SitesBLAST
Comparing CCNA_03184 FitnessBrowser__Caulo:CCNA_03184 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)
6es9A Methylsuccinyl-coa dehydrogenase of paracoccus denitrificans with bound flavin adenine dinucleotide (see paper)
65% identity, 94% coverage: 34:561/564 of query aligns to 25:545/545 of 6es9A
- active site: F281 (= F297), T282 (= T298), A408 (= A424), R541 (= R557)
- binding coenzyme a: R75 (= R85), F467 (= F483), W470 (≠ H486)
- binding flavin-adenine dinucleotide: Q50 (= Q60), A279 (= A295), F281 (= F297), T282 (= T298), G287 (= G303), S288 (= S304), W312 (= W328), I313 (= I329), T314 (= T330), E374 (= E390), R434 (= R450), Q436 (= Q452), F437 (= F453), L441 (≠ I457), F444 (= F460), Q502 (= Q518), I503 (= I519), G505 (= G521), G506 (= G522), F528 (= F544), A531 (= A547), E533 (= E549), I534 (= I550)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
40% identity, 68% coverage: 182:563/564 of query aligns to 7:379/383 of 4iv6B
- active site: L121 (≠ F297), T122 (= T298), G240 (≠ A424), E361 (= E545), K373 (≠ R557)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ F297), T122 (= T298), G126 (≠ T302), G127 (= G303), S128 (= S304), W152 (= W328), I153 (= I329), S154 (≠ T330), R266 (= R450), S268 (≠ Q452), F269 (= F453), I273 (= I457), H276 (≠ F460), V279 (= V463), R334 (≠ Q518), V335 (≠ I519), G338 (= G522), L356 (≠ I540), G360 (≠ F544), T363 (≠ A547), E365 (= E549), I366 (= I550)
8ciwA Methylsuccinyl-coa dehydrogenase from pseudomonas migulae with bound fad and (2s)-methylsuccinyl-coa (see paper)
43% identity, 69% coverage: 174:561/564 of query aligns to 149:548/555 of 8ciwA
- binding flavin-adenine dinucleotide: I275 (≠ A295), I277 (≠ F297), T278 (= T298), G283 (= G303), S284 (= S304), W308 (= W328), T310 (= T330), R437 (= R450), V439 (≠ Q452), F440 (= F453), L444 (≠ I457), Q504 (= Q518), I505 (= I519), G508 (= G522), F530 (= F544), E535 (= E549), T536 (≠ I550)
- binding (2S)-Methylsuccinyl-CoA: R242 (= R262), S284 (= S304), V286 (≠ L306), H332 (≠ Y351), Y370 (= Y385), F401 (= F414), Y402 (≠ K415), M405 (= M418), M408 (≠ F421), R412 (= R425), R418 (= R431), F530 (= F544), E531 (= E545), G532 (= G546), R544 (= R557)
Sites not aligning to the query:
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
36% identity, 68% coverage: 179:560/564 of query aligns to 6:377/378 of 5ol2F
- active site: L124 (≠ F297), T125 (= T298), G241 (≠ A424), G374 (≠ R557)
- binding calcium ion: E29 (= E202), E33 (≠ D207), R35 (≠ L209)
- binding coenzyme a persulfide: L238 (≠ F421), R242 (= R425), E362 (= E545), G363 (= G546)
- binding flavin-adenine dinucleotide: F122 (≠ A295), L124 (≠ F297), T125 (= T298), P127 (= P300), T131 (≠ S304), F155 (≠ W328), I156 (= I329), T157 (= T330), E198 (vs. gap), R267 (= R450), F270 (= F453), L274 (≠ I457), F277 (= F460), Q335 (= Q518), L336 (≠ I519), G338 (= G521), G339 (= G522), Y361 (≠ F544), T364 (≠ A547), E366 (= E549)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
37% identity, 68% coverage: 177:559/564 of query aligns to 2:378/378 of 4n5fA
- active site: L126 (≠ F297), T127 (= T298), G243 (≠ A424), E364 (= E545), R376 (= R557)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ F297), T127 (= T298), G132 (= G303), S133 (= S304), F157 (≠ W328), T159 (= T330), T210 (≠ E390), Y363 (≠ F544), T366 (≠ A547), E368 (= E549), M372 (≠ Q553)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
37% identity, 66% coverage: 191:560/564 of query aligns to 19:377/379 of 1ukwB
- active site: L124 (≠ F297), S125 (≠ T298), T241 (≠ A424), E362 (= E545), R374 (= R557)
- binding cobalt (ii) ion: D145 (= D318), H146 (≠ S319)
- binding flavin-adenine dinucleotide: F122 (≠ A295), L124 (≠ F297), S125 (≠ T298), G130 (= G303), S131 (= S304), W155 (= W328), S157 (≠ T330), K200 (≠ V382), L357 (≠ I540), Y361 (≠ F544), E362 (= E545), T364 (≠ A547), E366 (= E549), L370 (≠ Q553)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
37% identity, 66% coverage: 191:560/564 of query aligns to 19:377/379 of 1ukwA
- active site: L124 (≠ F297), S125 (≠ T298), T241 (≠ A424), E362 (= E545), R374 (= R557)
- binding flavin-adenine dinucleotide: F122 (≠ A295), L124 (≠ F297), S125 (≠ T298), G130 (= G303), S131 (= S304), W155 (= W328), S157 (≠ T330), L357 (≠ I540), Y361 (≠ F544), E362 (= E545), T364 (≠ A547), E366 (= E549), L370 (≠ Q553)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
35% identity, 72% coverage: 153:560/564 of query aligns to 15:407/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
36% identity, 68% coverage: 177:560/564 of query aligns to 7:380/384 of 1jqiA
- active site: G377 (≠ R557)
- binding acetoacetyl-coenzyme a: L95 (≠ I265), F125 (≠ A295), S134 (= S304), F234 (= F414), M238 (= M418), Q239 (≠ A419), L241 (≠ F421), D242 (≠ E422), R245 (= R425), Y364 (≠ F544), E365 (= E545), G366 (= G546)
- binding flavin-adenine dinucleotide: F125 (≠ A295), L127 (≠ F297), S128 (≠ T298), G133 (= G303), S134 (= S304), W158 (= W328), T160 (= T330), R270 (= R450), F273 (= F453), L280 (≠ F460), Q338 (= Q518), I339 (= I519), G342 (= G522), I360 (= I540), T367 (≠ A547), E369 (= E549), I370 (= I550)
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
37% identity, 67% coverage: 177:556/564 of query aligns to 5:378/395 of 3mpiC
- active site: I128 (≠ F297), T129 (= T298), T245 (≠ A424), E367 (= E545)
- binding flavin-adenine dinucleotide: I128 (≠ F297), T129 (= T298), G134 (= G303), S135 (= S304), W159 (= W328), I160 (= I329), S161 (≠ T330), M365 (≠ I543), V366 (≠ F544), S369 (≠ A547), N371 (≠ E549), M375 (≠ Q553)
- binding glutaryl-coenzyme A: R87 (= R262), F126 (≠ A295), S135 (= S304), V137 (≠ L306), S181 (≠ D350), F239 (≠ M418), R246 (= R425), N315 (≠ C494), V366 (≠ F544), E367 (= E545), G368 (= G546), I376 (≠ V554)
Sites not aligning to the query:
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
37% identity, 67% coverage: 177:556/564 of query aligns to 5:378/389 of C3UVB0
- A80 (≠ S250) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (= R262) binding
- V88 (≠ S263) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ A266) binding
- FGIT 126:129 (≠ AVFT 295:298) binding
- S135 (= S304) binding ; binding
- WIS 159:161 (≠ WIT 328:330) binding
- S181 (≠ D350) binding
- R271 (= R450) binding
- FQMN 281:284 (≠ FPRV 460:463) binding
- R340 (≠ Q518) binding
- A344 (≠ G522) binding
- V366 (≠ F544) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ EGAGE 545:549) binding
Sites not aligning to the query:
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
37% identity, 67% coverage: 177:556/564 of query aligns to 5:378/393 of 3mpjB
- active site: I128 (≠ F297), T129 (= T298), T245 (≠ A424), E367 (= E545)
- binding flavin-adenine dinucleotide: F126 (≠ A295), I128 (≠ F297), T129 (= T298), G134 (= G303), S135 (= S304), W159 (= W328), I160 (= I329), S161 (≠ T330), V366 (≠ F544), S369 (≠ A547), N371 (≠ E549), M375 (≠ Q553)
- binding : H36 (≠ E208), F37 (≠ L209), Y39 (≠ P211), A164 (= A333), Q165 (≠ R334), D167 (= D336), N193 (≠ G364)
Sites not aligning to the query:
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
36% identity, 68% coverage: 177:560/564 of query aligns to 34:407/412 of P16219
- G90 (= G234) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E248) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 295:304, 40% identical) binding in other chain
- R171 (≠ E314) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 328:330) binding in other chain
- A192 (= A335) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G353) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R450) binding
- Q308 (≠ P461) binding in other chain
- R325 (= R478) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ A506) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIHGG 518:522) binding
- R380 (= R533) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ AGE 547:549) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
37% identity, 68% coverage: 179:559/564 of query aligns to 6:376/376 of 4m9aB
- active site: L124 (≠ F297), T125 (= T298), G241 (≠ A424), E362 (= E545), R374 (= R557)
- binding dihydroflavine-adenine dinucleotide: F122 (≠ A295), T125 (= T298), G130 (= G303), S131 (= S304), F155 (≠ W328), T157 (= T330), T208 (≠ E390), Y361 (≠ F544), T364 (≠ A547), E366 (= E549), M370 (≠ Q553)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
36% identity, 68% coverage: 177:560/564 of query aligns to 4:377/381 of 8sgsA
- binding coenzyme a: S131 (= S304), A133 (≠ L306), N177 (≠ D350), F231 (= F414), M235 (= M418), L238 (≠ F421), I312 (≠ D495), E362 (= E545), G363 (= G546)
- binding flavin-adenine dinucleotide: F122 (≠ A295), L124 (≠ F297), S125 (≠ T298), G130 (= G303), S131 (= S304), W155 (= W328), T157 (= T330), R267 (= R450), F270 (= F453), L274 (≠ I457), L277 (≠ F460), Q335 (= Q518), I336 (= I519), G338 (= G521), G339 (= G522), I357 (= I540), I360 (= I543), Y361 (≠ F544), T364 (≠ A547), E366 (= E549)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
36% identity, 68% coverage: 177:560/564 of query aligns to 7:380/385 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 (≠ N523), T347 (≠ M527), E348 (= E528)
- binding flavin-adenine dinucleotide: F125 (≠ A295), L127 (≠ F297), S128 (≠ T298), G133 (= G303), S134 (= S304), W158 (= W328), T160 (= T330), R270 (= R450), F273 (= F453), L280 (≠ F460), V282 (≠ R462), Q338 (= Q518), I339 (= I519), G342 (= G522), I360 (= I540), Y364 (≠ F544), T367 (≠ A547), E369 (= E549), I370 (= I550), L373 (≠ Q553)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
36% identity, 68% coverage: 177:560/564 of query aligns to 10:383/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ A295), L130 (≠ F297), S131 (≠ T298), G136 (= G303), S137 (= S304), W161 (= W328), T163 (= T330), T214 (≠ E390), R273 (= R450), F276 (= F453), L280 (≠ I457), L283 (≠ F460), V285 (≠ R462), Q341 (= Q518), I342 (= I519), G345 (= G522), I363 (= I540), Y367 (≠ F544), T370 (≠ A547), E372 (= E549), L376 (≠ Q553)
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
35% identity, 68% coverage: 176:561/564 of query aligns to 1:384/388 of 2a1tC
- active site: V127 (≠ F297), T128 (= T298), T247 (≠ A424), E368 (= E545), R380 (= R557)
- binding flavin-adenine dinucleotide: Y125 (≠ A295), V127 (≠ F297), T128 (= T298), G133 (= G303), S134 (= S304), Q155 (≠ N325), W158 (= W328), W158 (= W328), I159 (= I329), T160 (= T330), R273 (= R450), T275 (≠ Q452), F276 (= F453), L280 (≠ I457), H283 (≠ F460), I286 (≠ V463), Q341 (= Q518), I342 (= I519), G345 (= G522), I363 (= I540), T370 (≠ A547), Q372 (≠ E549)
P11310 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; Medium chain acyl-CoA dehydrogenase; MCADH; EC 1.3.8.7 from Homo sapiens (Human) (see 16 papers)
35% identity, 69% coverage: 174:561/564 of query aligns to 32:417/421 of P11310
- Y67 (≠ W203) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (≠ V223) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (≠ S235) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (≠ M237) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (≠ V245) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (≠ L269) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 295:304, 50% identical) binding in other chain
- S167 (= S304) binding
- W191 (= W328) mutation to A: Loss of electron transfer to ETF.; mutation to F: Reduces rate of electron transfer to ETF about six-fold.
- WIT 191:193 (= WIT 328:330) binding in other chain
- T193 (= T330) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (= E379) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (≠ E422) binding
- T280 (≠ A424) mutation to E: Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410.
- R281 (= R425) binding ; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ RKQ 450:452) binding
- HQ 316:317 (≠ FP 460:461) binding in other chain
- K329 (≠ E473) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ QIHGG 518:522) binding
- E384 (= E528) mutation to A: Reduces rate of electron transfer to ETF three-fold.; mutation to Q: Reduces rate of electron transfer to ETF two-fold.
- E401 (= E545) active site, Proton acceptor; binding ; mutation to G: Changed substrate specificity towards longer acyl chains; when associated with E-280.; mutation to Q: Loss of acyl-CoA dehydrogenase activity.; mutation to T: Loss of acyl-CoA dehydrogenase activity; when associated with E-280.
- EGTSQ 401:405 (≠ EGAGE 545:549) binding in other chain
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
35% identity, 67% coverage: 180:557/564 of query aligns to 3:378/385 of 3mdeA
- active site: V125 (≠ F297), T126 (= T298), T245 (≠ A424), E366 (= E545), R378 (= R557)
- binding octanoyl-coenzyme a: T86 (≠ S258), E89 (≠ T261), L93 (≠ I265), S132 (= S304), V134 (≠ L306), S181 (≠ T348), F235 (= F414), M239 (= M418), F242 (= F421), R314 (= R493), Y365 (≠ F544), E366 (= E545), G367 (= G546)
- binding flavin-adenine dinucleotide: Y123 (≠ A295), V125 (≠ F297), T126 (= T298), G131 (= G303), S132 (= S304), W156 (= W328), I157 (= I329), T158 (= T330), R271 (= R450), T273 (≠ Q452), F274 (= F453), L278 (≠ I457), H281 (≠ F460), Q339 (= Q518), V340 (≠ I519), G343 (= G522), I361 (= I540), T368 (≠ A547), Q370 (≠ E549)
Query Sequence
>CCNA_03184 FitnessBrowser__Caulo:CCNA_03184
MTDTVSENTNETLILPGLTGLLREAADAVALFVAEAKPAVLAHIAPQGGKVDRKLADVHQ
HRVHGYGWYASYAELMNQVAGWAQRLEAEGRFGEIEALLAQLLFSEYSAQLVGGVPMNQG
EIVRPQHLVEDRAVLNRLTSEAMTRLAAEGGSQAVKARIAQRLAEARGRPTLEQTGLDET
FEMIRDQFHAFAEEKVTPFAHEWHLKDELIPLELVQELGELGVFGLTIPEEFGGSGMGKT
AMCVVSEELSRAWIGVGSLATRSEIAGELILTGGTDAQKEYWLPRIASAEILPTAVFTEP
NTGSDLGALRTRAELKGDSYVVTGNKTWITHAARADVMTLLVRTDPATTDYRGLSMLLAP
KPRGTDEAPFPAEGMSGGEIGVIGYRGMKEYELGFDGFTVPAENLLGGVTGQGFKQLMAT
FESARIQTAARAVGVAQAALEVGLSYALDRKQFGQPIFDFPRVHNKLAMMAAEIMGVRQL
TYFAAHQKDEGKRCDLEAGMAKLIAARVAWAAADNALQIHGGNGFAMEYAASRLLADARI
LNIFEGAGEIQAQVIARRLLDGGN
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