SitesBLAST
Comparing Dsui_2302 FitnessBrowser__PS:Dsui_2302 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)
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)
44% identity, 100% coverage: 1:597/597 of query aligns to 1:591/591 of A3SI50
- M161 (= M162) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S171) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F196) mutation to A: Almost completely abolishes the activity.
- S197 (≠ T198) mutation to A: Retains 3.6% of wild-type activity.
- K223 (= K224) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ N284) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ R285) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ E288) mutation to A: Retains 97% of wild-type activity.
- F287 (= F291) 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)
35% identity, 96% coverage: 1:572/597 of query aligns to 1:586/611 of Q3L887
6ksaB Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c18coa (see paper)
35% identity, 96% coverage: 1:572/597 of query aligns to 4:586/611 of 6ksaB
- binding flavin-adenine dinucleotide: M165 (= M162), L167 (= L164), T168 (= T165), G173 (= G170), S174 (= S171), F199 (= F196), I200 (= I197), T201 (= T198), R329 (= R323), I348 (= I339), H351 (= H342), Q423 (= Q413), T424 (≠ V414), G426 (= G416), G427 (= G417), I445 (= I435), Y449 (= Y439), T452 (= T442)
- binding magnesium ion: H388 (≠ R382), Y475 (≠ A465), E479 (= E469)
- binding stearoyl-coenzyme a: W115 (≠ T110), M133 (= M128), M137 (≠ A133), A163 (≠ G160), M165 (= M162), L167 (= L164), S174 (= S171), V176 (≠ L173), T227 (≠ V223), K228 (= K224), I293 (≠ L287), F297 (= F291), Q302 (≠ A296), R304 (= R298), Y449 (= Y439), A450 (≠ E440), I455 (= I445), D459 (= D449), R463 (= R453), K464 (= K454)
6lq8A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c22coa (see paper)
35% identity, 96% coverage: 1:572/597 of query aligns to 1:582/607 of 6lq8A
- binding coenzyme a: M162 (= M162), L164 (= L164), S171 (= S171), V173 (≠ L173), T224 (≠ V223), K225 (= K224), I290 (≠ L287), F294 (= F291), R301 (= R298), A447 (≠ E440), G448 (= G441), I452 (= I445), D456 (= D449), R460 (= R453), K461 (= K454)
- binding docosanoic acid: G96 (≠ A94), L97 (≠ C95), Q111 (≠ S109), M130 (= M128), G133 (= G132), M134 (≠ A133), E136 (= E135), I137 (≠ A136), M162 (= M162), T198 (= T198), Q299 (≠ A296), A300 (= A297), Y446 (= Y439), A447 (≠ E440)
- binding flavin-adenine dinucleotide: M162 (= M162), L164 (= L164), T165 (= T165), G170 (= G170), S171 (= S171), F196 (= F196), I197 (= I197), T198 (= T198), R326 (= R323), 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)
35% identity, 96% coverage: 1:572/597 of query aligns to 1:582/607 of 6lq7A
- binding coenzyme a: M162 (= M162), L164 (= L164), S171 (= S171), V173 (≠ L173), T224 (≠ V223), K225 (= K224), I290 (≠ L287), F294 (= F291), R301 (= R298), A447 (≠ E440), G448 (= G441), I452 (= I445), D456 (= D449), R460 (= R453), K461 (= K454)
- binding flavin-adenine dinucleotide: M162 (= M162), L164 (= L164), T165 (= T165), G170 (= G170), S171 (= S171), F196 (= F196), I197 (= I197), T198 (= T198), R326 (= R323), I345 (= I339), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442)
- binding heptadecanoic acid: M130 (= M128), A160 (≠ G160), Q299 (≠ A296), Y446 (= Y439), A447 (≠ E440)
6lq6A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c20coa (see paper)
35% identity, 96% coverage: 1:572/597 of query aligns to 1:582/607 of 6lq6A
- binding coenzyme a: M162 (= M162), L164 (= L164), S171 (= S171), V173 (≠ L173), T224 (≠ V223), K225 (= K224), I290 (≠ L287), F294 (= F291), R301 (= R298), A447 (≠ E440), G448 (= G441), I452 (= I445), D456 (= D449), R460 (= R453), K461 (= K454)
- binding icosanoic acid: G96 (≠ A94), M130 (= M128), G133 (= G132), M134 (≠ A133), E136 (= E135), A160 (≠ G160), Q299 (≠ A296), M303 (≠ A300), A447 (≠ E440)
- binding flavin-adenine dinucleotide: M162 (= M162), L164 (= L164), T165 (= T165), G170 (= G170), S171 (= S171), F196 (= F196), I197 (= I197), T198 (= T198), T266 (= T264), R326 (= R323), 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)
35% identity, 96% coverage: 1:572/597 of query aligns to 1:582/607 of 6lq1A
- binding coenzyme a: M162 (= M162), S171 (= S171), V173 (≠ L173), T224 (≠ V223), I290 (≠ L287), F294 (= F291), R301 (= R298), A447 (≠ E440), I452 (= I445), D456 (= D449), R460 (= R453), K461 (= K454)
- binding flavin-adenine dinucleotide: L164 (= L164), T165 (= T165), G170 (= G170), S171 (= S171), F196 (= F196), I197 (= I197), T198 (= T198), T266 (= T264), R326 (= R323), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442)
- binding octanoic acid (caprylic acid): M130 (= M128), 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)
35% identity, 96% coverage: 1:572/597 of query aligns to 1:582/607 of 6lq0A
- binding hexanoic acid: M303 (≠ A300), Y446 (= Y439), A447 (≠ E440)
- binding coenzyme a: S171 (= S171), V173 (≠ L173), T224 (≠ V223), K225 (= K224), I290 (≠ L287), F294 (= F291), R301 (= R298), A447 (≠ E440), G448 (= G441), I452 (= I445), D456 (= D449), R460 (= R453), K461 (= K454)
- binding flavin-adenine dinucleotide: M162 (= M162), L164 (= L164), T165 (= T165), G170 (= G170), S171 (= S171), F196 (= F196), I197 (= I197), T198 (= T198), R326 (= R323), I345 (= I339), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442), Q455 (≠ N448)
6lpyA Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c4coa (see paper)
35% identity, 96% coverage: 1:572/597 of query aligns to 1:582/607 of 6lpyA
- binding butanoic acid: Y446 (= Y439), A447 (≠ E440)
- binding coenzyme a: M162 (= M162), L164 (= L164), S171 (= S171), V173 (≠ L173), T224 (≠ V223), K225 (= K224), I290 (≠ L287), F294 (= F291), R301 (= R298), A447 (≠ E440), I452 (= I445), D456 (= D449), R460 (= R453), K461 (= K454), R464 (= R457)
- binding flavin-adenine dinucleotide: M162 (= M162), L164 (= L164), T165 (= T165), G170 (= G170), S171 (= S171), F196 (= F196), I197 (= I197), T198 (= T198), R326 (= R323), 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)
35% identity, 96% coverage: 1:572/597 of query aligns to 1:583/608 of 6ksbA
- binding coenzyme a: M162 (= M162), S171 (= S171), V173 (≠ L173), T224 (≠ V223), K225 (= K224), I290 (≠ L287), F294 (= F291), E298 (≠ N295), R301 (= R298), A447 (≠ E440), G448 (= G441), I452 (= I445), D456 (= D449), R460 (= R453), K461 (= K454)
- binding flavin-adenine dinucleotide: L164 (= L164), T165 (= T165), G170 (= G170), S171 (= S171), F196 (= F196), I197 (= I197), T198 (= T198), T266 (= T264), R326 (= R323), I345 (= I339), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442), Q455 (≠ N448)
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)
35% identity, 96% coverage: 1:572/597 of query aligns to 1:586/611 of O53666
- MVLT 162:165 (≠ MNLT 162:165) binding
- S171 (= S171) binding ; binding ; mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- T198 (= T198) binding
- TK 224:225 (≠ VK 223:224) binding
- K225 (= K224) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- F294 (= F291) mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R301 (= R298) binding ; mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R326 (= R323) binding
- K338 (≠ R332) binding
- QTLGG 420:424 (≠ QVHGG 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)
35% identity, 96% coverage: 1:572/597 of query aligns to 1:582/607 of 6kseA
- active site: L164 (= L164), T165 (= T165), A300 (= A297), R460 (= R453)
- binding flavin-adenine dinucleotide: M162 (= M162), L164 (= L164), T165 (= T165), G170 (= G170), S171 (= S171), F196 (= F196), T198 (= T198), R326 (= R323), Q328 (= Q325), I345 (= I339), H348 (= H342), Q420 (= Q413), T421 (≠ V414), G423 (= G416), G424 (= G417), I442 (= I435), Y446 (= Y439), T449 (= T442)
- binding stearoyl-coenzyme a: D93 (≠ T91), H115 (≠ N113), W126 (≠ S124), G130 (≠ M128), G133 (= G132), F134 (≠ A133), M162 (= M162), S171 (= S171), T224 (≠ V223), K225 (= K224), I290 (≠ L287), F294 (= F291), A300 (= A297), R301 (= R298), Y446 (= Y439), A447 (≠ E440), I452 (= I445), D456 (= D449), R460 (= R453), K461 (= K454)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
32% identity, 56% coverage: 111:446/597 of query aligns to 75:373/383 of 1bucA
- active site: L128 (= L164), T129 (= T165), G246 (≠ A297), E367 (= E440)
- binding acetoacetyl-coenzyme a: L96 (≠ T131), F126 (≠ M162), G134 (= G170), T135 (≠ S171), T162 (= T198), N182 (≠ V223), H183 (≠ K224), F236 (≠ L287), M240 (≠ F291), M241 (≠ I292), L243 (≠ M294), D244 (≠ N295), T317 (≠ P377), Y366 (= Y439), E367 (= E440), G368 (= G441)
- binding flavin-adenine dinucleotide: F126 (≠ M162), L128 (= L164), T129 (= T165), G134 (= G170), T135 (≠ S171), F160 (= F196), T162 (= T198), Y366 (= Y439), T369 (= T442), E371 (≠ A444)
Sites not aligning to the query:
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
32% identity, 56% coverage: 111:446/597 of query aligns to 75:373/383 of Q06319
- E367 (= E440) active site, Proton acceptor; mutation to Q: Loss of activity.
7w0jE Acyl-coa dehydrogenase, tfu_1647
32% identity, 62% coverage: 79:446/597 of query aligns to 41:372/382 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 (= R323), Q272 (= Q325), F273 (≠ G326), I277 (= I339), F280 (≠ H342), I283 (≠ V345), Q339 (= Q413), L340 (≠ V414), G343 (= G417), Y365 (= Y439), E366 (= E440), T368 (= T442), Q370 (≠ A444), I371 (= I445)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
32% identity, 62% coverage: 79:446/597 of query aligns to 40:371/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S171), T134 (≠ L173), R180 (≠ K224), R234 (≠ E288), L237 (≠ F291), R238 (≠ I292), L240 (≠ M294), D241 (≠ N295), R244 (= R298), E365 (= E440), G366 (= G441)
- binding flavin-adenine dinucleotide: Y123 (≠ M162), L125 (= L164), S126 (≠ T165), G131 (= G170), S132 (= S171), W156 (≠ F196), I157 (= I197), T158 (= T198), I360 (= I435), T367 (= T442), Q369 (≠ A444)
Sites not aligning to the query:
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
32% identity, 62% coverage: 79:446/597 of query aligns to 40:371/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ M162), L125 (= L164), S126 (≠ T165), G131 (= G170), S132 (= S171), W156 (≠ F196), I157 (= I197), T158 (= T198), I360 (= I435), Y364 (= Y439), T367 (= T442), Q369 (≠ A444)
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)
30% identity, 62% coverage: 79:446/597 of query aligns to 31:359/369 of 3pfdC
- active site: L116 (= L164), S117 (≠ T165), T233 (≠ A297), E353 (= E440)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M162), L116 (= L164), S117 (≠ T165), G122 (= G170), S123 (= S171), W147 (≠ F196), I148 (= I197), T149 (= T198), R259 (= R323), F262 (≠ R332), V266 (≠ I339), N269 (≠ H342), Q326 (= Q413), L327 (≠ V414), G330 (= G417), I348 (= I435), Y352 (= Y439), T355 (= T442), Q357 (≠ A444)
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, 69% coverage: 35:445/597 of query aligns to 6:368/380 of 4l1fA
- active site: L125 (= L164), T126 (= T165), G242 (≠ A297), E363 (= E440)
- binding coenzyme a persulfide: T132 (≠ S171), H179 (≠ K224), F232 (≠ L287), M236 (≠ F291), E237 (≠ I292), L239 (≠ M294), D240 (≠ N295), R243 (= R298), Y362 (= Y439), E363 (= E440), G364 (= G441)
- binding flavin-adenine dinucleotide: F123 (≠ M162), L125 (= L164), T126 (= T165), G131 (= G170), T132 (≠ S171), F156 (= F196), I157 (= I197), T158 (= T198), R268 (= R323), Q270 (= Q325), F271 (≠ G326), I275 (= I339), F278 (≠ H342), L281 (≠ V345), Q336 (= Q413), I337 (≠ V414), G340 (= G417), I358 (= I435), Y362 (= Y439), T365 (= T442), Q367 (≠ A444)
- binding 1,3-propandiol: Q10 (≠ D39)
Sites not aligning to the query:
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
30% identity, 63% coverage: 80:453/597 of query aligns to 39:375/378 of 5ol2F
- active site: L124 (= L164), T125 (= T165), G241 (≠ A297), G374 (= G452)
- binding coenzyme a persulfide: L238 (≠ M294), R242 (= R298), E362 (= E440), G363 (= G441)
- binding flavin-adenine dinucleotide: F122 (≠ M162), L124 (= L164), T125 (= T165), P127 (= P167), T131 (≠ S171), F155 (= F196), I156 (= I197), T157 (= T198), E198 (= E254), R267 (= R323), F270 (≠ R332), L274 (≠ I339), F277 (≠ H342), Q335 (= Q413), L336 (≠ V414), G338 (= G416), G339 (= G417), Y361 (= Y439), T364 (= T442), E366 (≠ A444)
Sites not aligning to the query:
Query Sequence
>Dsui_2302 FitnessBrowser__PS:Dsui_2302
MSQYNAPLRDMHFVMKELAGLEQVVQLPGYEEVDTDLSDAILEEASKFAGNVLSPINFSG
DQEGSKWHDKAVTVPAGFKEAYTQFAENGWTALACSPEFGGQGLPKLISTAVNEMWKSAN
MAFSLCPMLTTGAIEALMTAGSDALKQKFLPKMVSGEWTGTMNLTEPSAGSDLAAVRTRA
EPQGDGSYKIFGQKIFITYGDHNMTENIVHLVLARLPNAPEGVKGISLFVVPKFMVKDDG
SLGERNDAYCVSIEHKLGIHASPTAVMAFGDHGGAVGYLVGEENRGLEYMFIMMNAARFA
VGMEGVALAERAYQQAVWYAKDRIQGTELGVRGGPKVSILKHPDVRRLLMSMRSQTEAAR
ALAYVVAAAMDAAKHHPDEAVRAANQAFADLMIPVVKGHSTEMSIEVASEGVQVHGGMGF
IEETGAAQHLRDARITAIYEGTTAIQANDLIGRKMAREGGATIKAVIAEMRKLDAKLAAQ
NGADFVAIRKRFAAGVDALEQAANWIVAIFKDDIKAAHAGSVPFLRLLGIVAGGWQMARA
ALVAQEKIAGGDSDPFYAAKIVTARFFADHQLTKAQGLTDSIVDGATGTLALAEELF
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