SitesBLAST
Comparing 3608348 Dshi_1750 acyl-CoA dehydrogenase domain protein (RefSeq) 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)
1rx0C Crystal structure of isobutyryl-coa dehydrogenase complexed with substrate/ligand. (see paper)
53% identity, 98% coverage: 5:377/381 of query aligns to 9:381/383 of 1rx0C
- active site: L128 (= L124), T129 (= T125), G244 (= G240), E366 (= E362), R378 (= R374)
- binding methacrylyl-coenzyme a: I93 (= I89), Y126 (= Y122), S135 (= S131), V238 (≠ M234), L241 (= L237), N242 (≠ D238), R245 (= R241), V316 (≠ T312), E366 (= E362), G367 (= G363), L375 (= L371), R378 (= R374)
- binding flavin-adenine dinucleotide: Y126 (= Y122), L128 (= L124), T129 (= T125), G134 (= G130), S135 (= S131), F159 (= F155), I160 (= I156), S161 (= S157), R270 (= R266), F273 (= F269), N280 (≠ F276), L283 (= L279), Q339 (= Q335), M340 (≠ L336), G342 (= G338), G343 (= G339), Y344 (= Y340), L365 (= L361), S368 (≠ T364), E370 (= E366)
1rx0A Crystal structure of isobutyryl-coa dehydrogenase complexed with substrate/ligand. (see paper)
53% identity, 98% coverage: 5:377/381 of query aligns to 10:382/384 of 1rx0A
- active site: L129 (= L124), T130 (= T125), G245 (= G240), E367 (= E362), R379 (= R374)
- binding flavin-adenine dinucleotide: Y127 (= Y122), L129 (= L124), T130 (= T125), G135 (= G130), S136 (= S131), F160 (= F155), I161 (= I156), S162 (= S157), W207 (= W202), R271 (= R266), F274 (= F269), L278 (≠ I273), N281 (≠ F276), L284 (= L279), Q340 (= Q335), M341 (≠ L336), G343 (= G338), G344 (= G339), Y345 (= Y340), L366 (= L361), S369 (≠ T364), E371 (= E366)
Q9UKU7 Isobutyryl-CoA dehydrogenase, mitochondrial; IBDH; Activator-recruited cofactor 42 kDa component; ARC42; Acyl-CoA dehydrogenase family member 8; ACAD-8; EC 1.3.8.5 from Homo sapiens (Human) (see 3 papers)
53% identity, 98% coverage: 5:377/381 of query aligns to 41:413/415 of Q9UKU7
- G137 (= G101) to R: in IBDD; loss of protein solubility; complete loss of isobutyryl-CoA dehydrogenase activity; dbSNP:rs371449613
- 158:167 (vs. 122:131, 100% identical) binding in other chain
- S167 (= S131) binding
- FIS 191:193 (= FIS 155:157) binding in other chain
- NGGR 274:277 (≠ DGGR 238:241) binding
- R302 (= R266) binding ; to Q: in IBDD; no effect on localization to the mitochondrion; complete loss of isobutyryl-CoA dehydrogenase activity; loss of protein expression in patient cells; dbSNP:rs121908422
- NQ 312:313 (≠ FQ 276:277) binding
- A320 (= A284) to T: in IBDD; decreased isobutyryl-CoA dehydrogenase activity; less than 20% of wild-type; dbSNP:rs200620279
- QMHGG 371:375 (≠ QLHGG 335:339) binding
- SNE 400:402 (≠ TNE 364:366) binding in other chain
- R410 (= R374) binding
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
42% identity, 99% coverage: 1:379/381 of query aligns to 1:379/379 of 1ukwB
- active site: L124 (= L124), S125 (≠ T125), T241 (≠ G240), E362 (= E362), R374 (= R374)
- binding cobalt (ii) ion: D145 (≠ E145), H146 (≠ G146)
- binding flavin-adenine dinucleotide: F122 (≠ Y122), L124 (= L124), S125 (≠ T125), G130 (= G130), S131 (= S131), W155 (≠ F155), S157 (= S157), K200 (= K199), L357 (≠ V357), Y361 (≠ L361), E362 (= E362), T364 (= T364), E366 (= E366), L370 (= L370)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
42% identity, 99% coverage: 1:379/381 of query aligns to 1:379/379 of 1ukwA
- active site: L124 (= L124), S125 (≠ T125), T241 (≠ G240), E362 (= E362), R374 (= R374)
- binding flavin-adenine dinucleotide: F122 (≠ Y122), L124 (= L124), S125 (≠ T125), G130 (= G130), S131 (= S131), W155 (≠ F155), S157 (= S157), L357 (≠ V357), Y361 (≠ L361), E362 (= E362), T364 (= T364), E366 (= E366), L370 (= L370)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
41% identity, 99% coverage: 1:377/381 of query aligns to 1:378/380 of 4l1fA
- active site: L125 (= L124), T126 (= T125), G242 (= G240), E363 (= E362), R375 (= R374)
- binding coenzyme a persulfide: T132 (≠ S131), H179 (≠ R177), F232 (= F230), M236 (= M234), E237 (≠ M235), L239 (= L237), D240 (= D238), R243 (= R241), Y362 (≠ L361), E363 (= E362), G364 (= G363), R375 (= R374)
- binding flavin-adenine dinucleotide: F123 (≠ Y122), L125 (= L124), T126 (= T125), G131 (= G130), T132 (≠ S131), F156 (= F155), I157 (= I156), T158 (≠ S157), R268 (= R266), Q270 (≠ A268), F271 (= F269), I275 (= I273), F278 (= F276), L281 (= L279), Q336 (= Q335), I337 (≠ L336), G340 (= G339), I358 (≠ V357), Y362 (≠ L361), T365 (= T364), Q367 (≠ E366)
- binding 1,3-propandiol: L5 (= L5), Q10 (≠ S10)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
39% identity, 98% coverage: 6:377/381 of query aligns to 5:377/378 of 5ol2F
- active site: L124 (= L124), T125 (= T125), G241 (= G240), G374 (≠ R374)
- binding calcium ion: E29 (≠ A30), E33 (≠ D34), R35 (≠ T36)
- binding coenzyme a persulfide: L238 (= L237), R242 (= R241), E362 (= E362), G363 (= G363)
- binding flavin-adenine dinucleotide: F122 (≠ Y122), L124 (= L124), T125 (= T125), P127 (= P127), T131 (≠ S131), F155 (= F155), I156 (= I156), T157 (≠ S157), E198 (= E197), R267 (= R266), F270 (= F269), L274 (≠ I273), F277 (= F276), Q335 (= Q335), L336 (= L336), G338 (= G338), G339 (= G339), Y361 (≠ L361), T364 (= T364), E366 (= E366)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
41% identity, 99% coverage: 1:377/381 of query aligns to 1:382/383 of 1bucA
- active site: L128 (= L124), T129 (= T125), G246 (= G240), E367 (= E362), G379 (≠ R374)
- binding acetoacetyl-coenzyme a: L96 (≠ M92), F126 (≠ Y122), G134 (= G130), T135 (≠ S131), T162 (≠ S157), N182 (≠ P176), H183 (≠ R177), F236 (= F230), M240 (= M234), M241 (= M235), L243 (= L237), D244 (= D238), T317 (= T312), Y366 (≠ L361), E367 (= E362), G368 (= G363)
- binding flavin-adenine dinucleotide: F126 (≠ Y122), L128 (= L124), T129 (= T125), G134 (= G130), T135 (≠ S131), F160 (= F155), T162 (≠ S157), Y366 (≠ L361), T369 (= T364), E371 (= E366), M375 (≠ L370)
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
41% identity, 99% coverage: 1:377/381 of query aligns to 1:382/383 of Q06319
- E367 (= E362) active site, Proton acceptor; mutation to Q: Loss of activity.
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
40% identity, 99% coverage: 1:376/381 of query aligns to 2:378/378 of 4n5fA
- active site: L126 (= L124), T127 (= T125), G243 (= G240), E364 (= E362), R376 (= R374)
- binding dihydroflavine-adenine dinucleotide: L126 (= L124), T127 (= T125), G132 (= G130), S133 (= S131), F157 (= F155), T159 (≠ S157), T210 (= T207), Y363 (≠ L361), T366 (= T364), E368 (= E366), M372 (≠ L370)
7w0jE Acyl-coa dehydrogenase, tfu_1647
39% identity, 99% coverage: 2:377/381 of query aligns to 1:381/382 of 7w0jE
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-azanyl-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate: S127 (≠ T125), W157 (≠ F155), R270 (= R266), Q272 (≠ A268), F273 (= F269), I277 (= I273), F280 (= F276), I283 (≠ L279), Q339 (= Q335), L340 (= L336), G343 (= G339), Y365 (≠ L361), E366 (= E362), T368 (= T364), Q370 (≠ E366), I371 (= I367)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
39% identity, 98% coverage: 6:377/381 of query aligns to 7:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S131), T134 (≠ A133), R180 (vs. gap), R234 (= R231), L237 (≠ M234), R238 (≠ M235), L240 (= L237), D241 (= D238), R244 (= R241), E365 (= E362), G366 (= G363), R377 (= R374)
- binding flavin-adenine dinucleotide: Y123 (= Y122), L125 (= L124), S126 (≠ T125), G131 (= G130), S132 (= S131), W156 (≠ F155), I157 (= I156), T158 (≠ S157), I360 (≠ V357), T367 (= T364), Q369 (≠ E366)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
39% identity, 98% coverage: 6:377/381 of query aligns to 7:380/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (= Y122), L125 (= L124), S126 (≠ T125), G131 (= G130), S132 (= S131), W156 (≠ F155), I157 (= I156), T158 (≠ S157), I360 (≠ V357), Y364 (≠ L361), T367 (= T364), Q369 (≠ E366)
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
41% identity, 98% coverage: 5:376/381 of query aligns to 1:368/370 of 2dvlA
- active site: L121 (= L124), T122 (= T125), G233 (= G240), E354 (= E362), R366 (= R374)
- binding flavin-adenine dinucleotide: L121 (= L124), T122 (= T125), G127 (= G130), S128 (= S131), W152 (≠ F155), I153 (= I156), T154 (≠ S157), T356 (= T364), E358 (= E366)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
39% identity, 97% coverage: 7:377/381 of query aligns to 4:373/374 of 5lnxD
- active site: L122 (= L124), T123 (= T125), G239 (= G240), E358 (= E362), K370 (≠ R374)
- binding flavin-adenine dinucleotide: L122 (= L124), T123 (= T125), G128 (= G130), S129 (= S131), F153 (= F155), T155 (≠ S157), R265 (= R266), Q267 (≠ A268), F268 (= F269), I272 (= I273), N275 (≠ F276), I278 (≠ L279), Q331 (= Q335), I332 (≠ L336), G335 (= G339), Y357 (≠ L361), T360 (= T364), E362 (= E366)
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
39% identity, 98% coverage: 2:376/381 of query aligns to 1:376/376 of 4m9aB
- active site: L124 (= L124), T125 (= T125), G241 (= G240), E362 (= E362), R374 (= R374)
- binding dihydroflavine-adenine dinucleotide: F122 (≠ Y122), T125 (= T125), G130 (= G130), S131 (= S131), F155 (= F155), T157 (≠ S157), T208 (= T207), Y361 (≠ L361), T364 (= T364), E366 (= E366), M370 (≠ L370)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
37% identity, 99% coverage: 5:381/381 of query aligns to 34:411/412 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)
37% identity, 99% coverage: 5:381/381 of query aligns to 7:384/384 of 1jqiA
- active site: G377 (≠ R374)
- binding acetoacetyl-coenzyme a: L95 (≠ M92), F125 (≠ Y122), S134 (= S131), F234 (= F230), M238 (= M234), Q239 (≠ M235), L241 (= L237), D242 (= D238), R245 (= R241), Y364 (≠ L361), E365 (= E362), G366 (= G363)
- binding flavin-adenine dinucleotide: F125 (≠ Y122), L127 (= L124), S128 (≠ T125), G133 (= G130), S134 (= S131), W158 (≠ F155), T160 (≠ S157), R270 (= R266), F273 (= F269), L280 (≠ F276), Q338 (= Q335), I339 (≠ L336), G342 (= G339), I360 (≠ V357), T367 (= T364), E369 (= E366), I370 (= I367)
Q9VSA3 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; EC 1.3.8.7 from Drosophila melanogaster (Fruit fly) (see paper)
35% identity, 99% coverage: 3:381/381 of query aligns to 35:416/419 of Q9VSA3
- S347 (≠ T312) modified: Phosphoserine; by Pink1; mutation to A: Prevents phosphorylation by Pink1. Does not rescue climbing and flight defects in Pink1 mutants.; mutation to D: Phosphomimetic mutant that fully rescues climbing defects and significantly improves flight defects, and thorax and wing posture phenotypes in Pink1 mutants. No effect on acyl-CoA dehydrogenase activity.; mutation to DD: Phosphomimetic mutant that fully rescues climbing defects and significantly improves flight defects, and thorax and wing posture phenotypes in Pink1 mutants. No effect on acyl-CoA dehydrogenase activity.
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)
37% identity, 98% coverage: 5:376/381 of query aligns to 57:428/432 of P45954
- V137 (≠ A85) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (= F86) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 122:131, 60% identical) binding in other chain
- S183 (= S131) binding
- WIS 207:209 (≠ FIS 155:157) binding in other chain
- S210 (≠ G158) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ P176) binding
- L255 (≠ W202) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ F230) binding
- NEGR 291:294 (≠ DGGR 238:241) binding
- I316 (≠ M263) to V: in dbSNP:rs1131430
- R319 (= R266) binding
- Q330 (= Q277) binding
- EWMGG 387:391 (≠ QLHGG 335:339) binding
- A416 (≠ T364) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TNE 364:366) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
Query Sequence
>3608348 Dshi_1750 acyl-CoA dehydrogenase domain protein (RefSeq)
MDFALSEEQSAIFDMARDFGAENIAPHALAWEKDGTIPKTLWPELAALGFGGLYVTEESG
GSGLSRLDATLVFEALSMACPSVAAFLSIHNMCAAMLDKFGSDDVKARFLPPALTMETVF
SYCLTEPGSGSDAAALKTRAERTNEGYRLTGTKAFISGGGYSDAYIVMARTGEDGPRGIS
SLIVEDGAPGLSFGGLEDKMGWRAQPTRQVQLDDCAVPAANLLGEEGAGFRYAMMGLDGG
RLNIAACSLGAAQAALDATVAYMGERRAFGKPIDQFQALQFRLADAEIELQAARVFLRQA
AWKLDQGAPDATTHCAMAKKFVTEAGSRVADQCLQLHGGYGYLADYGIEKLVRDLRVHQI
LEGTNEIMRLLTARALLAARR
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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