SitesBLAST
Comparing BPHYT_RS32685 FitnessBrowser__BFirm:BPHYT_RS32685 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)
36% identity, 87% coverage: 30:364/387 of query aligns to 29:360/378 of 5ol2F
- active site: L124 (≠ V124), T125 (= T125), G241 (≠ E245)
- binding calcium ion: E29 (≠ K30), E33 (≠ A34), R35 (≠ G36)
- binding coenzyme a persulfide: L238 (= L242), R242 (= R246)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), T125 (= T125), P127 (= P127), T131 (= T131), F155 (≠ W155), I156 (= I156), T157 (≠ S157), E198 (≠ Q202), R267 (= R271), F270 (= F274), L274 (≠ I278), F277 (≠ N281), Q335 (= Q339), L336 (≠ F340), G338 (= G342), G339 (= G343)
Sites not aligning to the query:
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
34% identity, 96% coverage: 10:381/387 of query aligns to 7:376/383 of 4iv6B
- active site: L121 (≠ V124), T122 (= T125), G240 (≠ E245), E361 (≠ P366), K373 (≠ E378)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ V124), T122 (= T125), G126 (≠ T129), G127 (= G130), S128 (≠ T131), W152 (= W155), I153 (= I156), S154 (= S157), R266 (= R271), S268 (≠ V273), F269 (= F274), I273 (= I278), H276 (≠ N281), V279 (= V284), R334 (≠ Q339), V335 (≠ F340), G338 (= G343), L356 (= L361), G360 (≠ A365), T363 (≠ S368), E365 (≠ N370), I366 (≠ L371)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
34% identity, 96% coverage: 12:382/387 of query aligns to 9:374/374 of 5lnxD
- active site: L122 (≠ V124), T123 (= T125), G239 (≠ E245), E358 (≠ P366), K370 (≠ E378)
- binding flavin-adenine dinucleotide: L122 (≠ V124), T123 (= T125), G128 (= G130), S129 (≠ T131), F153 (≠ W155), T155 (≠ S157), R265 (= R271), Q267 (≠ V273), F268 (= F274), I272 (= I278), N275 (= N281), I278 (≠ V284), Q331 (= Q339), I332 (≠ F340), G335 (= G343), Y357 (≠ A365), T360 (≠ S368), E362 (≠ N370)
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)
34% identity, 91% coverage: 12:364/387 of query aligns to 4:351/369 of 3pfdC
- active site: L116 (≠ V124), S117 (≠ T125), T233 (≠ E245)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M122), L116 (≠ V124), S117 (≠ T125), G122 (= G130), S123 (≠ T131), W147 (= W155), I148 (= I156), T149 (≠ S157), R259 (= R271), F262 (= F274), V266 (≠ I278), N269 (= N281), Q326 (= Q339), L327 (≠ F340), G330 (= G343), I348 (≠ L361)
Sites not aligning to the query:
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
30% identity, 95% coverage: 12:380/387 of query aligns to 13:377/381 of 2jifA
- active site: L125 (≠ V124), S126 (≠ T125), G242 (≠ E245), E363 (≠ P366), K375 (≠ E378)
- binding coenzyme a persulfide: S132 (≠ T131), S134 (≠ T133), Y178 (≠ V177), Y232 (≠ F235), I236 (≠ L239), L239 (= L242), N240 (= N243), R243 (= R246), Y362 (≠ A365), E363 (≠ P366), G364 (≠ I367), I368 (≠ L371)
- binding flavin-adenine dinucleotide: F123 (≠ M122), L125 (≠ V124), S126 (≠ T125), G131 (= G130), S132 (≠ T131), W156 (= W155), I157 (= I156), S158 (= S157), K201 (≠ I204), T209 (= T212), R268 (= R271), F271 (= F274), L275 (≠ I278), F278 (≠ N281), L281 (≠ V284), E336 (≠ Q339), W337 (≠ F340), G340 (= G343), N367 (= N370), I368 (≠ L371)
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)
30% identity, 95% coverage: 12:380/387 of query aligns to 64:428/432 of P45954
- V137 (≠ A85) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (vs. gap) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 122:131, 20% identical) binding in other chain
- S183 (≠ T131) binding
- WIS 207:209 (= WIS 155:157) binding in other chain
- S210 (≠ R158) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ V177) binding
- L255 (≠ M207) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ F235) binding
- NEGR 291:294 (≠ NAER 243:246) binding
- I316 (≠ A268) to V: in dbSNP:rs1131430
- R319 (= R271) binding
- Q330 (= Q282) binding
- EWMGG 387:391 (≠ QFHGG 339:343) binding
- A416 (≠ S368) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ STN 368:370) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
32% identity, 91% coverage: 12:364/387 of query aligns to 10:360/379 of 6fahD
- active site: L124 (≠ V124), T125 (= T125), G241 (≠ E245)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), T125 (= T125), R152 (≠ Q152), F155 (≠ W155), T157 (≠ S157), E198 (≠ V201), R267 (= R271), Q269 (≠ V273), F270 (= F274), I274 (= I278), F277 (≠ N281), Q335 (= Q339), I336 (≠ F340), G339 (= G343)
Sites not aligning to the query:
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
33% identity, 96% coverage: 14:384/387 of query aligns to 13:380/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (≠ T131), L133 (≠ T133), K178 (≠ E182), F231 (= F235), M235 (≠ L239), L238 (= L242), N241 (≠ E245), R242 (= R246), Y362 (≠ A365), T363 (≠ I367), G364 (≠ S368), R375 (≠ H379)
- binding flavin-adenine dinucleotide: L122 (≠ M122), A124 (≠ V124), T125 (= T125), G130 (= G130), S131 (≠ T131), F155 (≠ W155), I156 (= I156), T157 (≠ S157), K200 (≠ I204), N208 (≠ T212), L358 (= L361), T365 (= T369), Q367 (≠ L371), I368 (= I372)
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
33% identity, 96% coverage: 14:384/387 of query aligns to 11:378/378 of 7p9xA
- binding 1-monoenoyl-CoA: L82 (≠ A85), D89 (≠ Y91), S129 (≠ T131), L131 (≠ T133), K176 (≠ E182), F229 (= F235), M233 (≠ L239), L236 (= L242), R240 (= R246), Y360 (≠ A365), T361 (≠ I367), G362 (≠ S368), R373 (≠ H379)
- binding flavin-adenine dinucleotide: A122 (≠ V124), T123 (= T125), G128 (= G130), S129 (≠ T131), F153 (≠ W155), I154 (= I156), T155 (≠ S157), N206 (≠ T212), L356 (= L361), Y360 (≠ A365), T363 (= T369), Q365 (≠ L371), I366 (= I372)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
30% identity, 98% coverage: 3:382/387 of query aligns to 6:378/379 of 1ukwB
- active site: L124 (≠ V124), S125 (≠ T125), T241 (≠ E245), E362 (≠ P366), R374 (≠ E378)
- binding cobalt (ii) ion: D145 (= D145), H146 (≠ R146)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), S125 (≠ T125), G130 (= G130), S131 (≠ T131), W155 (= W155), S157 (= S157), K200 (≠ I204), L357 (= L361), Y361 (≠ A365), E362 (≠ P366), T364 (≠ S368), E366 (≠ N370), L370 (≠ S374)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
30% identity, 98% coverage: 3:382/387 of query aligns to 6:378/379 of 1ukwA
- active site: L124 (≠ V124), S125 (≠ T125), T241 (≠ E245), E362 (≠ P366), R374 (≠ E378)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), S125 (≠ T125), G130 (= G130), S131 (≠ T131), W155 (= W155), S157 (= S157), L357 (= L361), Y361 (≠ A365), E362 (≠ P366), T364 (≠ S368), E366 (≠ N370), L370 (≠ S374)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
30% identity, 96% coverage: 10:381/387 of query aligns to 10:377/380 of 4l1fA
- active site: L125 (≠ V124), T126 (= T125), G242 (≠ E245), E363 (≠ P366), R375 (≠ H379)
- binding coenzyme a persulfide: T132 (= T131), H179 (≠ E182), F232 (= F235), M236 (≠ L239), E237 (≠ D240), L239 (= L242), D240 (≠ N243), R243 (= R246), Y362 (≠ A365), E363 (≠ P366), G364 (≠ S368), R375 (≠ H379)
- binding flavin-adenine dinucleotide: F123 (≠ M122), L125 (≠ V124), T126 (= T125), G131 (= G130), T132 (= T131), F156 (≠ W155), I157 (= I156), T158 (≠ S157), R268 (= R271), Q270 (≠ V273), F271 (= F274), I275 (= I278), F278 (≠ N281), L281 (≠ V284), Q336 (= Q339), I337 (≠ F340), G340 (= G343), I358 (≠ L361), Y362 (≠ A365), T365 (= T369), Q367 (≠ L371)
- binding 1,3-propandiol: Q10 (= Q10)
Sites not aligning to the query:
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
29% identity, 98% coverage: 7:386/387 of query aligns to 36:412/412 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)
29% identity, 97% coverage: 7:381/387 of query aligns to 9:380/384 of 1jqiA
- active site: G377 (≠ E378)
- binding acetoacetyl-coenzyme a: L95 (≠ M90), F125 (≠ M122), S134 (≠ T131), F234 (= F235), M238 (≠ L239), Q239 (≠ D240), L241 (= L242), D242 (≠ N243), R245 (= R246), Y364 (≠ A365), E365 (≠ P366), G366 (≠ I367)
- binding flavin-adenine dinucleotide: F125 (≠ M122), L127 (≠ V124), S128 (≠ T125), G133 (= G130), S134 (≠ T131), W158 (= W155), T160 (≠ S157), R270 (= R271), F273 (= F274), L280 (≠ N281), Q338 (= Q339), I339 (≠ F340), G342 (= G343), I360 (≠ L361), T367 (≠ S368), E369 (≠ N370), I370 (≠ L371)
7szvA Crystal structure of acyl-coa dehydrogenase from mycobacterium marinum in complex with fda
31% identity, 98% coverage: 4:383/387 of query aligns to 1:372/372 of 7szvA
- binding dihydroflavine-adenine dinucleotide: L122 (≠ V124), T123 (= T125), F153 (≠ W155), I154 (= I156), T155 (≠ S157), K194 (≠ M207), R261 (= R271), S263 (≠ V273), Y271 (≠ N281), I274 (≠ V284), Q329 (= Q339), V330 (≠ F340), G332 (= G342), G333 (= G343), T358 (≠ S368), E360 (≠ N370)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
29% identity, 98% coverage: 7:386/387 of query aligns to 9:385/385 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 (≠ F344), T347 (≠ C348), E348 (= E349)
- binding flavin-adenine dinucleotide: F125 (≠ M122), L127 (≠ V124), S128 (≠ T125), G133 (= G130), S134 (≠ T131), W158 (= W155), T160 (≠ S157), R270 (= R271), F273 (= F274), L280 (≠ N281), V282 (≠ G283), Q338 (= Q339), I339 (≠ F340), G342 (= G343), I360 (≠ L361), Y364 (≠ A365), T367 (≠ S368), E369 (≠ N370), I370 (≠ L371), L373 (≠ S374)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
29% identity, 98% coverage: 7:386/387 of query aligns to 36:412/412 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. 122:131, 30% identical) binding in other chain
- R171 (≠ E141) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WIS 155:157) binding in other chain
- A192 (≠ S162) 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 (≠ S299) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ A327) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QFHGG 339:343) binding
- R380 (= R354) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ STN 368:370) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
29% identity, 97% coverage: 7:381/387 of query aligns to 12:383/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ M122), L130 (≠ V124), S131 (≠ T125), G136 (= G130), S137 (≠ T131), W161 (= W155), T163 (≠ S157), T214 (= T212), R273 (= R271), F276 (= F274), L280 (≠ I278), L283 (≠ N281), V285 (≠ G283), Q341 (= Q339), I342 (≠ F340), G345 (= G343), I363 (≠ L361), Y367 (≠ A365), T370 (≠ S368), E372 (≠ N370), L376 (≠ S374)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
29% identity, 97% coverage: 7:381/387 of query aligns to 6:377/381 of 8sgsA
- binding coenzyme a: S131 (≠ T131), A133 (≠ T133), N177 (≠ S181), F231 (= F235), M235 (≠ L239), L238 (= L242), I312 (≠ G316), E362 (≠ P366), G363 (≠ I367)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), S125 (≠ T125), G130 (= G130), S131 (≠ T131), W155 (= W155), T157 (≠ S157), R267 (= R271), F270 (= F274), L274 (≠ I278), L277 (≠ N281), Q335 (= Q339), I336 (≠ F340), G338 (= G342), G339 (= G343), I357 (≠ L361), I360 (≠ V364), Y361 (≠ A365), T364 (≠ S368), E366 (≠ N370)
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
32% identity, 100% coverage: 1:386/387 of query aligns to 1:387/389 of C3UVB0
- A80 (≠ N77) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ A85) binding
- V88 (≠ C86) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ Q89) binding
- FGIT 126:129 (≠ MGVT 122:125) binding
- S135 (≠ T131) binding ; binding
- WIS 159:161 (= WIS 155:157) binding
- S181 (= S181) binding
- R271 (= R271) binding
- FQMN 281:284 (≠ NQGV 281:284) binding
- R340 (≠ Q339) binding
- A344 (≠ G343) binding
- V366 (≠ A365) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ PISTN 366:370) binding
- R385 (≠ P384) binding
Query Sequence
>BPHYT_RS32685 FitnessBrowser__BFirm:BPHYT_RS32685
MQTTQQDSFQDIREAVRDLCQQFSGEYFRKIDEARGYPEEFVDALTKAGWLAALIPQDFG
GSGLGLTEASVIMEEINRAGGNSGACHGQMYNMGTLLRHGSEEQKQKYLPKIACGDLRLQ
SMGVTEPSTGTDTTKIKTTAERRGDRYVINGQKVWISRVQHSDLMILLARTTPLADVKKK
SEGMSIFIVDLREAIGHGMTVQPILNMVNHETNELFFDNLEIPAENLIGEEGQGFKYILD
GLNAERTLIAAECIGDGYWFVDKVTEYAKERVVFGRPIGQNQGVQFPIARSFVNVEAASL
MRFEAARRFDAHQPCGAQANMAKLLAADASWEAANACLQFHGGFGFACEYDVERKFRETR
LYQVAPISTNLILSYVAEHILGLPRSF
Or try a new SitesBLAST search
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