SitesBLAST
Comparing Pf1N1B4_966 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_966 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)
56% 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)
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
53% 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 (≠ Y38)
- 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)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
37% identity, 97% coverage: 11:375/378 of query aligns to 38:403/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
37% identity, 97% coverage: 11:378/378 of query aligns to 11:379/384 of 1jqiA
- active site: G377 (≠ R376)
- binding acetoacetyl-coenzyme a: L95 (≠ I94), F125 (≠ I124), S134 (= S133), F234 (= F233), M238 (= M237), Q239 (= Q238), L241 (= L240), D242 (≠ P241), R245 (= R244), Y364 (= Y363), E365 (≠ A364), G366 (= G365)
- binding flavin-adenine dinucleotide: F125 (≠ I124), L127 (≠ M126), S128 (≠ T127), G133 (= G132), S134 (= S133), W158 (≠ F157), T160 (= T159), R270 (= R269), F273 (= F272), L280 (≠ F279), Q338 (= Q337), I339 (≠ L338), G342 (= G341), I360 (≠ V359), T367 (= T366), E369 (= E368), I370 (= I369)
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
- binding 1-monoenoyl-CoA: L82 (≠ I86), D89 (= D93), S129 (= S133), L131 (= L135), K176 (= K180), F229 (= F233), M233 (= M237), L236 (= L240), R240 (= R244), Y360 (= Y363), T361 (≠ A364), G362 (= G365), R373 (= R376)
- binding flavin-adenine dinucleotide: A122 (≠ M126), T123 (= T127), G128 (= G132), S129 (= S133), F153 (= F157), I154 (= I158), T155 (= T159), N206 (≠ T210), L356 (≠ V359), Y360 (= Y363), T363 (= T366), Q365 (≠ E368), I366 (= I369)
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)
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)
35% identity, 97% coverage: 11:378/378 of query aligns to 1:367/369 of 3pfdC
- active site: L116 (≠ M126), S117 (≠ T127), T233 (≠ E243), E353 (≠ A364), R365 (= R376)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ I124), L116 (≠ M126), S117 (≠ T127), G122 (= G132), S123 (= S133), W147 (≠ F157), I148 (= I158), T149 (= T159), R259 (= R269), F262 (= F272), V266 (≠ I276), N269 (≠ F279), Q326 (= Q337), L327 (= L338), G330 (= G341), I348 (≠ V359), Y352 (= Y363), T355 (= T366), Q357 (≠ E368)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
35% identity, 99% coverage: 6:378/378 of query aligns to 5:378/378 of 4n5fA
- active site: L126 (≠ M126), T127 (= T127), G243 (≠ E243), E364 (≠ A364), R376 (= R376)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M126), T127 (= T127), G132 (= G132), S133 (= S133), F157 (= F157), T159 (= T159), T210 (= T210), Y363 (= Y363), T366 (= T366), E368 (= E368), M372 (≠ E372)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
35% identity, 98% coverage: 8:378/378 of query aligns to 7:379/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S133), T134 (≠ L135), R180 (vs. gap), R234 (≠ A234), L237 (≠ M237), R238 (≠ Q238), L240 (= L240), D241 (≠ P241), R244 (= R244), E365 (≠ A364), G366 (= G365), R377 (= R376)
- binding flavin-adenine dinucleotide: Y123 (≠ I124), L125 (≠ M126), S126 (≠ T127), G131 (= G132), S132 (= S133), W156 (≠ F157), I157 (= I158), T158 (= T159), I360 (≠ V359), T367 (= T366), Q369 (≠ E368)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
35% identity, 98% coverage: 8:378/378 of query aligns to 7:379/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ I124), L125 (≠ M126), S126 (≠ T127), G131 (= G132), S132 (= S133), W156 (≠ F157), I157 (= I158), T158 (= T159), I360 (≠ V359), Y364 (= Y363), T367 (= T366), Q369 (≠ E368)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
36% identity, 98% coverage: 7:375/378 of query aligns to 3:373/379 of 6fahD
- active site: L124 (≠ M126), T125 (= T127), G241 (≠ E243)
- binding flavin-adenine dinucleotide: F122 (≠ I124), L124 (≠ M126), T125 (= T127), R152 (≠ S154), F155 (= F157), T157 (= T159), E198 (≠ L200), R267 (= R269), Q269 (≠ A271), F270 (= F272), I274 (= I276), F277 (= F279), Q335 (= Q337), I336 (≠ L338), G339 (= G341), Y361 (= Y363), T364 (= T366), Q366 (≠ E368)
Sites not aligning to the query:
7w0jE Acyl-coa dehydrogenase, tfu_1647
35% identity, 98% coverage: 8:378/378 of query aligns to 8:380/382 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 (≠ T127), W157 (≠ F157), R270 (= R269), Q272 (≠ A271), F273 (= F272), I277 (= I276), F280 (= F279), I283 (≠ T282), Q339 (= Q337), L340 (= L338), G343 (= G341), Y365 (= Y363), E366 (≠ A364), T368 (= T366), Q370 (≠ E368), I371 (= I369)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
36% identity, 97% coverage: 11:378/378 of query aligns to 11:379/385 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 (≠ Y342), T347 (≠ W346), E348 (= E347)
- binding flavin-adenine dinucleotide: F125 (≠ I124), L127 (≠ M126), S128 (≠ T127), G133 (= G132), S134 (= S133), W158 (≠ F157), T160 (= T159), R270 (= R269), F273 (= F272), L280 (≠ F279), V282 (≠ N281), Q338 (= Q337), I339 (≠ L338), G342 (= G341), I360 (≠ V359), Y364 (= Y363), T367 (= T366), E369 (= E368), I370 (= I369), L373 (≠ E372)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
36% identity, 97% coverage: 11:378/378 of query aligns to 8:376/381 of 8sgsA
- binding coenzyme a: S131 (= S133), A133 (≠ L135), N177 (≠ A179), F231 (= F233), M235 (= M237), L238 (= L240), I312 (≠ V314), E362 (≠ A364), G363 (= G365)
- binding flavin-adenine dinucleotide: F122 (≠ I124), L124 (≠ M126), S125 (≠ T127), G130 (= G132), S131 (= S133), W155 (≠ F157), T157 (= T159), R267 (= R269), F270 (= F272), L274 (≠ I276), L277 (≠ F279), Q335 (= Q337), I336 (≠ L338), G338 (= G340), G339 (= G341), I357 (≠ V359), I360 (= I362), Y361 (= Y363), T364 (= T366), E366 (= E368)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
36% identity, 97% coverage: 11:378/378 of query aligns to 38:406/412 of P16219
- G90 (= G63) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E77) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 124:133, 60% identical) binding in other chain
- R171 (≠ V143) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ FIT 157:159) binding in other chain
- A192 (= A164) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G181) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R269) binding
- Q308 (= Q280) binding in other chain
- R325 (= R297) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ T325) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QLHGG 337:341) binding
- R380 (= R352) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TNE 366:368) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
Query Sequence
>Pf1N1B4_966 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_966
MIPRTLFSSEHELFRDSVRTFLEKEAVPFHGQWEKQGYIDRQLWNKAGEAGMLCSHLPEE
YGGLGADFLYSAVVIEEVGRLGLTGIGFSLHSDIVAPYILHYGSEALKHKYLPKLVSGEM
VTAIAMTEPGAGSDLQGVKTTAVLDGDEYVINGSKTFITNGFLADLVIVVAKTDPKAGAK
GTSLFLVEANTPGFAKGRRLEKVGMKAQDTSELFFQDVRVPKENLLGQAGMGFAYLMQEL
PQERLTVAVGGLASAEAALQWTLDYTRERKAFGKAIADFQNTRFKLAEMATEIQIGRVFV
DRCLELHLQGKLDVPTAAMAKYWGTDLQCKVLDECVQLHGGYGFMWEYPIARAWADARVQ
RIYAGTNEIMKEIIARSL
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