SitesBLAST
Comparing BPHYT_RS03780 FitnessBrowser__BFirm:BPHYT_RS03780 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)
3gqtC Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment (1,4-dimethyl-1,2,3,4- tetrahydroquinoxalin-6-yl)methylamine (see paper)
90% identity, 99% coverage: 5:395/396 of query aligns to 1:385/385 of 3gqtC
- active site: L135 (= L139), T136 (= T140), A250 (= A254), E365 (= E375), R377 (= R387)
- binding 1-(1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methanamine: W166 (= W170), K210 (= K214), L213 (= L217), T218 (= T222), Y364 (= Y374)
3eonC 2.55a crystal structure of native glutaryl-coa dehydrogenase from burkholderia pseudomallei in complex with a small molecule (see paper)
89% identity, 98% coverage: 5:394/396 of query aligns to 1:382/382 of 3eonC
3gncA Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment 6421 (see paper)
89% identity, 99% coverage: 4:394/396 of query aligns to 1:380/380 of 3gncA
3d6bC 2.2 a crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei (see paper)
88% identity, 98% coverage: 5:394/396 of query aligns to 1:377/377 of 3d6bC
2r0nA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
68% identity, 98% coverage: 6:395/396 of query aligns to 1:388/390 of 2r0nA
- active site: L133 (= L139), T134 (= T140), A247 (= A254), E368 (= E375), R380 (= R387)
- binding flavin-adenine dinucleotide: F131 (= F137), L133 (= L139), T134 (= T140), G139 (= G145), S140 (= S146), W166 (= W170), I167 (= I171), T168 (= T172), Y367 (= Y374), T370 (= T377), D372 (= D379)
- binding 3-thiaglutaryl-CoA: R92 (= R98), S93 (= S99), V97 (= V103), P142 (= P148), G238 (≠ R245), F241 (= F248), L244 (= L251), N245 (= N252), P318 (≠ V325), Y367 (= Y374), E368 (= E375), I377 (= I384)
1sirA The crystal structure and mechanism of human glutaryl-coa dehydrogenase (see paper)
68% identity, 98% coverage: 6:395/396 of query aligns to 1:388/390 of 1sirA
- active site: L133 (= L139), T134 (= T140), A247 (= A254), E368 (= E375), R380 (= R387)
- binding flavin-adenine dinucleotide: F131 (= F137), L133 (= L139), T134 (= T140), G139 (= G145), S140 (= S146), W166 (= W170), I167 (= I171), T168 (= T172), Y367 (= Y374), T370 (= T377)
- binding s-4-nitrobutyryl-coa: S93 (= S99), S140 (= S146), F241 (= F248), G242 (≠ T249), L244 (= L251), N245 (= N252), R248 (= R255), P318 (≠ V325), Y367 (= Y374), E368 (= E375), R380 (= R387)
2r0mA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
68% identity, 98% coverage: 6:395/396 of query aligns to 1:388/390 of 2r0mA
- active site: L133 (= L139), T134 (= T140), A247 (= A254), D368 (≠ E375), R380 (= R387)
- binding 4-nitrobutanoic acid: L101 (= L107), Y367 (= Y374), D368 (≠ E375)
- binding flavin-adenine dinucleotide: F131 (= F137), L133 (= L139), T134 (= T140), G139 (= G145), S140 (= S146), W166 (= W170), I167 (= I171), T168 (= T172), L210 (= L217), Y367 (= Y374), T370 (= T377)
2ebaA Crystal structure of the putative glutaryl-coa dehydrogenase from thermus thermophilus
49% identity, 96% coverage: 15:395/396 of query aligns to 7:380/380 of 2ebaA
- active site: L131 (= L139), T132 (= T140), A239 (= A254), E360 (= E375), R372 (= R387)
- binding flavin-adenine dinucleotide: L131 (= L139), T132 (= T140), G136 (≠ H144), G137 (= G145), S138 (= S146), W161 (= W170), T163 (= T172), R265 (= R280), L272 (= L287), K275 (≠ N290), D333 (= D348), I334 (≠ M349), G337 (= G352), T355 (≠ V370), T358 (= T373), Y359 (= Y374), T362 (= T377)
3sf6A Crystal structure of glutaryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
47% identity, 97% coverage: 10:395/396 of query aligns to 5:386/387 of 3sf6A
- active site: L134 (= L139), T135 (= T140), A245 (= A254), E366 (= E375), Q378 (≠ R387)
- binding dihydroflavine-adenine dinucleotide: F132 (= F137), L134 (= L139), T135 (= T140), G140 (= G145), S141 (= S146), W165 (= W170), I166 (= I171), T167 (= T172), S361 (≠ V370), T364 (= T373), Y365 (= Y374), T368 (= T377), E370 (≠ D379), M371 (≠ I380)
3swoA Crystal structure of a glutaryl-coa dehydrogenase from mycobacterium smegmatis in complex with fadh2 (see paper)
45% identity, 96% coverage: 16:395/396 of query aligns to 13:387/388 of 3swoA
- active site: L135 (= L139), T136 (= T140), A246 (= A254), E367 (= E375), K379 (≠ R387)
- binding dihydroflavine-adenine dinucleotide: F133 (= F137), L135 (= L139), T136 (= T140), G141 (= G145), S142 (= S146), W166 (= W170), I167 (= I171), T168 (= T172), R272 (= R280), V274 (≠ Q282), F275 (= F283), L279 (= L287), Y282 (≠ N290), T340 (≠ D348), L341 (≠ M349), G344 (= G352), I347 (= I355), T365 (= T373), Y366 (= Y374), T369 (= T377), E371 (≠ D379), M372 (≠ I380)
2ix6A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 (see paper)
37% identity, 98% coverage: 7:395/396 of query aligns to 33:412/416 of 2ix6A
- active site: L158 (= L139), T159 (= T140), S271 (≠ A254), E392 (= E375), R404 (= R387)
- binding flavin-adenine dinucleotide: T159 (= T140), G164 (= G145), S165 (= S146), W189 (= W170), N239 (≠ T222), R297 (= R280), F300 (= F283), L304 (= L287), F307 (≠ N290), N310 (≠ I293), E365 (≠ D348), L366 (≠ M349), G369 (= G352), I372 (= I355), Y391 (= Y374), T394 (= T377), D396 (= D379)
2ix5A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 in complex with acetoacetyl-coa (see paper)
37% identity, 98% coverage: 7:395/396 of query aligns to 33:412/415 of 2ix5A
- active site: L158 (= L139), T159 (= T140), S271 (≠ A254), E392 (= E375), R404 (= R387)
- binding acetoacetyl-coenzyme a: S165 (= S146), A167 (≠ P148), S168 (≠ G149), F261 (≠ L244), L268 (= L251), R272 (= R255), E392 (= E375), G393 (= G376), R404 (= R387)
- binding flavin-adenine dinucleotide: L158 (= L139), T159 (= T140), G164 (= G145), S165 (= S146), W189 (= W170), N239 (≠ T222), R297 (= R280), F300 (= F283), L304 (= L287), F307 (≠ N290), L309 (= L292), N310 (≠ I293), E365 (≠ D348), L366 (≠ M349), G368 (= G351), G369 (= G352), Y391 (= Y374), T394 (= T377), D396 (= D379), I397 (= I380)
Q96329 Acyl-coenzyme A oxidase 4, peroxisomal; AOX 4; G6p; Short-chain acyl-CoA oxidase; AtCX4; AtG6; SAOX; EC 1.3.3.6 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 98% coverage: 7:395/396 of query aligns to 49:428/436 of Q96329
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
36% identity, 94% coverage: 15:388/396 of query aligns to 1:376/380 of 4l1fA
- active site: L125 (= L139), T126 (= T140), G242 (≠ A254), E363 (= E375), R375 (= R387)
- binding coenzyme a persulfide: T132 (≠ S146), H179 (≠ D192), F232 (≠ L244), M236 (≠ F248), E237 (≠ T249), L239 (= L251), D240 (≠ N252), R243 (= R255), Y362 (= Y374), E363 (= E375), G364 (= G376), R375 (= R387)
- binding flavin-adenine dinucleotide: F123 (= F137), L125 (= L139), T126 (= T140), G131 (= G145), T132 (≠ S146), F156 (≠ W170), I157 (= I171), T158 (= T172), R268 (= R280), Q270 (= Q282), F271 (= F283), I275 (≠ L287), F278 (≠ N290), L281 (≠ I293), Q336 (≠ D348), I337 (≠ M349), G340 (= G352), I358 (≠ V370), Y362 (= Y374), T365 (= T377), Q367 (≠ D379)
- binding 1,3-propandiol: L5 (= L19), Q10 (≠ R24)
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
39% identity, 93% coverage: 19:387/396 of query aligns to 1:366/370 of 2dvlA
- active site: L121 (= L139), T122 (= T140), G233 (≠ A254), E354 (= E375), R366 (= R387)
- binding flavin-adenine dinucleotide: L121 (= L139), T122 (= T140), G127 (= G145), S128 (= S146), W152 (= W170), I153 (= I171), T154 (= T172), T356 (= T377), E358 (≠ D379)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
38% identity, 92% coverage: 24:387/396 of query aligns to 11:370/374 of 5lnxD
- active site: L122 (= L139), T123 (= T140), G239 (≠ A254), E358 (= E375), K370 (≠ R387)
- binding flavin-adenine dinucleotide: L122 (= L139), T123 (= T140), G128 (= G145), S129 (= S146), F153 (≠ W170), T155 (= T172), R265 (= R280), Q267 (= Q282), F268 (= F283), I272 (≠ L287), N275 (= N290), I278 (= I293), Q331 (≠ D348), I332 (≠ M349), G335 (= G352), Y357 (= Y374), T360 (= T377), E362 (≠ D379)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
35% identity, 94% coverage: 15:387/396 of query aligns to 2:376/378 of 4n5fA
- active site: L126 (= L139), T127 (= T140), G243 (≠ A254), E364 (= E375), R376 (= R387)
- binding dihydroflavine-adenine dinucleotide: L126 (= L139), T127 (= T140), G132 (= G145), S133 (= S146), F157 (≠ W170), T159 (= T172), T210 (= T222), Y363 (= Y374), T366 (= T377), E368 (≠ D379), M372 (≠ L383)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
35% identity, 93% coverage: 19:388/396 of query aligns to 8:383/387 of 1ivhA
- active site: M130 (≠ L139), S131 (≠ T140), E249 (≠ A254), A370 (≠ E375), R382 (= R387)
- binding coenzyme a persulfide: S137 (= S146), S185 (≠ I194), R186 (= R195), V239 (≠ L244), Y240 (≠ R245), M243 (≠ F248), E249 (≠ A254), R250 (= R255), G369 (≠ Y374), A370 (≠ E375), G371 (= G376), V375 (≠ I380)
- binding flavin-adenine dinucleotide: L128 (≠ F137), M130 (≠ L139), S131 (≠ T140), G136 (= G145), S137 (= S146), W161 (= W170), T163 (= T172), R275 (= R280), F278 (= F283), F285 (≠ N290), M288 (≠ I293), Q343 (≠ D348), C344 (≠ M349), G347 (= G352), T372 (= T377), E374 (≠ D379)
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)
35% identity, 93% coverage: 19:388/396 of query aligns to 45:420/426 of P26440
- 165:174 (vs. 137:146, 50% identical) binding
- S174 (= S146) binding
- WIT 198:200 (= WIT 170:172) binding
- SR 222:223 (≠ IR 194:195) binding
- G250 (≠ A219) to A: in IVA; uncertain significance
- Y277 (≠ R245) binding
- DLER 284:287 (≠ NSAR 252:255) binding
- E286 (≠ A254) 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 (= A259) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R280) binding
- Q323 (= Q291) binding
- I379 (≠ R347) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ DMLGG 348:352) binding
- R398 (≠ V366) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ V371) to N: in IVA; uncertain significance
- A407 (≠ E375) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ EG 375:376) binding
- TSE 409:411 (≠ THD 377:379) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
35% identity, 93% coverage: 19:388/396 of query aligns to 12:387/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T140), G140 (= G145), S141 (= S146), W165 (= W170), T167 (= T172), R279 (= R280), F282 (= F283), I286 (≠ L287), F289 (≠ N290), Q347 (≠ D348), C348 (≠ M349), G351 (= G352), L369 (≠ V370), G375 (= G376), T376 (= T377), L382 (= L383)
Query Sequence
>BPHYT_RS03780 FitnessBrowser__BFirm:BPHYT_RS03780
MAEAAQFHWEDPLLLDQQLTEDERMVRDAAAAYSQDKLQPRVLEAFRHEKTDIEIFREMG
ELGLLGPTIPEQYGGPGLNYVAYGLIAREVERVDSGYRSMMSVQSSLVMVPIYEFGSEAQ
KQKYLPKLATGEWIGCFGLTEPNHGSDPGSMVTRAKKVDGGYSLSGSKMWITNSPIADVF
VVWAKLEEDGKDAIRGFILEKGWKGLSAPTIHSKVGLRASITGEIVLDEVFVPEENRFPE
VSGLRGPFTCLNSARYGIAWGALGAAESCWHTARQYVLDRKQFGRPLAANQLIQKKLADM
QTEITLGLQGVLRLGRMKDEGTAAVEITSIMKRNSCGKALDIARLARDMLGGNGISDEFG
IARHLVNLEVVNTYEGTHDIHALILGRAQTGIQAFF
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