SitesBLAST
Comparing CCNA_01368 FitnessBrowser__Caulo:CCNA_01368 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)
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)
32% identity, 100% coverage: 1:404/404 of query aligns to 1:395/400 of I6YCA3
- IGYS 127:130 (≠ QGYS 126:129) binding
- T136 (≠ S135) binding
- S162 (≠ T166) binding
- E247 (= E249) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ SNE 389:391) binding
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
33% identity, 100% coverage: 1:404/404 of query aligns to 1:382/386 of 4x28A
- active site: Y122 (= Y128), S123 (= S129), E240 (= E249), G365 (= G387), M377 (≠ K399)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), S123 (= S129), G128 (= G134), T129 (≠ S135), W153 (= W164), S155 (≠ T166), F363 (≠ I385), T367 (≠ S389), E369 (= E391), V370 (≠ I392)
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: 50:404/404 of query aligns to 388:709/711 of P96855
- E581 (= E249) 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.
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, 99% coverage: 1:398/404 of query aligns to 1:376/387 of P71858
- E241 (= E249) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
32% identity, 97% coverage: 12:404/404 of query aligns to 8:377/380 of 6wy9A
- active site: Y122 (= Y128), T123 (≠ S129), E237 (= E249), T372 (≠ K399)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), T123 (≠ S129), G128 (= G134), T129 (≠ S135), F153 (≠ W164), S155 (≠ T166), F358 (≠ I385), V362 (≠ S389), E364 (= E391)
6wy8B Tcur3481-tcur3483 steroid acad (see paper)
31% identity, 97% coverage: 12:404/404 of query aligns to 12:381/384 of 6wy8B
- active site: Y126 (= Y128), T127 (≠ S129), E241 (= E249), T376 (≠ K399)
- binding flavin-adenine dinucleotide: I124 (≠ Q126), Y126 (= Y128), T127 (≠ S129), G132 (= G134), T133 (≠ S135), F157 (≠ W164), S159 (≠ T166), V359 (≠ K382), F362 (≠ I385), G363 (≠ Y386), V366 (≠ S389), E368 (= E391)
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
28% identity, 87% coverage: 50:401/404 of query aligns to 45:378/380 of 2pg0A
- active site: M124 (≠ Y128), T125 (≠ S129), E243 (= E249), A364 (≠ G387), R376 (≠ K399)
- binding flavin-adenine dinucleotide: I122 (≠ Q126), M124 (≠ Y128), T125 (≠ S129), G130 (= G134), S131 (= S135), F155 (≠ W164), I156 (≠ T165), T157 (= T166), R269 (≠ L274), F272 (≠ D277), F279 (≠ D284), Q337 (≠ E342), L338 (≠ A343), G340 (= G345), G341 (≠ H346), V359 (≠ K382), I362 (= I385), Y363 (= Y386), T366 (≠ S389), E368 (= E391), M369 (≠ I392)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
31% identity, 88% coverage: 50:403/404 of query aligns to 45:378/379 of 1ukwB
- active site: L124 (≠ Y128), S125 (= S129), T241 (≠ E249), E362 (≠ G387), R374 (≠ K399)
- binding cobalt (ii) ion: D145 (= D150), H146 (≠ Y155)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W164), S157 (≠ T166), K200 (≠ L210), L357 (≠ K382), Y361 (= Y386), E362 (≠ G387), T364 (≠ S389), E366 (= E391), L370 (≠ N395)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
31% identity, 88% coverage: 50:403/404 of query aligns to 45:378/379 of 1ukwA
- active site: L124 (≠ Y128), S125 (= S129), T241 (≠ E249), E362 (≠ G387), R374 (≠ K399)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W164), S157 (≠ T166), L357 (≠ K382), Y361 (= Y386), E362 (≠ G387), T364 (≠ S389), E366 (= E391), L370 (≠ N395)
8hk0B Crystal structure of fic32-33 complex from streptomyces ficellus nrrl 8067 (see paper)
29% identity, 95% coverage: 15:398/404 of query aligns to 24:370/379 of 8hk0B
- binding flavin-adenine dinucleotide: V126 (≠ Q126), Y128 (= Y128), T129 (≠ S129), G134 (= G134), S135 (= S135), F159 (≠ W164), S160 (≠ T165), L161 (≠ T166), G354 (≠ T376), S358 (≠ Y386), T361 (≠ S389), E363 (= E391)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
27% identity, 99% coverage: 5:402/404 of query aligns to 3:377/379 of 6fahD
- active site: L124 (≠ Y128), T125 (≠ S129), G241 (≠ E249), G374 (≠ K399)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), T125 (≠ S129), R152 (≠ Q161), F155 (≠ W164), T157 (= T166), E198 (= E213), R267 (≠ L274), Q269 (≠ D276), F270 (≠ D277), I274 (≠ L281), F277 (≠ D284), Q335 (≠ E342), I336 (≠ A343), G339 (≠ H346), Y361 (= Y386), T364 (≠ S389), Q366 (≠ E391)
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, 97% coverage: 10:402/404 of query aligns to 2:368/369 of 3pfdC
- active site: L116 (≠ Y128), S117 (= S129), T233 (≠ E249), E353 (≠ G387), R365 (≠ K399)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ Q126), L116 (≠ Y128), S117 (= S129), G122 (= G134), S123 (= S135), W147 (= W164), I148 (≠ T165), T149 (= T166), R259 (≠ G278), F262 (≠ L281), V266 (≠ M286), N269 (≠ R289), Q326 (≠ E342), L327 (≠ A343), G330 (≠ H346), I348 (≠ K382), Y352 (= Y386), T355 (≠ S389), Q357 (≠ E391)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
26% identity, 99% coverage: 5:402/404 of query aligns to 53:427/430 of P51174
- K318 (≠ S275) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ D279) 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.
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
29% identity, 77% coverage: 93:402/404 of query aligns to 86:376/383 of 4iv6B
- active site: L121 (≠ Y128), T122 (≠ S129), G240 (≠ S251), E361 (vs. gap), K373 (= K399)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ Y128), T122 (≠ S129), G126 (≠ A133), G127 (= G134), S128 (= S135), W152 (= W164), I153 (≠ T165), S154 (≠ T166), R266 (≠ G278), S268 (≠ A280), F269 (≠ L281), I273 (≠ P285), H276 (≠ K288), V279 (= V291), R334 (≠ E342), V335 (≠ A343), G338 (≠ H346), L356 (≠ T383), G360 (= G387), T363 (≠ S389), E365 (= E391), I366 (= I392)
1egcA Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa (see paper)
27% identity, 86% coverage: 54:399/404 of query aligns to 51:379/387 of 1egcA
- active site: V126 (≠ Y128), T127 (≠ S129), E246 (= E249), G367 (= G387), R379 (≠ K399)
- binding octanoyl-coenzyme a: E90 (≠ G93), L94 (≠ V97), Y124 (≠ Q126), S133 (= S135), V135 (≠ L137), N182 (≠ G189), F236 (≠ W239), M240 (≠ K243), F243 (≠ L246), D244 (≠ A247), R247 (= R250), Y366 (= Y386), G367 (= G387), G368 (= G388)
- binding flavin-adenine dinucleotide: Y124 (≠ Q126), V126 (≠ Y128), T127 (≠ S129), G132 (= G134), S133 (= S135), W157 (= W164), T159 (= T166), R272 (≠ L274), T274 (≠ D276), F275 (≠ D277), L279 (= L281), H282 (≠ D284), I285 (≠ F287), Q340 (≠ E342), I341 (≠ A343), G344 (≠ H346), I362 (≠ T376), I365 (= I385), Y366 (= Y386), T369 (≠ S389), Q371 (≠ E391)
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, 98% coverage: 5:401/404 of query aligns to 57:428/432 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. 126:135, 60% identical) binding in other chain
- S183 (= S135) binding
- WIS 207:209 (≠ WTT 164:166) binding in other chain
- S210 (≠ M167) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ I186) binding
- L255 (vs. gap) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ W239) binding
- NEGR 291:294 (≠ AHER 247:250) binding
- I316 (= I266) to V: in dbSNP:rs1131430
- R319 (≠ L274) binding
- Q330 (≠ P285) binding
- EWMG--G 387:391 (≠ EAAGHYG 342:348) binding
- A416 (≠ S389) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ SNE 389:391) 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)
29% identity, 98% coverage: 5:401/404 of query aligns to 6:377/381 of 2jifA
- active site: L125 (≠ Y128), S126 (= S129), G242 (≠ E249), E363 (≠ G387), K375 (= K399)
- binding coenzyme a persulfide: S132 (= S135), S134 (≠ L137), Y178 (≠ I186), Y232 (≠ W239), I236 (≠ K243), L239 (= L246), N240 (≠ A247), R243 (= R250), Y362 (= Y386), E363 (≠ G387), G364 (= G388), I368 (= I392)
- binding flavin-adenine dinucleotide: F123 (≠ Q126), L125 (≠ Y128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W164), I157 (≠ T165), S158 (≠ T166), K201 (≠ T209), T209 (≠ V216), R268 (≠ L274), F271 (≠ D277), L275 (= L281), F278 (≠ D284), L281 (≠ F287), E336 (= E342), W337 (≠ A343), G340 (= G348), N367 (≠ E391), I368 (= I392)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
27% identity, 99% coverage: 3:402/404 of query aligns to 1:377/378 of 5ol2F
- active site: L124 (≠ Y128), T125 (≠ S129), G241 (≠ E249), G374 (≠ K399)
- binding calcium ion: E29 (≠ K31), E33 (≠ G35), R35 (≠ E37)
- binding coenzyme a persulfide: L238 (= L246), R242 (= R250), E362 (≠ G387), G363 (= G388)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), T125 (≠ S129), P127 (= P131), T131 (≠ S135), F155 (≠ W164), I156 (≠ T165), T157 (= T166), E198 (≠ V204), R267 (≠ L274), F270 (≠ D277), L274 (= L281), F277 (≠ D284), Q335 (≠ E342), L336 (≠ A343), G338 (= G345), G339 (≠ H346), Y361 (= Y386), T364 (≠ S389), E366 (= E391)
2z1qB Crystal structure of acyl coa dehydrogenase
28% identity, 99% coverage: 5:402/404 of query aligns to 19:409/549 of 2z1qB
- active site: L144 (≠ Y128), T145 (≠ S129), G259 (≠ A247), E394 (≠ G387), G406 (≠ K399)
- binding flavin-adenine dinucleotide: Y142 (≠ Q126), L144 (≠ Y128), T145 (≠ S129), G150 (= G134), S151 (= S135), W177 (= W164), S179 (≠ T166), R285 (≠ L274), F288 (≠ D277), I292 (≠ L281), F295 (≠ D284), I298 (≠ F287), H369 (≠ A344), G370 (= G345), F393 (≠ Y386), I399 (= I392)
Sites not aligning to the query:
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
29% identity, 98% coverage: 6:401/404 of query aligns to 6:377/378 of 3r7kA
- active site: V126 (≠ Y128), T127 (≠ S129), E242 (= E249), G363 (= G387), K375 (= K399)
- binding dihydroflavine-adenine dinucleotide: V126 (≠ Y128), T127 (≠ S129), G132 (= G134), S133 (= S135), F157 (≠ W164), I158 (≠ T165), T159 (= T166), R268 (≠ L274), T270 (≠ D276), F271 (≠ D277), L275 (= L281), R278 (≠ D284), I281 (≠ F287), Q336 (≠ E342), I337 (≠ A343), G340 (≠ H346), I358 (≠ K382), T365 (≠ S389), E367 (= E391)
Query Sequence
>CCNA_01368 FitnessBrowser__Caulo:CCNA_01368
MNLDFSPEDLAFRDEVRAFIAENYPAGLRDKQEEGEEMAKEDFLSWHRVLANKGWVAPAW
PTQYGGPGWTSVQRYIWSEETARADCVPILPFGINMVGPVIYTFGTPEQKERFLPGTLSG
DIWWSQGYSEPGAGSDLASLKTKAERFTGDDGKEYYLVNGQKTWTTMAQHGDWIFCLVRT
DPNAKIQEGISFLLIDMKSPGVTVRPIITLGGEHEVNEVWFENVKVPVENRIYDENKGWT
CAKFLLAHERSGIAGVARSKRGIERIRQIASTELSDDGDALIKDPMFKRKVAELEIDLTA
LEYTELRTLAGEAAGRGPGPESSVLKIKGTEIQQRLTELALEAAGHYGAPYFRGFPKDGD
NAHPIGPEFAHRAAPTYFNVRKTSIYGGSNEIQRNIIAKMVLGL
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