SitesBLAST
Comparing Ga0059261_3681 FitnessBrowser__Korea:Ga0059261_3681 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)
52% identity, 99% coverage: 6:380/380 of query aligns to 9:383/383 of 1rx0C
- active site: L128 (= L125), T129 (= T126), G244 (= G241), E366 (= E363), R378 (= R375)
- binding methacrylyl-coenzyme a: I93 (= I90), Y126 (= Y123), S135 (= S132), V238 (≠ M235), L241 (= L238), N242 (≠ D239), R245 (= R242), V316 (≠ T313), E366 (= E363), G367 (= G364), L375 (≠ I372), R378 (= R375)
- binding flavin-adenine dinucleotide: Y126 (= Y123), L128 (= L125), T129 (= T126), G134 (= G131), S135 (= S132), F159 (= F156), I160 (= I157), S161 (= S158), R270 (= R267), F273 (= F270), N280 (≠ F277), L283 (≠ T280), Q339 (= Q336), M340 (≠ L337), G342 (= G339), G343 (= G340), Y344 (= Y341), L365 (= L362), S368 (≠ T365), E370 (≠ Q367)
1rx0A Crystal structure of isobutyryl-coa dehydrogenase complexed with substrate/ligand. (see paper)
52% identity, 99% coverage: 6:380/380 of query aligns to 10:384/384 of 1rx0A
- active site: L129 (= L125), T130 (= T126), G245 (= G241), E367 (= E363), R379 (= R375)
- binding flavin-adenine dinucleotide: Y127 (= Y123), L129 (= L125), T130 (= T126), G135 (= G131), S136 (= S132), F160 (= F156), I161 (= I157), S162 (= S158), W207 (= W203), R271 (= R267), F274 (= F270), L278 (≠ I274), N281 (≠ F277), L284 (≠ T280), Q340 (= Q336), M341 (≠ L337), G343 (= G339), G344 (= G340), Y345 (= Y341), L366 (= L362), S369 (≠ T365), E371 (≠ Q367)
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)
52% identity, 99% coverage: 6:380/380 of query aligns to 41:415/415 of Q9UKU7
- G137 (= G102) to R: in IBDD; loss of protein solubility; complete loss of isobutyryl-CoA dehydrogenase activity; dbSNP:rs371449613
- 158:167 (vs. 123:132, 90% identical) binding in other chain
- S167 (= S132) binding
- FIS 191:193 (= FIS 156:158) binding in other chain
- NGGR 274:277 (≠ DGGR 239:242) binding
- R302 (= R267) 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 277:278) binding
- A320 (= A285) to T: in IBDD; decreased isobutyryl-CoA dehydrogenase activity; less than 20% of wild-type; dbSNP:rs200620279
- QMHGG 371:375 (≠ QLHGG 336:340) binding
- SNE 400:402 (≠ TNQ 365:367) binding in other chain
- R410 (= R375) binding
7w0jE Acyl-coa dehydrogenase, tfu_1647
45% identity, 99% coverage: 4:379/380 of query aligns to 2:382/382 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 (≠ T126), W157 (≠ F156), R270 (= R267), Q272 (= Q269), F273 (= F270), I277 (= I274), F280 (= F277), I283 (≠ T280), Q339 (= Q336), L340 (= L337), G343 (= G340), Y365 (≠ L362), E366 (= E363), T368 (= T365), Q370 (= Q367), I371 (≠ V368)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
45% identity, 99% coverage: 4:379/380 of query aligns to 1:381/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S132), T134 (≠ A134), R180 (vs. gap), R234 (= R232), L237 (≠ M235), R238 (≠ M236), L240 (= L238), D241 (= D239), R244 (= R242), E365 (= E363), G366 (= G364), R377 (= R375)
- binding flavin-adenine dinucleotide: Y123 (= Y123), L125 (= L125), S126 (≠ T126), G131 (= G131), S132 (= S132), W156 (≠ F156), I157 (= I157), T158 (≠ S158), I360 (≠ V358), T367 (= T365), Q369 (= Q367)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
45% identity, 99% coverage: 4:379/380 of query aligns to 1:381/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (= Y123), L125 (= L125), S126 (≠ T126), G131 (= G131), S132 (= S132), W156 (≠ F156), I157 (= I157), T158 (≠ S158), I360 (≠ V358), Y364 (≠ L362), T367 (= T365), Q369 (= Q367)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
43% identity, 99% coverage: 4:379/380 of query aligns to 1:378/378 of 5ol2F
- active site: L124 (= L125), T125 (= T126), G241 (= G241), G374 (≠ R375)
- binding calcium ion: E29 (= E31), E33 (≠ K35), R35 (≠ I37)
- binding coenzyme a persulfide: L238 (= L238), R242 (= R242), E362 (= E363), G363 (= G364)
- binding flavin-adenine dinucleotide: F122 (≠ Y123), L124 (= L125), T125 (= T126), P127 (= P128), T131 (≠ S132), F155 (= F156), I156 (= I157), T157 (≠ S158), E198 (= E198), R267 (= R267), F270 (= F270), L274 (≠ I274), F277 (= F277), Q335 (= Q336), L336 (= L337), G338 (= G339), G339 (= G340), Y361 (≠ L362), T364 (= T365), E366 (≠ Q367)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
44% identity, 99% coverage: 4:379/380 of query aligns to 3:379/380 of 4l1fA
- active site: L125 (= L125), T126 (= T126), G242 (= G241), E363 (= E363), R375 (= R375)
- binding coenzyme a persulfide: T132 (≠ S132), H179 (≠ K178), F232 (= F231), M236 (= M235), E237 (≠ M236), L239 (= L238), D240 (= D239), R243 (= R242), Y362 (≠ L362), E363 (= E363), G364 (= G364), R375 (= R375)
- binding flavin-adenine dinucleotide: F123 (≠ Y123), L125 (= L125), T126 (= T126), G131 (= G131), T132 (≠ S132), F156 (= F156), I157 (= I157), T158 (≠ S158), R268 (= R267), Q270 (= Q269), F271 (= F270), I275 (= I274), F278 (= F277), L281 (≠ T280), Q336 (= Q336), I337 (≠ L337), G340 (= G340), I358 (≠ V358), Y362 (≠ L362), T365 (= T365), Q367 (= Q367)
- binding 1,3-propandiol: L5 (= L6), Q10 (≠ R11)
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)
41% identity, 97% coverage: 12:379/380 of query aligns to 3:369/369 of 3pfdC
- active site: L116 (= L125), S117 (≠ T126), T233 (≠ G241), E353 (= E363), R365 (= R375)
- binding dihydroflavine-adenine dinucleotide: Y114 (= Y123), L116 (= L125), S117 (≠ T126), G122 (= G131), S123 (= S132), W147 (≠ F156), I148 (= I157), T149 (≠ S158), R259 (= R267), F262 (= F270), V266 (≠ I274), N269 (≠ F277), Q326 (= Q336), L327 (= L337), G330 (= G340), I348 (≠ V358), Y352 (≠ L362), T355 (= T365), Q357 (= Q367)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
38% identity, 98% coverage: 4:377/380 of query aligns to 3:376/379 of 1ukwB
- active site: L124 (= L125), S125 (≠ T126), T241 (≠ G241), E362 (= E363), R374 (= R375)
- binding cobalt (ii) ion: D145 (= D146), H146 (= H147)
- binding flavin-adenine dinucleotide: F122 (≠ Y123), L124 (= L125), S125 (≠ T126), G130 (= G131), S131 (= S132), W155 (≠ F156), S157 (= S158), K200 (= K200), L357 (≠ V358), Y361 (≠ L362), E362 (= E363), T364 (= T365), E366 (≠ Q367), L370 (≠ M371)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
38% identity, 98% coverage: 4:377/380 of query aligns to 3:376/379 of 1ukwA
- active site: L124 (= L125), S125 (≠ T126), T241 (≠ G241), E362 (= E363), R374 (= R375)
- binding flavin-adenine dinucleotide: F122 (≠ Y123), L124 (= L125), S125 (≠ T126), G130 (= G131), S131 (= S132), W155 (≠ F156), S157 (= S158), L357 (≠ V358), Y361 (≠ L362), E362 (= E363), T364 (= T365), E366 (≠ Q367), L370 (≠ M371)
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
39% identity, 98% coverage: 4:376/380 of query aligns to 4:379/385 of 3mdeA
- active site: V125 (≠ L125), T126 (= T126), T245 (≠ G241), E366 (= E363), R378 (= R375)
- binding octanoyl-coenzyme a: T86 (≠ A86), E89 (≠ S89), L93 (≠ M93), S132 (= S132), V134 (≠ A134), S181 (≠ P177), F235 (= F231), M239 (= M235), F242 (≠ L238), R314 (≠ D311), Y365 (≠ L362), E366 (= E363), G367 (= G364)
- binding flavin-adenine dinucleotide: Y123 (= Y123), V125 (≠ L125), T126 (= T126), G131 (= G131), S132 (= S132), W156 (≠ F156), I157 (= I157), T158 (≠ S158), R271 (= R267), T273 (≠ Q269), F274 (= F270), L278 (≠ I274), H281 (≠ F277), Q339 (= Q336), V340 (≠ L337), G343 (= G340), I361 (≠ V358), T368 (= T365), Q370 (= Q367)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
39% identity, 98% coverage: 4:376/380 of query aligns to 4:379/385 of 3mddA
- active site: V125 (≠ L125), T126 (= T126), T245 (≠ G241), E366 (= E363), R378 (= R375)
- binding flavin-adenine dinucleotide: Y123 (= Y123), T126 (= T126), G131 (= G131), S132 (= S132), W156 (≠ F156), T158 (≠ S158), R271 (= R267), T273 (≠ Q269), F274 (= F270), H281 (≠ F277), Q339 (= Q336), V340 (≠ L337), G343 (= G340), I361 (≠ V358), T368 (= T365), Q370 (= Q367)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
39% identity, 98% coverage: 4:376/380 of query aligns to 4:379/385 of 1udyA
- active site: V125 (≠ L125), T126 (= T126), T245 (≠ G241), E366 (= E363), R378 (= R375)
- binding 3-thiaoctanoyl-coenzyme a: L93 (≠ M93), Y123 (= Y123), S132 (= S132), S181 (≠ P177), F235 (= F231), M239 (= M235), F242 (≠ L238), V249 (≠ I245), R314 (≠ D311), Y365 (≠ L362), E366 (= E363), G367 (= G364), I371 (≠ V368), I375 (= I372)
- binding flavin-adenine dinucleotide: Y123 (= Y123), T126 (= T126), G131 (= G131), S132 (= S132), W156 (≠ F156), T158 (≠ S158), T273 (≠ Q269), F274 (= F270), Q339 (= Q336), V340 (≠ L337), G343 (= G340), T368 (= T365), Q370 (= Q367)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
39% identity, 98% coverage: 4:376/380 of query aligns to 39:414/421 of P41367
- 158:167 (vs. 123:132, 70% identical) binding in other chain
- S167 (= S132) binding
- WIT 191:193 (≠ FIS 156:158) binding in other chain
- S216 (≠ P177) binding
- D278 (= D239) binding
- R281 (= R242) binding
- RKT 306:308 (≠ RKQ 267:269) binding
- HQ 316:317 (≠ FQ 277:278) binding in other chain
- R349 (≠ D311) binding
- T351 (= T313) binding
- QVFGG 374:378 (≠ QLHGG 336:340) binding
- E401 (= E363) active site, Proton acceptor; binding
- GTAQ 402:405 (≠ GTNQ 364:367) binding in other chain
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
41% identity, 97% coverage: 8:377/380 of query aligns to 4:372/374 of 5lnxD
- active site: L122 (= L125), T123 (= T126), G239 (= G241), E358 (= E363), K370 (≠ R375)
- binding flavin-adenine dinucleotide: L122 (= L125), T123 (= T126), G128 (= G131), S129 (= S132), F153 (= F156), T155 (≠ S158), R265 (= R267), Q267 (= Q269), F268 (= F270), I272 (= I274), N275 (≠ F277), I278 (≠ T280), Q331 (= Q336), I332 (≠ L337), G335 (= G340), Y357 (≠ L362), T360 (= T365), E362 (≠ Q367)
Q9VSA3 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; EC 1.3.8.7 from Drosophila melanogaster (Fruit fly) (see paper)
38% identity, 98% coverage: 4:377/380 of query aligns to 35:411/419 of Q9VSA3
- S347 (≠ T313) 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.
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
38% identity, 98% coverage: 4:376/380 of query aligns to 6:381/388 of 2a1tC
- active site: V127 (≠ L125), T128 (= T126), T247 (≠ G241), E368 (= E363), R380 (= R375)
- binding flavin-adenine dinucleotide: Y125 (= Y123), V127 (≠ L125), T128 (= T126), G133 (= G131), S134 (= S132), Q155 (≠ S153), W158 (≠ F156), W158 (≠ F156), I159 (= I157), T160 (≠ S158), R273 (= R267), T275 (≠ Q269), F276 (= F270), L280 (≠ I274), H283 (≠ F277), I286 (≠ T280), Q341 (= Q336), I342 (≠ L337), G345 (= G340), I363 (≠ V358), T370 (= T365), Q372 (= Q367)
P11310 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; Medium chain acyl-CoA dehydrogenase; MCADH; EC 1.3.8.7 from Homo sapiens (Human) (see 16 papers)
38% identity, 98% coverage: 4:376/380 of query aligns to 39:414/421 of P11310
- Y67 (≠ W32) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (≠ F51) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (≠ I63) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (= L65) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (= I73) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (≠ M97) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 123:132, 70% identical) binding in other chain
- S167 (= S132) binding
- W191 (≠ F156) mutation to A: Loss of electron transfer to ETF.; mutation to F: Reduces rate of electron transfer to ETF about six-fold.
- WIT 191:193 (≠ FIS 156:158) binding in other chain
- T193 (≠ S158) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (= E198) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (= D239) binding
- T280 (≠ G241) mutation to E: Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410.
- R281 (= R242) binding ; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ RKQ 267:269) binding
- HQ 316:317 (≠ FQ 277:278) binding in other chain
- K329 (≠ E290) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ QLHGG 336:340) binding
- E384 (≠ D346) mutation to A: Reduces rate of electron transfer to ETF three-fold.; mutation to Q: Reduces rate of electron transfer to ETF two-fold.
- E401 (= E363) active site, Proton acceptor; binding ; mutation to G: Changed substrate specificity towards longer acyl chains; when associated with E-280.; mutation to Q: Loss of acyl-CoA dehydrogenase activity.; mutation to T: Loss of acyl-CoA dehydrogenase activity; when associated with E-280.
- EGTSQ 401:405 (≠ EGTNQ 363:367) binding in other chain
1egcA Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa (see paper)
37% identity, 98% coverage: 4:376/380 of query aligns to 5:380/387 of 1egcA
- active site: V126 (≠ L125), T127 (= T126), E246 (≠ G241), G367 (≠ E363), R379 (= R375)
- binding octanoyl-coenzyme a: E90 (≠ S89), L94 (≠ M93), Y124 (= Y123), S133 (= S132), V135 (≠ A134), N182 (≠ P177), F236 (= F231), M240 (= M235), F243 (≠ L238), D244 (= D239), R247 (= R242), Y366 (≠ L362), G367 (≠ E363), G368 (= G364)
- binding flavin-adenine dinucleotide: Y124 (= Y123), V126 (≠ L125), T127 (= T126), G132 (= G131), S133 (= S132), W157 (≠ F156), T159 (≠ S158), R272 (= R267), T274 (≠ Q269), F275 (= F270), L279 (≠ I274), H282 (≠ F277), I285 (≠ T280), Q340 (= Q336), I341 (≠ L337), G344 (= G340), I362 (≠ V358), I365 (= I361), Y366 (≠ L362), T369 (= T365), Q371 (= Q367)
Query Sequence
>Ga0059261_3681 FitnessBrowser__Korea:Ga0059261_3681
MEQFDLNEDQRAIQEMARKFTADAITPHAAEWDEKHIFPRETVKAAAELGFGAIYVSEES
GGIGLGRLESALIMEAMAYGCPATSAFISIHNMASWMIDRFGSQAVKDKYLPRLVTADWL
ASYCLTEPSSGSDAAALKTTAKRDGDHFIVNGSKQFISGAGENELYVTMVRTGADGPKGI
SCLAIEKDMPGVSFGANERKLGWHAQPTRQVTFDNVRVPVENLVGGEGEGFRIAMMGLDG
GRLNIGACSLGGAQRCLDEAVQYTKDRKQFGSAIADFQNTQFMLADMATELEAARALLYL
AAAKVTSNAPDKTKFAAMAKRFATDTGSSVVDRALQLHGGYGYLMDYPIERFWRDLRVHS
ILEGTNQVMRMIVGRELTRQ
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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