SitesBLAST
Comparing 6937588 Sama_1743 acyl-CoA dehydrogenase family protein (RefSeq) 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)
42% identity, 99% coverage: 1:573/578 of query aligns to 1:586/591 of A3SI50
- M161 (= M164) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S173) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F198) mutation to A: Almost completely abolishes the activity.
- S197 (≠ T200) mutation to A: Retains 3.6% of wild-type activity.
- K223 (≠ N222) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ N279) mutation to A: Retains 18% of wild-type activity.
- K281 (= K280) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ A283) mutation to A: Retains 97% of wild-type activity.
- F287 (= F286) mutation to A: Retains 76% of wild-type activity.
- Y434 (= Y433) mutation to A: Retains 51% of wild-type activity.
- E435 (= E434) mutation to A: Loss of activity.
- R448 (= R447) mutation to A: Retains 44% of wild-type activity.
6ksaB Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c18coa (see paper)
31% identity, 100% coverage: 1:578/578 of query aligns to 4:611/611 of 6ksaB
- binding flavin-adenine dinucleotide: M165 (= M164), L167 (≠ M166), T168 (= T167), G173 (= G172), S174 (= S173), F199 (= F198), I200 (= I199), T201 (= T200), R329 (= R318), I348 (= I333), H351 (= H336), Q423 (= Q407), T424 (≠ V408), G426 (= G410), G427 (= G411), I445 (= I429), Y449 (= Y433), T452 (= T436)
- binding magnesium ion: H388 (≠ A379), Y475 (≠ T456), E479 (≠ F460)
- binding stearoyl-coenzyme a: W115 (≠ V112), M133 (≠ L131), M137 (≠ A135), A163 (≠ G162), M165 (= M164), L167 (≠ M166), S174 (= S173), V176 (≠ L175), T227 (≠ S221), K228 (≠ N222), I293 (≠ L282), F297 (= F286), Q302 (≠ Y291), R304 (= R293), Y449 (= Y433), A450 (≠ E434), I455 (= I439), D459 (= D443), R463 (= R447), K464 (= K448)
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: 1:578/578 of query aligns to 1:611/611 of Q3L887
6ksbA Crystal structure of e447a m130g acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c16coa (see paper)
32% identity, 100% coverage: 1:578/578 of query aligns to 1:608/608 of 6ksbA
- binding coenzyme a: M162 (= M164), S171 (= S173), V173 (≠ L175), T224 (≠ S221), K225 (≠ N222), I290 (≠ L282), F294 (= F286), E298 (≠ N290), R301 (= R293), A447 (≠ E434), G448 (= G435), I452 (= I439), D456 (= D443), R460 (= R447), K461 (= K448)
- binding flavin-adenine dinucleotide: L164 (≠ M166), T165 (= T167), G170 (= G172), S171 (= S173), F196 (= F198), I197 (= I199), T198 (= T200), T266 (= T262), R326 (= R318), I345 (= I333), H348 (= H336), Q420 (= Q407), T421 (≠ V408), G423 (= G410), G424 (= G411), I442 (= I429), Y446 (= Y433), T449 (= T436), Q455 (≠ I442)
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)
37% identity, 75% coverage: 35:466/578 of query aligns to 33:482/611 of O53666
- MVLT 162:165 (≠ MDMT 164:167) binding
- S171 (= S173) binding ; binding ; mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- T198 (= T200) binding
- TK 224:225 (≠ SN 221:222) binding
- K225 (≠ N222) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- F294 (= F286) mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R301 (= R293) binding ; mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R326 (= R318) binding
- K338 (≠ S326) binding
- QTLGG 420:424 (≠ QVFGG 407:411) binding
- E447 (= E434) binding ; mutation to A: Loss of activity.
- T449 (= T436) binding
- D456 (= D443) binding
- R460 (= R447) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- RK 460:461 (= RK 447:448) binding
6lq8A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c22coa (see paper)
31% identity, 100% coverage: 1:578/578 of query aligns to 1:607/607 of 6lq8A
- binding coenzyme a: M162 (= M164), L164 (≠ M166), S171 (= S173), V173 (≠ L175), T224 (≠ S221), K225 (≠ N222), I290 (≠ L282), F294 (= F286), R301 (= R293), A447 (≠ E434), G448 (= G435), I452 (= I439), D456 (= D443), R460 (= R447), K461 (= K448)
- binding docosanoic acid: G96 (≠ S96), L97 (≠ G97), Q111 (≠ G111), M130 (≠ L131), G133 (= G134), M134 (≠ A135), E136 (≠ L137), I137 (≠ A138), M162 (= M164), T198 (= T200), Q299 (≠ Y291), A300 (≠ E292), Y446 (= Y433), A447 (≠ E434)
- binding flavin-adenine dinucleotide: M162 (= M164), L164 (≠ M166), T165 (= T167), G170 (= G172), S171 (= S173), F196 (= F198), I197 (= I199), T198 (= T200), R326 (= R318), I345 (= I333), H348 (= H336), Q420 (= Q407), T421 (≠ V408), G423 (= G410), G424 (= G411), I442 (= I429), Y446 (= Y433), T449 (= T436)
6lq7A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c17coa (see paper)
31% identity, 100% coverage: 1:578/578 of query aligns to 1:607/607 of 6lq7A
- binding coenzyme a: M162 (= M164), L164 (≠ M166), S171 (= S173), V173 (≠ L175), T224 (≠ S221), K225 (≠ N222), I290 (≠ L282), F294 (= F286), R301 (= R293), A447 (≠ E434), G448 (= G435), I452 (= I439), D456 (= D443), R460 (= R447), K461 (= K448)
- binding flavin-adenine dinucleotide: M162 (= M164), L164 (≠ M166), T165 (= T167), G170 (= G172), S171 (= S173), F196 (= F198), I197 (= I199), T198 (= T200), R326 (= R318), I345 (= I333), H348 (= H336), Q420 (= Q407), T421 (≠ V408), G423 (= G410), G424 (= G411), I442 (= I429), Y446 (= Y433), T449 (= T436)
- binding heptadecanoic acid: M130 (≠ L131), A160 (≠ G162), Q299 (≠ Y291), Y446 (= Y433), A447 (≠ E434)
6lq6A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c20coa (see paper)
31% identity, 100% coverage: 1:578/578 of query aligns to 1:607/607 of 6lq6A
- binding coenzyme a: M162 (= M164), L164 (≠ M166), S171 (= S173), V173 (≠ L175), T224 (≠ S221), K225 (≠ N222), I290 (≠ L282), F294 (= F286), R301 (= R293), A447 (≠ E434), G448 (= G435), I452 (= I439), D456 (= D443), R460 (= R447), K461 (= K448)
- binding icosanoic acid: G96 (≠ S96), M130 (≠ L131), G133 (= G134), M134 (≠ A135), E136 (≠ L137), A160 (≠ G162), Q299 (≠ Y291), M303 (≠ A295), A447 (≠ E434)
- binding flavin-adenine dinucleotide: M162 (= M164), L164 (≠ M166), T165 (= T167), G170 (= G172), S171 (= S173), F196 (= F198), I197 (= I199), T198 (= T200), T266 (= T262), R326 (= R318), H348 (= H336), Q420 (= Q407), T421 (≠ V408), G423 (= G410), G424 (= G411), I442 (= I429), Y446 (= Y433), T449 (= T436)
6lq1A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c8coa (see paper)
31% identity, 100% coverage: 1:578/578 of query aligns to 1:607/607 of 6lq1A
- binding coenzyme a: M162 (= M164), S171 (= S173), V173 (≠ L175), T224 (≠ S221), I290 (≠ L282), F294 (= F286), R301 (= R293), A447 (≠ E434), I452 (= I439), D456 (= D443), R460 (= R447), K461 (= K448)
- binding flavin-adenine dinucleotide: L164 (≠ M166), T165 (= T167), G170 (= G172), S171 (= S173), F196 (= F198), I197 (= I199), T198 (= T200), T266 (= T262), R326 (= R318), H348 (= H336), Q420 (= Q407), T421 (≠ V408), G423 (= G410), G424 (= G411), I442 (= I429), Y446 (= Y433), T449 (= T436)
- binding octanoic acid (caprylic acid): M130 (≠ L131), M162 (= M164), Y446 (= Y433), A447 (≠ E434)
6lq0A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c6coa (see paper)
31% identity, 100% coverage: 1:578/578 of query aligns to 1:607/607 of 6lq0A
- binding hexanoic acid: M303 (≠ A295), Y446 (= Y433), A447 (≠ E434)
- binding coenzyme a: S171 (= S173), V173 (≠ L175), T224 (≠ S221), K225 (≠ N222), I290 (≠ L282), F294 (= F286), R301 (= R293), A447 (≠ E434), G448 (= G435), I452 (= I439), D456 (= D443), R460 (= R447), K461 (= K448)
- binding flavin-adenine dinucleotide: M162 (= M164), L164 (≠ M166), T165 (= T167), G170 (= G172), S171 (= S173), F196 (= F198), I197 (= I199), T198 (= T200), R326 (= R318), I345 (= I333), H348 (= H336), Q420 (= Q407), T421 (≠ V408), G423 (= G410), G424 (= G411), I442 (= I429), Y446 (= Y433), T449 (= T436), Q455 (≠ I442)
6lpyA Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c4coa (see paper)
31% identity, 100% coverage: 1:578/578 of query aligns to 1:607/607 of 6lpyA
- binding butanoic acid: Y446 (= Y433), A447 (≠ E434)
- binding coenzyme a: M162 (= M164), L164 (≠ M166), S171 (= S173), V173 (≠ L175), T224 (≠ S221), K225 (≠ N222), I290 (≠ L282), F294 (= F286), R301 (= R293), A447 (≠ E434), I452 (= I439), D456 (= D443), R460 (= R447), K461 (= K448), R464 (≠ G451)
- binding flavin-adenine dinucleotide: M162 (= M164), L164 (≠ M166), T165 (= T167), G170 (= G172), S171 (= S173), F196 (= F198), I197 (= I199), T198 (= T200), R326 (= R318), I345 (= I333), H348 (= H336), Q420 (= Q407), T421 (≠ V408), G423 (= G410), G424 (= G411), I442 (= I429), Y446 (= Y433), T449 (= T436)
6kseA Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria tuberculosisin complex with c18coa (see paper)
33% identity, 94% coverage: 35:578/578 of query aligns to 33:607/607 of 6kseA
- active site: L164 (≠ M166), T165 (= T167), A300 (≠ E292), R460 (= R447)
- binding flavin-adenine dinucleotide: M162 (= M164), L164 (≠ M166), T165 (= T167), G170 (= G172), S171 (= S173), F196 (= F198), T198 (= T200), R326 (= R318), Q328 (= Q320), I345 (= I333), H348 (= H336), Q420 (= Q407), T421 (≠ V408), G423 (= G410), G424 (= G411), I442 (= I429), Y446 (= Y433), T449 (= T436)
- binding stearoyl-coenzyme a: D93 (≠ V93), H115 (≠ D115), W126 (≠ N126), G130 (≠ S130), G133 (= G134), F134 (≠ A135), M162 (= M164), S171 (= S173), T224 (≠ S221), K225 (≠ N222), I290 (≠ L282), F294 (= F286), A300 (≠ E292), R301 (= R293), Y446 (= Y433), A447 (≠ E434), I452 (= I439), D456 (= D443), R460 (= R447), K461 (= K448)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
33% identity, 61% coverage: 91:440/578 of query aligns to 46:364/374 of 5lnxD
- active site: L122 (≠ M166), T123 (= T167), G239 (≠ E292), E358 (= E434)
- binding flavin-adenine dinucleotide: L122 (≠ M166), T123 (= T167), G128 (= G172), S129 (= S173), F153 (= F198), T155 (= T200), R265 (= R318), Q267 (= Q320), F268 (≠ A329), I272 (= I333), N275 (≠ H336), I278 (≠ V339), Q331 (= Q407), I332 (≠ V408), G335 (= G411), Y357 (= Y433), T360 (= T436), E362 (≠ G438)
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)
31% identity, 63% coverage: 81:442/578 of query aligns to 31:361/369 of 3pfdC
- active site: L116 (≠ M166), S117 (≠ T167), T233 (≠ E292), E353 (= E434)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M164), L116 (≠ M166), S117 (≠ T167), G122 (= G172), S123 (= S173), W147 (≠ F198), I148 (= I199), T149 (= T200), R259 (= R318), F262 (≠ A329), V266 (≠ I333), N269 (≠ H336), Q326 (= Q407), L327 (≠ V408), G330 (= G411), I348 (= I429), Y352 (= Y433), T355 (= T436), Q357 (≠ G438)
Sites not aligning to the query:
3nf4A Crystal structure of acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to flavin adenine dinucleotide (see paper)
31% identity, 71% coverage: 30:442/578 of query aligns to 2:362/369 of 3nf4A
- active site: L127 (≠ M166), S128 (≠ T167), G240 (≠ E292), E354 (= E434)
- binding flavin-adenine dinucleotide: Y125 (≠ M164), L127 (≠ M166), S128 (≠ T167), G133 (= G172), S134 (= S173), W158 (≠ F198), T160 (= T200), I349 (= I429), T356 (= T436), Q358 (≠ G438), I359 (= I439)
Sites not aligning to the query:
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
30% identity, 63% coverage: 81:442/578 of query aligns to 40:373/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S173), T134 (≠ L175), R180 (≠ N222), R234 (≠ A283), L237 (≠ F286), R238 (≠ T287), L240 (≠ M289), D241 (≠ N290), R244 (= R293), E365 (= E434), G366 (= G435)
- binding flavin-adenine dinucleotide: Y123 (≠ M164), L125 (≠ M166), S126 (≠ T167), G131 (= G172), S132 (= S173), W156 (≠ F198), I157 (= I199), T158 (= T200), I360 (= I429), T367 (= T436), Q369 (≠ G438)
Sites not aligning to the query:
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
30% identity, 63% coverage: 81:442/578 of query aligns to 40:373/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ M164), L125 (≠ M166), S126 (≠ T167), G131 (= G172), S132 (= S173), W156 (≠ F198), I157 (= I199), T158 (= T200), I360 (= I429), Y364 (= Y433), T367 (= T436), Q369 (≠ G438)
7w0jE Acyl-coa dehydrogenase, tfu_1647
30% identity, 63% coverage: 81:442/578 of query aligns to 41:374/382 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 (≠ T167), W157 (≠ F198), R270 (= R318), Q272 (= Q320), F273 (vs. gap), I277 (≠ V324), F280 (≠ T327), I283 (≠ V339), Q339 (= Q407), L340 (≠ V408), G343 (= G411), Y365 (= Y433), E366 (= E434), T368 (= T436), Q370 (≠ G438), I371 (= I439)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
30% identity, 63% coverage: 82:447/578 of query aligns to 39:375/378 of 5ol2F
- active site: L124 (≠ M166), T125 (= T167), G241 (≠ E292), G374 (= G446)
- binding coenzyme a persulfide: L238 (≠ M289), R242 (= R293), E362 (= E434), G363 (= G435)
- binding flavin-adenine dinucleotide: F122 (≠ M164), L124 (≠ M166), T125 (= T167), P127 (= P169), T131 (≠ S173), F155 (= F198), I156 (= I199), T157 (= T200), E198 (= E252), R267 (= R318), F270 (≠ A329), L274 (≠ I333), F277 (≠ H336), Q335 (= Q407), L336 (≠ V408), G338 (= G410), G339 (= G411), Y361 (= Y433), T364 (= T436), E366 (≠ G438)
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, 61% coverage: 89:442/578 of query aligns to 47:371/380 of 4l1fA
- active site: L125 (≠ M166), T126 (= T167), G242 (≠ E292), E363 (= E434)
- binding coenzyme a persulfide: T132 (≠ S173), H179 (≠ N222), F232 (≠ L282), M236 (≠ F286), E237 (≠ T287), L239 (≠ M289), D240 (≠ N290), R243 (= R293), Y362 (= Y433), E363 (= E434), G364 (= G435)
- binding flavin-adenine dinucleotide: F123 (≠ M164), L125 (≠ M166), T126 (= T167), G131 (= G172), T132 (≠ S173), F156 (= F198), I157 (= I199), T158 (= T200), R268 (= R318), Q270 (= Q320), F271 (vs. gap), I275 (≠ V324), F278 (≠ T327), L281 (≠ V339), Q336 (= Q407), I337 (≠ V408), G340 (= G411), I358 (= I429), Y362 (= Y433), T365 (= T436), Q367 (≠ G438)
Sites not aligning to the query:
Query Sequence
>6937588 Sama_1743 acyl-CoA dehydrogenase family protein (RefSeq)
MNPYQAPLGEMRFLLEHVFNAQATWQGLASLDGMVDMDTALAILEEAAKLNSELVHPINR
AGDEEGVGFSDGRVTTPKGYKEAYNAFVEGGWVGLSGDPEYGGMGMPKMLGVLVDEMGYS
ACNAFNLYGSLTAGAALAINAHGTEELKSTYLPKLYSGEWAGAMDMTEPQAGSDLRHIRT
RAEPQEDGSYLITGSKIFITGGDQDLTENVIHLVLAKISGSNTLSLFLVPKIGVDDQGNL
TEPNGVSVGSIEHKMGLKGSATCVMNFDSARGWLIGRENKGLACMFTMMNYERLAIGIQG
LGSAQAAVQMASDYARERLQGNAVGSTAAADPILVHGDVRRMLLTTRTLTDAGRALAVHT
GKQLDLAKFADDDAVKTKAGRYVGLLTPVAKAFLTDRGLDITIMAQQVFGGHGYIRETGI
EQLVRDTRIAQIYEGTNGIQAIDFLGRKVTGDNLATVKEFIAEHIEVLSDTCDKANSLRV
GFADFVAVATWINDNKLSRPALINSVAVEMLDAFGYLLYGYYHLLMRDAARAADSEFAAA
KAAYCDYYFAKLMPRADALLRAAKAGDELLMSLPETCF
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