SitesBLAST
Comparing CCNA_01883 FitnessBrowser__Caulo:CCNA_01883 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
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, 63% coverage: 1:245/390 of query aligns to 1:242/387 of P71858
- E241 (= E244) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
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: 1:390/390 of query aligns to 1:395/400 of I6YCA3
- IGYS 127:130 (≠ QGYS 126:129) binding
- T136 (≠ S135) binding
- S162 (= S161) binding
- E247 (= E244) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ SNE 375:377) binding
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
34% identity, 100% coverage: 1:390/390 of query aligns to 1:382/386 of 4x28A
- active site: Y122 (= Y128), S123 (= S129), E240 (= E244), G365 (= G373), M377 (≠ R385)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), S123 (= S129), G128 (= G134), T129 (≠ S135), W153 (= W159), S155 (= S161), F363 (≠ I371), T367 (≠ S375), E369 (= E377), V370 (≠ I378)
6wy8B Tcur3481-tcur3483 steroid acad (see paper)
34% identity, 100% coverage: 1:390/390 of query aligns to 1:381/384 of 6wy8B
- active site: Y126 (= Y128), T127 (≠ S129), E241 (= E244), T376 (≠ R385)
- binding flavin-adenine dinucleotide: I124 (≠ Q126), Y126 (= Y128), T127 (≠ S129), G132 (= G134), T133 (≠ S135), F157 (≠ W159), S159 (= S161), V359 (= V368), F362 (≠ I371), G363 (≠ Y372), V366 (≠ S375), E368 (= E377)
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: 47:390/390 of query aligns to 385:709/711 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.
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
34% identity, 98% coverage: 10:390/390 of query aligns to 6:377/380 of 6wy9A
- active site: Y122 (= Y128), T123 (≠ S129), E237 (= E244), T372 (≠ R385)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), T123 (≠ S129), G128 (= G134), T129 (≠ S135), F153 (≠ W159), S155 (= S161), F358 (≠ I371), V362 (≠ S375), E364 (= E377)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
31% identity, 98% coverage: 6:388/390 of query aligns to 7:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S135), T134 (≠ L137), R180 (≠ A183), R234 (≠ S235), L237 (≠ K238), R238 (≠ V239), L240 (= L241), D241 (= D242), R244 (= R245), E365 (≠ G373), G366 (= G374), R377 (= R385)
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), L125 (≠ Y128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), T158 (≠ S161), I360 (≠ V368), T367 (≠ S375), Q369 (≠ E377)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
31% identity, 98% coverage: 6:388/390 of query aligns to 7:380/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), L125 (≠ Y128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), T158 (≠ S161), I360 (≠ V368), Y364 (= Y372), T367 (≠ S375), Q369 (≠ E377)
7w0jE Acyl-coa dehydrogenase, tfu_1647
31% identity, 98% coverage: 6:388/390 of query aligns to 8:381/382 of 7w0jE
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-azanyl-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate: S127 (= S129), W157 (= W159), R270 (≠ T269), Q272 (≠ V271), F273 (≠ G272), I277 (≠ L276), F280 (≠ D279), I283 (≠ V282), Q339 (≠ E337), L340 (= L338), G343 (= G350), Y365 (= Y372), E366 (≠ G373), T368 (≠ S375), Q370 (≠ E377), I371 (= I378)
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
28% identity, 98% coverage: 5:386/390 of query aligns to 5:377/380 of 2pg0A
- active site: M124 (≠ Y128), T125 (≠ S129), E243 (= E244), A364 (≠ G373), R376 (= R385)
- binding flavin-adenine dinucleotide: I122 (≠ Q126), M124 (≠ Y128), T125 (≠ S129), G130 (= G134), S131 (= S135), F155 (≠ W159), I156 (≠ T160), T157 (≠ S161), R269 (≠ T269), F272 (≠ G272), F279 (≠ D279), Q337 (≠ E337), L338 (= L338), G340 (= G340), G341 (≠ A345), V359 (= V368), I362 (= I371), Y363 (= Y372), T366 (≠ S375), E368 (= E377), M369 (≠ I378)
6es9A Methylsuccinyl-coa dehydrogenase of paracoccus denitrificans with bound flavin adenine dinucleotide (see paper)
29% identity, 97% coverage: 12:388/390 of query aligns to 168:544/545 of 6es9A
- active site: F281 (≠ Y128), T282 (≠ S129), A408 (≠ E244), R541 (= R385)
- binding coenzyme a: F467 (≠ R302), W470 (≠ A305)
- binding flavin-adenine dinucleotide: A279 (≠ Q126), F281 (≠ Y128), T282 (≠ S129), G287 (= G134), S288 (= S135), W312 (= W159), I313 (≠ T160), T314 (≠ S161), E374 (≠ T211), R434 (≠ T269), Q436 (≠ V271), F437 (≠ G272), L441 (= L276), F444 (≠ D279), Q502 (≠ E337), I503 (≠ L338), G505 (= G340), G506 (≠ Y341), F528 (≠ Y372), A531 (≠ S375), E533 (= E377), I534 (= I378)
Sites not aligning to the query:
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)
30% identity, 97% coverage: 11:388/390 of query aligns to 3:368/369 of 3pfdC
- active site: L116 (≠ Y128), S117 (= S129), T233 (≠ E244), E353 (≠ G373), R365 (= R385)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ Q126), L116 (≠ Y128), S117 (= S129), G122 (= G134), S123 (= S135), W147 (= W159), I148 (≠ T160), T149 (≠ S161), R259 (≠ T269), F262 (≠ G272), V266 (≠ L276), N269 (≠ D279), Q326 (≠ E337), L327 (= L338), G330 (≠ A343), I348 (≠ V368), Y352 (= Y372), T355 (≠ S375), Q357 (≠ E377)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
29% identity, 99% coverage: 3:388/390 of query aligns to 1:377/378 of 5ol2F
- active site: L124 (≠ Y128), T125 (≠ S129), G241 (≠ E244), G374 (≠ R385)
- binding calcium ion: E29 (≠ R31), E33 (≠ G35), R35 (= R37)
- binding coenzyme a persulfide: L238 (= L241), R242 (= R245), E362 (≠ G373), G363 (= G374)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), T125 (≠ S129), P127 (= P131), T131 (≠ S135), F155 (≠ W159), I156 (≠ T160), T157 (≠ S161), E198 (≠ P201), R267 (≠ T269), F270 (≠ G272), L274 (= L276), F277 (≠ D279), Q335 (≠ E337), L336 (= L338), G338 (= G340), G339 (= G350), Y361 (= Y372), T364 (≠ S375), E366 (= E377)
1egcA Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa (see paper)
29% identity, 99% coverage: 1:388/390 of query aligns to 3:382/387 of 1egcA
- active site: V126 (≠ Y128), T127 (≠ S129), E246 (= E244), G367 (= G373), R379 (= R385)
- binding octanoyl-coenzyme a: E90 (≠ G93), L94 (≠ I97), Y124 (≠ Q126), S133 (= S135), V135 (≠ L137), N182 (≠ G184), F236 (≠ W234), M240 (≠ K238), F243 (≠ L241), D244 (= D242), R247 (= R245), Y366 (= Y372), G367 (= G373), G368 (= G374)
- binding flavin-adenine dinucleotide: Y124 (≠ Q126), V126 (≠ Y128), T127 (≠ S129), G132 (= G134), S133 (= S135), W157 (= W159), T159 (≠ S161), R272 (≠ T269), T274 (≠ V271), F275 (≠ G272), L279 (= L276), H282 (≠ D279), I285 (≠ V282), Q340 (≠ E337), I341 (≠ L338), G344 (≠ Y341), I362 (≠ V368), I365 (= I371), Y366 (= Y372), T369 (≠ S375), Q371 (≠ E377)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
29% identity, 100% coverage: 1:389/390 of query aligns to 37:417/421 of P41367
- 158:167 (vs. 126:135, 40% identical) binding in other chain
- S167 (= S135) binding
- WIT 191:193 (≠ WTS 159:161) binding in other chain
- S216 (≠ G184) binding
- D278 (= D242) binding
- R281 (= R245) binding
- RKT 306:308 (≠ TMV 269:271) binding
- HQ 316:317 (≠ DP 279:280) binding in other chain
- R349 (≠ D312) binding
- T351 (≠ G314) binding
- QVFGG 374:378 (≠ ELQGY 337:341) binding
- E401 (≠ G373) active site, Proton acceptor; binding
- GTAQ 402:405 (≠ GSNE 374:377) binding in other chain
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
29% identity, 100% coverage: 1:389/390 of query aligns to 2:382/385 of 3mdeA
- active site: V125 (≠ Y128), T126 (≠ S129), T245 (≠ E244), E366 (≠ G373), R378 (= R385)
- binding octanoyl-coenzyme a: T86 (≠ F90), E89 (≠ G93), L93 (≠ I97), S132 (= S135), V134 (≠ L137), S181 (≠ G184), F235 (≠ W234), M239 (≠ K238), F242 (≠ L241), R314 (≠ D312), Y365 (= Y372), E366 (≠ G373), G367 (= G374)
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), V125 (≠ Y128), T126 (≠ S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), T158 (≠ S161), R271 (≠ T269), T273 (≠ V271), F274 (≠ G272), L278 (= L276), H281 (≠ D279), Q339 (≠ E337), V340 (≠ L338), G343 (≠ Y341), I361 (≠ V368), T368 (≠ S375), Q370 (≠ E377)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
29% identity, 100% coverage: 1:389/390 of query aligns to 2:382/385 of 3mddA
- active site: V125 (≠ Y128), T126 (≠ S129), T245 (≠ E244), E366 (≠ G373), R378 (= R385)
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), T126 (≠ S129), G131 (= G134), S132 (= S135), W156 (= W159), T158 (≠ S161), R271 (≠ T269), T273 (≠ V271), F274 (≠ G272), H281 (≠ D279), Q339 (≠ E337), V340 (≠ L338), G343 (≠ Y341), I361 (≠ V368), T368 (≠ S375), Q370 (≠ E377)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
29% identity, 100% coverage: 1:389/390 of query aligns to 2:382/385 of 1udyA
- active site: V125 (≠ Y128), T126 (≠ S129), T245 (≠ E244), E366 (≠ G373), R378 (= R385)
- binding 3-thiaoctanoyl-coenzyme a: L93 (≠ I97), Y123 (≠ Q126), S132 (= S135), S181 (≠ G184), F235 (≠ W234), M239 (≠ K238), F242 (≠ L241), V249 (≠ T248), R314 (≠ D312), Y365 (= Y372), E366 (≠ G373), G367 (= G374), I371 (= I378), I375 (= I382)
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), T126 (≠ S129), G131 (= G134), S132 (= S135), W156 (= W159), T158 (≠ S161), T273 (≠ V271), F274 (≠ G272), Q339 (≠ E337), V340 (≠ L338), G343 (≠ Y341), T368 (≠ S375), Q370 (≠ E377)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
30% identity, 88% coverage: 45:389/390 of query aligns to 37:374/374 of 5lnxD
- active site: L122 (≠ Y128), T123 (≠ S129), G239 (≠ E244), E358 (≠ G373), K370 (≠ R385)
- binding flavin-adenine dinucleotide: L122 (≠ Y128), T123 (≠ S129), G128 (= G134), S129 (= S135), F153 (≠ W159), T155 (≠ S161), R265 (≠ T269), Q267 (≠ V271), F268 (≠ G272), I272 (≠ L276), N275 (≠ D279), I278 (≠ V282), Q331 (≠ V336), I332 (≠ E337), G335 (= G340), Y357 (= Y372), T360 (≠ S375), E362 (= E377)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
29% identity, 98% coverage: 5:386/390 of query aligns to 53:425/430 of P51174
- K318 (≠ M270) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ R274) 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.
Query Sequence
>CCNA_01883 FitnessBrowser__Caulo:CCNA_01883
MNLDLTPEQSAFRDEVRAFFAENVPESFKSRVRAGMRLEPHEFTQWQKLLYARGWGAPSW
PKEYGGTGWDPTKLYIFETEASRADAPVQFHQGLELIGPIIFTFGSPEQKAKYLPAIVSG
DDWWCQGYSEPNSGSDLASLSTRAVRDGNEYVINGQKAWTSYAHVANRMFLLARTDPDAR
KQAGISLFLIDIDTPGVTIRPVVTMDEIHHTNEVFLDNVRVPPSALLGEEGMGWSYGKVL
LDRERGVTAATTTRLAQQLRGARKVAAETMVGGRSLLDDPRVADRLAQFELEVMALEGMV
MRTMAEATSGQDSGPRASMIKIRWSELLQQITEYWVELQGYDAMAFAPLGPFEAPDAWAA
KGMIYSRVTSIYGGSNEIQRNIIARRALGL
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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