SitesBLAST
Comparing BPHYT_RS20325 FitnessBrowser__BFirm:BPHYT_RS20325 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)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
41% identity, 94% coverage: 8:370/388 of query aligns to 18:378/378 of 5ol2F
- active site: L124 (= L114), T125 (= T115), G241 (≠ Q233), G374 (≠ K366)
- binding calcium ion: E29 (= E19), E33 (≠ A23), R35 (≠ A25)
- binding coenzyme a persulfide: L238 (= L230), R242 (= R234), E362 (= E354), G363 (= G355)
- binding flavin-adenine dinucleotide: F122 (= F112), L124 (= L114), T125 (= T115), P127 (= P117), T131 (≠ S121), F155 (= F145), I156 (= I146), T157 (= T147), E198 (≠ Y189), R267 (= R259), F270 (= F262), L274 (≠ V266), F277 (= F269), Q335 (= Q327), L336 (≠ M328), G338 (= G330), G339 (= G331), Y361 (= Y353), T364 (= T356), E366 (≠ Q358)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
41% identity, 95% coverage: 5:371/388 of query aligns to 13:378/383 of 4iv6B
- active site: L121 (= L114), T122 (= T115), G240 (≠ Q233), E361 (= E354), K373 (= K366)
- binding dihydroflavine-adenine dinucleotide: L121 (= L114), T122 (= T115), G126 (≠ A119), G127 (= G120), S128 (= S121), W152 (≠ F145), I153 (= I146), S154 (≠ T147), R266 (= R259), S268 (≠ Q261), F269 (= F262), I273 (≠ V266), H276 (≠ F269), V279 (= V272), R334 (≠ Q327), V335 (≠ M328), G338 (= G331), L356 (≠ A349), G360 (≠ Y353), T363 (= T356), E365 (≠ Q358), I366 (= I359)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
41% identity, 94% coverage: 5:369/388 of query aligns to 13:373/374 of 5lnxD
- active site: L122 (= L114), T123 (= T115), G239 (≠ Q233), E358 (= E354), K370 (= K366)
- binding flavin-adenine dinucleotide: L122 (= L114), T123 (= T115), G128 (= G120), S129 (= S121), F153 (= F145), T155 (= T147), R265 (= R259), Q267 (= Q261), F268 (= F262), I272 (≠ V266), N275 (≠ F269), I278 (≠ V272), Q331 (= Q327), I332 (≠ M328), G335 (= G331), Y357 (= Y353), T360 (= T356), E362 (≠ Q358)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
38% identity, 91% coverage: 18:371/388 of query aligns to 28:379/379 of 6fahD
- active site: L124 (= L114), T125 (= T115), G241 (≠ Q233), G374 (≠ K366)
- binding flavin-adenine dinucleotide: F122 (= F112), L124 (= L114), T125 (= T115), R152 (≠ S142), F155 (= F145), T157 (= T147), E198 (≠ Y189), R267 (= R259), Q269 (= Q261), F270 (= F262), I274 (≠ V266), F277 (= F269), Q335 (= Q327), I336 (≠ M328), G339 (= G331), Y361 (= Y353), T364 (= T356), Q366 (= Q358)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
39% identity, 94% coverage: 6:370/388 of query aligns to 17:379/380 of 4l1fA
- active site: L125 (= L114), T126 (= T115), G242 (≠ Q233), E363 (= E354), R375 (≠ K366)
- binding coenzyme a persulfide: T132 (≠ S121), H179 (≠ G169), F232 (= F223), M236 (= M227), E237 (≠ K228), L239 (= L230), D240 (≠ N231), R243 (= R234), Y362 (= Y353), E363 (= E354), G364 (= G355), R375 (≠ K366)
- binding flavin-adenine dinucleotide: F123 (= F112), L125 (= L114), T126 (= T115), G131 (= G120), T132 (≠ S121), F156 (= F145), I157 (= I146), T158 (= T147), R268 (= R259), Q270 (= Q261), F271 (= F262), I275 (≠ V266), F278 (= F269), L281 (≠ V272), Q336 (= Q327), I337 (≠ M328), G340 (= G331), I358 (≠ A349), Y362 (= Y353), T365 (= T356), Q367 (= Q358)
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, 93% coverage: 5:366/388 of query aligns to 19:382/387 of 1ivhA
- active site: M130 (≠ L114), S131 (≠ T115), E249 (≠ Q233), A370 (≠ E354), R382 (≠ K366)
- binding coenzyme a persulfide: S137 (= S121), S185 (≠ A168), R186 (≠ G169), V239 (≠ F223), Y240 (≠ R224), M243 (= M227), E249 (≠ Q233), R250 (= R234), G369 (≠ Y353), A370 (≠ E354), G371 (= G355), V375 (≠ I359)
- binding flavin-adenine dinucleotide: L128 (≠ F112), M130 (≠ L114), S131 (≠ T115), G136 (= G120), S137 (= S121), W161 (≠ F145), T163 (= T147), R275 (= R259), F278 (= F262), F285 (= F269), M288 (≠ V272), Q343 (= Q327), C344 (≠ M328), G347 (= G331), T372 (= T356), E374 (≠ Q358)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
36% identity, 93% coverage: 5:366/388 of query aligns to 23:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T115), G140 (= G120), S141 (= S121), W165 (≠ F145), T167 (= T147), R279 (= R259), F282 (= F262), I286 (≠ V266), F289 (= F269), Q347 (= Q327), C348 (≠ M328), G351 (= G331), L369 (≠ A349), G375 (= G355), T376 (= T356), L382 (= L362)
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, 93% coverage: 5:366/388 of query aligns to 56:419/426 of P26440
- 165:174 (vs. 112:121, 60% identical) binding
- S174 (= S121) binding
- WIT 198:200 (≠ FIT 145:147) binding
- SR 222:223 (≠ AG 168:169) binding
- G250 (= G196) to A: in IVA; uncertain significance
- Y277 (≠ R224) binding
- DLER 284:287 (≠ NKQR 231:234) binding
- E286 (≠ Q233) 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 (= A238) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R259) binding
- Q323 (= Q270) binding
- I379 (≠ V326) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QMLGG 327:331) binding
- R398 (= R345) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ F350) to N: in IVA; uncertain significance
- A407 (≠ E354) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ EG 354:355) binding
- TSE 409:411 (≠ TTQ 356:358) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
2uxwA Crystal structure of human very long chain acyl-coa dehydrogenase (acadvl)
38% identity, 93% coverage: 5:365/388 of query aligns to 41:405/567 of 2uxwA
- active site: L148 (= L114), T149 (= T115), G272 (≠ Q233), E394 (= E354)
- binding flavin-adenine dinucleotide: F146 (= F112), L148 (= L114), T149 (= T115), G154 (= G120), S155 (= S121), W181 (≠ F145), I182 (= I146), S183 (≠ T147), F393 (≠ Y353), T396 (= T356), D398 (≠ Q358), I399 (= I359)
- binding trans delta2 palmitenoyl-coenzymea: V96 (≠ A62), G107 (≠ R73), L110 (≠ V76), F146 (= F112), L269 (= L230), F393 (≠ Y353), E394 (= E354), G395 (= G355)
Sites not aligning to the query:
3b96A Structural basis for substrate fatty-acyl chain specificity: crystal structure of human very-long-chain acyl-coa dehydrogenase (see paper)
38% identity, 93% coverage: 5:365/388 of query aligns to 41:405/554 of 3b96A
- active site: L148 (= L114), T149 (= T115), G272 (≠ Q233), E394 (= E354)
- binding flavin-adenine dinucleotide: F146 (= F112), L148 (= L114), T149 (= T115), G154 (= G120), S155 (= S121), W181 (≠ F145), I182 (= I146), S183 (≠ T147), I389 (≠ A349), F393 (≠ Y353), T396 (= T356), D398 (≠ Q358), I399 (= I359)
- binding tetradecanoyl-coa: V96 (≠ A62), G107 (≠ R73), F146 (= F112), L269 (= L230), F393 (≠ Y353), E394 (= E354)
Sites not aligning to the query:
7s7gA Crystal structure analysis of human vlcad
38% identity, 93% coverage: 5:365/388 of query aligns to 41:405/571 of 7s7gA
- binding flavin-adenine dinucleotide: F146 (= F112), L148 (= L114), T149 (= T115), G154 (= G120), S155 (= S121), W181 (≠ F145), I182 (= I146), S183 (≠ T147), I389 (≠ A349), T396 (= T356), D398 (≠ Q358), I399 (= I359)
Sites not aligning to the query:
P49748 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; VLCAD; EC 1.3.8.9 from Homo sapiens (Human) (see 8 papers)
38% identity, 93% coverage: 5:365/388 of query aligns to 109:473/655 of P49748
- 214:223 (vs. 112:121, 70% identical) binding
- WIS 249:251 (≠ FIT 145:147) binding
- F458 (= F350) to L: in ACADVLD; loss of acyl-CoA dehydrogenase activity; Loss of FAD cofactor-binding; dbSNP:rs118204017; mutation to T: Decreased acyl-CoA dehydrogenase activity. Decreased affinity for acyl-CoA. No effect on FAD cofactor-binding.; mutation to V: Loss of acyl-CoA dehydrogenase activity. Loss of FAD cofactor-binding.; mutation to Y: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. Decreased FAD cofactor-binding.
- FEG 461:463 (≠ YEG 353:355) binding
- E462 (= E354) active site, Proton acceptor; mutation to D: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. No effect on FAD cofactor-binding.; mutation to Q: Loss of acyl-CoA dehydrogenase activity. No effect on FAD cofactor-binding.
- TND 464:466 (≠ TTQ 356:358) binding
Sites not aligning to the query:
- 1:40 modified: transit peptide, Mitochondrion
- 490 A → P: in ACADVLD; decreased association with mitochondrial inner membrane; may affect substrate specificity, possibly reducing the affinity for long-chain acyl-CoA substrates; dbSNP:rs759775666; mutation A->G,V,S,D,H: Changed substrate specificity with decreased affinity for tetradecanoyl-CoA and hexadecanoyl-CoA.
- 502 L → P: in ACADVLD; decreased association with mitochondrial inner membrane; decreased specific activity towards several substrates in vitro
- 534 E → K: in ACADVLD; uncertain significance; dbSNP:rs2230180
- 562 binding
- 583 S → W: in ACADVLD; Loss of homodimerization; loss of localization to mitochondrial inner membrane; dbSNP:rs1085307648
Q9H845 Complex I assembly factor ACAD9, mitochondrial; Acyl-CoA dehydrogenase family member 9; ACAD-9; EC 1.3.8.- from Homo sapiens (Human) (see 4 papers)
36% identity, 98% coverage: 1:380/388 of query aligns to 70:460/621 of Q9H845
- R193 (= R127) to W: in MC1DN20; uncertain significance; dbSNP:rs377547811
- S234 (≠ P166) to F: in MC1DN20; uncertain significance
- G303 (≠ Q233) to S: in MC1DN20; uncertain significance; dbSNP:rs143383023
- A326 (≠ T256) to T: in MC1DN20; uncertain significance; dbSNP:rs115532916
- E413 (= E341) to K: in MC1DN20; uncertain significance; dbSNP:rs149753643
- E426 (= E354) mutation to Q: Loss of long-chain-acyl-CoA dehydrogenase activity. Does not affect mitochondrial complex I assembly.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
8phfA Cryo-em structure of human acad9-s191a (see paper)
37% identity, 96% coverage: 1:372/388 of query aligns to 33:407/547 of 8phfA
- binding flavin-adenine dinucleotide: T144 (= T115), W176 (≠ F145), K225 (= K191), R292 (= R259), Q294 (= Q261), F295 (= F262), F302 (= F269), L304 (= L271), I305 (≠ V272), I363 (≠ M328), G365 (= G330), G366 (= G331), F388 (≠ Y353), E393 (≠ Q358), M397 (≠ L362)
Sites not aligning to the query:
8pheA Acad9-wt in complex with ecsit-cter (see paper)
37% identity, 96% coverage: 1:372/388 of query aligns to 33:407/551 of 8pheA
- binding : L143 (= L114), D151 (= D122), A153 (≠ T124), S154 (≠ A125), I155 (≠ L126), K202 (vs. gap), I205 (= I171), F256 (= F223), M260 (= M227), F295 (= F262), N296 (≠ G263), I394 (= I359), Y398 (≠ N363), L401 (≠ K366), Q405 (≠ R370)
Sites not aligning to the query:
2z1qB Crystal structure of acyl coa dehydrogenase
40% identity, 95% coverage: 8:376/388 of query aligns to 38:416/549 of 2z1qB
- active site: L144 (= L114), T145 (= T115), G259 (≠ Q233), E394 (= E354), G406 (≠ K366)
- binding flavin-adenine dinucleotide: Y142 (≠ F112), L144 (= L114), T145 (= T115), G150 (= G120), S151 (= S121), W177 (≠ F145), S179 (≠ T147), R285 (= R259), F288 (= F262), I292 (≠ V266), F295 (= F269), I298 (≠ V272), H369 (≠ L329), G370 (= G330), F393 (≠ Y353), I399 (= I359)
Sites not aligning to the query:
8ca1B Cryo-em structure of the acadvl dimer from mus musculus. (see paper)
36% identity, 94% coverage: 1:365/388 of query aligns to 39:407/589 of 8ca1B
- binding flavin-adenine dinucleotide: F148 (= F112), T151 (= T115), G156 (= G120), S157 (= S121), W183 (≠ F145), S185 (≠ T147), R300 (= R259), Q302 (= Q261), F303 (= F262), I307 (≠ V266), V312 (≠ L271), I313 (≠ V272), Q369 (= Q327), I370 (≠ M328), F395 (≠ Y353), D400 (≠ Q358), I401 (= I359)
P50544 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; MVLCAD; VLCAD; EC 1.3.8.9 from Mus musculus (Mouse) (see paper)
36% identity, 94% coverage: 1:365/388 of query aligns to 106:474/656 of P50544
- C238 (vs. gap) modified: S-nitrosocysteine
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
42% identity, 95% coverage: 1:370/388 of query aligns to 8:370/370 of 2dvlA
- active site: L121 (= L114), T122 (= T115), G233 (≠ Q233), E354 (= E354), R366 (≠ K366)
- binding flavin-adenine dinucleotide: L121 (= L114), T122 (= T115), G127 (= G120), S128 (= S121), W152 (≠ F145), I153 (= I146), T154 (= T147), T356 (= T356), E358 (≠ Q358)
5iduC Crystal structure of an acyl-coa dehydrogenase domain protein from burkholderia phymatum bound to fad
44% identity, 77% coverage: 81:377/388 of query aligns to 112:405/405 of 5iduC
- active site: L145 (= L114), S146 (≠ T115), F260 (≠ Q233), E381 (= E354), R393 (≠ K366)
- binding flavin-adenine dinucleotide: F143 (= F112), L145 (= L114), S146 (≠ T115), G151 (= G120), S152 (= S121), W176 (≠ F145), S178 (≠ T147), R286 (= R259), M288 (≠ Q261), F296 (= F269), Q354 (= Q327), L355 (≠ M328), G358 (= G331), A376 (= A349), Y380 (= Y353), A383 (≠ T356), E385 (≠ Q358)
Query Sequence
>BPHYT_RS20325 FitnessBrowser__BFirm:BPHYT_RS20325
MLAGVAKFVRDEAIPRENEIEQADAVPADLVQRMRELGYFGWSIPRDFGGAGLSTEQLVR
GAFELSQASVAFRARVGTNTGIGSEALVADGTDTQKQRYLPRLASGEFTGAFALTEPDAG
SDATALRTTARRDGDHYILDGSKCFITNAPIADLFTVMARTELAKPGAGGISAFLVERGT
PGLSTSAPYDKMGQAGSPVGDVVFEGCRVPAANLIGGKEGMGFRTAMKVLNKQRIHLAAL
CTGPAMRMLEEAVAYTSRREQFGKPVAEFQLVQALIAECQTEIYAARSMILETARKRDAG
EDVALEASMCKMFASEMCGRVADRAVQMLGGRGYLAGNAVERFYRDVRAFRIYEGTTQIH
QLNIAKITLRRAAERDQAKVRADAACAA
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