SitesBLAST
Comparing N515DRAFT_3819 FitnessBrowser__Dyella79:N515DRAFT_3819 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)
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
46% identity, 81% coverage: 2:444/546 of query aligns to 1:451/503 of 6sdaB
- active site: M171 (= M169), T172 (= T170), T296 (= T289), R439 (= R432)
- binding flavin-adenine dinucleotide: Q169 (= Q167), M171 (= M169), T172 (= T170), G177 (= G175), S178 (= S176), F208 (= F201), T209 (≠ S202), R322 (= R315), F325 (= F318), L329 (= L322), H332 (≠ Q325), E400 (= E393), M401 (≠ C394), G404 (= G397), Y407 (= Y400), W426 (= W419), T429 (= T422), N431 (= N424), L435 (= L428)
- binding decanoyl-CoA: C128 (= C126), G177 (= G175), S178 (= S176), S230 (≠ P223), V286 (= V279), A290 (= A283), L293 (= L286), N294 (= N287), R297 (= R290), R377 (= R370), W426 (= W419), E427 (= E420)
6sd8X Bd2924 apo-form (see paper)
46% identity, 81% coverage: 2:444/546 of query aligns to 1:451/503 of 6sd8X
- active site: M171 (= M169), T172 (= T170), T296 (= T289), R439 (= R432)
- binding flavin-adenine dinucleotide: Q169 (= Q167), M171 (= M169), T172 (= T170), G176 (= G174), G177 (= G175), S178 (= S176), F208 (= F201), T209 (≠ S202), R322 (= R315), F325 (= F318), L329 (= L322), H332 (≠ Q325), M401 (≠ C394), G404 (= G397), W426 (= W419), T429 (= T422), V432 (= V425), L435 (= L428)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
39% identity, 93% coverage: 2:508/546 of query aligns to 34:563/617 of Q9XWZ2
- E91 (≠ R59) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ A120) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ E122) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G175) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G399) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R411) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
39% identity, 93% coverage: 2:508/546 of query aligns to 16:545/593 of 4y9jB
- active site: M190 (= M169), T191 (= T170), T315 (= T289), E446 (= E420), R458 (= R432)
- binding flavin-adenine dinucleotide: Q188 (= Q167), M190 (= M169), T191 (= T170), G196 (= G175), S197 (= S176), F223 (= F201), S224 (= S202), S225 (= S203), R341 (= R315), V343 (≠ A317), F344 (= F318), Q348 (≠ L322), E419 (= E393), C420 (= C394), G422 (= G396), G423 (= G397), Y426 (= Y400), W445 (= W419), T448 (= T422), V451 (= V425), L454 (= L428)
- binding S-{(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} undecanethioate: S143 (≠ T125), A147 (= A129), Q188 (= Q167), S197 (= S176), S249 (≠ P223), R303 (≠ H277), V305 (= V279), S309 (≠ A283), L312 (= L286), N313 (= N287), R316 (= R290), A322 (≠ C296), R396 (= R370), W445 (= W419), E446 (= E420), V451 (= V425), R458 (= R432)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
36% identity, 69% coverage: 62:438/546 of query aligns to 67:443/541 of P33224
- 182:191 (vs. 167:176, 60% identical) binding
- T185 (= T170) binding
- S191 (= S176) binding
- FFS 216:218 (≠ FSS 201:203) binding
- S218 (= S203) binding
- 423:433 (vs. 418:428, 55% identical) binding
- N429 (= N424) binding
- R437 (= R432) mutation to Q: Does not affect DNA binding affinity.
Sites not aligning to the query:
- 518 R→Q: Reduces DNA binding affinity.
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
36% identity, 69% coverage: 62:438/546 of query aligns to 67:443/540 of 3u33A
- active site: M184 (= M169), T185 (= T170), T298 (= T289), E425 (= E420), R437 (= R432)
- binding flavin-adenine dinucleotide: M182 (≠ Q167), M184 (= M169), T185 (= T170), G190 (= G175), S191 (= S176), F216 (= F201), S218 (= S203), R324 (= R315), F327 (= F318), L331 (= L322), Q334 (= Q325), M337 (≠ H328), E398 (= E393), V399 (≠ C394), G401 (= G396), G402 (= G397), W424 (= W419), G426 (= G421), S427 (≠ T422), N429 (= N424), L433 (= L428)
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
34% identity, 71% coverage: 62:451/546 of query aligns to 63:452/541 of 5ez3B
- active site: M181 (= M169), T182 (= T170), T295 (= T289), E423 (= E420), R435 (= R432)
- binding flavin-adenine dinucleotide: M181 (= M169), T182 (= T170), G186 (= G174), G187 (= G175), T188 (≠ S176), F213 (= F201), S215 (= S203), R321 (= R315), F324 (= F318), L328 (= L322), Q331 (= Q325), M334 (≠ H328), E396 (= E393), C397 (= C394), G399 (= G396), G400 (= G397), W422 (= W419), E423 (= E420), S425 (≠ T422), N427 (= N424), L431 (= L428)
A3SI50 3-methylmercaptopropionyl-CoA dehydrogenase; MMPA-CoA dehydrogenase; EC 1.3.99.41 from Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM) (see paper)
28% identity, 66% coverage: 116:477/546 of query aligns to 114:496/591 of A3SI50
- M161 (≠ Q167) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S176) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F201) mutation to A: Almost completely abolishes the activity.
- S197 (= S203) mutation to A: Retains 3.6% of wild-type activity.
- K223 (≠ G224) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ E276) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ H277) mutation to A: Retains 54% of wild-type activity.
- R284 (= R280) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ A283) mutation to A: Retains 76% of wild-type activity.
- Y434 (≠ W419) mutation to A: Retains 51% of wild-type activity.
- E435 (= E420) mutation to A: Loss of activity.
- R448 (= R432) mutation to A: Retains 44% of wild-type activity.
Q3L887 Broad-specificity linear acyl-CoA dehydrogenase FadE5; Long-chain-acyl-CoA dehydrogenase; Medium-chain-acyl-CoA dehydrogenase; Short-chain-acyl-CoA dehydrogenase; EC 1.3.8.8; EC 1.3.8.7; EC 1.3.8.1 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
29% identity, 49% coverage: 163:429/546 of query aligns to 158:456/611 of Q3L887
Sites not aligning to the query:
6ksbA Crystal structure of e447a m130g acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c16coa (see paper)
28% identity, 49% coverage: 163:429/546 of query aligns to 158:456/608 of 6ksbA
- binding coenzyme a: M162 (≠ Q167), S171 (= S176), V173 (= V178), T224 (≠ P223), K225 (≠ G224), I290 (≠ V279), F294 (≠ A283), E298 (≠ N287), R301 (= R290), A447 (≠ E420), G448 (= G421), I452 (≠ V425), D456 (= D429)
- binding flavin-adenine dinucleotide: L164 (≠ M169), T165 (= T170), G170 (= G175), S171 (= S176), F196 (= F201), I197 (≠ S202), T198 (≠ S203), T266 (= T259), R326 (= R315), I345 (≠ L327), H348 (≠ Q330), Q420 (≠ E393), T421 (≠ C394), G423 (= G396), G424 (= G397), I442 (≠ V415), Y446 (≠ W419), T449 (= T422), Q455 (≠ L428)
Sites not aligning to the query:
6ksaB Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c18coa (see paper)
28% identity, 49% coverage: 163:429/546 of query aligns to 161:459/611 of 6ksaB
- binding flavin-adenine dinucleotide: M165 (≠ Q167), L167 (≠ M169), T168 (= T170), G173 (= G175), S174 (= S176), F199 (= F201), I200 (≠ S202), T201 (≠ S203), R329 (= R315), I348 (≠ L327), H351 (≠ Q330), Q423 (≠ E393), T424 (≠ C394), G426 (= G396), G427 (= G397), I445 (≠ V415), Y449 (≠ W419), T452 (= T422)
- binding magnesium ion: H388 (vs. gap)
- binding stearoyl-coenzyme a: A163 (≠ S165), M165 (≠ Q167), L167 (≠ M169), S174 (= S176), V176 (= V178), T227 (≠ P223), K228 (≠ G224), I293 (≠ V279), F297 (≠ A283), Q302 (≠ V288), R304 (= R290), Y449 (≠ W419), A450 (≠ E420), I455 (≠ V425), D459 (= D429)
Sites not aligning to the query:
6lq8A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c22coa (see paper)
28% identity, 49% coverage: 163:429/546 of query aligns to 158:456/607 of 6lq8A
- binding coenzyme a: M162 (≠ Q167), L164 (≠ M169), S171 (= S176), V173 (= V178), T224 (≠ P223), K225 (≠ G224), I290 (≠ V279), F294 (≠ A283), R301 (= R290), A447 (≠ E420), G448 (= G421), I452 (≠ V425), D456 (= D429)
- binding docosanoic acid: M162 (≠ Q167), T198 (≠ S203), Q299 (≠ V288), A300 (≠ T289), Y446 (≠ W419), A447 (≠ E420)
- binding flavin-adenine dinucleotide: M162 (≠ Q167), L164 (≠ M169), T165 (= T170), G170 (= G175), S171 (= S176), F196 (= F201), I197 (≠ S202), T198 (≠ S203), R326 (= R315), I345 (≠ L327), H348 (≠ Q330), Q420 (≠ E393), T421 (≠ C394), G423 (= G396), G424 (= G397), I442 (≠ V415), Y446 (≠ W419), T449 (= T422)
Sites not aligning to the query:
6lq7A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c17coa (see paper)
28% identity, 49% coverage: 163:429/546 of query aligns to 158:456/607 of 6lq7A
- binding coenzyme a: M162 (≠ Q167), L164 (≠ M169), S171 (= S176), V173 (= V178), T224 (≠ P223), K225 (≠ G224), I290 (≠ V279), F294 (≠ A283), R301 (= R290), A447 (≠ E420), G448 (= G421), I452 (≠ V425), D456 (= D429)
- binding flavin-adenine dinucleotide: M162 (≠ Q167), L164 (≠ M169), T165 (= T170), G170 (= G175), S171 (= S176), F196 (= F201), I197 (≠ S202), T198 (≠ S203), R326 (= R315), I345 (≠ L327), H348 (≠ Q330), Q420 (≠ E393), T421 (≠ C394), G423 (= G396), G424 (= G397), I442 (≠ V415), Y446 (≠ W419), T449 (= T422)
- binding heptadecanoic acid: A160 (≠ S165), Q299 (≠ V288), Y446 (≠ W419), A447 (≠ E420)
Sites not aligning to the query:
6lq6A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c20coa (see paper)
28% identity, 49% coverage: 163:429/546 of query aligns to 158:456/607 of 6lq6A
- binding coenzyme a: M162 (≠ Q167), L164 (≠ M169), S171 (= S176), V173 (= V178), T224 (≠ P223), K225 (≠ G224), I290 (≠ V279), F294 (≠ A283), R301 (= R290), A447 (≠ E420), G448 (= G421), I452 (≠ V425), D456 (= D429)
- binding icosanoic acid: A160 (≠ S165), Q299 (≠ V288), M303 (≠ W292), A447 (≠ E420)
- binding flavin-adenine dinucleotide: M162 (≠ Q167), L164 (≠ M169), T165 (= T170), G170 (= G175), S171 (= S176), F196 (= F201), I197 (≠ S202), T198 (≠ S203), T266 (= T259), R326 (= R315), H348 (≠ Q330), Q420 (≠ E393), T421 (≠ C394), G423 (= G396), G424 (= G397), I442 (≠ V415), Y446 (≠ W419), T449 (= T422)
Sites not aligning to the query:
6lq1A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c8coa (see paper)
28% identity, 49% coverage: 163:429/546 of query aligns to 158:456/607 of 6lq1A
- binding coenzyme a: M162 (≠ Q167), S171 (= S176), V173 (= V178), T224 (≠ P223), I290 (≠ V279), F294 (≠ A283), R301 (= R290), A447 (≠ E420), I452 (≠ V425), D456 (= D429)
- binding flavin-adenine dinucleotide: L164 (≠ M169), T165 (= T170), G170 (= G175), S171 (= S176), F196 (= F201), I197 (≠ S202), T198 (≠ S203), T266 (= T259), R326 (= R315), H348 (≠ Q330), Q420 (≠ E393), T421 (≠ C394), G423 (= G396), G424 (= G397), I442 (≠ V415), Y446 (≠ W419), T449 (= T422)
- binding octanoic acid (caprylic acid): M162 (≠ Q167), Y446 (≠ W419), A447 (≠ E420)
Sites not aligning to the query:
6lq0A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c6coa (see paper)
28% identity, 49% coverage: 163:429/546 of query aligns to 158:456/607 of 6lq0A
- binding hexanoic acid: M303 (≠ W292), Y446 (≠ W419), A447 (≠ E420)
- binding coenzyme a: S171 (= S176), V173 (= V178), T224 (≠ P223), K225 (≠ G224), I290 (≠ V279), F294 (≠ A283), R301 (= R290), A447 (≠ E420), G448 (= G421), I452 (≠ V425), D456 (= D429)
- binding flavin-adenine dinucleotide: M162 (≠ Q167), L164 (≠ M169), T165 (= T170), G170 (= G175), S171 (= S176), F196 (= F201), I197 (≠ S202), T198 (≠ S203), R326 (= R315), I345 (≠ L327), H348 (≠ Q330), Q420 (≠ E393), T421 (≠ C394), G423 (= G396), G424 (= G397), I442 (≠ V415), Y446 (≠ W419), T449 (= T422), Q455 (≠ L428)
Sites not aligning to the query:
6lpyA Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c4coa (see paper)
28% identity, 49% coverage: 163:429/546 of query aligns to 158:456/607 of 6lpyA
- binding butanoic acid: Y446 (≠ W419), A447 (≠ E420)
- binding coenzyme a: M162 (≠ Q167), L164 (≠ M169), S171 (= S176), V173 (= V178), T224 (≠ P223), K225 (≠ G224), I290 (≠ V279), F294 (≠ A283), R301 (= R290), A447 (≠ E420), I452 (≠ V425), D456 (= D429)
- binding flavin-adenine dinucleotide: M162 (≠ Q167), L164 (≠ M169), T165 (= T170), G170 (= G175), S171 (= S176), F196 (= F201), I197 (≠ S202), T198 (≠ S203), R326 (= R315), I345 (≠ L327), H348 (≠ Q330), Q420 (≠ E393), T421 (≠ C394), G423 (= G396), G424 (= G397), I442 (≠ V415), Y446 (≠ W419), T449 (= T422)
Sites not aligning to the query:
O53666 Broad-specificity linear acyl-CoA dehydrogenase FadE5; Long-chain-acyl-CoA dehydrogenase; Medium-chain-acyl-CoA dehydrogenase; Short-chain-acyl-CoA dehydrogenase; EC 1.3.8.8; EC 1.3.8.7; EC 1.3.8.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
29% identity, 49% coverage: 163:429/546 of query aligns to 158:456/611 of O53666
- MVLT 162:165 (≠ QWMT 167:170) binding
- S171 (= S176) binding ; binding ; mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- T198 (≠ S203) binding
- TK 224:225 (≠ PG 223:224) binding
- K225 (≠ G224) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- F294 (≠ A283) mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R301 (= R290) binding ; mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R326 (= R315) binding
- K338 (vs. gap) binding
- QTLGG 420:424 (≠ ECFGG 393:397) binding
- E447 (= E420) binding ; mutation to A: Loss of activity.
- T449 (= T422) binding
- D456 (= D429) binding
Sites not aligning to the query:
- 460 R→A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- 460:461 binding
6kseA Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria tuberculosisin complex with c18coa (see paper)
29% identity, 49% coverage: 163:429/546 of query aligns to 158:456/607 of 6kseA
- active site: L164 (≠ M169), T165 (= T170), A300 (≠ T289)
- binding flavin-adenine dinucleotide: M162 (≠ Q167), L164 (≠ M169), T165 (= T170), G170 (= G175), S171 (= S176), F196 (= F201), T198 (≠ S203), R326 (= R315), Q328 (vs. gap), I345 (≠ L322), H348 (≠ Q325), Q420 (≠ E393), T421 (≠ C394), G423 (= G396), G424 (= G397), I442 (≠ V415), Y446 (≠ W419), T449 (= T422)
- binding stearoyl-coenzyme a: M162 (≠ Q167), S171 (= S176), T224 (≠ P223), K225 (≠ G224), I290 (≠ V279), F294 (≠ A283), A300 (≠ T289), R301 (= R290), Y446 (≠ W419), A447 (≠ E420), I452 (≠ V425), D456 (= D429)
Sites not aligning to the query:
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
28% identity, 58% coverage: 108:425/546 of query aligns to 72:367/379 of 6fahD
- active site: L124 (= L164), T125 (= T170), G241 (≠ T289)
- binding flavin-adenine dinucleotide: F122 (= F162), L124 (= L164), T125 (= T170), R152 (= R198), F155 (= F201), T157 (≠ S202), E198 (≠ K249), R267 (= R315), Q269 (≠ A317), F270 (= F318), I274 (≠ L322), F277 (≠ Q325), Q335 (≠ E393), I336 (≠ C394), G339 (= G397), Y361 (≠ W419), T364 (= T422), Q366 (≠ N424)
Sites not aligning to the query:
Query Sequence
>N515DRAFT_3819 FitnessBrowser__Dyella79:N515DRAFT_3819
MGFLQEAPQLAHPYRDDRLLVDLLDRVLPAGRRAAIDADLDALGDYARLAWRRVCTTTRR
KPVLTQWDAWGRRVDRIELTPAWQEGPLLTTRHAVLAAGHEAHPEARVEEFARVYLYHLA
SEFYTCPLAMTDGAATALKASGNATLIERALPHFLSRDPANFWLSGQWMTENAGGSDVGN
TETVARRDVDGQWRLYGRKWFSSAVVGEAALALARPEGAGVGPGALALFYVETMDDGQRK
PELVIDRLKDKLGTHELPTAEIHLEGLPAWPVGELEHGVRQVAPMLNVTRSWNAICAVAS
MSRALQLARDYARRRQAFGRTLAEQPLHAQTLAGMQAEFEAAFALSFEVAHLLGRTEQHA
ATPQEAALLRLLTPLAKLWTGKLAIKLCSEALECFGGAGYIEDTGLPQLLRDAQVYAIWE
GTTNVLSLDALRALAGKAPGALRECIGHWLADSDDMHATSAVQHTLDAAMRWLDARGGQR
DELEAGARGLAITLARCAAAALLARQAAWARRQRGDQRPGAALRRFVSHGLDRLDTLDAA
DTALLA
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