SitesBLAST
Comparing WP_068459994.1 NCBI__GCF_001541235.1:WP_068459994.1 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)
8pngA Crystal structure of the apo acyl-coa dehydrogenase fade2 (pa0508) from pseudomonas aeruginosa
52% identity, 100% coverage: 1:588/588 of query aligns to 3:594/594 of 8pngA
- binding flavin-adenine dinucleotide: M166 (= M163), L168 (= L165), T169 (= T166), G174 (= G171), T175 (= T172), F200 (= F197), T202 (≠ S199), R324 (= R321), S327 (≠ G324), H346 (= H339), V349 (= V342), Q417 (= Q410), I418 (≠ V411), G421 (= G414), H422 (= H415), I439 (= I432), Y443 (= Y436), T446 (= T439), I449 (≠ V442)
8pnsA Crystal structure of the acyl-coa dehydrogenase pa0506 (fade1) from pseudomonas aeruginosa
48% identity, 99% coverage: 4:588/588 of query aligns to 3:596/600 of 8pnsA
- binding octanoyl-coenzyme a: M162 (= M163), T171 (= T172), L173 (= L174), T223 (≠ V224), L284 (= L285), F288 (= F289), M291 (= M292), Y439 (= Y436), E440 (= E437), D449 (= D446), R453 (= R450), K454 (= K451)
- binding flavin-adenine dinucleotide: L164 (= L165), T165 (= T166), G170 (= G171), T171 (= T172), F196 (= F197), S198 (= S199), R320 (= R321), Q322 (= Q323), M323 (≠ G324), I339 (= I336), H342 (= H339), Q413 (= Q410), I414 (≠ V411), G417 (= G414), I435 (= I432), Y439 (= Y436), T442 (= T439)
8pu5B Crystal structure of the acyl-coa dehydrogenase fade1(pa0506) e441a from pseudomonas aeruginosa complexed with c16coa
48% identity, 99% coverage: 4:588/588 of query aligns to 2:595/599 of 8pu5B
- binding Palmitoyl-CoA: L109 (≠ I111), G127 (= G129), M161 (= M163), T170 (= T172), L172 (= L174), T222 (≠ V224), L283 (= L285), F287 (= F289), M290 (= M292), N291 (= N293), R294 (= R296), Y438 (= Y436), A439 (≠ E437), D448 (= D446), R452 (= R450), K453 (= K451)
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)
47% identity, 100% coverage: 1:588/588 of query aligns to 1:591/591 of A3SI50
- M161 (= M163) mutation to A: Retains 37% of wild-type activity.
- T170 (= T172) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F197) mutation to A: Almost completely abolishes the activity.
- S197 (= S199) mutation to A: Retains 3.6% of wild-type activity.
- K223 (= K225) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ G282) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ R283) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ N286) mutation to A: Retains 97% of wild-type activity.
- F287 (= F289) mutation to A: Retains 76% of wild-type activity.
- Y434 (= Y436) mutation to A: Retains 51% of wild-type activity.
- E435 (= E437) mutation to A: Loss of activity.
- R448 (= R450) mutation to A: Retains 44% of wild-type activity.
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)
31% identity, 100% coverage: 1:588/588 of query aligns to 1:611/611 of O53666
- MVLT 162:165 (≠ MALT 163:166) binding FAD
- S171 (≠ T172) binding a 2,3-saturated acyl-CoA; binding FAD; mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- T198 (≠ S199) binding FAD
- TK 224:225 (≠ VK 224:225) binding a 2,3-saturated acyl-CoA
- K225 (= K225) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- F294 (= F289) mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R301 (= R296) binding a 2,3-saturated acyl-CoA; mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R326 (= R321) binding FAD
- K338 (≠ G329) binding a 2,3-saturated acyl-CoA
- QTLGG 420:424 (≠ QVFGG 410:414) binding FAD
- E447 (= E437) binding a 2,3-saturated acyl-CoA; mutation to A: Loss of activity.
- T449 (= T439) binding FAD
- D456 (= D446) binding a 2,3-saturated acyl-CoA
- R460 (= R450) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- RK 460:461 (= RK 450:451) binding a 2,3-saturated acyl-CoA
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)
31% identity, 100% coverage: 1:588/588 of query aligns to 1:611/611 of Q3L887
- MVLT 162:165 (≠ MALT 163:166) binding FAD
- S171 (≠ T172) binding a 2,3-saturated acyl-CoA; binding FAD
- T198 (≠ S199) binding FAD
- TK 224:225 (≠ VK 224:225) binding a 2,3-saturated acyl-CoA
- R301 (= R296) binding a 2,3-saturated acyl-CoA
- R326 (= R321) binding FAD
- K338 (≠ G329) binding a 2,3-saturated acyl-CoA
- QTLGG 420:424 (≠ QVFGG 410:414) binding FAD
- E447 (= E437) binding a 2,3-saturated acyl-CoA; mutation to A: Loss of activity.
- T449 (= T439) binding FAD
- D456 (= D446) binding a 2,3-saturated acyl-CoA
- RK 460:461 (= RK 450:451) binding a 2,3-saturated acyl-CoA
6kseA Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria tuberculosisin complex with c18coa (see paper)
31% identity, 100% coverage: 1:588/588 of query aligns to 1:607/607 of 6kseA
- active site: L164 (= L165), T165 (= T166), A300 (≠ E295), R460 (= R450)
- binding flavin-adenine dinucleotide: M162 (= M163), L164 (= L165), T165 (= T166), G170 (= G171), S171 (≠ T172), F196 (= F197), T198 (≠ S199), R326 (= R321), Q328 (= Q323), I345 (= I336), H348 (= H339), Q420 (= Q410), T421 (≠ V411), G423 (= G413), G424 (= G414), I442 (= I432), Y446 (= Y436), T449 (= T439)
- binding stearoyl-coenzyme a: D93 (≠ P92), H115 (≠ D114), W126 (≠ G125), G130 (= G129), G133 (= G133), F134 (≠ A134), M162 (= M163), S171 (≠ T172), T224 (≠ V224), K225 (= K225), I290 (≠ L285), F294 (= F289), A300 (≠ E295), R301 (= R296), Y446 (= Y436), A447 (≠ E437), I452 (≠ V442), D456 (= D446), R460 (= R450), K461 (= K451)
6ksaB Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c18coa (see paper)
31% identity, 100% coverage: 1:588/588 of query aligns to 4:611/611 of 6ksaB
- binding flavin-adenine dinucleotide: M165 (= M163), L167 (= L165), T168 (= T166), G173 (= G171), S174 (≠ T172), F199 (= F197), I200 (= I198), T201 (≠ S199), R329 (= R321), I348 (= I336), H351 (= H339), Q423 (= Q410), T424 (≠ V411), G426 (= G413), G427 (= G414), I445 (= I432), Y449 (= Y436), T452 (= T439)
- binding magnesium ion: H388 (≠ A376), Y475 (≠ L466), E479 (≠ D470)
- binding stearoyl-coenzyme a: W115 (≠ I111), M133 (≠ L126), M137 (≠ L130), A163 (≠ G161), M165 (= M163), L167 (= L165), S174 (≠ T172), V176 (≠ L174), T227 (≠ V224), K228 (= K225), I293 (≠ L285), F297 (= F289), Q302 (≠ A294), R304 (= R296), Y449 (= Y436), A450 (≠ E437), I455 (≠ V442), D459 (= D446), R463 (= R450), K464 (= K451)
6ksbA Crystal structure of e447a m130g acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c16coa (see paper)
31% identity, 100% coverage: 1:588/588 of query aligns to 1:608/608 of 6ksbA
- binding coenzyme a: M162 (= M163), S171 (≠ T172), V173 (≠ L174), T224 (≠ V224), K225 (= K225), I290 (≠ L285), F294 (= F289), E298 (≠ N293), R301 (= R296), A447 (≠ E437), G448 (= G438), I452 (≠ V442), D456 (= D446), R460 (= R450), K461 (= K451)
- binding flavin-adenine dinucleotide: L164 (= L165), T165 (= T166), G170 (= G171), S171 (≠ T172), F196 (= F197), I197 (= I198), T198 (≠ S199), T266 (= T265), R326 (= R321), I345 (= I336), H348 (= H339), Q420 (= Q410), T421 (≠ V411), G423 (= G413), G424 (= G414), I442 (= I432), Y446 (= Y436), T449 (= T439), Q455 (≠ M445)
6lq8A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c22coa (see paper)
31% identity, 100% coverage: 1:588/588 of query aligns to 1:607/607 of 6lq8A
- binding coenzyme a: M162 (= M163), L164 (= L165), S171 (≠ T172), V173 (≠ L174), T224 (≠ V224), K225 (= K225), I290 (≠ L285), F294 (= F289), R301 (= R296), A447 (≠ E437), G448 (= G438), I452 (≠ V442), D456 (= D446), R460 (= R450), K461 (= K451)
- binding docosanoic acid: G96 (≠ S95), L97 (≠ G96), Q111 (= Q110), M130 (≠ L126), G133 (= G129), M134 (≠ L130), E136 (= E136), I137 (≠ A137), M162 (= M163), T198 (≠ S199), Q299 (≠ A294), A300 (≠ E295), Y446 (= Y436), A447 (≠ E437)
- binding flavin-adenine dinucleotide: M162 (= M163), L164 (= L165), T165 (= T166), G170 (= G171), S171 (≠ T172), F196 (= F197), I197 (= I198), T198 (≠ S199), R326 (= R321), I345 (= I336), H348 (= H339), Q420 (= Q410), T421 (≠ V411), G423 (= G413), G424 (= G414), I442 (= I432), Y446 (= Y436), T449 (= T439)
6lq7A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c17coa (see paper)
31% identity, 100% coverage: 1:588/588 of query aligns to 1:607/607 of 6lq7A
- binding coenzyme a: M162 (= M163), L164 (= L165), S171 (≠ T172), V173 (≠ L174), T224 (≠ V224), K225 (= K225), I290 (≠ L285), F294 (= F289), R301 (= R296), A447 (≠ E437), G448 (= G438), I452 (≠ V442), D456 (= D446), R460 (= R450), K461 (= K451)
- binding flavin-adenine dinucleotide: M162 (= M163), L164 (= L165), T165 (= T166), G170 (= G171), S171 (≠ T172), F196 (= F197), I197 (= I198), T198 (≠ S199), R326 (= R321), I345 (= I336), H348 (= H339), Q420 (= Q410), T421 (≠ V411), G423 (= G413), G424 (= G414), I442 (= I432), Y446 (= Y436), T449 (= T439)
- binding heptadecanoic acid: M130 (≠ L126), A160 (≠ G161), Q299 (≠ A294), Y446 (= Y436), A447 (≠ E437)
6lq6A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c20coa (see paper)
31% identity, 100% coverage: 1:588/588 of query aligns to 1:607/607 of 6lq6A
- binding coenzyme a: M162 (= M163), L164 (= L165), S171 (≠ T172), V173 (≠ L174), T224 (≠ V224), K225 (= K225), I290 (≠ L285), F294 (= F289), R301 (= R296), A447 (≠ E437), G448 (= G438), I452 (≠ V442), D456 (= D446), R460 (= R450), K461 (= K451)
- binding icosanoic acid: G96 (≠ S95), M130 (≠ L126), G133 (= G129), M134 (≠ L130), E136 (= E136), A160 (≠ G161), Q299 (≠ A294), M303 (≠ F298), A447 (≠ E437)
- binding flavin-adenine dinucleotide: M162 (= M163), L164 (= L165), T165 (= T166), G170 (= G171), S171 (≠ T172), F196 (= F197), I197 (= I198), T198 (≠ S199), T266 (= T265), R326 (= R321), H348 (= H339), Q420 (= Q410), T421 (≠ V411), G423 (= G413), G424 (= G414), I442 (= I432), Y446 (= Y436), T449 (= T439)
6lq1A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c8coa (see paper)
31% identity, 100% coverage: 1:588/588 of query aligns to 1:607/607 of 6lq1A
- binding coenzyme a: M162 (= M163), S171 (≠ T172), V173 (≠ L174), T224 (≠ V224), I290 (≠ L285), F294 (= F289), R301 (= R296), A447 (≠ E437), I452 (≠ V442), D456 (= D446), R460 (= R450), K461 (= K451)
- binding flavin-adenine dinucleotide: L164 (= L165), T165 (= T166), G170 (= G171), S171 (≠ T172), F196 (= F197), I197 (= I198), T198 (≠ S199), T266 (= T265), R326 (= R321), H348 (= H339), Q420 (= Q410), T421 (≠ V411), G423 (= G413), G424 (= G414), I442 (= I432), Y446 (= Y436), T449 (= T439)
- binding octanoic acid (caprylic acid): M130 (≠ L126), M162 (= M163), Y446 (= Y436), A447 (≠ E437)
6lq0A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c6coa (see paper)
31% identity, 100% coverage: 1:588/588 of query aligns to 1:607/607 of 6lq0A
- binding hexanoic acid: M303 (≠ F298), Y446 (= Y436), A447 (≠ E437)
- binding coenzyme a: S171 (≠ T172), V173 (≠ L174), T224 (≠ V224), K225 (= K225), I290 (≠ L285), F294 (= F289), R301 (= R296), A447 (≠ E437), G448 (= G438), I452 (≠ V442), D456 (= D446), R460 (= R450), K461 (= K451)
- binding flavin-adenine dinucleotide: M162 (= M163), L164 (= L165), T165 (= T166), G170 (= G171), S171 (≠ T172), F196 (= F197), I197 (= I198), T198 (≠ S199), R326 (= R321), I345 (= I336), H348 (= H339), Q420 (= Q410), T421 (≠ V411), G423 (= G413), G424 (= G414), I442 (= I432), Y446 (= Y436), T449 (= T439), Q455 (≠ M445)
6lpyA Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c4coa (see paper)
31% identity, 100% coverage: 1:588/588 of query aligns to 1:607/607 of 6lpyA
- binding butanoic acid: Y446 (= Y436), A447 (≠ E437)
- binding coenzyme a: M162 (= M163), L164 (= L165), S171 (≠ T172), V173 (≠ L174), T224 (≠ V224), K225 (= K225), I290 (≠ L285), F294 (= F289), R301 (= R296), A447 (≠ E437), I452 (≠ V442), D456 (= D446), R460 (= R450), K461 (= K451), R464 (≠ L454)
- binding flavin-adenine dinucleotide: M162 (= M163), L164 (= L165), T165 (= T166), G170 (= G171), S171 (≠ T172), F196 (= F197), I197 (= I198), T198 (≠ S199), R326 (= R321), I345 (= I336), H348 (= H339), Q420 (= Q410), T421 (≠ V411), G423 (= G413), G424 (= G414), I442 (= I432), Y446 (= Y436), T449 (= T439)
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)
31% identity, 62% coverage: 80:443/588 of query aligns to 31:359/369 of 3pfdC
- active site: L116 (= L165), S117 (≠ T166), T233 (≠ E295), E353 (= E437)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M163), L116 (= L165), S117 (≠ T166), G122 (= G171), S123 (≠ T172), W147 (≠ F197), I148 (= I198), T149 (≠ S199), R259 (= R321), F262 (vs. gap), V266 (≠ I336), N269 (≠ H339), Q326 (= Q410), L327 (≠ V411), G330 (= G414), I348 (= I432), Y352 (= Y436), T355 (= T439), Q357 (≠ G441)
Sites not aligning to the query:
3nf4A Crystal structure of acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to flavin adenine dinucleotide (see paper)
30% identity, 71% coverage: 34:448/588 of query aligns to 7:365/369 of 3nf4A
- active site: L127 (= L165), S128 (≠ T166), G240 (≠ E295), E354 (= E437)
- binding flavin-adenine dinucleotide: Y125 (≠ M163), L127 (= L165), S128 (≠ T166), G133 (= G171), S134 (≠ T172), W158 (≠ F197), T160 (≠ S199), I349 (= I432), T356 (= T439), Q358 (≠ G441), I359 (≠ V442)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
30% identity, 59% coverage: 100:445/588 of query aligns to 56:366/374 of 5lnxD
- active site: L122 (= L165), T123 (= T166), G239 (≠ E295), E358 (= E437)
- binding flavin-adenine dinucleotide: L122 (= L165), T123 (= T166), G128 (= G171), S129 (≠ T172), F153 (= F197), T155 (≠ S199), R265 (= R321), Q267 (= Q323), F268 (vs. gap), I272 (= I336), N275 (≠ H339), I278 (≠ V342), Q331 (= Q410), I332 (≠ V411), G335 (= G414), Y357 (= Y436), T360 (= T439), E362 (≠ G441)
Sites not aligning to the query:
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
28% identity, 74% coverage: 14:447/588 of query aligns to 22:437/503 of 6sdaB
- active site: M171 (≠ L165), T172 (= T166), T296 (≠ E295)
- binding flavin-adenine dinucleotide: Q169 (≠ M163), M171 (≠ L165), T172 (= T166), G177 (= G171), S178 (≠ T172), F208 (= F197), T209 (≠ I198), R322 (= R321), F325 (≠ R331), L329 (≠ I336), H332 (= H339), E400 (≠ Q410), M401 (≠ V411), G404 (= G414), Y407 (= Y417), W426 (≠ Y436), T429 (= T439), N431 (≠ G441), L435 (≠ M445)
- binding decanoyl-CoA: C128 (≠ L126), G177 (= G171), S178 (≠ T172), S230 (≠ V224), V286 (≠ L285), A290 (≠ F289), L293 (≠ M292), N294 (= N293), R297 (= R296), R377 (≠ A387), W426 (≠ Y436), E427 (= E437)
Sites not aligning to the query:
6sd8X Bd2924 apo-form (see paper)
28% identity, 74% coverage: 14:447/588 of query aligns to 22:437/503 of 6sd8X
- active site: M171 (≠ L165), T172 (= T166), T296 (≠ E295)
- binding flavin-adenine dinucleotide: Q169 (≠ M163), M171 (≠ L165), T172 (= T166), G176 (≠ A170), G177 (= G171), S178 (≠ T172), F208 (= F197), T209 (≠ I198), R322 (= R321), F325 (≠ R331), L329 (≠ I336), H332 (= H339), M401 (≠ V411), G404 (= G414), W426 (≠ Y436), T429 (= T439), V432 (= V442), L435 (≠ M445)
Sites not aligning to the query:
Query Sequence
>WP_068459994.1 NCBI__GCF_001541235.1:WP_068459994.1
MSSYMPPTDDIGFLLKSVFGFDAQIAALPGHEELTADFAIAVLEEAGRFCSEVLEPLNRP
GDEEGARIVDGAVVTPKGVKEAYRAFVEAGWPGLSGDVAFGGQGLPRVVQILLDEMLSAT
NMSFGLFPGLTRGAVEAIAHHASDELKAIWLPKMVAGEWTGAMALTEASAGTDLGLLSTR
AEPVGDGSYRITGTKIFISSGDHDFGGNIVHLVLARLPDAPKGVKGISLFLAPKFLLNDD
GSLGERNAMSVGSLEHKMGIHAQPTCVMNYDGAIGWLVGEPGRGLNAMFTMMNAERLFVG
IQGLGIAEAATQKGVAYARERLQGRSLDGARGPVPIIEHADVRRMLMTGRALADGCRALA
IWTALQMDIAAGHPDAATRAEADGMVALLTPVVKAAFTDFGFDVAVLSQQVFGGHGYIRE
WGMEQFVRDARITQIYEGTNGVQAMDLAGRKLSLEGGALPKRFFDLVRRDVESAAATAPG
AKAVWAEVLAALARLESTTAALQAASQSDAAAVGSAATDYLKLFALTAIGWMWVRMAVAA
RAGDTPLEQRKVMIARFYCERLLPQTQGLAAAIAAGSSSTMALPEDLF
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