L343), G340 (= G345), G341 (= G346), Y342 (= Y347), V359 (= V364), I362 (= I367), Y363 (= Y368), T366 (= T371), E368 (= E373), M369 (≠ I374)
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
45% identity, 98% coverage: 10:383/383 of query aligns to 53:426/430 of P28330
- E291 (= E248) 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 (≠ M260) to T: in dbSNP:rs1801204
- K333 (= K290) to Q: in dbSNP:rs2286963
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
45% identity, 98% coverage: 10:383/383 of query aligns to 53:426/430 of P51174
- K318 (≠ E275) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ G279) 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.
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
38% identity, 98% coverage: 10:383/383 of query aligns to 5:377/380 of 4l1fA
- active site: L125 (≠ M129), T126 (= T130), G242 (≠ E248), E363 (≠ G369), R375 (= R381)
- binding coenzyme a persulfide: F123 (≠ L127), T132 (≠ S136), A134 (≠ V138), V178 (≠ S182), H179 (≠ K183), F232 (= F238), M236 (= M242), E237 (≠ Q243), L239 (= L245), D240 (≠ P246), R243 (= R249), S313 (≠ V319), Y362 (= Y368), E363 (≠ G369), G364 (= G370), V368 (≠ I374), R375 (= R381)
- binding flavin-adenine dinucleotide: F123 (≠ L127), L125 (≠ M129), T126 (= T130), G131 (= G135), T132 (≠ S136), F156 (= F160), I157 (= I161), T158 (= T162), T209 (= T214), R268 (= R274), Q270 (≠ A276), F271 (= F277), I275 (≠ L281), F278 (= F284), L281 (≠ T287), Q336 (= Q342), I337 (≠ L343), G339 (= G345), G340 (= G346), Y341 (= Y347), I358 (≠ V364), Y362 (= Y368), T365 (= T371), Q367 (≠ E373), I371 (≠ E377)
- binding 1,3-propandiol: L5 (≠ M10), T6 (= T11), Q10 (= Q15)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
37% identity, 97% coverage: 13:383/383 of query aligns to 5:372/374 of 5lnxD
- active site: L122 (≠ M129), T123 (= T130), G239 (≠ E248), E358 (≠ G369), K370 (≠ R381)
- binding flavin-adenine dinucleotide: F120 (≠ L127), L122 (≠ M129), T123 (= T130), G128 (= G135), S129 (= S136), F153 (= F160), I154 (= I161), T155 (= T162), R265 (= R274), Q267 (≠ A276), F268 (= F277), I272 (≠ L281), N275 (≠ F284), I278 (≠ T287), Q331 (= Q342), I332 (≠ L343), G334 (= G345), G335 (= G346), Y336 (= Y347), Y357 (= Y368), T360 (= T371), E362 (= E373)
5ol2C The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
37% identity, 97% coverage: 11:383/383 of query aligns to 5:376/378 of 5ol2C
- active site: L124 (≠ M129), T125 (= T130), G241 (≠ E248), G374 (≠ R381)
- binding calcium ion: E29 (≠ T35), E33 (≠ Q39)
- binding coenzyme a persulfide: T125 (= T130), T131 (≠ S136), S134 (≠ Q139), F231 (= F238), M235 (= M242), L238 (= L245), R242 (= R249), E362 (≠ G369), G363 (= G370), V367 (≠ I374)
- binding flavin-adenine dinucleotide: F122 (≠ L127), L124 (≠ M129), T125 (= T130), P127 (= P132), G130 (= G135), T131 (≠ S136), F155 (= F160), F155 (= F160), I156 (= I161), T157 (= T162), T208 (= T214), R267 (= R274), Q269 (≠ A276), F270 (= F277), L274 (= L281), F277 (= F284), T280 (= T287), Q335 (= Q342), L336 (= L343), H337 (= H344), G338 (= G345), G339 (= G346), Y340 (= Y347), Y340 (= Y347), T343 (≠ M350), D345 (≠ E352), Y346 (= Y353), I357 (≠ V364), I360 (= I367), Y361 (= Y368), G363 (= G370), T364 (= T371), E366 (= E373)
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
36% identity, 98% coverage: 8:383/383 of query aligns to 3:377/378 of 3r7kA
- active site: V126 (≠ M129), T127 (= T130), E242 (= E248), G363 (= G369), K375 (≠ R381)
- binding dihydroflavine-adenine dinucleotide: L124 (= L127), V126 (≠ M129), T127 (= T130), G132 (= G135), S133 (= S136), F157 (= F160), I158 (= I161), T159 (= T162), W204 (≠ L209), R268 (= R274), T270 (≠ A276), F271 (= F277), L275 (= L281), R278 (≠ F284), I281 (≠ T287), Q336 (= Q342), I337 (≠ L343), G339 (= G345), G340 (= G346), Y343 (≠ F349), I358 (≠ V364), I361 (= I367), G362 (≠ Y368), T365 (= T371), E367 (= E373), I368 (= I374), E371 (= E377)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
34% identity, 98% coverage: 10:383/383 of query aligns to 8:384/387 of 1ivhA
- active site: M130 (= M129), S131 (≠ T130), E249 (= E248), A370 (≠ G369), R382 (= R381)
- binding coenzyme a persulfide: M130 (= M129), G136 (= G135), S137 (= S136), V139 (= V138), V140 (≠ Q139), S185 (= S182), R186 (≠ K183), V239 (≠ F238), Y240 (= Y239), M243 (= M242), L246 (= L245), D247 (≠ P246), E249 (= E248), R250 (= R249), G369 (≠ Y368), A370 (≠ G369), G371 (= G370), V375 (≠ I374), R382 (= R381)
- binding flavin-adenine dinucleotide: L128 (= L127), A129 (= A128), M130 (= M129), S131 (≠ T130), G136 (= G135), S137 (= S136), W161 (≠ F160), I162 (= I161), T163 (= T162), T216 (= T214), R275 (= R274), A277 (= A276), F278 (= F277), I282 (≠ L281), F285 (= F284), L287 (≠ N286), M288 (≠ T287), Q343 (= Q342), C344 (≠ L343), G346 (= G345), G347 (= G346), L365 (≠ V364), I368 (= I367), T372 (= T371), E374 (= E373), L378 (≠ E377)
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)
34% identity, 98% coverage: 10:383/383 of query aligns to 45:421/426 of P26440
- 165:174 (vs. 127:136, 70% identical) binding
- S174 (= S136) binding
- WIT 198:200 (≠ FIT 160:162) binding
- SR 222:223 (≠ SK 182:183) binding
- G250 (≠ A211) to A: in IVA; unknown pathological significance
- Y277 (= Y239) binding
- DLER 284:287 (≠ PQER 246:249) binding
- E286 (= E248) 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 (= A253) to V: in IVA; unknown pathological significance; dbSNP:rs886042098
- R312 (= R274) binding
- Q323 (= Q285) binding
- I379 (≠ V341) to T: in IVA; unknown pathological significance
- QCFGG 380:384 (≠ QLHGG 342:346) binding
- R398 (≠ T360) to Q: in IVA; unknown pathological significance; dbSNP:rs1477527791
- Y403 (≠ Q365) to N: in IVA; unknown pathological significance
- A407 (≠ G369) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ GG 369:370) binding
- TSE 409:411 (≠ TNE 371:373) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
37% identity, 98% coverage: 10:383/383 of query aligns to 4:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: L84 (≠ S88), I87 (≠ H91), D91 (≠ S95), S131 (= S136), L133 (≠ V138), L134 (≠ Q139), T157 (= T162), S177 (= S182), K178 (= K183), F231 (= F238), M235 (= M242), L238 (= L245), N241 (≠ E248), R242 (= R249), Y362 (= Y368), T363 (≠ G369), G364 (= G370), I368 (= I374), R375 (= R381)
- binding flavin-adenine dinucleotide: L122 (= L127), A124 (≠ M129), T125 (= T130), G130 (= G135), S131 (= S136), F155 (= F160), I156 (= I161), T157 (= T162), K200 (= K206), N208 (≠ T214), L358 (≠ V364), Y362 (= Y368), G364 (= G370), T365 (= T371), Q367 (≠ E373), I368 (= I374)
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
37% identity, 98% coverage: 10:383/383 of query aligns to 2:375/378 of 7p9xA