SitesBLAST
Comparing GFF2427 FitnessBrowser__psRCH2:GFF2427 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)
47% identity, 96% coverage: 13:388/392 of query aligns to 54:427/430 of P51174
- K318 (≠ R279) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ Q283) 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)
46% identity, 95% coverage: 17:388/392 of query aligns to 56:427/430 of P28330
- E291 (= E252) 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 (≠ I264) to T: in dbSNP:rs1801204
- K333 (≠ T294) to Q: in dbSNP:rs2286963
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
43% identity, 95% coverage: 16:387/392 of query aligns to 7:378/380 of 2pg0A
- active site: M124 (= M135), T125 (= T136), E243 (= E252), A364 (= A373), R376 (= R385)
- binding flavin-adenine dinucleotide: I122 (= I133), M124 (= M135), T125 (= T136), G130 (= G141), S131 (= S142), F155 (= F166), I156 (= I167), T157 (= T168), R269 (= R278), F272 (= F281), F279 (= F288), Q337 (= Q346), L338 (= L347), G340 (= G349), G341 (= G350), V359 (≠ I368), I362 (= I371), Y363 (= Y372), T366 (= T375), E368 (= E377), M369 (≠ I378)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
38% identity, 95% coverage: 17:389/392 of query aligns to 5:374/374 of 5lnxD
- active site: L122 (≠ M135), T123 (= T136), G239 (≠ E252), E358 (≠ A373), K370 (≠ R385)
- binding flavin-adenine dinucleotide: L122 (≠ M135), T123 (= T136), G128 (= G141), S129 (= S142), F153 (= F166), T155 (= T168), R265 (= R278), Q267 (≠ A280), F268 (= F281), I272 (= I285), N275 (≠ F288), I278 (≠ T291), Q331 (= Q346), I332 (≠ L347), G335 (= G350), Y357 (= Y372), T360 (= T375), E362 (= E377)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
39% identity, 95% coverage: 16:387/392 of query aligns to 8:378/378 of 4n5fA
- active site: L126 (≠ M135), T127 (= T136), G243 (≠ E252), E364 (≠ A373), R376 (= R385)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M135), T127 (= T136), G132 (= G141), S133 (= S142), F157 (= F166), T159 (= T168), T210 (= T219), Y363 (= Y372), T366 (= T375), E368 (= E377), M372 (≠ E381)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
36% identity, 95% coverage: 16:388/392 of query aligns to 7:378/380 of 4l1fA
- active site: L125 (≠ M135), T126 (= T136), G242 (≠ E252), E363 (≠ A373), R375 (= R385)
- binding coenzyme a persulfide: T132 (≠ S142), H179 (≠ R189), F232 (= F242), M236 (= M246), E237 (≠ Q247), L239 (= L249), D240 (≠ P250), R243 (= R253), Y362 (= Y372), E363 (≠ A373), G364 (= G374), R375 (= R385)
- binding flavin-adenine dinucleotide: F123 (≠ I133), L125 (≠ M135), T126 (= T136), G131 (= G141), T132 (≠ S142), F156 (= F166), I157 (= I167), T158 (= T168), R268 (= R278), Q270 (≠ A280), F271 (= F281), I275 (= I285), F278 (= F288), L281 (≠ T291), Q336 (= Q346), I337 (≠ L347), G340 (= G350), I358 (= I368), Y362 (= Y372), T365 (= T375), Q367 (≠ E377)
- binding 1,3-propandiol: Q10 (≠ T19)
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)
36% identity, 94% coverage: 16:385/392 of query aligns to 10:382/387 of 1ivhA
- active site: M130 (= M135), S131 (≠ T136), E249 (= E252), A370 (= A373), R382 (= R385)
- binding coenzyme a persulfide: S137 (= S142), S185 (≠ A188), R186 (= R189), V239 (≠ F242), Y240 (≠ A243), M243 (= M246), E249 (= E252), R250 (= R253), G369 (≠ Y372), A370 (= A373), G371 (= G374), V375 (≠ I378)
- binding flavin-adenine dinucleotide: L128 (≠ I133), M130 (= M135), S131 (≠ T136), G136 (= G141), S137 (= S142), W161 (≠ F166), T163 (= T168), R275 (= R278), F278 (= F281), F285 (= F288), M288 (≠ T291), Q343 (= Q346), C344 (≠ L347), G347 (= G350), T372 (= T375), E374 (= E377)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
36% identity, 94% coverage: 16:385/392 of query aligns to 14:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T136), G140 (= G141), S141 (= S142), W165 (≠ F166), T167 (= T168), R279 (= R278), F282 (= F281), I286 (= I285), F289 (= F288), Q347 (= Q346), C348 (≠ L347), G351 (= G350), L369 (≠ I368), G375 (= G374), T376 (= T375), L382 (≠ E381)
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)
36% identity, 94% coverage: 16:385/392 of query aligns to 47:419/426 of P26440
- 165:174 (vs. 133:142, 70% identical) binding
- S174 (= S142) binding
- WIT 198:200 (≠ FIT 166:168) binding
- SR 222:223 (≠ AR 188:189) binding
- G250 (≠ A216) to A: in IVA; uncertain significance
- Y277 (≠ A243) binding
- DLER 284:287 (≠ PRER 250:253) binding
- E286 (= E252) 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 (= A257) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R278) binding
- Q323 (= Q289) binding
- I379 (≠ L345) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QLFGG 346:350) binding
- R398 (≠ V364) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ Q369) to N: in IVA; uncertain significance
- A407 (= A373) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (= AG 373:374) binding
- TSE 409:411 (= TSE 375:377) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
2d29A Structural study on project id tt0172 from thermus thermophilus hb8
40% identity, 96% coverage: 14:388/392 of query aligns to 8:383/386 of 2d29A
- active site: L126 (≠ M135), T127 (= T136), G247 (≠ E252), E368 (≠ A373), R380 (= R385)
- binding flavin-adenine dinucleotide: L126 (≠ M135), T127 (= T136), G132 (= G141), S133 (= S142), F157 (= F166), I158 (= I167), T159 (= T168), L363 (≠ I368), T370 (= T375), E372 (= E377)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
36% identity, 92% coverage: 28:388/392 of query aligns to 18:377/378 of 5ol2F
- active site: L124 (≠ M135), T125 (= T136), G241 (≠ E252), G374 (≠ R385)
- binding calcium ion: E29 (≠ Q39), E33 (≠ D43), R35 (≠ Q45)
- binding coenzyme a persulfide: L238 (= L249), R242 (= R253), E362 (≠ A373), G363 (= G374)
- binding flavin-adenine dinucleotide: F122 (≠ I133), L124 (≠ M135), T125 (= T136), P127 (= P138), T131 (≠ S142), F155 (= F166), I156 (= I167), T157 (= T168), E198 (≠ I209), R267 (= R278), F270 (= F281), L274 (≠ I285), F277 (= F288), Q335 (= Q346), L336 (= L347), G338 (= G349), G339 (= G350), Y361 (= Y372), T364 (= T375), E366 (= E377)
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
38% identity, 93% coverage: 24:388/392 of query aligns to 20:375/377 of 4ktoA
- active site: M130 (= M135), S131 (≠ T136), E239 (= E252), A360 (= A373), R372 (= R385)
- binding flavin-adenine dinucleotide: L128 (≠ I133), M130 (= M135), S131 (≠ T136), M155 (≠ V165), W156 (≠ F166), T158 (= T168), R265 (= R278), F268 (= F281), I272 (= I285), F275 (= F288), M278 (≠ T291), Q333 (= Q346), A334 (≠ L347), G337 (= G350), L355 (≠ I368), G359 (≠ Y372), T362 (= T375), E364 (= E377)
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: 16:388/392 of query aligns to 36:407/412 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)
35% identity, 95% coverage: 16:388/392 of query aligns to 9:380/384 of 1jqiA
- active site: G377 (≠ R385)
- binding acetoacetyl-coenzyme a: L95 (≠ I103), F125 (≠ I133), S134 (= S142), F234 (= F242), M238 (= M246), Q239 (= Q247), L241 (= L249), D242 (≠ P250), R245 (= R253), Y364 (= Y372), E365 (≠ A373), G366 (= G374)
- binding flavin-adenine dinucleotide: F125 (≠ I133), L127 (≠ M135), S128 (≠ T136), G133 (= G141), S134 (= S142), W158 (≠ F166), T160 (= T168), R270 (= R278), F273 (= F281), L280 (≠ F288), Q338 (= Q346), I339 (≠ L347), G342 (= G350), I360 (= I368), T367 (= T375), E369 (= E377), I370 (= I378)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
36% identity, 95% coverage: 15:388/392 of query aligns to 9:380/385 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 (≠ Y351), T347 (≠ L355), E348 (= E356)
- binding flavin-adenine dinucleotide: F125 (≠ I133), L127 (≠ M135), S128 (≠ T136), G133 (= G141), S134 (= S142), W158 (≠ F166), T160 (= T168), R270 (= R278), F273 (= F281), L280 (≠ F288), V282 (≠ N290), Q338 (= Q346), I339 (≠ L347), G342 (= G350), I360 (= I368), Y364 (= Y372), T367 (= T375), E369 (= E377), I370 (= I378), L373 (≠ E381)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
36% identity, 95% coverage: 15:388/392 of query aligns to 6:377/381 of 8sgsA
- binding coenzyme a: S131 (= S142), A133 (≠ L144), N177 (≠ A188), F231 (= F242), M235 (= M246), L238 (= L249), I312 (≠ S323), E362 (≠ A373), G363 (= G374)
- binding flavin-adenine dinucleotide: F122 (≠ I133), L124 (≠ M135), S125 (≠ T136), G130 (= G141), S131 (= S142), W155 (≠ F166), T157 (= T168), R267 (= R278), F270 (= F281), L274 (≠ I285), L277 (≠ F288), Q335 (= Q346), I336 (≠ L347), G338 (= G349), G339 (= G350), I357 (= I368), I360 (= I371), Y361 (= Y372), T364 (= T375), E366 (= E377)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
36% identity, 95% coverage: 15:388/392 of query aligns to 12:383/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ I133), L130 (≠ M135), S131 (≠ T136), G136 (= G141), S137 (= S142), W161 (≠ F166), T163 (= T168), T214 (= T219), R273 (= R278), F276 (= F281), L280 (≠ I285), L283 (≠ F288), V285 (≠ N290), Q341 (= Q346), I342 (≠ L347), G345 (= G350), I363 (= I368), Y367 (= Y372), T370 (= T375), E372 (= E377), L376 (≠ E381)
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, 95% coverage: 15:388/392 of query aligns to 36:407/412 of P16219
- G90 (= G70) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E84) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 133:142, 60% identical) binding in other chain
- R171 (≠ Q152) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ FIT 166:168) binding in other chain
- A192 (= A173) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G190) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R278) binding
- Q308 (= Q289) binding in other chain
- R325 (= R306) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S334) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QLFGG 346:350) binding
- R380 (= R361) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (= TSE 375:377) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
35% identity, 95% coverage: 16:387/392 of query aligns to 6:376/376 of 4m9aB
- active site: L124 (≠ M135), T125 (= T136), G241 (≠ E252), E362 (≠ A373), R374 (= R385)
- binding dihydroflavine-adenine dinucleotide: F122 (≠ I133), T125 (= T136), G130 (= G141), S131 (= S142), F155 (= F166), T157 (= T168), T208 (= T219), Y361 (= Y372), T364 (= T375), E366 (= E377), M370 (≠ E381)
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)
31% identity, 97% coverage: 9:387/392 of query aligns to 52:428/432 of P45954
- V137 (≠ S95) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ G96) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 133:142, 50% identical) binding in other chain
- S183 (= S142) binding
- WIS 207:209 (≠ FIT 166:168) binding in other chain
- S210 (≠ N169) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ A188) binding
- L255 (≠ Q214) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ F242) binding
- NEGR 291:294 (≠ PRER 250:253) binding
- I316 (≠ V275) to V: in dbSNP:rs1131430
- R319 (= R278) binding
- Q330 (= Q289) binding
- EWMGG 387:391 (≠ QLFGG 346:350) binding
- A416 (≠ T375) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TSE 375:377) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
Query Sequence
>GFF2427 FitnessBrowser__psRCH2:GFF2427
MNEQTLRGADCATSEDDQTLFQDSVRRFLQQEVAPHYEQWEADHQLPRALWHRLGEAGLL
GVDLPEQLGGCAAGVETCLMICEEISRQGFGGLASGYNIHANIVMPYIHHLGNPAQQACW
LPRMAAGEVLGAIAMTEPGAGSDLAAMRASAQKVPGGWKLNGSKVFITNGLLADMVIVCA
KTDPNARARGVSLFLVDTTLPGFSRGKAIRKIGQHASDTAELFFDDLIVPEDALLGDAGK
GFAYLMQELPRERLGVAAQAIGAIDGALQLTLDYVQQRRAFGQRIADFQNTRFTLAEVRA
HLEMGRAYFEKCLQRYARGEMSSTDAAALKLMLSEMQCRCVDQCLQLFGGYGYTLEYPIS
RFYVDARIQTIYAGTSEIMKEVIARDMLGPVA
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