SitesBLAST
Comparing H281DRAFT_01204 FitnessBrowser__Burk376:H281DRAFT_01204 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)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
78% identity, 100% coverage: 1:377/377 of query aligns to 2:378/378 of 4n5fA
- active site: L126 (= L125), T127 (= T126), G243 (= G242), E364 (= E363), R376 (= R375)
- binding dihydroflavine-adenine dinucleotide: L126 (= L125), T127 (= T126), G132 (= G131), S133 (= S132), F157 (= F156), T159 (= T158), T210 (= T209), Y363 (= Y362), T366 (= T365), E368 (= E367), M372 (= M371)
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
79% identity, 100% coverage: 2:377/377 of query aligns to 1:376/376 of 4m9aB
- active site: L124 (= L125), T125 (= T126), G241 (= G242), E362 (= E363), R374 (= R375)
- binding dihydroflavine-adenine dinucleotide: F122 (= F123), T125 (= T126), G130 (= G131), S131 (= S132), F155 (= F156), T157 (= T158), T208 (= T209), Y361 (= Y362), T364 (= T365), E366 (= E367), M370 (= M371)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
51% identity, 99% coverage: 4:377/377 of query aligns to 1:372/374 of 5lnxD
- active site: L122 (= L125), T123 (= T126), G239 (= G242), E358 (= E363), K370 (≠ R375)
- binding flavin-adenine dinucleotide: L122 (= L125), T123 (= T126), G128 (= G131), S129 (= S132), F153 (= F156), T155 (= T158), R265 (= R268), Q267 (= Q270), F268 (= F271), I272 (≠ L275), N275 (≠ H278), I278 (= I281), Q331 (= Q336), I332 (= I337), G335 (= G340), Y357 (= Y362), T360 (= T365), E362 (= E367)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
50% identity, 98% coverage: 7:377/377 of query aligns to 9:379/384 of 1jqiA
- active site: G377 (≠ R375)
- binding acetoacetyl-coenzyme a: L95 (≠ V93), F125 (= F123), S134 (= S132), F234 (≠ L232), M238 (≠ L236), Q239 (≠ S237), L241 (= L239), D242 (≠ E240), R245 (= R243), Y364 (= Y362), E365 (= E363), G366 (= G364)
- binding flavin-adenine dinucleotide: F125 (= F123), L127 (= L125), S128 (≠ T126), G133 (= G131), S134 (= S132), W158 (≠ F156), T160 (= T158), R270 (= R268), F273 (= F271), L280 (≠ H278), Q338 (= Q336), I339 (= I337), G342 (= G340), I360 (= I358), T367 (= T365), E369 (= E367), I370 (≠ V368)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
50% identity, 98% coverage: 7:377/377 of query aligns to 36:406/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
47% identity, 98% coverage: 6:374/377 of query aligns to 5:373/378 of 5ol2F
- active site: L124 (= L125), T125 (= T126), G241 (= G242)
- binding calcium ion: E29 (≠ Q30), E33 (≠ D34), R35 (≠ Q36)
- binding coenzyme a persulfide: L238 (= L239), R242 (= R243), E362 (= E363), G363 (= G364)
- binding flavin-adenine dinucleotide: F122 (= F123), L124 (= L125), T125 (= T126), P127 (= P128), T131 (≠ S132), F155 (= F156), I156 (≠ V157), T157 (= T158), E198 (= E199), R267 (= R268), F270 (= F271), L274 (= L275), F277 (≠ H278), Q335 (= Q336), L336 (≠ I337), G338 (= G339), G339 (= G340), Y361 (= Y362), T364 (= T365), E366 (= E367)
Sites not aligning to the query:
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
50% identity, 98% coverage: 7:377/377 of query aligns to 12:382/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (= F123), L130 (= L125), S131 (≠ T126), G136 (= G131), S137 (= S132), W161 (≠ F156), T163 (= T158), T214 (= T209), R273 (= R268), F276 (= F271), L280 (= L275), L283 (≠ H278), V285 (≠ T280), Q341 (= Q336), I342 (= I337), G345 (= G340), I363 (= I358), Y367 (= Y362), T370 (= T365), E372 (= E367), L376 (≠ M371)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
50% identity, 98% coverage: 7:377/377 of query aligns to 9:379/385 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 (≠ Y341), T347 (≠ E345), E348 (≠ D346)
- binding flavin-adenine dinucleotide: F125 (= F123), L127 (= L125), S128 (≠ T126), G133 (= G131), S134 (= S132), W158 (≠ F156), T160 (= T158), R270 (= R268), F273 (= F271), L280 (≠ H278), V282 (≠ T280), Q338 (= Q336), I339 (= I337), G342 (= G340), I360 (= I358), Y364 (= Y362), T367 (= T365), E369 (= E367), I370 (≠ V368), L373 (≠ M371)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
50% identity, 98% coverage: 7:377/377 of query aligns to 6:376/381 of 8sgsA
- binding coenzyme a: S131 (= S132), A133 (= A134), N177 (≠ K178), F231 (≠ L232), M235 (≠ L236), L238 (= L239), I312 (≠ L313), E362 (= E363), G363 (= G364)
- binding flavin-adenine dinucleotide: F122 (= F123), L124 (= L125), S125 (≠ T126), G130 (= G131), S131 (= S132), W155 (≠ F156), T157 (= T158), R267 (= R268), F270 (= F271), L274 (= L275), L277 (≠ H278), Q335 (= Q336), I336 (= I337), G338 (= G339), G339 (= G340), I357 (= I358), I360 (= I361), Y361 (= Y362), T364 (= T365), E366 (= E367)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
50% identity, 98% coverage: 7:377/377 of query aligns to 36:406/412 of P16219
- G90 (= G61) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E75) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 123:132, 60% identical) binding in other chain
- R171 (≠ V142) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ FVT 156:158) binding in other chain
- A192 (= A163) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G180) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R268) binding
- Q308 (= Q279) binding in other chain
- R325 (= R296) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S324) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIHGG 336:340) binding
- R380 (= R351) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (= TSE 365:367) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
47% identity, 99% coverage: 1:375/377 of query aligns to 1:375/380 of 4l1fA
- active site: L125 (= L125), T126 (= T126), G242 (= G242), E363 (= E363), R375 (= R375)
- binding coenzyme a persulfide: T132 (≠ S132), H179 (≠ R179), F232 (≠ L232), M236 (≠ L236), E237 (≠ S237), L239 (= L239), D240 (≠ E240), R243 (= R243), Y362 (= Y362), E363 (= E363), G364 (= G364), R375 (= R375)
- binding flavin-adenine dinucleotide: F123 (= F123), L125 (= L125), T126 (= T126), G131 (= G131), T132 (≠ S132), F156 (= F156), I157 (≠ V157), T158 (= T158), R268 (= R268), Q270 (= Q270), F271 (= F271), I275 (≠ L275), F278 (≠ H278), L281 (≠ I281), Q336 (= Q336), I337 (= I337), G340 (= G340), I358 (= I358), Y362 (= Y362), T365 (= T365), Q367 (≠ E367)
- binding 1,3-propandiol: L5 (≠ Y5), Q10 (≠ R10)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
49% identity, 98% coverage: 7:377/377 of query aligns to 3:366/371 of 2vigB
- active site: L121 (= L125), S122 (≠ T126), G231 (= G242), E352 (= E363), G364 (≠ R375)
- binding coenzyme a persulfide: S128 (= S132), F221 (≠ L232), M225 (≠ L236), Q226 (≠ S237), L228 (= L239), D229 (≠ E240), R232 (= R243), E352 (= E363), G353 (= G364), I357 (≠ V368)
- binding flavin-adenine dinucleotide: L121 (= L125), S122 (≠ T126), G127 (= G131), S128 (= S132), W152 (≠ F156), T154 (= T158), R257 (= R268), F260 (= F271), L264 (= L275), L267 (≠ H278), Q325 (= Q336), I326 (= I337), G329 (= G340), I347 (= I358), Y351 (= Y362), T354 (= T365), E356 (= E367)
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
52% identity, 99% coverage: 6:377/377 of query aligns to 2:368/370 of 2dvlA
- active site: L121 (= L125), T122 (= T126), G233 (= G242), E354 (= E363), R366 (= R375)
- binding flavin-adenine dinucleotide: L121 (= L125), T122 (= T126), G127 (= G131), S128 (= S132), W152 (≠ F156), I153 (≠ V157), T154 (= T158), T356 (= T365), E358 (= E367)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
44% identity, 98% coverage: 4:374/377 of query aligns to 2:373/379 of 6fahD
- active site: L124 (= L125), T125 (= T126), G241 (= G242)
- binding flavin-adenine dinucleotide: F122 (= F123), L124 (= L125), T125 (= T126), R152 (≠ S153), F155 (= F156), T157 (= T158), E198 (= E199), R267 (= R268), Q269 (= Q270), F270 (= F271), I274 (≠ L275), F277 (≠ H278), Q335 (= Q336), I336 (= I337), G339 (= G340), Y361 (= Y362), T364 (= T365), Q366 (≠ E367)
Sites not aligning to the query:
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
41% identity, 99% coverage: 5:377/377 of query aligns to 6:377/381 of 2jifA
- active site: L125 (= L125), S126 (≠ T126), G242 (= G242), E363 (= E363), K375 (≠ R375)
- binding coenzyme a persulfide: S132 (= S132), S134 (≠ A134), Y178 (≠ K178), Y232 (≠ L232), I236 (≠ L236), L239 (= L239), N240 (≠ E240), R243 (= R243), Y362 (= Y362), E363 (= E363), G364 (= G364), I368 (≠ V368)
- binding flavin-adenine dinucleotide: F123 (= F123), L125 (= L125), S126 (≠ T126), G131 (= G131), S132 (= S132), W156 (≠ F156), I157 (≠ V157), S158 (≠ T158), K201 (= K201), T209 (= T209), R268 (= R268), F271 (= F271), L275 (= L275), F278 (≠ H278), L281 (≠ I281), E336 (≠ Q336), W337 (≠ I337), G340 (= G340), N367 (≠ E367), I368 (≠ V368)
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)
41% identity, 99% coverage: 5:377/377 of query aligns to 57:428/432 of P45954
- V137 (≠ T85) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ L86) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 123:132, 70% identical) binding in other chain
- S183 (= S132) binding
- WIS 207:209 (≠ FVT 156:158) binding in other chain
- S210 (≠ N159) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ K178) binding
- L255 (≠ I204) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ L232) binding
- NEGR 291:294 (≠ EGGR 240:243) binding
- I316 (≠ A265) to V: in dbSNP:rs1131430
- R319 (= R268) binding
- Q330 (= Q279) binding
- EWMGG 387:391 (≠ QIHGG 336:340) binding
- A416 (≠ T365) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TSE 365:367) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
46% identity, 99% coverage: 1:372/377 of query aligns to 1:376/383 of 1bucA
- active site: L128 (= L125), T129 (= T126), G246 (= G242), E367 (= E363)
- binding acetoacetyl-coenzyme a: L96 (≠ V93), F126 (= F123), G134 (= G131), T135 (≠ S132), T162 (= T158), N182 (≠ K178), H183 (≠ R179), F236 (≠ L232), M240 (≠ L236), M241 (≠ S237), L243 (= L239), D244 (≠ E240), T317 (≠ L313), Y366 (= Y362), E367 (= E363), G368 (= G364)
- binding flavin-adenine dinucleotide: F126 (= F123), L128 (= L125), T129 (= T126), G134 (= G131), T135 (≠ S132), F160 (= F156), T162 (= T158), Y366 (= Y362), T369 (= T365), E371 (= E367), M375 (= M371)
Sites not aligning to the query:
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
46% identity, 99% coverage: 1:372/377 of query aligns to 1:376/383 of Q06319
- E367 (= E363) active site, Proton acceptor; mutation to Q: Loss of activity.
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)
44% identity, 97% coverage: 12:375/377 of query aligns to 4:365/369 of 3pfdC
- active site: L116 (= L125), S117 (≠ T126), T233 (≠ G242), E353 (= E363), R365 (= R375)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ F123), L116 (= L125), S117 (≠ T126), G122 (= G131), S123 (= S132), W147 (≠ F156), I148 (≠ V157), T149 (= T158), R259 (= R268), F262 (= F271), V266 (≠ L275), N269 (≠ H278), Q326 (= Q336), L327 (≠ I337), G330 (= G340), I348 (= I358), Y352 (= Y362), T355 (= T365), Q357 (≠ E367)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
45% identity, 99% coverage: 6:377/377 of query aligns to 7:379/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S132), T134 (≠ A134), R180 (= R179), R234 (= R233), L237 (= L236), R238 (≠ S237), L240 (= L239), D241 (≠ E240), R244 (= R243), E365 (= E363), G366 (= G364), R377 (= R375)
- binding flavin-adenine dinucleotide: Y123 (≠ F123), L125 (= L125), S126 (≠ T126), G131 (= G131), S132 (= S132), W156 (≠ F156), I157 (≠ V157), T158 (= T158), I360 (= I358), T367 (= T365), Q369 (≠ E367)
Query Sequence
>H281DRAFT_01204 FitnessBrowser__Burk376:H281DRAFT_01204
MDSFYTEEQRMIRDAARDFATERLAPNAAQWDRDAQLPADVVRQMGDLGFLGMIVPSQWG
GSYTDYVAYALALEEIAAGCAACATLMSVHNSVGCGPILNFGSDAQKDRYLHDLATGRRI
GAFCLTEPQAGSEANNLRTRAVLCDGKWILNGSKQFVTNGARADIAIVFAVTDPDRGKRG
LSAFIVPTDTPGFNVGKPEHKLGIRASDTCPISLDDCAVPDANLLGEPGEGLRIALSNLE
GGRIGIAAQAVGIARAAFDAARAYASERMQFGKALKDHQTIANMLADMATRLNAARLLVH
HAARLRSAGEPCLSEASQAKLFASEVAEEVCSNAIQIHGGYGYLEDYAVERHYRDARITQ
IYEGTSEVQRMVIARHV
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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