SitesBLAST
Comparing RR42_RS11345 FitnessBrowser__Cup4G11:RR42_RS11345 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 (≠ R274) 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)
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 (≠ V255) to T: in dbSNP:rs1801204
- K333 (≠ A285) to Q: in dbSNP:rs2286963
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
52% identity, 98% coverage: 9:378/378 of query aligns to 7:378/380 of 2pg0A
- active site: M124 (= M126), T125 (= T127), E243 (= E243), A364 (≠ G364), 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 (≠ A366), E368 (= E368), M369 (≠ I369)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
40% identity, 99% coverage: 6:378/378 of query aligns to 1:372/374 of 5lnxD
- active site: L122 (≠ M126), T123 (= T127), G239 (≠ E243), E358 (≠ G364), 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 (≠ V282), Q331 (= Q337), I332 (≠ L338), G335 (= G341), Y357 (= Y363), T360 (≠ A366), E362 (= E368)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
38% 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 (≠ R32), E33 (≠ Q36), R35 (≠ Y38)
- binding coenzyme a persulfide: L238 (= L240), R242 (= R244), E362 (≠ G364), 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 (≠ A366), E366 (= E368)
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
39% identity, 98% coverage: 8:378/378 of query aligns to 6:377/378 of 3r7kA
- active site: V126 (≠ M126), T127 (= T127), E242 (= E243), G363 (= G364), 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 (≠ V282), Q336 (= Q337), I337 (≠ L338), G340 (= G341), I358 (≠ V359), T365 (≠ A366), E367 (= E368)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
38% identity, 98% coverage: 7:378/378 of query aligns to 5:377/380 of 4l1fA
- active site: L125 (≠ M126), T126 (= T127), G242 (≠ E243), E363 (≠ G364), R375 (= R376)
- binding coenzyme a persulfide: T132 (≠ S133), H179 (≠ K180), F232 (= F233), M236 (= M237), E237 (≠ R238), L239 (= L240), D240 (≠ S241), R243 (= R244), Y362 (= Y363), E363 (≠ G364), 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 (≠ V282), Q336 (= Q337), I337 (≠ L338), G340 (= G341), I358 (≠ V359), Y362 (= Y363), T365 (≠ A366), Q367 (≠ E368)
- binding 1,3-propandiol: L5 (≠ F7), Q10 (≠ E12)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
37% identity, 98% coverage: 7:376/378 of query aligns to 8:382/387 of 1ivhA
- active site: M130 (= M126), S131 (≠ T127), E249 (= E243), A370 (≠ G364), R382 (= R376)
- binding coenzyme a persulfide: S137 (= S133), S185 (≠ A179), R186 (≠ K180), V239 (≠ F233), Y240 (≠ G234), M243 (= M237), E249 (= E243), R250 (= R244), G369 (≠ Y363), A370 (≠ G364), G371 (= G365), V375 (≠ I369)
- binding flavin-adenine dinucleotide: L128 (≠ I124), M130 (= M126), S131 (≠ T127), G136 (= G132), S137 (= S133), W161 (≠ F157), T163 (= T159), R275 (= R269), F278 (= F272), F285 (= F279), M288 (≠ V282), Q343 (= Q337), C344 (≠ L338), G347 (= G341), T372 (≠ A366), E374 (= E368)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
37% identity, 98% coverage: 7:376/378 of query aligns to 12:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T127), G140 (= G132), S141 (= S133), W165 (≠ F157), T167 (= T159), R279 (= R269), F282 (= F272), I286 (= I276), F289 (= F279), Q347 (= Q337), C348 (≠ L338), G351 (= G341), L369 (≠ V359), G375 (= G365), T376 (≠ A366), L382 (≠ E372)
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)
37% identity, 98% coverage: 7:376/378 of query aligns to 45:419/426 of P26440
- 165:174 (vs. 124:133, 60% identical) binding
- S174 (= S133) binding
- WIT 198:200 (≠ FIT 157:159) binding
- SR 222:223 (≠ AK 179:180) binding
- G250 (≠ A207) to A: in IVA; uncertain significance
- Y277 (≠ G234) binding
- DLER 284:287 (≠ SWER 241:244) binding
- E286 (= E243) 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 (= A248) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R269) binding
- Q323 (= Q280) binding
- I379 (≠ V336) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QLHGG 337:341) binding
- R398 (≠ A355) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ Q360) to N: in IVA; uncertain significance
- A407 (≠ G364) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ GG 364:365) binding
- TSE 409:411 (≠ ANE 366:368) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
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 (≠ G364), R376 (= R376)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M126), T127 (= T127), G132 (= G132), S133 (= S133), F157 (= F157), T159 (= T159), T210 (= T210), Y363 (= Y363), T366 (≠ A366), E368 (= E368), M372 (≠ E372)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
35% identity, 98% coverage: 7:378/378 of query aligns to 5:376/379 of 1ukwB
- active site: L124 (≠ M126), S125 (≠ T127), T241 (≠ E243), E362 (≠ G364), R374 (= R376)
- binding cobalt (ii) ion: D145 (= D147), H146 (= H148)
- binding flavin-adenine dinucleotide: F122 (≠ I124), L124 (≠ M126), S125 (≠ T127), G130 (= G132), S131 (= S133), W155 (≠ F157), S157 (≠ T159), K200 (= K202), L357 (≠ V359), Y361 (= Y363), E362 (≠ G364), T364 (≠ A366), E366 (= E368), L370 (≠ E372)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
35% identity, 98% coverage: 7:378/378 of query aligns to 5:376/379 of 1ukwA
- active site: L124 (≠ M126), S125 (≠ T127), T241 (≠ E243), E362 (≠ G364), R374 (= R376)
- binding flavin-adenine dinucleotide: F122 (≠ I124), L124 (≠ M126), S125 (≠ T127), G130 (= G132), S131 (= S133), W155 (≠ F157), S157 (≠ T159), L357 (≠ V359), Y361 (= Y363), E362 (≠ G364), T364 (≠ A366), E366 (= E368), L370 (≠ E372)
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 (≠ A366), Q366 (≠ E368)
Sites not aligning to the query:
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
32% identity, 98% coverage: 7:378/378 of query aligns to 6:377/381 of 2jifA
- active site: L125 (≠ M126), S126 (≠ T127), G242 (≠ E243), E363 (≠ G364), K375 (≠ R376)
- binding coenzyme a persulfide: S132 (= S133), S134 (≠ L135), Y178 (≠ A179), Y232 (≠ F233), I236 (≠ M237), L239 (= L240), N240 (≠ S241), R243 (= R244), Y362 (= Y363), E363 (≠ G364), G364 (= G365), I368 (= I369)
- binding flavin-adenine dinucleotide: F123 (≠ I124), L125 (≠ M126), S126 (≠ T127), G131 (= G132), S132 (= S133), W156 (≠ F157), I157 (= I158), S158 (≠ T159), K201 (= K202), T209 (= T210), R268 (= R269), F271 (= F272), L275 (≠ I276), F278 (= F279), L281 (≠ V282), E336 (≠ Q337), W337 (≠ L338), G340 (= G341), N367 (≠ E368), I368 (= I369)
P45954 Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial; SBCAD; 2-methyl branched chain acyl-CoA dehydrogenase; 2-MEBCAD; 2-methylbutyryl-coenzyme A dehydrogenase; 2-methylbutyryl-CoA dehydrogenase; EC 1.3.8.5 from Homo sapiens (Human) (see 6 papers)
32% identity, 98% coverage: 7:378/378 of query aligns to 57:428/432 of P45954
- V137 (≠ G87) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (= F88) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 124:133, 40% identical) binding in other chain
- S183 (= S133) binding
- WIS 207:209 (≠ FIT 157:159) binding in other chain
- S210 (≠ N160) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ A179) binding
- L255 (≠ M205) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ F233) binding
- NEGR 291:294 (≠ SWER 241:244) binding
- I316 (≠ T266) to V: in dbSNP:rs1131430
- R319 (= R269) binding
- Q330 (= Q280) binding
- EWMGG 387:391 (≠ QLHGG 337:341) binding
- A416 (= A366) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ ANE 366:368) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
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 (≠ G364), 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 (≠ A366), Q357 (≠ E368)
3p4tA Crystal structure of a putative acyl-coa dehydrogenase from mycobacterium smegmatis (see paper)
38% identity, 98% coverage: 8:378/378 of query aligns to 5:377/381 of 3p4tA
- active site: I125 (≠ M126), T126 (= T127), E241 (= E243), G363 (= G364), K375 (≠ R376)
- 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 (≠ I124), I125 (≠ M126), T126 (= T127), G130 (≠ T131), G131 (= G132), S132 (= S133), Y156 (≠ F157), I157 (= I158), T158 (= T159), K200 (= K202), R267 (= R269), T269 (≠ A271), L274 (≠ I276), R277 (≠ F279), Q336 (= Q337), L337 (= L338), G340 (= G341), I358 (≠ V359), T365 (≠ A366)
3oibA Crystal structure of a putative acyl-coa dehydrogenase from mycobacterium smegmatis, iodide soak (see paper)
38% identity, 98% coverage: 8:378/378 of query aligns to 5:377/381 of 3oibA
- active site: I125 (≠ M126), T126 (= T127), E241 (= E243), G363 (= G364), K375 (≠ R376)
- binding dihydroflavine-adenine dinucleotide: L123 (≠ I124), I125 (≠ M126), T126 (= T127), G131 (= G132), S132 (= S133), Y156 (≠ F157), I157 (= I158), T158 (= T159), K200 (= K202), R267 (= R269), T269 (≠ A271), L274 (≠ I276), R277 (≠ F279), Q336 (= Q337), L337 (= L338), G340 (= G341), I358 (≠ V359), T365 (≠ A366), E367 (= E368)
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: 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 (≠ G364), 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 (≠ A366), Q367 (≠ E368), I368 (= I369)
Query Sequence
>RR42_RS11345 FitnessBrowser__Cup4G11:RR42_RS11345
MIARTLFTEEHEMLRTAARRFMETEVAPHHERWEEQGYVDRDVWLKAGAAGFLCASMPEQ
YGGAGGDKLYSVVLMEEQARAGCTGLGFGLHSEIVAPYIEHYGSEYLKSAYLPKMAAGEM
IGAIAMTEPGTGSDLQGIKATAVRHGDHYLLNGSKTFITNGWHADLVIVVAKTDPQAGAK
GISLFVVDTSMPGFSKGKRLKKAGMKAQDTAELFFDNVRVPVANLLGDEGQGFGYLMREL
SWERLQIAITAVAAVEAGLEWTLAYTRDRKAFKRPISEFQTVAHALADIRTELEMGRVFV
DRCLQLVLEGKLDAATASMAKYWTTEMQFRALDRCVQLHGGYGYMWEYPITRAWADARVQ
RIYGGANEIMKELISRNL
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