SitesBLAST
Comparing BPHYT_RS25400 FitnessBrowser__BFirm:BPHYT_RS25400 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)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
49% identity, 98% coverage: 8:380/381 of query aligns to 5:378/378 of 4n5fA
- active site: L126 (= L128), T127 (= T129), G243 (= G245), E364 (= E366), R376 (= R378)
- binding dihydroflavine-adenine dinucleotide: L126 (= L128), T127 (= T129), G132 (= G134), S133 (= S135), F157 (= F159), T159 (≠ S161), T210 (= T212), Y363 (= Y365), T366 (= T368), E368 (≠ H370), M372 (≠ L374)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
44% identity, 98% coverage: 9:380/381 of query aligns to 5:377/380 of 4l1fA
- active site: L125 (= L128), T126 (= T129), G242 (= G245), E363 (= E366), R375 (= R378)
- binding coenzyme a persulfide: T132 (≠ S135), H179 (≠ R182), F232 (≠ Y235), M236 (= M239), E237 (≠ A240), L239 (≠ V242), D240 (≠ S243), R243 (= R246), Y362 (= Y365), E363 (= E366), G364 (= G367), R375 (= R378)
- binding flavin-adenine dinucleotide: F123 (= F126), L125 (= L128), T126 (= T129), G131 (= G134), T132 (≠ S135), F156 (= F159), I157 (= I160), T158 (≠ S161), R268 (= R271), Q270 (≠ A273), F271 (≠ Y274), I275 (≠ L278), F278 (≠ L281), L281 (≠ V284), Q336 (= Q339), I337 (= I340), G340 (= G343), I358 (= I361), Y362 (= Y365), T365 (= T368), Q367 (≠ H370)
- binding 1,3-propandiol: L5 (= L9), Q10 (≠ T14)
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
47% identity, 98% coverage: 8:380/381 of query aligns to 3:376/376 of 4m9aB
- active site: L124 (= L128), T125 (= T129), G241 (= G245), E362 (= E366), R374 (= R378)
- binding dihydroflavine-adenine dinucleotide: F122 (= F126), T125 (= T129), G130 (= G134), S131 (= S135), F155 (= F159), T157 (≠ S161), T208 (= T212), Y361 (= Y365), T364 (= T368), E366 (≠ H370), M370 (≠ L374)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
43% identity, 97% coverage: 10:380/381 of query aligns to 3:372/374 of 5lnxD
- active site: L122 (= L128), T123 (= T129), G239 (= G245), E358 (= E366), K370 (≠ R378)
- binding flavin-adenine dinucleotide: L122 (= L128), T123 (= T129), G128 (= G134), S129 (= S135), F153 (= F159), T155 (≠ S161), R265 (= R271), Q267 (≠ A273), F268 (≠ Y274), I272 (≠ L278), N275 (≠ L281), I278 (≠ V284), Q331 (= Q339), I332 (= I340), G335 (= G343), Y357 (= Y365), T360 (= T368), E362 (≠ H370)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
43% identity, 98% coverage: 9:380/381 of query aligns to 5:376/379 of 1ukwB
- active site: L124 (= L128), S125 (≠ T129), T241 (≠ G245), E362 (= E366), R374 (= R378)
- binding cobalt (ii) ion: D145 (= D149), H146 (= H150)
- binding flavin-adenine dinucleotide: F122 (= F126), L124 (= L128), S125 (≠ T129), G130 (= G134), S131 (= S135), W155 (≠ F159), S157 (= S161), K200 (= K204), L357 (≠ I361), Y361 (= Y365), E362 (= E366), T364 (= T368), E366 (≠ H370), L370 (= L374)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
43% identity, 98% coverage: 9:380/381 of query aligns to 5:376/379 of 1ukwA
- active site: L124 (= L128), S125 (≠ T129), T241 (≠ G245), E362 (= E366), R374 (= R378)
- binding flavin-adenine dinucleotide: F122 (= F126), L124 (= L128), S125 (≠ T129), G130 (= G134), S131 (= S135), W155 (≠ F159), S157 (= S161), L357 (≠ I361), Y361 (= Y365), E362 (= E366), T364 (= T368), E366 (≠ H370), L370 (= L374)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
43% identity, 98% coverage: 9:380/381 of query aligns to 7:379/384 of 1jqiA
- active site: G377 (≠ R378)
- binding acetoacetyl-coenzyme a: L95 (≠ T97), F125 (= F126), S134 (= S135), F234 (≠ Y235), M238 (= M239), Q239 (≠ A240), L241 (≠ V242), D242 (≠ S243), R245 (= R246), Y364 (= Y365), E365 (= E366), G366 (= G367)
- binding flavin-adenine dinucleotide: F125 (= F126), L127 (= L128), S128 (≠ T129), G133 (= G134), S134 (= S135), W158 (≠ F159), T160 (≠ S161), R270 (= R271), F273 (≠ Y274), L280 (= L281), Q338 (= Q339), I339 (= I340), G342 (= G343), I360 (= I361), T367 (= T368), E369 (≠ H370), I370 (= I371)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
43% identity, 98% coverage: 9:380/381 of query aligns to 34:406/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
47% identity, 98% coverage: 9:380/381 of query aligns to 1:368/370 of 2dvlA
- active site: L121 (= L128), T122 (= T129), G233 (= G245), E354 (= E366), R366 (= R378)
- binding flavin-adenine dinucleotide: L121 (= L128), T122 (= T129), G127 (= G134), S128 (= S135), W152 (≠ F159), I153 (= I160), T154 (≠ S161), T356 (= T368), E358 (≠ H370)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
40% identity, 97% coverage: 10:380/381 of query aligns to 5:376/378 of 5ol2F
- active site: L124 (= L128), T125 (= T129), G241 (= G245), G374 (≠ R378)
- binding calcium ion: E29 (= E34), E33 (≠ Q38), R35 (≠ A40)
- binding coenzyme a persulfide: L238 (≠ V242), R242 (= R246), E362 (= E366), G363 (= G367)
- binding flavin-adenine dinucleotide: F122 (= F126), L124 (= L128), T125 (= T129), P127 (= P131), T131 (≠ S135), F155 (= F159), I156 (= I160), T157 (≠ S161), E198 (= E202), R267 (= R271), F270 (≠ Y274), L274 (= L278), F277 (≠ L281), Q335 (= Q339), L336 (≠ I340), G338 (= G342), G339 (= G343), Y361 (= Y365), T364 (= T368), E366 (≠ H370)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
42% identity, 98% coverage: 9:380/381 of query aligns to 4:376/381 of 8sgsA
- binding coenzyme a: S131 (= S135), A133 (≠ T137), N177 (≠ K181), F231 (≠ Y235), M235 (= M239), L238 (≠ V242), I312 (= I316), E362 (= E366), G363 (= G367)
- binding flavin-adenine dinucleotide: F122 (= F126), L124 (= L128), S125 (≠ T129), G130 (= G134), S131 (= S135), W155 (≠ F159), T157 (≠ S161), R267 (= R271), F270 (≠ Y274), L274 (= L278), L277 (= L281), Q335 (= Q339), I336 (= I340), G338 (= G342), G339 (= G343), I357 (= I361), I360 (= I364), Y361 (= Y365), T364 (= T368), E366 (≠ H370)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
42% identity, 98% coverage: 9:380/381 of query aligns to 10:382/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (= F126), L130 (= L128), S131 (≠ T129), G136 (= G134), S137 (= S135), W161 (≠ F159), T163 (≠ S161), T214 (= T212), R273 (= R271), F276 (≠ Y274), L280 (= L278), L283 (= L281), V285 (≠ A283), Q341 (= Q339), I342 (= I340), G345 (= G343), I363 (= I361), Y367 (= Y365), T370 (= T368), E372 (≠ H370), L376 (= L374)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
42% identity, 98% coverage: 9:380/381 of query aligns to 7:379/385 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 (≠ Y344), T347 (= T348), E348 (≠ D349)
- binding flavin-adenine dinucleotide: F125 (= F126), L127 (= L128), S128 (≠ T129), G133 (= G134), S134 (= S135), W158 (≠ F159), T160 (≠ S161), R270 (= R271), F273 (≠ Y274), L280 (= L281), V282 (≠ A283), Q338 (= Q339), I339 (= I340), G342 (= G343), I360 (= I361), Y364 (= Y365), T367 (= T368), E369 (≠ H370), I370 (= I371), L373 (= L374)
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: 9:380/381 of query aligns to 34:406/412 of P16219
- G90 (= G65) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E79) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 126:135, 60% identical) binding in other chain
- R171 (= R145) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ FIS 159:161) binding in other chain
- A192 (= A166) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G183) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R271) binding
- Q308 (= Q282) binding in other chain
- R325 (≠ W299) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S327) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIHGG 339:343) binding
- R380 (= R354) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TSH 368:370) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
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)
38% identity, 98% coverage: 9:381/381 of query aligns to 57:429/432 of P45954
- V137 (≠ T89) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ I90) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 126:135, 60% identical) binding in other chain
- S183 (= S135) binding
- WIS 207:209 (≠ FIS 159:161) binding in other chain
- S210 (≠ N162) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ K181) binding
- L255 (≠ Q207) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (= Y235) binding
- NEGR 291:294 (≠ SDGR 243:246) binding
- I316 (≠ A268) to V: in dbSNP:rs1131430
- R319 (= R271) binding
- Q330 (= Q282) binding
- EWMGG 387:391 (≠ QIHGG 339:343) binding
- A416 (≠ T368) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TSH 368:370) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
38% identity, 98% coverage: 9:381/381 of query aligns to 6:378/381 of 2jifA
- active site: L125 (= L128), S126 (≠ T129), G242 (= G245), E363 (= E366), K375 (≠ R378)
- binding coenzyme a persulfide: S132 (= S135), S134 (≠ T137), Y178 (≠ K181), Y232 (= Y235), I236 (≠ M239), L239 (≠ V242), N240 (≠ S243), R243 (= R246), Y362 (= Y365), E363 (= E366), G364 (= G367), I368 (= I371)
- binding flavin-adenine dinucleotide: F123 (= F126), L125 (= L128), S126 (≠ T129), G131 (= G134), S132 (= S135), W156 (≠ F159), I157 (= I160), S158 (= S161), K201 (= K204), T209 (= T212), R268 (= R271), F271 (≠ Y274), L275 (= L278), F278 (≠ L281), L281 (≠ V284), E336 (≠ Q339), W337 (≠ I340), G340 (= G343), N367 (≠ H370), I368 (= I371)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
40% identity, 97% coverage: 8:377/381 of query aligns to 2:373/379 of 6fahD
- active site: L124 (= L128), T125 (= T129), G241 (= G245)
- binding flavin-adenine dinucleotide: F122 (= F126), L124 (= L128), T125 (= T129), R152 (≠ T156), F155 (= F159), T157 (≠ S161), E198 (= E202), R267 (= R271), Q269 (≠ A273), F270 (≠ Y274), I274 (≠ L278), F277 (≠ L281), Q335 (= Q339), I336 (= I340), G339 (= G343), Y361 (= Y365), T364 (= T368), Q366 (≠ H370)
Sites not aligning to the query:
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
41% identity, 98% coverage: 9:380/381 of query aligns to 1:366/371 of 2vigB
- active site: L121 (= L128), S122 (≠ T129), G231 (= G245), E352 (= E366), G364 (≠ R378)
- binding coenzyme a persulfide: S128 (= S135), F221 (≠ Y235), M225 (= M239), Q226 (≠ A240), L228 (≠ V242), D229 (≠ S243), R232 (= R246), E352 (= E366), G353 (= G367), I357 (= I371)
- binding flavin-adenine dinucleotide: L121 (= L128), S122 (≠ T129), G127 (= G134), S128 (= S135), W152 (≠ F159), T154 (≠ S161), R257 (= R271), F260 (≠ Y274), L264 (= L278), L267 (= L281), Q325 (= Q339), I326 (= I340), G329 (= G343), I347 (= I361), Y351 (= Y365), T354 (= T368), E356 (≠ H370)
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)
40% identity, 96% coverage: 16:380/381 of query aligns to 4:367/369 of 3pfdC
- active site: L116 (= L128), S117 (≠ T129), T233 (≠ G245), E353 (= E366), R365 (= R378)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ F126), L116 (= L128), S117 (≠ T129), G122 (= G134), S123 (= S135), W147 (≠ F159), I148 (= I160), T149 (≠ S161), R259 (= R271), F262 (≠ Y274), V266 (≠ L278), N269 (≠ L281), Q326 (= Q339), L327 (≠ I340), G330 (= G343), I348 (= I361), Y352 (= Y365), T355 (= T368), Q357 (≠ H370)
7szvA Crystal structure of acyl-coa dehydrogenase from mycobacterium marinum in complex with fda
38% identity, 98% coverage: 9:380/381 of query aligns to 2:370/372 of 7szvA
- binding dihydroflavine-adenine dinucleotide: L122 (= L128), T123 (= T129), F153 (= F159), I154 (= I160), T155 (≠ S161), K194 (= K204), R261 (= R271), S263 (≠ A273), Y271 (≠ L281), I274 (≠ V284), Q329 (= Q339), V330 (≠ I340), G332 (= G342), G333 (= G343), T358 (= T368), E360 (≠ H370)
Query Sequence
>BPHYT_RS25400 FitnessBrowser__BFirm:BPHYT_RS25400
MTDSNRSFLTEQQTLIRDTARRVANEIIAPTAAERDLQSAWPRSELKALAELGFLGMLIP
EQYGGSGAGILDFCIAQHEFAAVDAGLATIMHVHNFTALTIVEHGTETQKQRYLPAMACG
ESIGAFLLTEPHAGSDTASLRASARREGDHYVLNGTKQFISNGSEAGVGIAFAITDKAAG
KRGASTFIIDPNAPGYSVTRIESKLGQHTAHTAQIALEGYRVPAENLLGLEGDGYRTVMA
GVSDGRIGIAFISAGVARGALDAAVKYAREREAYGGPLTKLQAVAFDLADMAAQVDVAWQ
YCLHAARLRDAGFDCIKEASIAKLFASEIAEKVCSDALQIHGGYGYLTDFPVERYLRDVR
ICKIYEGTSHIQKLIISRNLD
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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