SitesBLAST
Comparing 5209711 FitnessBrowser__PV4:5209711 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)
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)
51% identity, 100% coverage: 1:595/596 of query aligns to 1:591/591 of A3SI50
- M161 (= M162) mutation to A: Retains 37% of wild-type activity.
- T170 (= T171) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F196) mutation to A: Almost completely abolishes the activity.
- S197 (= S198) mutation to A: Retains 3.6% of wild-type activity.
- K223 (= K224) mutation to A: Retains 9.4% of wild-type activity.
- H280 (= H281) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ Q282) mutation to A: Retains 54% of wild-type activity.
- R284 (= R285) mutation to A: Retains 97% of wild-type activity.
- F287 (= F288) mutation to A: Retains 76% of wild-type activity.
- Y434 (= Y439) mutation to A: Retains 51% of wild-type activity.
- E435 (= E440) mutation to A: Loss of activity.
- R448 (= R453) 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)
32% identity, 100% coverage: 1:595/596 of query aligns to 1:611/611 of Q3L887
6lq8A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c22coa (see paper)
32% identity, 100% coverage: 1:595/596 of query aligns to 1:607/607 of 6lq8A
- binding coenzyme a: M162 (= M162), L164 (= L164), S171 (≠ T171), V173 (≠ L173), T224 (≠ V223), K225 (= K224), I290 (≠ L284), F294 (= F288), R301 (= R295), A447 (≠ E440), G448 (= G441), I452 (≠ V445), D456 (= D449), R460 (= R453), K461 (= K454)
- binding docosanoic acid: G96 (≠ T94), L97 (≠ S95), Q111 (≠ G109), M130 (= M125), G133 (= G128), M134 (≠ L129), E136 (≠ H131), I137 (≠ G132), M162 (= M162), T198 (≠ S198), Q299 (≠ E293), A300 (= A294), Y446 (= Y439), A447 (≠ E440)
- binding flavin-adenine dinucleotide: M162 (= M162), L164 (= L164), T165 (= T165), G170 (= G170), S171 (≠ T171), F196 (= F196), I197 (= I197), T198 (≠ S198), R326 (= R320), I345 (= I339), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442)
6lq7A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c17coa (see paper)
32% identity, 100% coverage: 1:595/596 of query aligns to 1:607/607 of 6lq7A
- binding coenzyme a: M162 (= M162), L164 (= L164), S171 (≠ T171), V173 (≠ L173), T224 (≠ V223), K225 (= K224), I290 (≠ L284), F294 (= F288), R301 (= R295), A447 (≠ E440), G448 (= G441), I452 (≠ V445), D456 (= D449), R460 (= R453), K461 (= K454)
- binding flavin-adenine dinucleotide: M162 (= M162), L164 (= L164), T165 (= T165), G170 (= G170), S171 (≠ T171), F196 (= F196), I197 (= I197), T198 (≠ S198), R326 (= R320), I345 (= I339), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442)
- binding heptadecanoic acid: M130 (= M125), A160 (≠ G160), Q299 (≠ E293), Y446 (= Y439), A447 (≠ E440)
6lq6A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c20coa (see paper)
32% identity, 100% coverage: 1:595/596 of query aligns to 1:607/607 of 6lq6A
- binding coenzyme a: M162 (= M162), L164 (= L164), S171 (≠ T171), V173 (≠ L173), T224 (≠ V223), K225 (= K224), I290 (≠ L284), F294 (= F288), R301 (= R295), A447 (≠ E440), G448 (= G441), I452 (≠ V445), D456 (= D449), R460 (= R453), K461 (= K454)
- binding icosanoic acid: G96 (≠ T94), M130 (= M125), G133 (= G128), M134 (≠ L129), E136 (≠ H131), A160 (≠ G160), Q299 (≠ E293), M303 (≠ G297), A447 (≠ E440)
- binding flavin-adenine dinucleotide: M162 (= M162), L164 (= L164), T165 (= T165), G170 (= G170), S171 (≠ T171), F196 (= F196), I197 (= I197), T198 (≠ S198), T266 (= T264), R326 (= R320), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442)
6lq1A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c8coa (see paper)
32% identity, 100% coverage: 1:595/596 of query aligns to 1:607/607 of 6lq1A
- binding coenzyme a: M162 (= M162), S171 (≠ T171), V173 (≠ L173), T224 (≠ V223), I290 (≠ L284), F294 (= F288), R301 (= R295), A447 (≠ E440), I452 (≠ V445), D456 (= D449), R460 (= R453), K461 (= K454)
- binding flavin-adenine dinucleotide: L164 (= L164), T165 (= T165), G170 (= G170), S171 (≠ T171), F196 (= F196), I197 (= I197), T198 (≠ S198), T266 (= T264), R326 (= R320), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442)
- binding octanoic acid (caprylic acid): M130 (= M125), M162 (= M162), Y446 (= Y439), A447 (≠ E440)
6lq0A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c6coa (see paper)
32% identity, 100% coverage: 1:595/596 of query aligns to 1:607/607 of 6lq0A
- binding hexanoic acid: M303 (≠ G297), Y446 (= Y439), A447 (≠ E440)
- binding coenzyme a: S171 (≠ T171), V173 (≠ L173), T224 (≠ V223), K225 (= K224), I290 (≠ L284), F294 (= F288), R301 (= R295), A447 (≠ E440), G448 (= G441), I452 (≠ V445), D456 (= D449), R460 (= R453), K461 (= K454)
- binding flavin-adenine dinucleotide: M162 (= M162), L164 (= L164), T165 (= T165), G170 (= G170), S171 (≠ T171), F196 (= F196), I197 (= I197), T198 (≠ S198), R326 (= R320), I345 (= I339), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442), Q455 (≠ L448)
6lpyA Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c4coa (see paper)
32% identity, 100% coverage: 1:595/596 of query aligns to 1:607/607 of 6lpyA
- binding butanoic acid: Y446 (= Y439), A447 (≠ E440)
- binding coenzyme a: M162 (= M162), L164 (= L164), S171 (≠ T171), V173 (≠ L173), T224 (≠ V223), K225 (= K224), I290 (≠ L284), F294 (= F288), R301 (= R295), A447 (≠ E440), I452 (≠ V445), D456 (= D449), R460 (= R453), K461 (= K454), R464 (≠ A457)
- binding flavin-adenine dinucleotide: M162 (= M162), L164 (= L164), T165 (= T165), G170 (= G170), S171 (≠ T171), F196 (= F196), I197 (= I197), T198 (≠ S198), R326 (= R320), I345 (= I339), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442)
6ksbA Crystal structure of e447a m130g acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c16coa (see paper)
32% identity, 100% coverage: 1:595/596 of query aligns to 1:608/608 of 6ksbA
- binding coenzyme a: M162 (= M162), S171 (≠ T171), V173 (≠ L173), T224 (≠ V223), K225 (= K224), I290 (≠ L284), F294 (= F288), E298 (≠ N292), R301 (= R295), A447 (≠ E440), G448 (= G441), I452 (≠ V445), D456 (= D449), R460 (= R453), K461 (= K454)
- binding flavin-adenine dinucleotide: L164 (= L164), T165 (= T165), G170 (= G170), S171 (≠ T171), F196 (= F196), I197 (= I197), T198 (≠ S198), T266 (= T264), R326 (= R320), I345 (= I339), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442), Q455 (≠ L448)
6ksaB Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c18coa (see paper)
32% identity, 100% coverage: 1:595/596 of query aligns to 4:611/611 of 6ksaB
- binding flavin-adenine dinucleotide: M165 (= M162), L167 (= L164), T168 (= T165), G173 (= G170), S174 (≠ T171), F199 (= F196), I200 (= I197), T201 (≠ S198), R329 (= R320), I348 (= I339), H351 (= H342), Q423 (= Q413), T424 (≠ V414), G426 (= G416), G427 (= G417), I445 (= I435), Y449 (= Y439), T452 (= T442)
- binding magnesium ion: H388 (≠ D378), Y475 (≠ L465), E479 (≠ M469)
- binding stearoyl-coenzyme a: W115 (≠ V110), M133 (= M125), M137 (≠ L129), A163 (≠ G160), M165 (= M162), L167 (= L164), S174 (≠ T171), V176 (≠ L173), T227 (≠ V223), K228 (= K224), I293 (≠ L284), F297 (= F288), Q302 (≠ E293), R304 (= R295), Y449 (= Y439), A450 (≠ E440), I455 (≠ V445), D459 (= D449), R463 (= R453), K464 (= K454)
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)
33% identity, 100% coverage: 1:595/596 of query aligns to 1:611/611 of O53666
- MVLT 162:165 (≠ MNLT 162:165) binding
- S171 (≠ T171) binding ; binding ; mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- T198 (≠ S198) binding
- TK 224:225 (≠ VK 223:224) binding
- K225 (= K224) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- F294 (= F288) mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R301 (= R295) binding ; mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R326 (= R320) binding
- K338 (≠ S332) binding
- QTLGG 420:424 (≠ QVYGG 413:417) binding
- E447 (= E440) binding ; mutation to A: Loss of activity.
- T449 (= T442) binding
- D456 (= D449) binding
- R460 (= R453) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- RK 460:461 (= RK 453:454) binding
6kseA Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria tuberculosisin complex with c18coa (see paper)
33% identity, 100% coverage: 1:595/596 of query aligns to 1:607/607 of 6kseA
- active site: L164 (= L164), T165 (= T165), A300 (= A294), R460 (= R453)
- binding flavin-adenine dinucleotide: M162 (= M162), L164 (= L164), T165 (= T165), G170 (= G170), S171 (≠ T171), F196 (= F196), T198 (≠ S198), R326 (= R320), Q328 (= Q322), I345 (= I339), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442)
- binding stearoyl-coenzyme a: D93 (≠ A91), H115 (≠ T113), W126 (≠ A124), G130 (= G128), G133 (≠ A133), F134 (≠ Y134), M162 (= M162), S171 (≠ T171), T224 (≠ V223), K225 (= K224), I290 (≠ L284), F294 (= F288), A300 (= A294), R301 (= R295), Y446 (= Y439), A447 (≠ E440), I452 (≠ V445), D456 (= D449), R460 (= R453), K461 (= K454)
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, 65% coverage: 68:456/596 of query aligns to 23:368/369 of 3pfdC
- active site: L116 (= L164), S117 (≠ T165), T233 (≠ A294), E353 (= E440), R365 (= R453)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M162), L116 (= L164), S117 (≠ T165), G122 (= G170), S123 (≠ T171), W147 (≠ F196), I148 (= I197), T149 (≠ S198), R259 (= R320), F262 (vs. gap), V266 (≠ L326), N269 (= N356), Q326 (= Q413), L327 (≠ V414), G330 (= G417), I348 (= I435), Y352 (= Y439), T355 (= T442), Q357 (≠ G444)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
33% identity, 53% coverage: 141:456/596 of query aligns to 99:373/374 of 5lnxD
- active site: L122 (= L164), T123 (= T165), G239 (≠ A294), E358 (= E440), K370 (≠ R453)
- binding flavin-adenine dinucleotide: L122 (= L164), T123 (= T165), G128 (= G170), S129 (≠ T171), F153 (= F196), T155 (≠ S198), R265 (= R320), Q267 (= Q322), F268 (vs. gap), I272 (= I339), N275 (≠ H342), I278 (≠ V345), Q331 (= Q413), I332 (≠ V414), G335 (= G417), Y357 (= Y439), T360 (= T442), E362 (≠ G444)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
32% identity, 54% coverage: 137:455/596 of query aligns to 97:377/378 of 5ol2F
- active site: L124 (= L164), T125 (= T165), G241 (≠ A294), G374 (= G452)
- binding coenzyme a persulfide: L238 (≠ M291), R242 (= R295), E362 (= E440), G363 (= G441)
- binding flavin-adenine dinucleotide: F122 (≠ M162), L124 (= L164), T125 (= T165), P127 (≠ A167), T131 (= T171), F155 (= F196), I156 (= I197), T157 (≠ S198), E198 (= E254), R267 (= R320), F270 (vs. gap), L274 (= L326), F277 (≠ V329), Q335 (= Q413), L336 (≠ V414), G338 (= G416), G339 (= G417), Y361 (= Y439), T364 (= T442), E366 (≠ G444)
Sites not aligning to the query:
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
30% identity, 62% coverage: 87:458/596 of query aligns to 47:380/380 of 4l1fA
- active site: L125 (= L164), T126 (= T165), G242 (≠ A294), E363 (= E440), R375 (= R453)
- binding coenzyme a persulfide: T132 (= T171), H179 (≠ K224), F232 (≠ L284), M236 (≠ F288), E237 (≠ T289), L239 (≠ M291), D240 (≠ N292), R243 (= R295), Y362 (= Y439), E363 (= E440), G364 (= G441), R375 (= R453)
- binding flavin-adenine dinucleotide: F123 (≠ M162), L125 (= L164), T126 (= T165), G131 (= G170), T132 (= T171), F156 (= F196), I157 (= I197), T158 (≠ S198), R268 (= R320), Q270 (= Q322), F271 (vs. gap), I275 (≠ L326), F278 (≠ V329), L281 (≠ R346), Q336 (= Q413), I337 (≠ V414), G340 (= G417), I358 (= I435), Y362 (= Y439), T365 (= T442), Q367 (≠ G444)
Sites not aligning to the query:
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
28% identity, 65% coverage: 68:456/596 of query aligns to 32:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (≠ T171), T134 (≠ L173), R180 (≠ K224), R234 (= R285), L237 (≠ F288), R238 (≠ T289), L240 (≠ M291), D241 (≠ N292), R244 (= R295), E365 (= E440), G366 (= G441), R377 (= R453)
- binding flavin-adenine dinucleotide: Y123 (≠ M162), L125 (= L164), S126 (≠ T165), G131 (= G170), S132 (≠ T171), W156 (≠ F196), I157 (= I197), T158 (≠ S198), I360 (= I435), T367 (= T442), Q369 (≠ G444)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
28% identity, 65% coverage: 68:456/596 of query aligns to 32:380/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ M162), L125 (= L164), S126 (≠ T165), G131 (= G170), S132 (≠ T171), W156 (≠ F196), I157 (= I197), T158 (≠ S198), I360 (= I435), Y364 (= Y439), T367 (= T442), Q369 (≠ G444)
7w0jE Acyl-coa dehydrogenase, tfu_1647
28% identity, 65% coverage: 68:456/596 of query aligns to 33:381/382 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 (≠ T165), W157 (≠ F196), R270 (= R320), Q272 (= Q322), F273 (vs. gap), I277 (≠ L326), F280 (≠ V329), I283 (≠ S332), Q339 (= Q413), L340 (≠ V414), G343 (= G417), Y365 (= Y439), E366 (= E440), T368 (= T442), Q370 (≠ G444), I371 (≠ V445)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
31% identity, 53% coverage: 141:456/596 of query aligns to 105:382/383 of 1bucA
- active site: L128 (= L164), T129 (= T165), G246 (≠ A294), E367 (= E440), G379 (≠ R453)
- binding acetoacetyl-coenzyme a: F126 (≠ M162), G134 (= G170), T135 (= T171), T162 (≠ S198), N182 (≠ V223), H183 (≠ K224), F236 (≠ L284), M240 (≠ F288), M241 (≠ T289), L243 (≠ M291), D244 (≠ N292), T317 (= T383), Y366 (= Y439), E367 (= E440), G368 (= G441)
- binding flavin-adenine dinucleotide: F126 (≠ M162), L128 (= L164), T129 (= T165), G134 (= G170), T135 (= T171), F160 (= F196), T162 (≠ S198), Y366 (= Y439), T369 (= T442), E371 (≠ G444), M375 (≠ D449)
Sites not aligning to the query:
Query Sequence
>5209711 FitnessBrowser__PV4:5209711
MPIYQAPLRDYQFILSELLNIYGRDDLQGFDEIDAELTDAILQGVADFTTEIMLPLNSQG
DTQGCQLVDGQVRTPEGFKDAYQQYVDNGWATLTSDPEYGGQGLPECIGVFATEMKTATN
MAFAMYPGLTHGAYAAIHAHGSDALKAKYLEKLVSGEWTGTMNLTEAHAGTDLALLRTKA
KPVGEDTYAISGEKIFISSGDHDLADNIVHLVLARLPDAPDGVKGISLFAVPKYLVNDDG
TLGCRNGVEASALEHKMGIHGNSTCVMVFDGAIGELVGEPHQGLRAMFTMMNEARLGVGV
QGLGVSEIAYQNALSYARERLQGRALSGVKESESPADPILVHGDVRRMLMAQKAFNQGAR
ALMGQQALWLDESHRHQDKAKATIAAKLAALFTPVVKGFVTDQGFKACVDAQQVYGGHGY
IHEWGMEQFVRDSRIAMIYEGTNGVQALDLVGRKLLADKGEALGLWSEMVKPFVAKYLED
EALKPYLMPLMEATTDLEKATQYIVANGVKNPDIIGAASMGYLQILGIVALGWMWARMAV
KSQQAMTAGEEEAFYANKLVTAKFYMSYWAPQTRSIRYQMERSCELLTQLQDSDFD
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