SitesBLAST
Comparing BPHYT_RS20780 FitnessBrowser__BFirm:BPHYT_RS20780 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)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
42% identity, 98% coverage: 4:375/381 of query aligns to 5:377/378 of 5ol2F
- active site: L124 (≠ I122), T125 (= T123), G241 (= G239), G374 (≠ R372)
- binding calcium ion: E29 (= E28), E33 (≠ D32), R35 (= R34)
- binding coenzyme a persulfide: L238 (= L236), R242 (= R240), E362 (= E360), G363 (= G361)
- binding flavin-adenine dinucleotide: F122 (≠ Y120), L124 (≠ I122), T125 (= T123), P127 (≠ A125), T131 (= T129), F155 (≠ W153), I156 (= I154), T157 (≠ H155), E198 (= E196), R267 (= R265), F270 (= F268), L274 (≠ I272), F277 (= F275), Q335 (= Q333), L336 (≠ I334), G338 (= G336), G339 (= G337), Y361 (= Y359), T364 (= T362), E366 (≠ Q364)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
46% identity, 96% coverage: 10:375/381 of query aligns to 9:373/374 of 5lnxD
- active site: L122 (≠ I122), T123 (= T123), G239 (= G239), E358 (= E360), K370 (≠ R372)
- binding flavin-adenine dinucleotide: L122 (≠ I122), T123 (= T123), G128 (= G128), S129 (≠ T129), F153 (≠ W153), T155 (≠ H155), R265 (= R265), Q267 (= Q267), F268 (= F268), I272 (= I272), N275 (≠ F275), I278 (= I278), Q331 (= Q333), I332 (= I334), G335 (= G337), Y357 (= Y359), T360 (= T362), E362 (≠ Q364)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
43% identity, 98% coverage: 1:375/381 of query aligns to 3:378/380 of 4l1fA
- active site: L125 (≠ I122), T126 (= T123), G242 (= G239), E363 (= E360), R375 (= R372)
- binding coenzyme a persulfide: T132 (= T129), H179 (≠ R176), F232 (= F229), M236 (= M233), E237 (≠ S234), L239 (= L236), D240 (= D237), R243 (= R240), Y362 (= Y359), E363 (= E360), G364 (= G361), R375 (= R372)
- binding flavin-adenine dinucleotide: F123 (≠ Y120), L125 (≠ I122), T126 (= T123), G131 (= G128), T132 (= T129), F156 (≠ W153), I157 (= I154), T158 (≠ H155), R268 (= R265), Q270 (= Q267), F271 (= F268), I275 (= I272), F278 (= F275), L281 (≠ I278), Q336 (= Q333), I337 (= I334), G340 (= G337), I358 (= I355), Y362 (= Y359), T365 (= T362), Q367 (= Q364)
- binding 1,3-propandiol: L5 (= L3), Q10 (= Q8)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
42% identity, 98% coverage: 1:375/381 of query aligns to 1:377/379 of 6fahD
- active site: L124 (≠ I122), T125 (= T123), G241 (= G239), G374 (≠ R372)
- binding flavin-adenine dinucleotide: F122 (≠ Y120), L124 (≠ I122), T125 (= T123), R152 (≠ A150), F155 (≠ W153), T157 (≠ H155), E198 (= E196), R267 (= R265), Q269 (= Q267), F270 (= F268), I274 (= I272), F277 (= F275), Q335 (= Q333), I336 (= I334), G339 (= G337), Y361 (= Y359), T364 (= T362), Q366 (= Q364)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
43% identity, 97% coverage: 4:374/381 of query aligns to 7:378/378 of 4n5fA
- active site: L126 (≠ I122), T127 (= T123), G243 (= G239), E364 (= E360), R376 (= R372)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ I122), T127 (= T123), G132 (= G128), S133 (≠ T129), F157 (≠ W153), T159 (≠ H155), T210 (≠ V206), Y363 (= Y359), T366 (= T362), E368 (≠ Q364), M372 (≠ T368)
Q9VSA3 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; EC 1.3.8.7 from Drosophila melanogaster (Fruit fly) (see paper)
43% identity, 98% coverage: 3:374/381 of query aligns to 37:411/419 of Q9VSA3
- S347 (= S310) 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.
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
42% identity, 98% coverage: 1:375/381 of query aligns to 4:381/385 of 3mdeA
- active site: V125 (≠ I122), T126 (= T123), T245 (≠ G239), E366 (= E360), R378 (= R372)
- binding octanoyl-coenzyme a: T86 (≠ D83), E89 (≠ G86), L93 (= L90), S132 (≠ T129), V134 (= V131), S181 (≠ R175), F235 (= F229), M239 (= M233), F242 (≠ L236), R314 (= R308), Y365 (= Y359), E366 (= E360), G367 (= G361)
- binding flavin-adenine dinucleotide: Y123 (= Y120), V125 (≠ I122), T126 (= T123), G131 (= G128), S132 (≠ T129), W156 (= W153), I157 (= I154), T158 (≠ H155), R271 (= R265), T273 (≠ Q267), F274 (= F268), L278 (≠ I272), H281 (≠ F275), Q339 (= Q333), V340 (≠ I334), G343 (= G337), I361 (= I355), T368 (= T362), Q370 (= Q364)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
42% identity, 98% coverage: 1:375/381 of query aligns to 4:381/385 of 3mddA
- active site: V125 (≠ I122), T126 (= T123), T245 (≠ G239), E366 (= E360), R378 (= R372)
- binding flavin-adenine dinucleotide: Y123 (= Y120), T126 (= T123), G131 (= G128), S132 (≠ T129), W156 (= W153), T158 (≠ H155), R271 (= R265), T273 (≠ Q267), F274 (= F268), H281 (≠ F275), Q339 (= Q333), V340 (≠ I334), G343 (= G337), I361 (= I355), T368 (= T362), Q370 (= Q364)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
42% identity, 98% coverage: 1:375/381 of query aligns to 4:381/385 of 1udyA
- active site: V125 (≠ I122), T126 (= T123), T245 (≠ G239), E366 (= E360), R378 (= R372)
- binding 3-thiaoctanoyl-coenzyme a: L93 (= L90), Y123 (= Y120), S132 (≠ T129), S181 (≠ R175), F235 (= F229), M239 (= M233), F242 (≠ L236), V249 (≠ I243), R314 (= R308), Y365 (= Y359), E366 (= E360), G367 (= G361), I371 (= I365), I375 (= I369)
- binding flavin-adenine dinucleotide: Y123 (= Y120), T126 (= T123), G131 (= G128), S132 (≠ T129), W156 (= W153), T158 (≠ H155), T273 (≠ Q267), F274 (= F268), Q339 (= Q333), V340 (≠ I334), G343 (= G337), T368 (= T362), Q370 (= Q364)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
42% identity, 98% coverage: 1:375/381 of query aligns to 39:416/421 of P41367
- 158:167 (vs. 120:129, 60% identical) binding in other chain
- S167 (≠ T129) binding
- WIT 191:193 (≠ WIH 153:155) binding in other chain
- S216 (≠ R175) binding
- D278 (= D237) binding
- R281 (= R240) binding
- RKT 306:308 (≠ RKQ 265:267) binding
- HQ 316:317 (≠ FQ 275:276) binding in other chain
- R349 (= R308) binding
- T351 (≠ S310) binding
- QVFGG 374:378 (≠ QIFGG 333:337) binding
- E401 (= E360) active site, Proton acceptor; binding
- GTAQ 402:405 (≠ GTNQ 361:364) binding in other chain
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
40% identity, 98% coverage: 1:375/381 of query aligns to 5:380/384 of 1jqiA
- active site: G377 (≠ R372)
- binding acetoacetyl-coenzyme a: L95 (= L95), F125 (≠ Y120), S134 (≠ T129), F234 (= F229), M238 (= M233), Q239 (≠ S234), L241 (= L236), D242 (= D237), R245 (= R240), Y364 (= Y359), E365 (= E360), G366 (= G361)
- binding flavin-adenine dinucleotide: F125 (≠ Y120), L127 (≠ I122), S128 (≠ T123), G133 (= G128), S134 (≠ T129), W158 (= W153), T160 (≠ H155), R270 (= R265), F273 (= F268), L280 (≠ F275), Q338 (= Q333), I339 (= I334), G342 (= G337), I360 (= I355), T367 (= T362), E369 (≠ Q364), I370 (= I365)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
40% identity, 98% coverage: 1:375/381 of query aligns to 32:407/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7w0jE Acyl-coa dehydrogenase, tfu_1647
42% identity, 98% coverage: 2:375/381 of query aligns to 6:381/382 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 (≠ T123), W157 (= W153), R270 (= R265), Q272 (= Q267), F273 (= F268), I277 (= I272), F280 (= F275), I283 (= I278), Q339 (= Q333), L340 (≠ I334), G343 (= G337), Y365 (= Y359), E366 (= E360), T368 (= T362), Q370 (= Q364), I371 (= I365)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
42% identity, 98% coverage: 2:375/381 of query aligns to 5:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (≠ T129), T134 (≠ V131), R180 (= R176), R234 (≠ H230), L237 (≠ M233), R238 (≠ S234), L240 (= L236), D241 (= D237), R244 (= R240), E365 (= E360), G366 (= G361), R377 (= R372)
- binding flavin-adenine dinucleotide: Y123 (= Y120), L125 (≠ I122), S126 (≠ T123), G131 (= G128), S132 (≠ T129), W156 (= W153), I157 (= I154), T158 (≠ H155), I360 (= I355), T367 (= T362), Q369 (= Q364)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
42% identity, 98% coverage: 2:375/381 of query aligns to 5:380/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (= Y120), L125 (≠ I122), S126 (≠ T123), G131 (= G128), S132 (≠ T129), W156 (= W153), I157 (= I154), T158 (≠ H155), I360 (= I355), Y364 (= Y359), T367 (= T362), Q369 (= Q364)
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: 7:375/381 of query aligns to 1:368/369 of 3pfdC
- active site: L116 (≠ I122), S117 (≠ T123), T233 (≠ G239), E353 (= E360), R365 (= R372)
- binding dihydroflavine-adenine dinucleotide: Y114 (= Y120), L116 (≠ I122), S117 (≠ T123), G122 (= G128), S123 (≠ T129), W147 (= W153), I148 (= I154), T149 (≠ H155), R259 (= R265), F262 (= F268), V266 (≠ I272), N269 (≠ F275), Q326 (= Q333), L327 (≠ I334), G330 (= G337), I348 (= I355), Y352 (= Y359), T355 (= T362), Q357 (= Q364)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
41% identity, 98% coverage: 1:375/381 of query aligns to 5:380/385 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 (≠ S338), T347 (≠ R342), E348 (≠ G343)
- binding flavin-adenine dinucleotide: F125 (≠ Y120), L127 (≠ I122), S128 (≠ T123), G133 (= G128), S134 (≠ T129), W158 (= W153), T160 (≠ H155), R270 (= R265), F273 (= F268), L280 (≠ F275), V282 (≠ G277), Q338 (= Q333), I339 (= I334), G342 (= G337), I360 (= I355), Y364 (= Y359), T367 (= T362), E369 (≠ Q364), I370 (= I365), L373 (≠ T368)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
41% identity, 98% coverage: 1:375/381 of query aligns to 8:383/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ Y120), L130 (≠ I122), S131 (≠ T123), G136 (= G128), S137 (≠ T129), W161 (= W153), T163 (≠ H155), T214 (≠ V206), R273 (= R265), F276 (= F268), L280 (≠ I272), L283 (≠ F275), V285 (≠ G277), Q341 (= Q333), I342 (= I334), G345 (= G337), I363 (= I355), Y367 (= Y359), T370 (= T362), E372 (≠ Q364), L376 (≠ T368)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
41% identity, 98% coverage: 1:375/381 of query aligns to 2:377/381 of 8sgsA
- binding coenzyme a: S131 (≠ T129), A133 (≠ V131), N177 (≠ R175), F231 (= F229), M235 (= M233), L238 (= L236), I312 (≠ S310), E362 (= E360), G363 (= G361)
- binding flavin-adenine dinucleotide: F122 (≠ Y120), L124 (≠ I122), S125 (≠ T123), G130 (= G128), S131 (≠ T129), W155 (= W153), T157 (≠ H155), R267 (= R265), F270 (= F268), L274 (≠ I272), L277 (≠ F275), Q335 (= Q333), I336 (= I334), G338 (= G336), G339 (= G337), I357 (= I355), I360 (= I358), Y361 (= Y359), T364 (= T362), E366 (≠ Q364)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
41% identity, 98% coverage: 1:375/381 of query aligns to 32:407/412 of P16219
- G90 (= G59) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E73) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 120:129, 20% identical) binding in other chain
- R171 (≠ M139) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WIH 153:155) binding in other chain
- A192 (= A160) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G177) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R265) binding
- Q308 (= Q276) binding in other chain
- R325 (= R293) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ G321) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIFGG 333:337) binding
- R380 (= R348) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TNQ 362:364) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
Query Sequence
>BPHYT_RS20780 FitnessBrowser__BFirm:BPHYT_RS20780
MKLSDTHQQIRETTRRFAQEVIRPITEELDRDERFPAEIYTQMGELGLFGITVPEAFGGA
GLDVTAYALVMEELSRGYASVADQCGLLELVGTLLSVHGTDSQRAKYMQPLLRAKLRPAY
CITEADAGTDVSGIRTTAMRTPDGWELSGAKLWIHNAPVADVAFVLARTDPAAGRRGMSI
FIVDCALAGVSKGAKEHKMGQRASQVGELHFDRVKLPQDALLGQEGRGFHIMMSVLDKGR
VGIAALAVGIAQAGLEAALDYAQTRKQFGSHIAEFQGIQWMLADMATDIQAARLLVHDAA
ERLEAGERASIACSMAKCFAGDTAVKHSANAVQIFGGSGYIRGYEVERLYRDAKITQIYE
GTNQIQRTIVARDLIANGATL
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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