SitesBLAST
Comparing AO356_17045 FitnessBrowser__pseudo5_N2C3_1:AO356_17045 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)
55% identity, 99% coverage: 4:378/378 of query aligns to 50:426/430 of P51174
- K318 (= K270) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (= K274) 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.
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
57% identity, 98% coverage: 10:378/378 of query aligns to 8:378/380 of 2pg0A
- active site: M124 (= M126), T125 (= T127), E243 (= E243), A364 (= A364), R376 (= R376)
- binding flavin-adenine dinucleotide: I122 (= I124), M124 (= M126), T125 (= T127), G130 (= G132), S131 (= S133), F155 (= F157), I156 (= I158), T157 (= T159), R269 (= R269), F272 (= F272), F279 (= F279), Q337 (= Q337), L338 (= L338), G340 (= G340), G341 (= G341), V359 (= V359), I362 (= I362), Y363 (= Y363), T366 (= T366), E368 (= E368), M369 (≠ I369)
8w0uA Human lcad complexed with acetoacetyl coenzyme a (see paper)
54% identity, 99% coverage: 4:378/378 of query aligns to 18:394/398 of 8w0uA
- binding acetoacetyl-coenzyme a: M140 (= M126), S147 (= S133), Q150 (= Q136), S193 (vs. gap), H196 (≠ K180), Y250 (≠ A234), E259 (= E243), R260 (= R244), Y379 (= Y363), G380 (≠ A364), G381 (= G365), I385 (= I369), L389 (≠ I373), R392 (= R376)
- binding flavin-adenine dinucleotide: I138 (= I124), M140 (= M126), T141 (= T127), G146 (= G132), S147 (= S133), F171 (= F157), S173 (≠ T159), R285 (= R269), F288 (= F272), L295 (≠ F279), Q353 (= Q337), L354 (= L338), G357 (= G341), V375 (= V359), Y379 (= Y363), T382 (= T366), E384 (= E368)
8w0tA Human lcad (see paper)
54% identity, 99% coverage: 4:378/378 of query aligns to 18:394/398 of 8w0tA
- binding flavin-adenine dinucleotide: I138 (= I124), M140 (= M126), T141 (= T127), G146 (= G132), S147 (= S133), F171 (= F157), I172 (= I158), S173 (≠ T159), R285 (= R269), F288 (= F272), L295 (≠ F279), Q353 (= Q337), L354 (= L338), G356 (= G340), G357 (= G341), V375 (= V359), T382 (= T366), E384 (= E368), I385 (= I369)
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
54% identity, 99% coverage: 4:378/378 of query aligns to 50:426/430 of P28330
- E291 (= E243) 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 (≠ A255) to T: in dbSNP:rs1801204
- K333 (= K285) to Q: in dbSNP:rs2286963
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
40% identity, 99% coverage: 6:378/378 of query aligns to 3:376/378 of 5ol2F
- active site: L124 (≠ M126), T125 (= T127), G241 (≠ E243), G374 (≠ R376)
- binding calcium ion: E29 (≠ Q32), E33 (≠ Q36), R35 (≠ H38)
- binding coenzyme a persulfide: L238 (= L240), R242 (= R244), E362 (≠ A364), G363 (= G365)
- binding flavin-adenine dinucleotide: F122 (≠ I124), L124 (≠ M126), T125 (= T127), P127 (= P129), T131 (≠ S133), F155 (= F157), I156 (= I158), T157 (= T159), E198 (≠ L200), R267 (= R269), F270 (= F272), L274 (≠ I276), F277 (= F279), Q335 (= Q337), L336 (= L338), G338 (= G340), G339 (= G341), Y361 (= Y363), T364 (= T366), E366 (= E368)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
42% identity, 98% coverage: 10:378/378 of query aligns to 5:372/374 of 5lnxD
- active site: L122 (≠ M126), T123 (= T127), G239 (≠ E243), E358 (≠ A364), K370 (≠ R376)
- binding flavin-adenine dinucleotide: L122 (≠ M126), T123 (= T127), G128 (= G132), S129 (= S133), F153 (= F157), T155 (= T159), R265 (= R269), Q267 (≠ A271), F268 (= F272), I272 (= I276), N275 (≠ F279), I278 (≠ T282), Q331 (= Q337), I332 (≠ L338), G335 (= G341), Y357 (= Y363), T360 (= T366), E362 (= E368)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
40% identity, 98% coverage: 7:378/378 of query aligns to 5:377/380 of 4l1fA
- active site: L125 (≠ M126), T126 (= T127), G242 (≠ E243), E363 (≠ A364), R375 (= R376)
- binding coenzyme a persulfide: T132 (≠ S133), H179 (≠ K180), F232 (= F233), M236 (= M237), E237 (≠ Q238), L239 (= L240), D240 (≠ P241), R243 (= R244), Y362 (= Y363), E363 (≠ A364), G364 (= G365), R375 (= R376)
- binding flavin-adenine dinucleotide: F123 (≠ I124), L125 (≠ M126), T126 (= T127), G131 (= G132), T132 (≠ S133), F156 (= F157), I157 (= I158), T158 (= T159), R268 (= R269), Q270 (≠ A271), F271 (= F272), I275 (= I276), F278 (= F279), L281 (≠ T282), Q336 (= Q337), I337 (≠ L338), G340 (= G341), I358 (≠ V359), Y362 (= Y363), T365 (= T366), Q367 (≠ E368)
- binding 1,3-propandiol: L5 (≠ F7), Q10 (≠ E12)
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
39% identity, 99% coverage: 3:378/378 of query aligns to 1:377/378 of 3r7kA
- active site: V126 (≠ M126), T127 (= T127), E242 (= E243), G363 (≠ A364), K375 (≠ R376)
- binding dihydroflavine-adenine dinucleotide: V126 (≠ M126), T127 (= T127), G132 (= G132), S133 (= S133), F157 (= F157), I158 (= I158), T159 (= T159), R268 (= R269), T270 (≠ A271), F271 (= F272), L275 (≠ I276), R278 (≠ F279), I281 (≠ T282), Q336 (= Q337), I337 (≠ L338), G340 (= G341), I358 (≠ V359), T365 (= T366), E367 (= E368)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
39% identity, 98% coverage: 7:378/378 of query aligns to 4:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S133), L133 (= L135), K178 (= K180), F231 (= F233), M235 (= M237), L238 (= L240), N241 (≠ E243), R242 (= R244), Y362 (= Y363), T363 (≠ A364), G364 (= G365), R375 (= R376)
- binding flavin-adenine dinucleotide: L122 (≠ I124), A124 (≠ M126), T125 (= T127), G130 (= G132), S131 (= S133), F155 (= F157), I156 (= I158), T157 (= T159), K200 (= K202), N208 (≠ T210), L358 (≠ V359), T365 (= T366), Q367 (≠ E368), I368 (= I369)
Q39QF5 Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase; CHeneCoA dehydrogenase; EC 1.3.8.10 from Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15) (see paper)
39% identity, 98% coverage: 7:378/378 of query aligns to 4:377/380 of Q39QF5
- D91 (= D93) mutation to E: Retains minor activity.; mutation to N: Loss of activity. Gains a low but significant C1,C2-dehydrogenation activity, but the C3,C6- and C3,C4-dehydrogenating activities are largely diminished; when associated with D-241.
- L122 (≠ I124) binding FAD
- A124 (≠ M126) binding FAD
- T125 (= T127) binding FAD
- S131 (= S133) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA; binding FAD
- T157 (= T159) binding FAD
- K178 (= K180) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- N241 (≠ E243) mutation to D: Shows decreased activity, with a shift towards C3,C4- versus C3,C6-dehydrogenation. Gains a low but significant C1,C2-dehydrogenation activity, but the C3,C6- and C3,C4-dehydrogenating activities are largely diminished; when associated with N-91.
- R242 (= R244) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- T363 (≠ A364) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA; mutation to V: Shows decreased activity, with a shift towards C3,C4- versus C3,C6-dehydrogenation.
- T365 (= T366) binding FAD
- Q367 (≠ E368) binding FAD
- R375 (= R376) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
39% identity, 98% coverage: 7:378/378 of query aligns to 2:375/378 of 7p9xA