SitesBLAST
Comparing CCNA_01875 FitnessBrowser__Caulo:CCNA_01875 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)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
41% identity, 97% coverage: 10:378/381 of query aligns to 11:378/378 of 5ol2F
- active site: L124 (= L123), T125 (= T124), G241 (= G241), G374 (≠ R374)
- binding calcium ion: E29 (≠ L28), E33 (≠ T32), R35 (≠ E34)
- binding coenzyme a persulfide: L238 (= L238), R242 (= R242), E362 (= E362), G363 (= G363)
- binding flavin-adenine dinucleotide: F122 (= F121), L124 (= L123), T125 (= T124), P127 (≠ A126), T131 (≠ S130), F155 (≠ Y154), I156 (= I155), T157 (= T156), E198 (= E198), R267 (= R267), F270 (= F270), L274 (≠ I274), F277 (= F277), Q335 (= Q335), L336 (≠ V336), G338 (= G338), G339 (= G339), Y361 (= Y361), T364 (≠ A364), E366 (≠ Q366)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
42% identity, 98% coverage: 8:379/381 of query aligns to 7:379/379 of 6fahD
- active site: L124 (= L123), T125 (= T124), G241 (= G241), G374 (≠ R374)
- binding flavin-adenine dinucleotide: F122 (= F121), L124 (= L123), T125 (= T124), R152 (≠ V151), F155 (≠ Y154), T157 (= T156), E198 (= E198), R267 (= R267), Q269 (= Q269), F270 (= F270), I274 (= I274), F277 (= F277), Q335 (= Q335), I336 (≠ V336), G339 (= G339), Y361 (= Y361), T364 (≠ A364), Q366 (= Q366)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
42% identity, 96% coverage: 12:375/381 of query aligns to 15:377/378 of 4n5fA
- active site: L126 (= L123), T127 (= T124), G243 (= G241), E364 (= E362), R376 (= R374)
- binding dihydroflavine-adenine dinucleotide: L126 (= L123), T127 (= T124), G132 (= G129), S133 (= S130), F157 (≠ Y154), T159 (= T156), T210 (≠ I208), Y363 (= Y361), T366 (≠ A364), E368 (≠ Q366), M372 (≠ L370)
7w0jE Acyl-coa dehydrogenase, tfu_1647
41% identity, 97% coverage: 9:378/381 of query aligns to 13:382/382 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 (≠ T124), W157 (≠ Y154), R270 (= R267), Q272 (= Q269), F273 (= F270), I277 (= I274), F280 (= F277), I283 (= I280), Q339 (= Q335), L340 (≠ V336), G343 (= G339), Y365 (= Y361), E366 (= E362), T368 (≠ A364), Q370 (= Q366), I371 (= I367)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
41% identity, 97% coverage: 9:378/381 of query aligns to 12:381/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S130), T134 (≠ S132), R180 (≠ A178), R234 (≠ T232), L237 (≠ M235), R238 (= R236), L240 (= L238), D241 (= D239), R244 (= R242), E365 (= E362), G366 (= G363), R377 (= R374)
- binding flavin-adenine dinucleotide: Y123 (≠ F121), L125 (= L123), S126 (≠ T124), G131 (= G129), S132 (= S130), W156 (≠ Y154), I157 (= I155), T158 (= T156), I360 (= I357), T367 (≠ A364), Q369 (= Q366)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
41% identity, 97% coverage: 9:378/381 of query aligns to 12:381/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ F121), L125 (= L123), S126 (≠ T124), G131 (= G129), S132 (= S130), W156 (≠ Y154), I157 (= I155), T158 (= T156), I360 (= I357), Y364 (= Y361), T367 (≠ A364), Q369 (= Q366)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
39% identity, 96% coverage: 13:377/381 of query aligns to 12:373/374 of 5lnxD
- active site: L122 (= L123), T123 (= T124), G239 (= G241), E358 (= E362), K370 (≠ R374)
- binding flavin-adenine dinucleotide: L122 (= L123), T123 (= T124), G128 (= G129), S129 (= S130), F153 (≠ Y154), T155 (= T156), R265 (= R267), Q267 (= Q269), F268 (= F270), I272 (= I274), N275 (≠ F277), I278 (= I280), Q331 (= Q335), I332 (≠ V336), G335 (= G339), Y357 (= Y361), T360 (≠ A364), E362 (≠ Q366)
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
44% identity, 97% coverage: 10:378/381 of query aligns to 8:370/370 of 2dvlA
- active site: L121 (= L123), T122 (= T124), G233 (= G241), E354 (= E362), R366 (= R374)
- binding flavin-adenine dinucleotide: L121 (= L123), T122 (= T124), G127 (= G129), S128 (= S130), W152 (≠ Y154), I153 (= I155), T154 (= T156), T356 (≠ A364), E358 (≠ Q366)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
40% identity, 95% coverage: 15:377/381 of query aligns to 17:377/379 of 1ukwB
- active site: L124 (= L123), S125 (≠ T124), T241 (≠ G241), E362 (= E362), R374 (= R374)
- binding cobalt (ii) ion: D145 (= D144), H146 (= H145)
- binding flavin-adenine dinucleotide: F122 (= F121), L124 (= L123), S125 (≠ T124), G130 (= G129), S131 (= S130), W155 (≠ Y154), S157 (≠ T156), K200 (= K200), L357 (≠ I357), Y361 (= Y361), E362 (= E362), T364 (≠ A364), E366 (≠ Q366), L370 (= L370)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
40% identity, 95% coverage: 15:377/381 of query aligns to 17:377/379 of 1ukwA
- active site: L124 (= L123), S125 (≠ T124), T241 (≠ G241), E362 (= E362), R374 (= R374)
- binding flavin-adenine dinucleotide: F122 (= F121), L124 (= L123), S125 (≠ T124), G130 (= G129), S131 (= S130), W155 (≠ Y154), S157 (≠ T156), L357 (≠ I357), Y361 (= Y361), E362 (= E362), T364 (≠ A364), E366 (≠ Q366), L370 (= L370)
8pheA Acad9-wt in complex with ecsit-cter (see paper)
38% identity, 99% coverage: 5:381/381 of query aligns to 28:408/551 of 8pheA
- binding : L143 (= L123), D151 (= D131), A153 (= A133), S154 (= S134), I155 (≠ V135), K202 (vs. gap), I205 (≠ V180), F256 (= F231), M260 (= M235), F295 (= F270), N296 (≠ G271), I394 (= I367), Y398 (≠ I371), L401 (≠ R374), Q405 (≠ K378)
Sites not aligning to the query:
Q9H845 Complex I assembly factor ACAD9, mitochondrial; Acyl-CoA dehydrogenase family member 9; ACAD-9; EC 1.3.8.- from Homo sapiens (Human) (see 4 papers)
38% identity, 99% coverage: 5:381/381 of query aligns to 65:445/621 of Q9H845
- R193 (≠ Q136) to W: in MC1DN20; uncertain significance; dbSNP:rs377547811
- S234 (≠ K175) to F: in MC1DN20; uncertain significance
- G303 (= G241) to S: in MC1DN20; uncertain significance; dbSNP:rs143383023
- A326 (= A264) to T: in MC1DN20; uncertain significance; dbSNP:rs115532916
- E413 (= E349) to K: in MC1DN20; uncertain significance; dbSNP:rs149753643
- E426 (= E362) mutation to Q: Loss of long-chain-acyl-CoA dehydrogenase activity. Does not affect mitochondrial complex I assembly.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
8phfA Cryo-em structure of human acad9-s191a (see paper)
38% identity, 99% coverage: 5:381/381 of query aligns to 28:408/547 of 8phfA
- binding flavin-adenine dinucleotide: T144 (= T124), W176 (≠ Y154), K225 (= K200), R292 (= R267), Q294 (= Q269), F295 (= F270), F302 (= F277), L304 (= L279), I305 (= I280), I363 (≠ V336), G365 (= G338), G366 (= G339), F388 (≠ Y361), E393 (≠ Q366), M397 (≠ L370)
Sites not aligning to the query:
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
41% identity, 96% coverage: 10:375/381 of query aligns to 11:375/376 of 4m9aB
- active site: L124 (= L123), T125 (= T124), G241 (= G241), E362 (= E362), R374 (= R374)
- binding dihydroflavine-adenine dinucleotide: F122 (= F121), T125 (= T124), G130 (= G129), S131 (= S130), F155 (≠ Y154), T157 (= T156), T208 (≠ I208), Y361 (= Y361), T364 (≠ A364), E366 (≠ Q366), M370 (≠ L370)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
41% identity, 89% coverage: 39:378/381 of query aligns to 41:379/380 of 4l1fA
- active site: L125 (= L123), T126 (= T124), G242 (= G241), E363 (= E362), R375 (= R374)
- binding coenzyme a persulfide: T132 (≠ S130), H179 (≠ A178), F232 (= F231), M236 (= M235), E237 (≠ R236), L239 (= L238), D240 (= D239), R243 (= R242), Y362 (= Y361), E363 (= E362), G364 (= G363), R375 (= R374)
- binding flavin-adenine dinucleotide: F123 (= F121), L125 (= L123), T126 (= T124), G131 (= G129), T132 (≠ S130), F156 (≠ Y154), I157 (= I155), T158 (= T156), R268 (= R267), Q270 (= Q269), F271 (= F270), I275 (= I274), F278 (= F277), L281 (≠ I280), Q336 (= Q335), I337 (≠ V336), G340 (= G339), I358 (= I357), Y362 (= Y361), T365 (≠ A364), Q367 (= Q366)
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)
39% identity, 97% coverage: 9:378/381 of query aligns to 3:369/369 of 3pfdC
- active site: L116 (= L123), S117 (≠ T124), T233 (≠ G241), E353 (= E362), R365 (= R374)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ F121), L116 (= L123), S117 (≠ T124), G122 (= G129), S123 (= S130), W147 (≠ Y154), I148 (= I155), T149 (= T156), R259 (= R267), F262 (= F270), V266 (≠ I274), N269 (≠ F277), Q326 (= Q335), L327 (≠ V336), G330 (= G339), I348 (= I357), Y352 (= Y361), T355 (≠ A364), Q357 (= Q366)
2uxwA Crystal structure of human very long chain acyl-coa dehydrogenase (acadvl)
39% identity, 96% coverage: 7:373/381 of query aligns to 34:405/567 of 2uxwA
- active site: L148 (= L123), T149 (= T124), G272 (= G241), E394 (= E362)
- binding flavin-adenine dinucleotide: F146 (= F121), L148 (= L123), T149 (= T124), G154 (= G129), S155 (= S130), W181 (≠ Y154), I182 (= I155), S183 (≠ T156), F393 (≠ Y361), T396 (≠ A364), D398 (≠ Q366), I399 (= I367)
- binding trans delta2 palmitenoyl-coenzymea: V96 (≠ I71), G107 (≠ R82), L110 (≠ F85), F146 (= F121), L269 (= L238), F393 (≠ Y361), E394 (= E362), G395 (= G363)
Sites not aligning to the query:
3b96A Structural basis for substrate fatty-acyl chain specificity: crystal structure of human very-long-chain acyl-coa dehydrogenase (see paper)
39% identity, 96% coverage: 7:373/381 of query aligns to 34:405/554 of 3b96A
- active site: L148 (= L123), T149 (= T124), G272 (= G241), E394 (= E362)
- binding flavin-adenine dinucleotide: F146 (= F121), L148 (= L123), T149 (= T124), G154 (= G129), S155 (= S130), W181 (≠ Y154), I182 (= I155), S183 (≠ T156), I389 (= I357), F393 (≠ Y361), T396 (≠ A364), D398 (≠ Q366), I399 (= I367)
- binding tetradecanoyl-coa: V96 (≠ I71), G107 (≠ R82), F146 (= F121), L269 (= L238), F393 (≠ Y361), E394 (= E362)
Sites not aligning to the query:
7s7gA Crystal structure analysis of human vlcad
39% identity, 96% coverage: 7:373/381 of query aligns to 34:405/571 of 7s7gA
- binding flavin-adenine dinucleotide: F146 (= F121), L148 (= L123), T149 (= T124), G154 (= G129), S155 (= S130), W181 (≠ Y154), I182 (= I155), S183 (≠ T156), I389 (= I357), T396 (≠ A364), D398 (≠ Q366), I399 (= I367)
Sites not aligning to the query:
P49748 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; VLCAD; EC 1.3.8.9 from Homo sapiens (Human) (see 8 papers)
39% identity, 96% coverage: 7:373/381 of query aligns to 102:473/655 of P49748
- 214:223 (vs. 121:130, 60% identical) binding
- WIS 249:251 (≠ YIT 154:156) binding
- F458 (= F358) to L: in ACADVLD; loss of acyl-CoA dehydrogenase activity; Loss of FAD cofactor-binding; dbSNP:rs118204017; mutation to T: Decreased acyl-CoA dehydrogenase activity. Decreased affinity for acyl-CoA. No effect on FAD cofactor-binding.; mutation to V: Loss of acyl-CoA dehydrogenase activity. Loss of FAD cofactor-binding.; mutation to Y: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. Decreased FAD cofactor-binding.
- FEG 461:463 (≠ YEG 361:363) binding
- E462 (= E362) active site, Proton acceptor; mutation to D: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. No effect on FAD cofactor-binding.; mutation to Q: Loss of acyl-CoA dehydrogenase activity. No effect on FAD cofactor-binding.
- TND 464:466 (≠ ASQ 364:366) binding
Sites not aligning to the query:
- 1:40 modified: transit peptide, Mitochondrion
- 490 A → P: in ACADVLD; decreased association with mitochondrial inner membrane; may affect substrate specificity, possibly reducing the affinity for long-chain acyl-CoA substrates; dbSNP:rs759775666; mutation A->G,V,S,D,H: Changed substrate specificity with decreased affinity for tetradecanoyl-CoA and hexadecanoyl-CoA.
- 502 L → P: in ACADVLD; decreased association with mitochondrial inner membrane; decreased specific activity towards several substrates in vitro
- 534 E → K: in ACADVLD; uncertain significance; dbSNP:rs2230180
- 562 binding
- 583 S → W: in ACADVLD; Loss of homodimerization; loss of localization to mitochondrial inner membrane; dbSNP:rs1085307648
Query Sequence
>CCNA_01875 FitnessBrowser__Caulo:CCNA_01875
MTDPDTLSALIDVIQRFVAERLRPIEGLVSETDEVPGSIIEEMKQLGLFGLSIPESYGGL
GLSLEEEARVIVAFCHTAPAFRSTFGTNVGIGSQGLVMFGDEAQKARWLPSIASGETITA
FALTEAEAGSDSASVQTRAVRDGDHYVLNGVKRYITNAGRANLFTVMARTDPNTKGGAGV
SAFLVPADLPGLSVGKPEKKMGQQGAHIHDVVFEDVRVPVENRLGAEGEGFTVAMRVLDR
GRVHISAVCVGVAERLIADCVAYASERKQFGQPIASFQLIQAMIADSKTEALAAKALVFD
TARKRDAGANVTLEAAATKLFASEMVGRVADRAVQVFGGAGYVADYGIERLYRDVRIFRI
YEGASQIQQLIIARETLKRGG
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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