SitesBLAST
Comparing BPHYT_RS06715 FitnessBrowser__BFirm:BPHYT_RS06715 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)
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
36% identity, 100% coverage: 1:398/398 of query aligns to 1:382/386 of 4x28A
- active site: Y122 (= Y128), S123 (= S129), E240 (= E244), G365 (= G381), M377 (≠ Q393)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), S123 (= S129), G128 (= G134), T129 (≠ S135), W153 (= W159), S155 (≠ T161), F363 (= F374), T367 (≠ S383), E369 (= E385), V370 (≠ I386)
I6YCA3 Acyl-CoA dehydrogenase FadE26; ACAD; 3-oxocholest-4-en-26-oyl-CoA dehydrogenase alpha subunit; EC 1.3.99.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
34% identity, 100% coverage: 1:398/398 of query aligns to 1:395/400 of I6YCA3
- IGYS 127:130 (≠ QGYS 126:129) binding
- T136 (≠ S135) binding
- S162 (≠ T161) binding
- E247 (= E244) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ SNE 383:385) binding
6wy8B Tcur3481-tcur3483 steroid acad (see paper)
32% identity, 100% coverage: 1:398/398 of query aligns to 1:381/384 of 6wy8B
- active site: Y126 (= Y128), T127 (≠ S129), E241 (= E244), T376 (≠ Q393)
- binding flavin-adenine dinucleotide: I124 (≠ Q126), Y126 (= Y128), T127 (≠ S129), G132 (= G134), T133 (≠ S135), F157 (≠ W159), S159 (≠ T161), V359 (≠ Y380), F362 (vs. gap), G363 (vs. gap), V366 (≠ S383), E368 (= E385)
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
32% identity, 98% coverage: 8:398/398 of query aligns to 4:377/380 of 6wy9A
- active site: Y122 (= Y128), T123 (≠ S129), E237 (= E244), T372 (≠ Q393)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), T123 (≠ S129), G128 (= G134), T129 (≠ S135), F153 (≠ W159), S155 (≠ T161), F358 (vs. gap), V362 (≠ S383), E364 (= E385)
P71858 Acyl-CoA dehydrogenase FadE29; ACAD; 3-oxo-23,24-bisnorchol-4-en-22-oyl-CoA dehydrogenase beta subunit; 3-oxo-4-pregnene-20-carboxyl-CoA dehydrogenase beta subunit; EC 1.3.99.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
40% identity, 64% coverage: 1:253/398 of query aligns to 1:250/387 of P71858
- E241 (= E244) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
P96855 Acyl-CoA dehydrogenase FadE34; ACAD; 3-oxochol-4-en-24-oyl-CoA dehydrogenase; EC 1.3.99.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
32% identity, 85% coverage: 60:398/398 of query aligns to 398:709/711 of P96855
- E581 (= E244) mutation to Q: Displays less than 1% activity with cholyl-CoA as substrate. Still binds FAD.
Sites not aligning to the query:
- 236 R→A: Displays less than 2% activity with cholyl-CoA as substrate. Cannot bind FAD.
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
31% identity, 88% coverage: 46:395/398 of query aligns to 42:378/380 of 2pg0A
- active site: M124 (≠ Y128), T125 (≠ S129), E243 (= E244), A364 (≠ G381), R376 (≠ Q393)
- binding flavin-adenine dinucleotide: I122 (≠ Q126), M124 (≠ Y128), T125 (≠ S129), G130 (= G134), S131 (= S135), F155 (≠ W159), I156 (≠ T160), T157 (= T161), R269 (≠ Q268), F272 (≠ N271), F279 (≠ D278), Q337 (≠ R354), L338 (≠ E355), G340 (≠ S357), G341 (≠ L358), V359 (≠ K376), I362 (= I379), Y363 (= Y380), T366 (≠ S383), E368 (= E385), M369 (≠ I386)
8hk0B Crystal structure of fic32-33 complex from streptomyces ficellus nrrl 8067 (see paper)
34% identity, 62% coverage: 1:248/398 of query aligns to 1:247/379 of 8hk0B
Sites not aligning to the query:
2z1qB Crystal structure of acyl coa dehydrogenase
30% identity, 87% coverage: 51:396/398 of query aligns to 66:409/549 of 2z1qB
- active site: L144 (vs. gap), T145 (≠ S129), G259 (= G242), E394 (≠ G381), G406 (≠ Q393)
- binding flavin-adenine dinucleotide: Y142 (= Y128), L144 (vs. gap), T145 (≠ S129), G150 (= G134), S151 (= S135), W177 (= W159), S179 (≠ T161), R285 (≠ Q268), F288 (≠ N271), I292 (≠ L275), F295 (≠ D278), I298 (≠ F281), H369 (= H356), G370 (≠ S357), F393 (≠ Y380), I399 (= I386)
Sites not aligning to the query:
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
27% identity, 98% coverage: 5:396/398 of query aligns to 53:427/430 of P51174
- K318 (= K269) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (= K273) modified: N6-acetyllysine; alternate; mutation to R: Reduces activity by 23%; reduces activity by 80% when associated with R-318.
Sites not aligning to the query:
- 42 modified: N6-acetyllysine; K→R: Reduces activity by 90% when associated with R-318 and R-322.
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
28% identity, 88% coverage: 48:396/398 of query aligns to 45:380/384 of 1jqiA
- active site: G377 (≠ Q393)
- binding acetoacetyl-coenzyme a: L95 (≠ M96), F125 (≠ Q126), S134 (= S135), F234 (≠ W234), M238 (≠ K238), Q239 (≠ Y239), L241 (= L241), D242 (≠ G242), R245 (= R245), Y364 (= Y380), E365 (≠ G381), G366 (= G382)
- binding flavin-adenine dinucleotide: F125 (≠ Q126), L127 (≠ Y128), S128 (= S129), G133 (= G134), S134 (= S135), W158 (= W159), T160 (= T161), R270 (≠ Q268), F273 (≠ N271), L280 (≠ D278), Q338 (≠ E336), I339 (≠ A337), G342 (≠ P340), I360 (≠ K376), T367 (≠ S383), E369 (= E385), I370 (= I386)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
28% identity, 88% coverage: 48:396/398 of query aligns to 72:407/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
27% identity, 98% coverage: 5:396/398 of query aligns to 3:377/379 of 6fahD
- active site: L124 (≠ Y128), T125 (≠ S129), G241 (≠ E244), G374 (≠ Q393)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), T125 (≠ S129), R152 (≠ Q156), F155 (≠ W159), T157 (= T161), E198 (≠ D208), R267 (≠ Q268), Q269 (≠ K270), F270 (≠ N271), I274 (≠ L275), F277 (≠ D278), Q335 (≠ R354), I336 (≠ E355), G339 (≠ L358), Y361 (= Y380), T364 (≠ S383), Q366 (≠ E385)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
28% identity, 88% coverage: 48:396/398 of query aligns to 72:407/412 of P16219
- G90 (= G66) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E80) 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 (≠ E145) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WTT 159:161) binding in other chain
- A192 (= A166) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G184) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (≠ Q268) binding
- Q308 (≠ P279) binding in other chain
- R325 (≠ E296) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ T324) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ EAVGP 336:340) binding
- R380 (= R354) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ SNE 383:385) 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
28% identity, 88% coverage: 48:396/398 of query aligns to 48:383/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ Q126), L130 (≠ Y128), S131 (= S129), G136 (= G134), S137 (= S135), W161 (= W159), T163 (= T161), T214 (≠ V211), R273 (≠ Q268), F276 (≠ N271), L280 (= L275), L283 (≠ D278), V285 (= V280), Q341 (≠ E336), I342 (≠ A337), G345 (≠ P340), I363 (≠ K376), Y367 (= Y380), T370 (≠ S383), E372 (= E385), L376 (≠ N389)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
28% identity, 88% coverage: 48:396/398 of query aligns to 42:377/381 of 8sgsA
- binding coenzyme a: S131 (= S135), A133 (≠ L137), N177 (≠ Q182), F231 (≠ W234), M235 (≠ K238), L238 (= L241), I312 (≠ G313), E362 (≠ G381), G363 (= G382)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W159), T157 (= T161), R267 (≠ Q268), F270 (≠ N271), L274 (= L275), L277 (≠ D278), Q335 (≠ E336), I336 (≠ A337), G338 (= G339), G339 (≠ P340), I357 (≠ K376), I360 (= I379), Y361 (= Y380), T364 (≠ S383), E366 (= E385)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
28% identity, 88% coverage: 48:396/398 of query aligns to 45:380/385 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 (≠ L341), T347 (≠ F345), E348 (≠ D346)
- binding flavin-adenine dinucleotide: F125 (≠ Q126), L127 (≠ Y128), S128 (= S129), G133 (= G134), S134 (= S135), W158 (= W159), T160 (= T161), R270 (≠ Q268), F273 (≠ N271), L280 (≠ D278), V282 (= V280), Q338 (≠ E336), I339 (≠ A337), G342 (≠ P340), I360 (≠ K376), Y364 (= Y380), T367 (≠ S383), E369 (= E385), I370 (= I386), L373 (≠ N389)
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
26% identity, 98% coverage: 5:396/398 of query aligns to 53:427/430 of P28330
- E291 (= E244) active site, Proton acceptor; mutation to Q: Loss of long-chain-acyl-CoA dehydrogenase activity. No effect on protein abundance. No effect on solubility. No effect on substrate binding.
- S303 (≠ R256) to T: in dbSNP:rs1801204
- K333 (= K284) to Q: in dbSNP:rs2286963
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
31% identity, 85% coverage: 58:395/398 of query aligns to 53:377/378 of 3r7kA
- active site: V126 (≠ Y128), T127 (≠ S129), E242 (= E244), G363 (= G381), K375 (≠ Q393)
- binding dihydroflavine-adenine dinucleotide: V126 (≠ Y128), T127 (≠ S129), G132 (= G134), S133 (= S135), F157 (≠ W159), I158 (≠ T160), T159 (= T161), R268 (≠ Q268), T270 (≠ K270), F271 (≠ N271), L275 (= L275), R278 (≠ D278), I281 (≠ F281), Q336 (≠ G339), I337 (≠ P340), G340 (≠ A343), I358 (≠ K376), T365 (≠ S383), E367 (= E385)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
26% identity, 94% coverage: 23:396/398 of query aligns to 14:378/380 of 4l1fA
- active site: L125 (≠ Y128), T126 (≠ S129), G242 (≠ E244), E363 (≠ G381), R375 (≠ Q393)
- binding coenzyme a persulfide: T132 (≠ S135), H179 (≠ E183), F232 (≠ W234), M236 (≠ K238), E237 (≠ Y239), L239 (= L241), D240 (≠ G242), R243 (= R245), Y362 (= Y380), E363 (≠ G381), G364 (= G382), R375 (≠ Q393)
- binding flavin-adenine dinucleotide: F123 (≠ Q126), L125 (≠ Y128), T126 (≠ S129), G131 (= G134), T132 (≠ S135), F156 (≠ W159), I157 (≠ T160), T158 (= T161), R268 (≠ Q268), Q270 (≠ K270), F271 (≠ N271), I275 (≠ L275), F278 (≠ D278), L281 (≠ F281), Q336 (≠ E336), I337 (≠ A337), G340 (≠ P340), I358 (≠ K376), Y362 (= Y380), T365 (≠ S383), Q367 (≠ E385)
Sites not aligning to the query:
Query Sequence
>BPHYT_RS06715 FitnessBrowser__BFirm:BPHYT_RS06715
MDLDYSPADNAFRADIRAWLEANLPRELSDKVLNHKRLAREDYAGWHKLLGTRGWSVIAW
PKEYGGPGWDATQRHIWDEECARIGAPSVLPFGVSMVAPVLMKYGNEAQKRHYLPRILDG
TDWWCQGYSEPGSGSDLASLRTRAERVGDHYVVNGQKTWTTLGQYADMMFCLVRTDGGAK
KQEGISFLLIDMKTPGITVRPIITLDEDHEVNEVFFEDVKVPVDNLVGEENRGWTYAKYL
LGHERTGIARVGQSKRELVFLKRLALNQKKNGKPLLQDPVFAAKVASLEIELMALEVTVQ
RVVANETGGRGPGPEASMLKIKGTEVQQALTELMFEAVGPLAAPFDVPFLEGEREHSLAG
DDDAAPLAAYYFNFRKTSIYGGSNEIQKNIIAQMILGL
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