SitesBLAST
Comparing Ac3H11_1711 FitnessBrowser__acidovorax_3H11:Ac3H11_1711 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: 1:393/393 of query aligns to 1:381/386 of 4x28A
- active site: Y122 (= Y128), S123 (= S129), E240 (= E244), G365 (= G377), M377 (≠ Q389)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), S123 (= S129), G128 (= G134), T129 (≠ S135), W153 (= W159), S155 (≠ T161), F363 (≠ I375), T367 (≠ S379), E369 (= E381), V370 (= V382)
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)
33% identity, 100% coverage: 1:393/393 of query aligns to 1:394/400 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 379:381) binding
6wy8B Tcur3481-tcur3483 steroid acad (see paper)
32% identity, 100% coverage: 1:393/393 of query aligns to 1:380/384 of 6wy8B
- active site: Y126 (= Y128), T127 (≠ S129), E241 (= E244), T376 (≠ Q389)
- binding flavin-adenine dinucleotide: I124 (≠ Q126), Y126 (= Y128), T127 (≠ S129), G132 (= G134), T133 (≠ S135), F157 (≠ W159), S159 (≠ T161), V359 (vs. gap), F362 (≠ I375), G363 (≠ Y376), V366 (≠ S379), E368 (= E381)
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
32% identity, 97% coverage: 12:393/393 of query aligns to 8:376/380 of 6wy9A
- active site: Y122 (= Y128), T123 (≠ S129), E237 (= E244), T372 (≠ Q389)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), T123 (≠ S129), G128 (= G134), T129 (≠ S135), F153 (≠ W159), S155 (≠ T161), F358 (≠ I375), V362 (≠ S379), E364 (= E381)
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)
33% identity, 100% coverage: 1:392/393 of query aligns to 1:380/387 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)
30% identity, 88% coverage: 50:393/393 of query aligns to 388:708/711 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.
8hk0B Crystal structure of fic32-33 complex from streptomyces ficellus nrrl 8067 (see paper)
29% identity, 99% coverage: 1:388/393 of query aligns to 1:370/379 of 8hk0B
- binding flavin-adenine dinucleotide: V126 (≠ Q126), Y128 (= Y128), T129 (≠ S129), G134 (= G134), S135 (= S135), F159 (≠ W159), S160 (≠ T160), L161 (≠ T161), G354 (≠ K372), S358 (≠ Y376), T361 (≠ S379), E363 (= E381)
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
30% identity, 88% coverage: 46:389/393 of query aligns to 42:376/380 of 2pg0A
- active site: M124 (≠ Y128), T125 (≠ S129), E243 (= E244), A364 (≠ G377), R376 (≠ Q389)
- binding flavin-adenine dinucleotide: I122 (≠ Q126), M124 (≠ Y128), T125 (≠ S129), G130 (= G134), S131 (= S135), F155 (≠ W159), I156 (≠ T160), T157 (= T161), R269 (= R263), F272 (≠ K266), F279 (≠ D273), Q337 (≠ L331), L338 (≠ A332), G340 (= G334), G341 (≠ P335), V359 (≠ K372), I362 (= I375), Y363 (= Y376), T366 (≠ S379), E368 (= E381), M369 (≠ V382)
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
29% identity, 99% coverage: 5:392/393 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 (≠ Q279) to Q: in dbSNP:rs2286963
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
28% identity, 99% coverage: 5:392/393 of query aligns to 53:427/430 of P51174
- K318 (= K262) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (= K266) 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.
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
33% identity, 62% coverage: 6:249/393 of query aligns to 6:247/378 of 3r7kA
Sites not aligning to the query:
- active site: 363, 375
- binding dihydroflavine-adenine dinucleotide: 268, 270, 271, 275, 278, 281, 336, 337, 340, 358, 365, 367
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
28% identity, 88% coverage: 50:393/393 of query aligns to 45:378/379 of 1ukwB
- active site: L124 (≠ Y128), S125 (= S129), T241 (≠ E244), E362 (≠ G377), R374 (≠ Q389)
- binding cobalt (ii) ion: D145 (= D149), H146 (≠ K150)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W159), S157 (≠ T161), K200 (= K203), L357 (≠ K372), Y361 (= Y376), E362 (≠ G377), T364 (≠ S379), E366 (= E381), L370 (≠ N385)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
28% identity, 88% coverage: 50:393/393 of query aligns to 45:378/379 of 1ukwA
- active site: L124 (≠ Y128), S125 (= S129), T241 (≠ E244), E362 (≠ G377), R374 (≠ Q389)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W159), S157 (≠ T161), L357 (≠ K372), Y361 (= Y376), E362 (≠ G377), T364 (≠ S379), E366 (= E381), L370 (≠ N385)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
25% identity, 99% coverage: 3:392/393 of query aligns to 1:377/379 of 6fahD
- active site: L124 (≠ Y128), T125 (≠ S129), G241 (≠ E244), G374 (≠ Q389)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), T125 (≠ S129), R152 (≠ Q156), F155 (≠ W159), T157 (= T161), E198 (vs. gap), R267 (vs. gap), Q269 (vs. gap), F270 (vs. gap), I274 (≠ V270), F277 (≠ D273), Q335 (≠ L331), I336 (≠ A332), G339 (≠ P335), Y361 (= Y376), T364 (≠ S379), Q366 (≠ E381)
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)
25% identity, 98% coverage: 5:391/393 of query aligns to 57:428/432 of P45954
- V137 (≠ I90) 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. 126:135, 50% identical) binding in other chain
- S183 (= S135) binding
- WIS 207:209 (≠ WTT 159:161) binding in other chain
- S210 (≠ L162) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ Q182) binding
- L255 (vs. gap) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ W234) binding
- NEGR 291:294 (≠ SHER 242:245) binding
- I316 (≠ S254) to V: in dbSNP:rs1131430
- R319 (≠ E257) binding
- Q330 (= Q274) binding
- E------WMGG 387:391 (≠ EEAMEAGWQGN 342:352) binding
- A416 (≠ S379) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ SNE 379:381) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
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)
27% identity, 87% coverage: 50:392/393 of query aligns to 37:368/369 of 3pfdC
- active site: L116 (≠ Y128), S117 (= S129), T233 (≠ E244), E353 (≠ G377), R365 (≠ Q389)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ Q126), L116 (≠ Y128), S117 (= S129), G122 (= G134), S123 (= S135), W147 (= W159), I148 (≠ T160), T149 (= T161), R259 (≠ E268), F262 (vs. gap), V266 (= V270), N269 (≠ D273), Q326 (≠ G334), L327 (≠ P335), G330 (≠ N352), I348 (≠ K372), Y352 (= Y376), T355 (≠ S379), Q357 (≠ E381)
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
25% identity, 98% coverage: 5:391/393 of query aligns to 6:377/381 of 2jifA
- active site: L125 (≠ Y128), S126 (= S129), G242 (≠ E244), E363 (≠ G377), K375 (≠ Q389)
- binding coenzyme a persulfide: S132 (= S135), S134 (≠ L137), Y178 (≠ Q182), Y232 (≠ W234), I236 (≠ K238), L239 (= L241), N240 (≠ S242), R243 (= R245), Y362 (= Y376), E363 (≠ G377), G364 (= G378), I368 (≠ V382)
- binding flavin-adenine dinucleotide: F123 (≠ Q126), L125 (≠ Y128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), S158 (≠ T161), K201 (≠ L204), T209 (≠ E208), R268 (≠ E257), F271 (≠ R260), L275 (≠ I264), F278 (≠ D273), L281 (≠ F276), E336 (= E342), W337 (= W349), G340 (≠ N352), N367 (≠ E381), I368 (≠ V382)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
26% identity, 86% coverage: 54:392/393 of query aligns to 46:376/383 of 4iv6B
- active site: L121 (≠ Y128), T122 (≠ S129), G240 (≠ A237), E361 (vs. gap), K373 (≠ Q389)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ Y128), T122 (≠ S129), G126 (≠ S133), G127 (= G134), S128 (= S135), W152 (= W159), I153 (≠ T160), S154 (≠ T161), R266 (≠ L258), S268 (≠ R260), F269 (≠ L261), I273 (≠ V270), H276 (≠ D273), V279 (≠ F276), R334 (≠ L331), V335 (≠ A332), G338 (≠ P335), L356 (≠ T373), G360 (= G377), T363 (≠ S379), E365 (= E381), I366 (≠ V382)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
26% identity, 87% coverage: 54:393/393 of query aligns to 85:417/421 of P41367
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
26% identity, 87% coverage: 54:393/393 of query aligns to 50:382/385 of 3mdeA
- active site: V125 (≠ Y128), T126 (≠ S129), T245 (≠ E244), E366 (≠ G377), R378 (≠ Q389)
- binding octanoyl-coenzyme a: T86 (≠ R88), E89 (≠ P91), L93 (≠ V95), S132 (= S135), V134 (≠ L137), S181 (≠ G184), F235 (≠ W234), M239 (≠ K238), F242 (≠ L241), R314 (≠ N306), Y365 (= Y376), E366 (≠ G377), G367 (= G378)
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), V125 (≠ Y128), T126 (≠ S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), T158 (= T161), R271 (≠ E268), T273 (≠ V270), F274 (≠ W271), L278 (≠ R275), H281 (≠ D278), Q339 (≠ L331), V340 (≠ A332), G343 (= G351), I361 (≠ K372), T368 (≠ S379), Q370 (≠ E381)
Query Sequence
>Ac3H11_1711 FitnessBrowser__acidovorax_3H11:Ac3H11_1711
MDLAFTPEEQAFRDEVRAWVHANLPQDISHKVHNALRLTRADMQGWAKILGKKGWLGFGW
PKEFGGPGWTAVQKHLFEEECALAGAPRIIPFGPVMVAPVIMAFGNAEQQKRFLPGIASG
EVWWSQGYSEPGSGSDLASVKTRAERVGDKYIVNGQKTWTTLGQHGDWMFNLVRTSNEGK
PQTGISFLLLDMKSKGVTVRPIKLLDGECEVNEVFFDNVEVPAENLIGEENKGWTYAKHL
LSHERTNIADVNRSKRELERLKRIAKTEGVWDDQRFRDQIALLEVDIVALEMLVLRVLSA
EKSGKNSLDIAGLLKIKGSEIQQRYAELMMLAAGPFSLPFIEEAMEAGWQGNFPGGVTAN
APLASTYFNLRKTTIYGGSNEVQRNIVAQTVLG
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