SitesBLAST
Comparing Ac3H11_2991 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) 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)
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
70% identity, 97% coverage: 9:394/396 of query aligns to 5:377/377 of 4ktoA
- active site: M130 (= M134), S131 (= S135), E239 (= E251), A360 (= A377), R372 (= R389)
- binding flavin-adenine dinucleotide: L128 (= L132), M130 (= M134), S131 (= S135), M155 (= M164), W156 (= W165), T158 (= T167), R265 (= R277), F268 (= F280), I272 (= I284), F275 (= F287), M278 (≠ I290), Q333 (= Q350), A334 (≠ I351), G337 (= G354), L355 (= L372), G359 (= G376), T362 (= T379), E364 (= E381)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
62% identity, 96% coverage: 14:394/396 of query aligns to 8:387/387 of 1ivhA
- active site: M130 (= M134), S131 (= S135), E249 (= E251), A370 (= A377), R382 (= R389)
- binding coenzyme a persulfide: S137 (= S141), S185 (≠ A187), R186 (= R188), V239 (≠ A241), Y240 (≠ K242), M243 (= M245), E249 (= E251), R250 (= R252), G369 (= G376), A370 (= A377), G371 (= G378), V375 (≠ I382)
- binding flavin-adenine dinucleotide: L128 (= L132), M130 (= M134), S131 (= S135), G136 (= G140), S137 (= S141), W161 (= W165), T163 (= T167), R275 (= R277), F278 (= F280), F285 (= F287), M288 (≠ I290), Q343 (= Q350), C344 (≠ I351), G347 (= G354), T372 (= T379), E374 (= E381)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
62% identity, 96% coverage: 14:394/396 of query aligns to 12:391/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S135), G140 (= G140), S141 (= S141), W165 (= W165), T167 (= T167), R279 (= R277), F282 (= F280), I286 (= I284), F289 (= F287), Q347 (= Q350), C348 (≠ I351), G351 (= G354), L369 (= L372), G375 (= G378), T376 (= T379), L382 (≠ M385)
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)
62% identity, 96% coverage: 14:394/396 of query aligns to 45:424/426 of P26440
- 165:174 (vs. 132:141, 90% identical) binding
- S174 (= S141) binding
- WIT 198:200 (= WIT 165:167) binding
- SR 222:223 (≠ AR 187:188) binding
- G250 (= G215) to A: in IVA; uncertain significance
- Y277 (≠ K242) binding
- DLER 284:287 (≠ DYER 249:252) binding
- E286 (= E251) 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 (≠ T256) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R277) binding
- Q323 (= Q288) binding
- I379 (≠ V349) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QIYGG 350:354) binding
- R398 (= R368) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (= Y373) to N: in IVA; uncertain significance
- A407 (= A377) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (= AG 377:378) binding
- TSE 409:411 (= TSE 379:381) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
43% identity, 94% coverage: 21:392/396 of query aligns to 9:373/374 of 5lnxD
- active site: L122 (≠ M134), T123 (≠ S135), G239 (≠ E251), E358 (≠ A377), K370 (≠ R389)
- binding flavin-adenine dinucleotide: L122 (≠ M134), T123 (≠ S135), G128 (= G140), S129 (= S141), F153 (≠ W165), T155 (= T167), R265 (= R277), Q267 (= Q279), F268 (= F280), I272 (= I284), N275 (≠ F287), I278 (= I290), Q331 (= Q350), I332 (= I351), G335 (= G354), Y357 (≠ G376), T360 (= T379), E362 (= E381)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
40% identity, 94% coverage: 21:392/396 of query aligns to 11:377/378 of 5ol2F
- active site: L124 (≠ M134), T125 (≠ S135), G241 (≠ E251), G374 (≠ R389)
- binding calcium ion: E29 (≠ D39), E33 (≠ S43), R35 (≠ Q45)
- binding coenzyme a persulfide: L238 (= L248), R242 (= R252), E362 (≠ A377), G363 (= G378)
- binding flavin-adenine dinucleotide: F122 (≠ L132), L124 (≠ M134), T125 (≠ S135), P127 (= P137), T131 (≠ S141), F155 (≠ W165), I156 (= I166), T157 (= T167), E198 (≠ L208), R267 (= R277), F270 (= F280), L274 (≠ I284), F277 (= F287), Q335 (= Q350), L336 (≠ I351), G338 (= G353), G339 (= G354), Y361 (≠ G376), T364 (= T379), E366 (= E381)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
38% identity, 96% coverage: 11:392/396 of query aligns to 4:380/384 of 1jqiA
- active site: G377 (≠ R389)
- binding acetoacetyl-coenzyme a: L95 (= L102), F125 (≠ L132), S134 (= S141), F234 (≠ A241), M238 (= M245), Q239 (≠ S246), L241 (= L248), D242 (= D249), R245 (= R252), Y364 (≠ G376), E365 (≠ A377), G366 (= G378)
- binding flavin-adenine dinucleotide: F125 (≠ L132), L127 (≠ M134), S128 (= S135), G133 (= G140), S134 (= S141), W158 (= W165), T160 (= T167), R270 (= R277), F273 (= F280), L280 (≠ F287), Q338 (= Q350), I339 (= I351), G342 (= G354), I360 (≠ L372), T367 (= T379), E369 (= E381), I370 (= I382)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
38% identity, 96% coverage: 11:392/396 of query aligns to 31:407/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
39% identity, 96% coverage: 11:392/396 of query aligns to 1:377/381 of 8sgsA
- binding coenzyme a: S131 (= S141), A133 (≠ V143), N177 (≠ A187), F231 (≠ A241), M235 (= M245), L238 (= L248), I312 (≠ R327), E362 (≠ A377), G363 (= G378)
- binding flavin-adenine dinucleotide: F122 (≠ L132), L124 (≠ M134), S125 (= S135), G130 (= G140), S131 (= S141), W155 (= W165), T157 (= T167), R267 (= R277), F270 (= F280), L274 (≠ I284), L277 (≠ F287), Q335 (= Q350), I336 (= I351), G338 (= G353), G339 (= G354), I357 (≠ L372), I360 (= I375), Y361 (≠ G376), T364 (= T379), E366 (= E381)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
39% identity, 96% coverage: 11:392/396 of query aligns to 4:380/385 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 (≠ N355), T347 (≠ N359), E348 (= E360)
- binding flavin-adenine dinucleotide: F125 (≠ L132), L127 (≠ M134), S128 (= S135), G133 (= G140), S134 (= S141), W158 (= W165), T160 (= T167), R270 (= R277), F273 (= F280), L280 (≠ F287), V282 (≠ L289), Q338 (= Q350), I339 (= I351), G342 (= G354), I360 (≠ L372), Y364 (≠ G376), T367 (= T379), E369 (= E381), I370 (= I382), L373 (≠ M385)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
39% identity, 96% coverage: 11:392/396 of query aligns to 31:407/412 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. 132:141, 70% identical) binding in other chain
- R171 (≠ E151) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 165:167) binding in other chain
- A192 (= A172) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G189) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R277) binding
- Q308 (= Q288) binding in other chain
- R325 (= R305) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ A338) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIYGG 350:354) binding
- R380 (= R365) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (= TSE 379:381) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
39% identity, 96% coverage: 11:392/396 of query aligns to 7:383/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L132), L130 (≠ M134), S131 (= S135), G136 (= G140), S137 (= S141), W161 (= W165), T163 (= T167), T214 (= T218), R273 (= R277), F276 (= F280), L280 (≠ I284), L283 (≠ F287), V285 (≠ L289), Q341 (= Q350), I342 (= I351), G345 (= G354), I363 (≠ L372), Y367 (≠ G376), T370 (= T379), E372 (= E381), L376 (≠ M385)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
38% identity, 97% coverage: 10:392/396 of query aligns to 1:378/380 of 4l1fA
- active site: L125 (≠ M134), T126 (≠ S135), G242 (≠ E251), E363 (≠ A377), R375 (= R389)
- binding coenzyme a persulfide: T132 (≠ S141), H179 (≠ R188), F232 (≠ A241), M236 (= M245), E237 (≠ S246), L239 (= L248), D240 (= D249), R243 (= R252), Y362 (≠ G376), E363 (≠ A377), G364 (= G378), R375 (= R389)
- binding flavin-adenine dinucleotide: F123 (≠ L132), L125 (≠ M134), T126 (≠ S135), G131 (= G140), T132 (≠ S141), F156 (≠ W165), I157 (= I166), T158 (= T167), R268 (= R277), Q270 (= Q279), F271 (= F280), I275 (= I284), F278 (= F287), L281 (≠ I290), Q336 (= Q350), I337 (= I351), G340 (= G354), I358 (≠ L372), Y362 (≠ G376), T365 (= T379), Q367 (≠ E381)
- binding 1,3-propandiol: L5 (= L14), Q10 (≠ D19)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
39% identity, 96% coverage: 14:392/396 of query aligns to 1:367/371 of 2vigB
- active site: L121 (≠ M134), S122 (= S135), G231 (≠ E251), E352 (≠ A377), G364 (≠ R389)
- binding coenzyme a persulfide: S128 (= S141), F221 (≠ A241), M225 (= M245), Q226 (≠ S246), L228 (= L248), D229 (= D249), R232 (= R252), E352 (≠ A377), G353 (= G378), I357 (= I382)
- binding flavin-adenine dinucleotide: L121 (≠ M134), S122 (= S135), G127 (= G140), S128 (= S141), W152 (= W165), T154 (= T167), R257 (= R277), F260 (= F280), L264 (≠ I284), L267 (≠ F287), Q325 (= Q350), I326 (= I351), G329 (= G354), I347 (≠ L372), Y351 (≠ G376), T354 (= T379), E356 (= E381)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
36% identity, 97% coverage: 10:393/396 of query aligns to 1:378/379 of 1ukwB
- active site: L124 (≠ M134), S125 (= S135), T241 (≠ E251), E362 (≠ A377), R374 (= R389)
- binding cobalt (ii) ion: D145 (≠ G155), H146 (≠ Y156)
- binding flavin-adenine dinucleotide: F122 (≠ L132), L124 (≠ M134), S125 (= S135), G130 (= G140), S131 (= S141), W155 (= W165), S157 (≠ T167), K200 (= K210), L357 (= L372), Y361 (≠ G376), E362 (≠ A377), T364 (= T379), E366 (= E381), L370 (≠ M385)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
36% identity, 97% coverage: 10:393/396 of query aligns to 1:378/379 of 1ukwA
- active site: L124 (≠ M134), S125 (= S135), T241 (≠ E251), E362 (≠ A377), R374 (= R389)
- binding flavin-adenine dinucleotide: F122 (≠ L132), L124 (≠ M134), S125 (= S135), G130 (= G140), S131 (= S141), W155 (= W165), S157 (≠ T167), L357 (= L372), Y361 (≠ G376), E362 (≠ A377), T364 (= T379), E366 (= E381), L370 (≠ M385)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
35% identity, 93% coverage: 21:387/396 of query aligns to 10:372/379 of 6fahD
- active site: L124 (≠ M134), T125 (≠ S135), G241 (≠ E251)
- binding flavin-adenine dinucleotide: F122 (≠ L132), L124 (≠ M134), T125 (≠ S135), R152 (≠ S162), F155 (≠ W165), T157 (= T167), E198 (≠ L208), R267 (= R277), Q269 (= Q279), F270 (= F280), I274 (= I284), F277 (= F287), Q335 (= Q350), I336 (= I351), G339 (= G354), Y361 (≠ G376), T364 (= T379), Q366 (≠ E381)
Sites not aligning to the query:
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
35% identity, 95% coverage: 16:391/396 of query aligns to 8:378/378 of 4n5fA
- active site: L126 (≠ M134), T127 (≠ S135), G243 (≠ E251), E364 (≠ A377), R376 (= R389)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M134), T127 (≠ S135), G132 (= G140), S133 (= S141), F157 (≠ W165), T159 (= T167), T210 (= T218), Y363 (≠ G376), T366 (= T379), E368 (= E381), M372 (= M385)
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
38% identity, 95% coverage: 10:387/396 of query aligns to 1:377/389 of C3UVB0
- A80 (≠ S86) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ G93) binding
- V88 (≠ L94) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ G97) binding
- FGIT 126:129 (≠ LAMS 132:135) binding
- S135 (= S141) binding ; binding
- WIS 159:161 (≠ WIT 165:167) binding
- S181 (≠ A187) binding
- R271 (= R277) binding
- FQMN 281:284 (≠ FQLI 287:290) binding
- R340 (≠ Q350) binding
- A344 (≠ G354) binding
- V366 (≠ G376) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ AGTSE 377:381) binding
Sites not aligning to the query:
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
38% identity, 95% coverage: 10:387/396 of query aligns to 1:377/393 of 3mpjB
- active site: I128 (≠ M134), T129 (≠ S135), T245 (≠ E251), E367 (≠ A377)
- binding flavin-adenine dinucleotide: F126 (≠ L132), I128 (≠ M134), T129 (≠ S135), G134 (= G140), S135 (= S141), W159 (= W165), I160 (= I166), S161 (≠ T167), V366 (≠ G376), S369 (≠ T379), N371 (≠ E381), M375 (= M385)
- binding : H36 (≠ Q45), F37 (= F46), Y39 (≠ M48), A164 (≠ P170), Q165 (≠ D171), D167 (= D173), N193 (≠ G198)
Sites not aligning to the query:
Query Sequence
>Ac3H11_2991 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4)
MSIPANLPGLNFQLGEDIDALRDAVRDFAQAEIAPRAADIDKSDQFPMDLWRKMGDLGVL
GITVPEQYGGAAMGYLAHMVAMEEISRASASVGLSYGAHSNLCVNQINRNGNEAQKAKYL
SKLISGEHVGALAMSEPGAGSDVISMKLKAEDKGGYYLLNGSKMWITNGPDADTLVVYAK
TEPELGARGVTAFLIEKGMKGFSIAQKLDKLGMRGSHTGELVFQDVEVPAENVLGGLNQG
AKVLMSGLDYERAVLTGGPLGIMQSVMDNVIPYIHDRKQFGQSIGEFQLIQGKVADMYTV
LQAGRSFAYTVAKNLDMLGTDHVRQVRKDCASVILWCAEKATWMAGEGVQIYGGNGYINE
YPLGRLWRDAKLYEIGAGTSEIRRMLIGRELFAETC
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