SitesBLAST
Comparing PfGW456L13_2591 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4) to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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
74% identity, 98% coverage: 6:385/387 of query aligns to 6:377/377 of 4ktoA
- active site: M130 (= M130), S131 (= S131), E239 (= E247), A360 (= A368), R372 (= R380)
- binding flavin-adenine dinucleotide: L128 (= L128), M130 (= M130), S131 (= S131), M155 (≠ T160), W156 (= W161), T158 (= T163), R265 (= R273), F268 (= F276), I272 (= I280), F275 (= F283), M278 (≠ I286), Q333 (= Q341), A334 (≠ I342), G337 (= G345), L355 (= L363), G359 (= G367), T362 (= T370), E364 (= E372)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
65% identity, 96% coverage: 10:380/387 of query aligns to 12:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S131), G140 (= G136), S141 (= S137), W165 (= W161), T167 (= T163), R279 (= R273), F282 (= F276), I286 (= I280), F289 (= F283), Q347 (= Q341), C348 (≠ I342), G351 (= G345), L369 (= L363), G375 (= G369), T376 (= T370), L382 (≠ M376)
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)
65% identity, 96% coverage: 10:380/387 of query aligns to 45:419/426 of P26440
- 165:174 (vs. 128:137, 100% identical) binding
- S174 (= S137) binding
- WIT 198:200 (= WIT 161:163) binding
- SR 222:223 (≠ -H 184) binding
- G250 (= G211) to A: in IVA; uncertain significance
- Y277 (≠ K238) binding
- DLER 284:287 (≠ DYER 245:248) binding
- E286 (= E247) 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 (≠ S252) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R273) binding
- Q323 (= Q284) binding
- I379 (= I340) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QILGG 341:345) binding
- R398 (= R359) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (= Y364) to N: in IVA; uncertain significance
- A407 (= A368) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (= AG 368:369) binding
- TSE 409:411 (= TSE 370:372) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
65% identity, 96% coverage: 10:380/387 of query aligns to 8:382/387 of 1ivhA
- active site: M130 (= M130), S131 (= S131), E249 (= E247), A370 (= A368), R382 (= R380)
- binding coenzyme a persulfide: S137 (= S137), S185 (vs. gap), R186 (≠ H184), V239 (= V237), Y240 (≠ K238), M243 (= M241), E249 (= E247), R250 (= R248), G369 (= G367), A370 (= A368), G371 (= G369), V375 (≠ I373)
- binding flavin-adenine dinucleotide: L128 (= L128), M130 (= M130), S131 (= S131), G136 (= G136), S137 (= S137), W161 (= W161), T163 (= T163), R275 (= R273), F278 (= F276), F285 (= F283), M288 (≠ I286), Q343 (= Q341), C344 (≠ I342), G347 (= G345), T372 (= T370), E374 (= E372)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
44% identity, 95% coverage: 16:383/387 of query aligns to 8:373/374 of 5lnxD
- active site: L122 (≠ M130), T123 (≠ S131), G239 (≠ E247), E358 (≠ A368), K370 (≠ R380)
- binding flavin-adenine dinucleotide: L122 (≠ M130), T123 (≠ S131), G128 (= G136), S129 (= S137), F153 (≠ W161), T155 (= T163), R265 (= R273), Q267 (= Q275), F268 (= F276), I272 (= I280), N275 (≠ F283), I278 (= I286), Q331 (= Q341), I332 (= I342), G335 (= G345), Y357 (≠ G367), T360 (= T370), E362 (= E372)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
41% identity, 98% coverage: 10:387/387 of query aligns to 7:384/384 of 1jqiA
- active site: G377 (≠ R380)
- binding acetoacetyl-coenzyme a: L95 (= L98), F125 (≠ L128), S134 (= S137), F234 (≠ V237), M238 (= M241), Q239 (≠ S242), L241 (= L244), D242 (= D245), R245 (= R248), Y364 (≠ G367), E365 (≠ A368), G366 (= G369)
- binding flavin-adenine dinucleotide: F125 (≠ L128), L127 (≠ M130), S128 (= S131), G133 (= G136), S134 (= S137), W158 (= W161), T160 (= T163), R270 (= R273), F273 (= F276), L280 (≠ F283), Q338 (= Q341), I339 (= I342), G342 (= G345), I360 (≠ L363), T367 (= T370), E369 (= E372), I370 (= I373)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
41% identity, 98% coverage: 10:387/387 of query aligns to 34:411/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
42% identity, 98% coverage: 10:387/387 of query aligns to 34:411/412 of P16219
- G90 (= G66) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E80) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 128:137, 60% identical) binding in other chain
- R171 (≠ D147) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 161:163) binding in other chain
- A192 (= A168) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G185) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R273) binding
- Q308 (= Q284) binding in other chain
- R325 (= R301) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ A329) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (= QILGG 341:345) binding
- R380 (= R356) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (= TSE 370:372) 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
42% identity, 98% coverage: 10:387/387 of query aligns to 10:387/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L128), L130 (≠ M130), S131 (= S131), G136 (= G136), S137 (= S137), W161 (= W161), T163 (= T163), T214 (= T214), R273 (= R273), F276 (= F276), L280 (≠ I280), L283 (≠ F283), V285 (≠ L285), Q341 (= Q341), I342 (= I342), G345 (= G345), I363 (≠ L363), Y367 (≠ G367), T370 (= T370), E372 (= E372), L376 (≠ M376)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
42% identity, 98% coverage: 10:387/387 of query aligns to 7:384/385 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 (≠ N346), T347 (≠ N350), E348 (= E351)
- binding flavin-adenine dinucleotide: F125 (≠ L128), L127 (≠ M130), S128 (= S131), G133 (= G136), S134 (= S137), W158 (= W161), T160 (= T163), R270 (= R273), F273 (= F276), L280 (≠ F283), V282 (≠ L285), Q338 (= Q341), I339 (= I342), G342 (= G345), I360 (≠ L363), Y364 (≠ G367), T367 (= T370), E369 (= E372), I370 (= I373), L373 (≠ M376)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
42% identity, 98% coverage: 10:387/387 of query aligns to 4:381/381 of 8sgsA
- binding coenzyme a: S131 (= S137), A133 (≠ V139), N177 (≠ P183), F231 (≠ V237), M235 (= M241), L238 (= L244), I312 (≠ R318), E362 (≠ A368), G363 (= G369)
- binding flavin-adenine dinucleotide: F122 (≠ L128), L124 (≠ M130), S125 (= S131), G130 (= G136), S131 (= S137), W155 (= W161), T157 (= T163), R267 (= R273), F270 (= F276), L274 (≠ I280), L277 (≠ F283), Q335 (= Q341), I336 (= I342), G338 (= G344), G339 (= G345), I357 (≠ L363), I360 (= I366), Y361 (≠ G367), T364 (= T370), E366 (= E372)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
39% identity, 98% coverage: 6:385/387 of query aligns to 1:380/380 of 4l1fA
- active site: L125 (≠ M130), T126 (≠ S131), G242 (≠ E247), E363 (≠ A368), R375 (= R380)
- binding coenzyme a persulfide: T132 (≠ S137), H179 (= H184), F232 (≠ V237), M236 (= M241), E237 (≠ S242), L239 (= L244), D240 (= D245), R243 (= R248), Y362 (≠ G367), E363 (≠ A368), G364 (= G369), R375 (= R380)
- binding flavin-adenine dinucleotide: F123 (≠ L128), L125 (≠ M130), T126 (≠ S131), G131 (= G136), T132 (≠ S137), F156 (≠ W161), I157 (= I162), T158 (= T163), R268 (= R273), Q270 (= Q275), F271 (= F276), I275 (= I280), F278 (= F283), L281 (≠ I286), Q336 (= Q341), I337 (= I342), G340 (= G345), I358 (≠ L363), Y362 (≠ G367), T365 (= T370), Q367 (≠ E372)
- binding 1,3-propandiol: L5 (= L10), Q10 (≠ D15)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
42% identity, 98% coverage: 10:387/387 of query aligns to 1:371/371 of 2vigB
- active site: L121 (≠ M130), S122 (= S131), G231 (≠ E247), E352 (≠ A368), G364 (≠ R380)
- binding coenzyme a persulfide: S128 (= S137), F221 (≠ V237), M225 (= M241), Q226 (≠ S242), L228 (= L244), D229 (= D245), R232 (= R248), E352 (≠ A368), G353 (= G369), I357 (= I373)
- binding flavin-adenine dinucleotide: L121 (≠ M130), S122 (= S131), G127 (= G136), S128 (= S137), W152 (= W161), T154 (= T163), R257 (= R273), F260 (= F276), L264 (≠ I280), L267 (≠ F283), Q325 (= Q341), I326 (= I342), G329 (= G345), I347 (≠ L363), Y351 (≠ G367), T354 (= T370), E356 (= E372)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
40% identity, 95% coverage: 16:384/387 of query aligns to 10:378/378 of 5ol2F
- active site: L124 (≠ M130), T125 (≠ S131), G241 (≠ E247), G374 (≠ R380)
- binding calcium ion: E29 (≠ Q35), E33 (≠ D39), R35 (≠ L41)
- binding coenzyme a persulfide: L238 (= L244), R242 (= R248), E362 (≠ A368), G363 (= G369)
- binding flavin-adenine dinucleotide: F122 (≠ L128), L124 (≠ M130), T125 (≠ S131), P127 (= P133), T131 (≠ S137), F155 (≠ W161), I156 (= I162), T157 (= T163), E198 (≠ F204), R267 (= R273), F270 (= F276), L274 (≠ I280), F277 (= F283), Q335 (= Q341), L336 (≠ I342), G338 (= G344), G339 (= G345), Y361 (≠ G367), T364 (= T370), E366 (= E372)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
38% identity, 95% coverage: 16:382/387 of query aligns to 12:378/378 of 4n5fA
- active site: L126 (≠ M130), T127 (≠ S131), G243 (≠ E247), E364 (≠ A368), R376 (= R380)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M130), T127 (≠ S131), G132 (= G136), S133 (= S137), F157 (≠ W161), T159 (= T163), T210 (= T214), Y363 (≠ G367), T366 (= T370), E368 (= E372), M372 (= M376)
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
39% identity, 96% coverage: 6:378/387 of query aligns to 1:377/389 of C3UVB0
- A80 (≠ S82) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ A89) binding
- V88 (≠ L90) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ G93) binding
- FGIT 126:129 (≠ LAMS 128:131) binding
- S135 (= S137) binding ; binding
- WIS 159:161 (≠ WIT 161:163) binding
- S181 (≠ P183) binding
- R271 (= R273) binding
- FQMN 281:284 (≠ FQLI 283:286) binding
- R340 (≠ Q341) binding
- A344 (≠ G345) binding
- V366 (≠ G367) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ AGTSE 368:372) binding
Sites not aligning to the query:
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
39% identity, 96% coverage: 6:378/387 of query aligns to 1:377/393 of 3mpjB
- active site: I128 (≠ M130), T129 (≠ S131), T245 (≠ E247), E367 (≠ A368)
- binding flavin-adenine dinucleotide: F126 (≠ L128), I128 (≠ M130), T129 (≠ S131), G134 (= G136), S135 (= S137), W159 (= W161), I160 (= I162), S161 (≠ T163), V366 (≠ G367), S369 (≠ T370), N371 (≠ E372), M375 (= M376)
- binding : H36 (≠ L41), F37 (= F42), Y39 (vs. gap), A164 (≠ P166), Q165 (≠ D167), D167 (≠ N169), N193 (≠ D194)
Sites not aligning to the query:
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
39% identity, 96% coverage: 6:378/387 of query aligns to 1:377/395 of 3mpiC
- active site: I128 (≠ M130), T129 (≠ S131), T245 (≠ E247), E367 (≠ A368)
- binding flavin-adenine dinucleotide: I128 (≠ M130), T129 (≠ S131), G134 (= G136), S135 (= S137), W159 (= W161), I160 (= I162), S161 (≠ T163), M365 (≠ I366), V366 (≠ G367), S369 (≠ T370), N371 (≠ E372), M375 (= M376)
- binding glutaryl-coenzyme A: R87 (≠ A89), F126 (≠ L128), S135 (= S137), V137 (= V139), S181 (≠ P183), F239 (≠ M241), R246 (= R248), N315 (≠ T317), V366 (≠ G367), E367 (≠ A368), G368 (= G369), I376 (≠ L377)
Sites not aligning to the query:
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)
38% identity, 95% coverage: 17:383/387 of query aligns to 4:368/369 of 3pfdC
- active site: L116 (≠ M130), S117 (= S131), T233 (≠ E247), E353 (≠ A368), R365 (= R380)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ L128), L116 (≠ M130), S117 (= S131), G122 (= G136), S123 (= S137), W147 (= W161), I148 (= I162), T149 (= T163), R259 (= R273), F262 (= F276), V266 (≠ I280), N269 (≠ F283), Q326 (= Q341), L327 (≠ I342), G330 (= G345), I348 (≠ L363), Y352 (≠ G367), T355 (= T370), Q357 (≠ E372)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
41% identity, 96% coverage: 13:383/387 of query aligns to 11:378/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S137), L133 (≠ V139), K178 (≠ H184), F231 (≠ V237), M235 (= M241), L238 (= L244), N241 (≠ E247), R242 (= R248), Y362 (≠ G367), T363 (≠ A368), G364 (= G369), R375 (= R380)
- binding flavin-adenine dinucleotide: L122 (= L128), A124 (≠ M130), T125 (≠ S131), G130 (= G136), S131 (= S137), F155 (≠ W161), I156 (= I162), T157 (= T163), K200 (= K206), N208 (≠ T214), L358 (= L363), T365 (= T370), Q367 (≠ E372), I368 (= I373)
Query Sequence
>PfGW456L13_2591 Isovaleryl-CoA dehydrogenase (EC 1.3.8.4)
MSYPSLNFALGETIDMLRDQVQSFVAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITV
PEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHEQKSKYLPKLI
SGEHIGALAMSEPNAGSDVVSMKLRADKRGDKYVLNGSKTWITNGPDANTYVIYAKTDLE
KGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVEVPEENILGVLNGGVKVL
MSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNAS
RAYLYAVAQACERGETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRD
AKLYEIGAGTSEIRRMLIGRELFNETR
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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