SitesBLAST
Comparing GFF2596 FitnessBrowser__Marino:GFF2596 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)
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
36% identity, 96% coverage: 6:377/386 of query aligns to 8:378/380 of 2pg0A
- active site: M124 (≠ V125), T125 (≠ S126), E243 (= E242), A364 (≠ G363), R376 (≠ K375)
- binding flavin-adenine dinucleotide: I122 (= I123), M124 (≠ V125), T125 (≠ S126), G130 (= G131), S131 (= S132), F155 (≠ W156), I156 (= I157), T157 (= T158), R269 (= R268), F272 (= F271), F279 (≠ N278), Q337 (= Q336), L338 (≠ Y337), G340 (= G339), G341 (= G340), V359 (≠ L358), I362 (= I361), Y363 (≠ G362), T366 (≠ A365), E368 (= E367), M369 (≠ I368)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
37% identity, 97% coverage: 3:377/386 of query aligns to 53:426/430 of P51174
- K318 (= K269) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ Q273) 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)
36% identity, 97% coverage: 3:375/386 of query aligns to 53:424/430 of P28330
- E291 (= E242) 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 (≠ L254) to T: in dbSNP:rs1801204
- K333 (≠ R284) to Q: in dbSNP:rs2286963
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
37% identity, 97% coverage: 4:378/386 of query aligns to 6:378/378 of 3r7kA
- active site: V126 (= V125), T127 (≠ S126), E242 (= E242), G363 (= G363), K375 (= K375)
- binding dihydroflavine-adenine dinucleotide: V126 (= V125), T127 (≠ S126), G132 (= G131), S133 (= S132), F157 (≠ W156), I158 (= I157), T159 (= T158), R268 (= R268), T270 (= T270), F271 (= F271), L275 (= L275), R278 (≠ N278), I281 (= I281), Q336 (= Q336), I337 (≠ Y337), G340 (= G340), I358 (≠ L358), T365 (≠ A365), E367 (= E367)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
35% identity, 95% coverage: 7:374/386 of query aligns to 11:376/384 of 1jqiA
- binding acetoacetyl-coenzyme a: L95 (≠ M93), F125 (≠ I123), S134 (= S132), F234 (= F232), M238 (= M236), Q239 (≠ L237), L241 (≠ F239), D242 (≠ Q240), R245 (= R243), Y364 (≠ G362), E365 (≠ G363), G366 (= G364)
- binding flavin-adenine dinucleotide: F125 (≠ I123), L127 (≠ V125), S128 (= S126), G133 (= G131), S134 (= S132), W158 (= W156), T160 (= T158), R270 (= R268), F273 (= F271), L280 (≠ N278), Q338 (= Q336), I339 (≠ Y337), G342 (= G340), I360 (≠ L358), T367 (≠ A365), E369 (= E367), I370 (= I368)
Sites not aligning to the query:
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
35% identity, 95% coverage: 7:374/386 of query aligns to 38:403/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
3p4tA Crystal structure of a putative acyl-coa dehydrogenase from mycobacterium smegmatis (see paper)
37% identity, 97% coverage: 4:378/386 of query aligns to 5:378/381 of 3p4tA
- active site: I125 (≠ V125), T126 (≠ S126), E241 (= E242), G363 (= G363), K375 (= K375)
- 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 (≠ I123), I125 (≠ V125), T126 (≠ S126), G130 (≠ A130), G131 (= G131), S132 (= S132), Y156 (≠ W156), I157 (= I157), T158 (= T158), K200 (= K201), R267 (= R268), T269 (= T270), L274 (= L275), R277 (≠ N278), Q336 (= Q336), L337 (≠ Y337), G340 (= G340), I358 (≠ L358), T365 (≠ A365)
3oibA Crystal structure of a putative acyl-coa dehydrogenase from mycobacterium smegmatis, iodide soak (see paper)
37% identity, 97% coverage: 4:378/386 of query aligns to 5:378/381 of 3oibA
- active site: I125 (≠ V125), T126 (≠ S126), E241 (= E242), G363 (= G363), K375 (= K375)
- binding dihydroflavine-adenine dinucleotide: L123 (≠ I123), I125 (≠ V125), T126 (≠ S126), G131 (= G131), S132 (= S132), Y156 (≠ W156), I157 (= I157), T158 (= T158), K200 (= K201), R267 (= R268), T269 (= T270), L274 (= L275), R277 (≠ N278), Q336 (= Q336), L337 (≠ Y337), G340 (= G340), I358 (≠ L358), T365 (≠ A365), E367 (= E367)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
36% identity, 96% coverage: 4:374/386 of query aligns to 5:373/378 of 5ol2F
- active site: L124 (≠ V125), T125 (≠ S126), G241 (≠ E242)
- binding calcium ion: E29 (= E28), E33 (≠ A32), R35 (≠ E34)
- binding coenzyme a persulfide: L238 (≠ F239), R242 (= R243), E362 (≠ G363), G363 (= G364)
- binding flavin-adenine dinucleotide: F122 (≠ I123), L124 (≠ V125), T125 (≠ S126), P127 (≠ V128), T131 (≠ S132), F155 (≠ W156), I156 (= I157), T157 (= T158), E198 (≠ L199), R267 (= R268), F270 (= F271), L274 (= L275), F277 (≠ N278), Q335 (= Q336), L336 (≠ Y337), G338 (= G339), G339 (= G340), Y361 (≠ G362), T364 (≠ A365), E366 (= E367)
Sites not aligning to the query:
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
35% identity, 95% coverage: 7:374/386 of query aligns to 11:376/385 of 7y0bA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: M343 (≠ N341), T347 (≠ W345), E348 (≠ D346)
- binding flavin-adenine dinucleotide: F125 (≠ I123), L127 (≠ V125), S128 (= S126), G133 (= G131), S134 (= S132), W158 (= W156), T160 (= T158), R270 (= R268), F273 (= F271), L280 (≠ N278), V282 (= V280), Q338 (= Q336), I339 (≠ Y337), G342 (= G340), I360 (≠ L358), Y364 (≠ G362), T367 (≠ A365), E369 (= E367), I370 (= I368), L373 (≠ G371)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
35% identity, 95% coverage: 7:374/386 of query aligns to 8:373/381 of 8sgsA
- binding coenzyme a: S131 (= S132), A133 (≠ V134), N177 (≠ H178), F231 (= F232), M235 (= M236), L238 (≠ F239), I312 (≠ T313), E362 (≠ G363), G363 (= G364)
- binding flavin-adenine dinucleotide: F122 (≠ I123), L124 (≠ V125), S125 (= S126), G130 (= G131), S131 (= S132), W155 (= W156), T157 (= T158), R267 (= R268), F270 (= F271), L274 (= L275), L277 (≠ N278), Q335 (= Q336), I336 (≠ Y337), G338 (= G339), G339 (= G340), I357 (≠ L358), I360 (= I361), Y361 (≠ G362), T364 (≠ A365), E366 (= E367)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
35% identity, 95% coverage: 7:374/386 of query aligns to 38:403/412 of P16219
- G90 (= G60) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E74) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 123:132, 50% identical) binding in other chain
- R171 (= R142) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 156:158) binding in other chain
- A192 (≠ S163) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ N180) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R268) binding
- Q308 (= Q279) binding in other chain
- R325 (= R296) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ G324) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QYWGG 336:340) binding
- R380 (= R351) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ ADE 365:367) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
35% identity, 95% coverage: 7:374/386 of query aligns to 14:379/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ I123), L130 (≠ V125), S131 (= S126), G136 (= G131), S137 (= S132), W161 (= W156), T163 (= T158), T214 (= T209), R273 (= R268), F276 (= F271), L280 (= L275), L283 (≠ N278), V285 (= V280), Q341 (= Q336), I342 (≠ Y337), G345 (= G340), I363 (≠ L358), Y367 (≠ G362), T370 (≠ A365), E372 (= E367), L376 (≠ G371)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
35% identity, 95% coverage: 7:374/386 of query aligns to 5:363/371 of 2vigB
- active site: L121 (≠ V125), S122 (= S126), G231 (≠ E242), E352 (≠ G363)
- binding coenzyme a persulfide: S128 (= S132), F221 (= F232), M225 (= M236), Q226 (≠ L237), L228 (≠ F239), D229 (≠ Q240), R232 (= R243), E352 (≠ G363), G353 (= G364), I357 (= I368)
- binding flavin-adenine dinucleotide: L121 (≠ V125), S122 (= S126), G127 (= G131), S128 (= S132), W152 (= W156), T154 (= T158), R257 (= R268), F260 (= F271), L264 (= L275), L267 (≠ N278), Q325 (= Q336), I326 (≠ Y337), G329 (= G340), I347 (≠ L358), Y351 (≠ G362), T354 (≠ A365), E356 (= E367)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
36% identity, 96% coverage: 6:377/386 of query aligns to 5:372/374 of 5lnxD
- active site: L122 (≠ V125), T123 (≠ S126), G239 (≠ E242), E358 (≠ G363), K370 (= K375)
- binding flavin-adenine dinucleotide: L122 (≠ V125), T123 (≠ S126), G128 (= G131), S129 (= S132), F153 (≠ W156), T155 (= T158), R265 (= R268), Q267 (≠ T270), F268 (= F271), I272 (≠ L275), N275 (= N278), I278 (= I281), Q331 (= Q336), I332 (≠ Y337), G335 (= G340), Y357 (≠ G362), T360 (≠ A365), E362 (= E367)
7szvA Crystal structure of acyl-coa dehydrogenase from mycobacterium marinum in complex with fda
35% identity, 97% coverage: 6:378/386 of query aligns to 5:371/372 of 7szvA
- binding dihydroflavine-adenine dinucleotide: L122 (≠ V125), T123 (≠ S126), F153 (≠ W156), I154 (= I157), T155 (= T158), K194 (= K201), R261 (= R268), S263 (≠ T270), Y271 (≠ N278), I274 (= I281), Q329 (= Q336), V330 (≠ Y337), G332 (= G339), G333 (= G340), T358 (≠ A365), E360 (= E367)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
35% identity, 95% coverage: 3:369/386 of query aligns to 5:369/380 of 4l1fA
- active site: L125 (≠ V125), T126 (≠ S126), G242 (≠ E242), E363 (≠ G363)
- binding coenzyme a persulfide: T132 (≠ S132), H179 (≠ K179), F232 (= F232), M236 (= M236), E237 (≠ L237), L239 (≠ F239), D240 (≠ Q240), R243 (= R243), Y362 (≠ G362), E363 (≠ G363), G364 (= G364)
- binding flavin-adenine dinucleotide: F123 (≠ I123), L125 (≠ V125), T126 (≠ S126), G131 (= G131), T132 (≠ S132), F156 (≠ W156), I157 (= I157), T158 (= T158), R268 (= R268), Q270 (≠ T270), F271 (= F271), I275 (≠ L275), F278 (≠ N278), L281 (≠ I281), Q336 (= Q336), I337 (≠ Y337), G340 (= G340), I358 (≠ L358), Y362 (≠ G362), T365 (≠ A365), Q367 (≠ E367)
- binding 1,3-propandiol: L5 (≠ F3), Q10 (≠ E8)
Sites not aligning to the query:
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
33% identity, 95% coverage: 3:368/386 of query aligns to 12:379/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S126), G140 (= G131), S141 (= S132), W165 (= W156), T167 (= T158), R279 (= R268), F282 (= F271), I286 (≠ L275), F289 (≠ N278), Q347 (= Q336), C348 (≠ Y337), G351 (= G340), L369 (= L358), G375 (= G364), T376 (≠ A365)
Sites not aligning to the query:
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
33% identity, 95% coverage: 3:368/386 of query aligns to 8:375/387 of 1ivhA
- active site: M130 (≠ V125), S131 (= S126), E249 (= E242), A370 (≠ G363)
- binding coenzyme a persulfide: S137 (= S132), S185 (≠ N180), R186 (≠ K181), V239 (≠ F232), Y240 (≠ M233), M243 (= M236), E249 (= E242), R250 (= R243), G369 (= G362), A370 (≠ G363), G371 (= G364), V375 (≠ I368)
- binding flavin-adenine dinucleotide: L128 (≠ I123), M130 (≠ V125), S131 (= S126), G136 (= G131), S137 (= S132), W161 (= W156), T163 (= T158), R275 (= R268), F278 (= F271), F285 (≠ N278), M288 (≠ I281), Q343 (= Q336), C344 (≠ Y337), G347 (= G340), T372 (≠ A365), E374 (= E367)
Sites not aligning to the query:
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)
33% identity, 95% coverage: 3:368/386 of query aligns to 45:412/426 of P26440
- 165:174 (vs. 123:132, 50% identical) binding
- S174 (= S132) binding
- WIT 198:200 (= WIT 156:158) binding
- SR 222:223 (≠ NK 180:181) binding
- G250 (≠ S206) to A: in IVA; uncertain significance
- Y277 (≠ M233) binding
- DLER 284:287 (≠ QEER 240:243) binding
- E286 (= E242) 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 (= A247) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R268) binding
- Q323 (= Q279) binding
- I379 (≠ L335) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QYWGG 336:340) binding
- R398 (= R354) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ V359) to N: in IVA; uncertain significance
- A407 (≠ G363) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ GG 363:364) binding
- TSE 409:411 (≠ ADE 365:367) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
Query Sequence
>GFF2596 FitnessBrowser__Marino:GFF2596
MKFTAEHEALRKTVRDFVEKEINPHCDEWEAAGEFPIHELFKKLGNLGILGIQKPEEYGG
MGLDYSYNLVAAEELGMAHCGGVPLAIGVQTDMCTPAISRFGSDELKRSFLAPAIAGDMV
GCIGVSEVGAGSDVAGMKTTARKDGDDYIINGSKMWITNSPKSDFICLLANTSDDKPHKN
KSLIIVPTKTPGISFSPHLNKLGMRSSETAQIFFDDVRVPQRYRIGAEGTGFMMQMLQFQ
EERIWGAANVIKALENCITKTIEYCRERKTFGQPLIDNQVIHFRLAELQTEVEALRALTY
QACELHVEGKDVTRLASMAKLKAGRLGREVTDSCLQYWGGNGYMWDNPISRAHRDVRLVS
IGGGADEIMLGIICKMMGTLPGKKRD
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