SitesBLAST
Comparing Ac3H11_2720 FitnessBrowser__acidovorax_3H11:Ac3H11_2720 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
49% identity, 96% coverage: 15:384/384 of query aligns to 5:378/380 of 2pg0A
- active site: M124 (= M134), T125 (≠ S135), E243 (= E249), A364 (≠ G370), R376 (= R382)
- binding flavin-adenine dinucleotide: I122 (= I132), M124 (= M134), T125 (≠ S135), G130 (= G140), S131 (= S141), F155 (= F165), I156 (= I166), T157 (= T167), R269 (= R275), F272 (= F278), F279 (= F285), Q337 (= Q343), L338 (= L344), G340 (= G346), G341 (= G347), V359 (= V365), I362 (= I368), Y363 (= Y369), T366 (= T372), E368 (= E374), M369 (≠ I375)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
46% identity, 98% coverage: 8:384/384 of query aligns to 46:426/430 of P51174
- K318 (= K276) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (= K280) 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.
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
43% identity, 98% coverage: 8:384/384 of query aligns to 46:426/430 of P28330
- E291 (= E249) 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 (≠ I261) to T: in dbSNP:rs1801204
- K333 (= K291) to Q: in dbSNP:rs2286963
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
37% identity, 94% coverage: 23:384/384 of query aligns to 10:372/374 of 5lnxD
- active site: L122 (≠ M134), T123 (≠ S135), G239 (≠ E249), E358 (≠ G370), K370 (≠ R382)
- binding flavin-adenine dinucleotide: L122 (≠ M134), T123 (≠ S135), G128 (= G140), S129 (= S141), F153 (= F165), T155 (= T167), R265 (= R275), Q267 (≠ V277), F268 (= F278), I272 (≠ V282), N275 (≠ F285), I278 (≠ T288), Q331 (= Q343), I332 (≠ L344), G335 (= G347), Y357 (= Y369), T360 (= T372), E362 (= E374)
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
36% identity, 96% coverage: 18:384/384 of query aligns to 8:377/378 of 3r7kA
- active site: V126 (≠ M134), T127 (≠ S135), E242 (= E249), G363 (= G370), K375 (≠ R382)
- binding dihydroflavine-adenine dinucleotide: V126 (≠ M134), T127 (≠ S135), G132 (= G140), S133 (= S141), F157 (= F165), I158 (= I166), T159 (= T167), R268 (= R275), T270 (≠ V277), F271 (= F278), L275 (≠ V282), R278 (≠ F285), I281 (≠ T288), Q336 (= Q343), I337 (≠ L344), G340 (= G347), I358 (≠ V365), T365 (= T372), E367 (= E374)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
35% identity, 95% coverage: 19:384/384 of query aligns to 8:376/378 of 5ol2F
- active site: L124 (≠ M134), T125 (≠ S135), G241 (≠ E249), G374 (≠ R382)
- binding calcium ion: E29 (≠ A40), E33 (= E44), R35 (≠ I46)
- binding coenzyme a persulfide: L238 (= L246), R242 (= R250), E362 (≠ G370), G363 (= G371)
- binding flavin-adenine dinucleotide: F122 (≠ I132), L124 (≠ M134), T125 (≠ S135), P127 (= P137), T131 (≠ S141), F155 (= F165), I156 (= I166), T157 (= T167), E198 (≠ L206), R267 (= R275), F270 (= F278), L274 (≠ V282), F277 (= F285), Q335 (= Q343), L336 (= L344), G338 (= G346), G339 (= G347), Y361 (= Y369), T364 (= T372), E366 (= E374)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
32% identity, 97% coverage: 11:384/384 of query aligns to 2:378/378 of 4n5fA
- active site: L126 (≠ M134), T127 (≠ S135), G243 (≠ E249), E364 (≠ G370), R376 (= R382)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M134), T127 (≠ S135), G132 (= G140), S133 (= S141), F157 (= F165), T159 (= T167), T210 (= T216), Y363 (= Y369), T366 (= T372), E368 (= E374), M372 (≠ E378)
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
36% identity, 96% coverage: 17:384/384 of query aligns to 12:374/377 of 4ktoA
- active site: M130 (= M134), S131 (= S135), E239 (= E249), A360 (≠ G370), R372 (= R382)
- binding flavin-adenine dinucleotide: L128 (≠ I132), M130 (= M134), S131 (= S135), M155 (≠ T164), W156 (≠ F165), T158 (= T167), R265 (= R275), F268 (= F278), I272 (≠ V282), F275 (= F285), M278 (≠ T288), Q333 (= Q343), A334 (≠ L344), G337 (= G347), L355 (≠ V365), G359 (≠ Y369), T362 (= T372), E364 (= E374)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
33% identity, 97% coverage: 12:384/384 of query aligns to 5:379/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S141), T134 (≠ L143), R180 (≠ K186), R234 (≠ K240), L237 (≠ T243), R238 (≠ H244), L240 (= L246), D241 (≠ A247), R244 (= R250), E365 (≠ G370), G366 (= G371), R377 (= R382)
- binding flavin-adenine dinucleotide: Y123 (≠ I132), L125 (≠ M134), S126 (= S135), G131 (= G140), S132 (= S141), W156 (≠ F165), I157 (= I166), T158 (= T167), I360 (≠ V365), T367 (= T372), Q369 (≠ E374)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
33% identity, 97% coverage: 12:384/384 of query aligns to 5:379/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ I132), L125 (≠ M134), S126 (= S135), G131 (= G140), S132 (= S141), W156 (≠ F165), I157 (= I166), T158 (= T167), I360 (≠ V365), Y364 (= Y369), T367 (= T372), Q369 (≠ E374)
7w0jE Acyl-coa dehydrogenase, tfu_1647
33% identity, 97% coverage: 12:384/384 of query aligns to 6:380/382 of 7w0jE
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-azanyl-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate: S127 (= S135), W157 (≠ F165), R270 (= R275), Q272 (≠ V277), F273 (= F278), I277 (≠ V282), F280 (= F285), I283 (≠ T288), Q339 (= Q343), L340 (= L344), G343 (= G347), Y365 (= Y369), E366 (≠ G370), T368 (= T372), Q370 (≠ E374), I371 (= I375)
3pfdC Crystal structure of an acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to reduced flavin adenine dinucleotide solved by combined iodide ion sad mr (see paper)
34% identity, 95% coverage: 19:384/384 of query aligns to 1:367/369 of 3pfdC
- active site: L116 (≠ M134), S117 (= S135), T233 (≠ E249), E353 (≠ G370), R365 (= R382)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ I132), L116 (≠ M134), S117 (= S135), G122 (= G140), S123 (= S141), W147 (≠ F165), I148 (= I166), T149 (= T167), R259 (= R275), F262 (= F278), V266 (= V282), N269 (≠ F285), Q326 (= Q343), L327 (= L344), G330 (= G347), I348 (≠ V365), Y352 (= Y369), T355 (= T372), Q357 (≠ E374)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
31% identity, 98% coverage: 10:384/384 of query aligns to 1:388/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S135), G140 (= G140), S141 (= S141), W165 (≠ F165), T167 (= T167), R279 (= R275), F282 (= F278), I286 (≠ V282), F289 (= F285), Q347 (= Q343), C348 (≠ L344), G351 (= G347), L369 (≠ V365), G375 (= G371), T376 (= T372), L382 (≠ E378)
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)
31% identity, 96% coverage: 15:384/384 of query aligns to 45:421/426 of P26440
- 165:174 (vs. 132:141, 70% identical) binding
- S174 (= S141) binding
- WIT 198:200 (≠ FIT 165:167) binding
- SR 222:223 (≠ AK 185:186) binding
- G250 (= G213) to A: in IVA; uncertain significance
- Y277 (≠ K240) binding
- DLER 284:287 (≠ AWER 247:250) binding
- E286 (= E249) 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 (≠ G254) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R275) binding
- Q323 (= Q286) binding
- I379 (≠ L342) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QLHGG 343:347) binding
- R398 (≠ V361) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ A366) to N: in IVA; uncertain significance
- A407 (≠ G370) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ GG 370:371) binding
- TSE 409:411 (= TSE 372:374) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
31% identity, 96% coverage: 15:384/384 of query aligns to 8:384/387 of 1ivhA
- active site: M130 (= M134), S131 (= S135), E249 (= E249), A370 (≠ G370), R382 (= R382)
- binding coenzyme a persulfide: S137 (= S141), S185 (≠ A185), R186 (≠ K186), V239 (≠ F239), Y240 (≠ K240), M243 (≠ T243), E249 (= E249), R250 (= R250), G369 (≠ Y369), A370 (≠ G370), G371 (= G371), V375 (≠ I375)
- binding flavin-adenine dinucleotide: L128 (≠ I132), M130 (= M134), S131 (= S135), G136 (= G140), S137 (= S141), W161 (≠ F165), T163 (= T167), R275 (= R275), F278 (= F278), F285 (= F285), M288 (≠ T288), Q343 (= Q343), C344 (≠ L344), G347 (= G347), T372 (= T372), E374 (= E374)
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
32% identity, 97% coverage: 14:384/384 of query aligns to 3:376/376 of 4m9aB
- active site: L124 (≠ M134), T125 (≠ S135), G241 (≠ E249), E362 (≠ G370), R374 (= R382)
- binding dihydroflavine-adenine dinucleotide: F122 (≠ I132), T125 (≠ S135), G130 (= G140), S131 (= S141), F155 (= F165), T157 (= T167), T208 (= T216), Y361 (= Y369), T364 (= T372), E366 (= E374), M370 (≠ E378)
2z1qB Crystal structure of acyl coa dehydrogenase
36% identity, 95% coverage: 15:380/384 of query aligns to 24:404/549 of 2z1qB
- active site: L144 (≠ M134), T145 (≠ S135), G259 (≠ E249), E394 (≠ G370)
- binding flavin-adenine dinucleotide: Y142 (≠ I132), L144 (≠ M134), T145 (≠ S135), G150 (= G140), S151 (= S141), W177 (≠ F165), S179 (≠ T167), R285 (= R275), F288 (= F278), I292 (≠ V282), F295 (= F285), I298 (≠ T288), H369 (= H345), G370 (= G346), F393 (≠ Y369), I399 (= I375)
Sites not aligning to the query:
3p4tA Crystal structure of a putative acyl-coa dehydrogenase from mycobacterium smegmatis (see paper)
34% identity, 96% coverage: 18:384/384 of query aligns to 7:377/381 of 3p4tA
- active site: I125 (≠ M134), T126 (≠ S135), E241 (= E249), G363 (= G370), K375 (≠ R382)
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-[(4aS,10aR)-7,8-dimethyl-2,4-dioxo-1,3,4,4a,5,10a-hexahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate: L123 (≠ I132), I125 (≠ M134), T126 (≠ S135), G130 (≠ I139), G131 (= G140), S132 (= S141), Y156 (≠ F165), I157 (= I166), T158 (= T167), K200 (= K208), R267 (= R275), T269 (≠ V277), L274 (≠ V282), R277 (≠ F285), Q336 (= Q343), L337 (= L344), G340 (= G347), I358 (≠ V365), T365 (= T372)
3oibA Crystal structure of a putative acyl-coa dehydrogenase from mycobacterium smegmatis, iodide soak (see paper)
34% identity, 96% coverage: 18:384/384 of query aligns to 7:377/381 of 3oibA
- active site: I125 (≠ M134), T126 (≠ S135), E241 (= E249), G363 (= G370), K375 (≠ R382)
- binding dihydroflavine-adenine dinucleotide: L123 (≠ I132), I125 (≠ M134), T126 (≠ S135), G131 (= G140), S132 (= S141), Y156 (≠ F165), I157 (= I166), T158 (= T167), K200 (= K208), R267 (= R275), T269 (≠ V277), L274 (≠ V282), R277 (≠ F285), Q336 (= Q343), L337 (= L344), G340 (= G347), I358 (≠ V365), T365 (= T372), E367 (= E374)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
32% identity, 96% coverage: 17:384/384 of query aligns to 7:376/379 of 1ukwB
- active site: L124 (≠ M134), S125 (= S135), T241 (≠ E249), E362 (≠ G370), R374 (= R382)
- binding cobalt (ii) ion: D145 (= D155), H146 (≠ I156)
- binding flavin-adenine dinucleotide: F122 (≠ I132), L124 (≠ M134), S125 (= S135), G130 (= G140), S131 (= S141), W155 (≠ F165), S157 (≠ T167), K200 (= K208), L357 (≠ V365), Y361 (= Y369), E362 (≠ G370), T364 (= T372), E366 (= E374), L370 (≠ E378)
Query Sequence
>Ac3H11_2720 FitnessBrowser__acidovorax_3H11:Ac3H11_2720
MASPQNQDISMRPVFREDHEQFREQARRFIEREIVPHLHAWEAEGIVPKSVWLKAGEAGL
LCSTVPEAYGGAGGDFGHSAVMIEELARVNATAVGFTTHSEIVAPYIVAYGTEEQKQRWL
PKMVSGETIGVIAMSEPGIGSDLRSMRTTAVRGEDIYTINGQKTFITNGGNADLAVTATK
LDPAAKELTLICVETDQPGFSKGRRLEKIGLKGQDTSELFFDNVSVPMANRLGEEGQGFK
YLTHQLAWERTIIGIRAAASIDSLIEQTIQYTRDRKVFGKTVFDFQNTKFKLAECKAQAT
MLRVFVDDCLAKAMRGELSAEVGAMCKLMGSEMQGKILDELLQLHGGYGFMSEYMISRAW
VDARVARIYGGTSEIMKEIISRSL
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory