SitesBLAST
Comparing RR42_RS05595 FitnessBrowser__Cup4G11:RR42_RS05595 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)
33% identity, 100% coverage: 1:400/400 of query aligns to 1:382/386 of 4x28A
- active site: Y122 (= Y128), S123 (= S129), E240 (= E246), G365 (= G383), M377 (≠ Q395)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), S123 (= S129), G128 (= G134), T129 (≠ S135), W153 (= W161), S155 (≠ T163), F363 (vs. gap), T367 (≠ S385), E369 (= E387), V370 (≠ I388)
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)
35% identity, 87% coverage: 54:400/400 of query aligns to 56:395/400 of I6YCA3
- IGYS 127:130 (≠ QGYS 126:129) binding
- T136 (≠ S135) binding
- S162 (≠ T163) binding
- E247 (= E246) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ SNE 385:387) binding
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)
35% identity, 88% coverage: 50:400/400 of query aligns to 388:709/711 of P96855
- E581 (= E246) 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.
6wy8B Tcur3481-tcur3483 steroid acad (see paper)
31% identity, 100% coverage: 1:400/400 of query aligns to 1:381/384 of 6wy8B
- active site: Y126 (= Y128), T127 (≠ S129), E241 (= E246), T376 (≠ Q395)
- binding flavin-adenine dinucleotide: I124 (≠ Q126), Y126 (= Y128), T127 (≠ S129), G132 (= G134), T133 (≠ S135), F157 (≠ W161), S159 (≠ T163), V359 (≠ Y382), F362 (vs. gap), G363 (vs. gap), V366 (≠ S385), E368 (= E387)
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
31% identity, 99% coverage: 7:400/400 of query aligns to 3:377/380 of 6wy9A
- active site: Y122 (= Y128), T123 (≠ S129), E237 (= E246), T372 (≠ Q395)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), T123 (≠ S129), G128 (= G134), T129 (≠ S135), F153 (≠ W161), S155 (≠ T163), F358 (≠ I381), V362 (≠ S385), E364 (= E387)
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)
37% identity, 73% coverage: 60:352/400 of query aligns to 58:347/387 of P71858
- E241 (= E246) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
31% identity, 88% coverage: 46:397/400 of query aligns to 42:378/380 of 2pg0A
- active site: M124 (≠ Y128), T125 (≠ S129), E243 (= E246), A364 (≠ G383), R376 (≠ Q395)
- binding flavin-adenine dinucleotide: I122 (≠ Q126), M124 (≠ Y128), T125 (≠ S129), G130 (= G134), S131 (= S135), F155 (≠ W161), I156 (≠ T162), T157 (= T163), R269 (≠ Q270), F272 (≠ N273), F279 (≠ D280), Q337 (≠ E338), L338 (≠ A339), G340 (= G341), G341 (≠ P342), V359 (≠ K378), I362 (= I381), Y363 (= Y382), T366 (≠ S385), E368 (= E387), M369 (≠ I388)
2z1qB Crystal structure of acyl coa dehydrogenase
30% identity, 86% coverage: 54:398/400 of query aligns to 69:409/549 of 2z1qB
- active site: L144 (vs. gap), T145 (≠ S129), G259 (= G244), E394 (≠ G383), G406 (≠ Q395)
- binding flavin-adenine dinucleotide: Y142 (= Y128), L144 (vs. gap), T145 (≠ S129), G150 (= G134), S151 (= S135), W177 (= W161), S179 (≠ T163), R285 (≠ Q270), F288 (≠ N273), I292 (≠ L277), F295 (≠ D280), I298 (≠ F283), H369 (= H358), G370 (≠ A359), F393 (≠ Y382), I399 (= I388)
Sites not aligning to the query:
8hk0B Crystal structure of fic32-33 complex from streptomyces ficellus nrrl 8067 (see paper)
31% identity, 63% coverage: 1:250/400 of query aligns to 1:247/379 of 8hk0B
Sites not aligning to the query:
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
26% identity, 99% coverage: 5:398/400 of query aligns to 3:377/379 of 6fahD
- active site: L124 (≠ Y128), T125 (≠ S129), G241 (≠ E246), G374 (≠ Q395)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), T125 (≠ S129), R152 (≠ Q158), F155 (≠ W161), T157 (= T163), E198 (= E210), R267 (≠ Q270), Q269 (≠ K272), F270 (≠ N273), I274 (≠ L277), F277 (≠ D280), Q335 (≠ H356), I336 (≠ E357), G339 (≠ V360), Y361 (= Y382), T364 (≠ S385), Q366 (≠ E387)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
26% identity, 94% coverage: 23:398/400 of query aligns to 14:378/380 of 4l1fA
- active site: L125 (≠ Y128), T126 (≠ S129), G242 (≠ E246), E363 (≠ G383), R375 (≠ Q395)
- binding coenzyme a persulfide: T132 (≠ S135), H179 (≠ E185), F232 (≠ W236), M236 (≠ K240), E237 (≠ Y241), L239 (= L243), D240 (≠ G244), R243 (= R247), Y362 (= Y382), E363 (≠ G383), G364 (= G384), R375 (≠ Q395)
- binding flavin-adenine dinucleotide: F123 (≠ Q126), L125 (≠ Y128), T126 (≠ S129), G131 (= G134), T132 (≠ S135), F156 (≠ W161), I157 (≠ T162), T158 (= T163), R268 (≠ Q270), Q270 (≠ K272), F271 (≠ N273), I275 (≠ L277), F278 (≠ D280), L281 (≠ F283), Q336 (≠ E338), I337 (≠ A339), G340 (≠ P342), I358 (≠ K378), Y362 (= Y382), T365 (≠ S385), Q367 (≠ E387)
Sites not aligning to the query:
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
28% identity, 87% coverage: 50:398/400 of query aligns to 44:377/378 of 5ol2F
- active site: L124 (≠ Y128), T125 (≠ S129), G241 (≠ E246), G374 (≠ Q395)
- binding coenzyme a persulfide: L238 (= L243), R242 (= R247), E362 (≠ G383), G363 (= G384)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), T125 (≠ S129), P127 (= P131), T131 (≠ S135), F155 (≠ W161), I156 (≠ T162), T157 (= T163), E198 (≠ P203), R267 (≠ Q270), F270 (≠ N273), L274 (= L277), F277 (≠ D280), Q335 (≠ E338), L336 (≠ A339), G338 (= G341), G339 (≠ P342), Y361 (= Y382), T364 (≠ S385), E366 (= E387)
Sites not aligning to the query:
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)
29% identity, 84% coverage: 63:397/400 of query aligns to 110:428/432 of P45954
- V137 (≠ L90) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ P91) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 124:135, 50% identical) binding in other chain
- S183 (= S135) binding
- WIS 207:209 (≠ WTT 161:163) binding in other chain
- S210 (≠ L164) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ Q184) binding
- L255 (vs. gap) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ W236) binding
- NEGR 291:294 (≠ GHER 244:247) binding
- I316 (≠ A267) to V: in dbSNP:rs1131430
- R319 (≠ Q270) binding
- Q330 (≠ P281) binding
- EWMGG 387:391 (≠ EAVGP 338:342) binding
- A416 (≠ S385) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ SNE 385:387) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
27% identity, 81% coverage: 76:398/400 of query aligns to 120:427/430 of P28330
- E291 (= E246) 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 (≠ R258) to T: in dbSNP:rs1801204
- K333 (= K286) to Q: in dbSNP:rs2286963
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
29% identity, 84% coverage: 63:397/400 of query aligns to 59:377/381 of 2jifA
- active site: L125 (≠ Y128), S126 (= S129), G242 (≠ E246), E363 (≠ G383), K375 (≠ Q395)
- binding coenzyme a persulfide: S132 (= S135), S134 (≠ L137), Y178 (≠ Q184), Y232 (≠ W236), I236 (≠ K240), L239 (= L243), N240 (≠ G244), R243 (= R247), Y362 (= Y382), E363 (≠ G383), G364 (= G384), I368 (= I388)
- binding flavin-adenine dinucleotide: F123 (≠ W124), L125 (≠ Y128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W161), I157 (≠ T162), S158 (≠ T163), K201 (≠ M206), T209 (≠ V213), R268 (≠ Q270), F271 (≠ N273), L275 (= L277), F278 (≠ D280), L281 (≠ F283), E336 (= E338), W337 (≠ A339), G340 (≠ P342), N367 (≠ E387), I368 (= I388)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
26% identity, 99% coverage: 5:398/400 of query aligns to 53:427/430 of P51174
- K318 (≠ Q271) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ R275) 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.
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
28% identity, 76% coverage: 85:389/400 of query aligns to 85:373/383 of 1bucA
- active site: L128 (≠ Y128), T129 (≠ S129), G246 (≠ E246), E367 (≠ G383)
- binding acetoacetyl-coenzyme a: L96 (≠ M96), F126 (≠ Q126), G134 (= G134), T135 (≠ S135), T162 (= T163), N182 (≠ Q184), H183 (≠ E185), F236 (≠ W236), M240 (≠ K240), M241 (≠ Y241), L243 (= L243), D244 (≠ G244), T317 (≠ G315), Y366 (= Y382), E367 (≠ G383), G368 (= G384)
- binding flavin-adenine dinucleotide: F126 (≠ Q126), L128 (≠ Y128), T129 (≠ S129), G134 (= G134), T135 (≠ S135), F160 (≠ W161), T162 (= T163), Y366 (= Y382), T369 (≠ S385), E371 (= E387)
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)
28% identity, 76% coverage: 85:389/400 of query aligns to 85:373/383 of Q06319
- E367 (≠ G383) active site, Proton acceptor; mutation to Q: Loss of activity.
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
29% identity, 85% coverage: 61:399/400 of query aligns to 56:378/379 of 1ukwB
- active site: L124 (≠ Y128), S125 (= S129), T241 (≠ E246), E362 (≠ G383), R374 (≠ Q395)
- binding cobalt (ii) ion: D145 (≠ K151), H146 (= H152)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W161), S157 (≠ T163), K200 (≠ I205), L357 (≠ K378), Y361 (= Y382), E362 (≠ G383), T364 (≠ S385), E366 (= E387), L370 (≠ N391)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
29% identity, 85% coverage: 61:399/400 of query aligns to 56:378/379 of 1ukwA
- active site: L124 (≠ Y128), S125 (= S129), T241 (≠ E246), E362 (≠ G383), R374 (≠ Q395)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W161), S157 (≠ T163), L357 (≠ K378), Y361 (= Y382), E362 (≠ G383), T364 (≠ S385), E366 (= E387), L370 (≠ N391)
Query Sequence
>RR42_RS05595 FitnessBrowser__Cup4G11:RR42_RS05595
MDLNYSASDDAFRAEVRGWLEANLPAEISSKILNHRRPNRDDLVRWHKLLAGRGWSAPHW
PVQYGGTGWNATQRHIWDEENARVGAPGVLPFGVAMVAPVIMKYGSEAQKSYYLPRILDC
TDWWCQGYSEPGSGSDLASLKTRAELTSDGKHYIVNGQKTWTTLGQHADMIFCLVRTDFE
AKKQEGISFLLIDMKTPGITVRPIIMLDEEHEVNEVFFDNVQVPVENRVGEENRGWTYAK
YLLGHERTGIARVGNSKRELGFLKRVAKQQQKNGRPLLEDPLFGAKVAALEIELMALELT
VLRVVSSESAGKGPGPEASMLKIKGTEIQQMLTELMVEAVGPYAQPFDTAYLECEHEHAV
TGYDDAAPLAAYYFNYRKTSIYGGSNEIQKNIISQMILGL
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