SitesBLAST
Comparing WP_037575735.1 NCBI__GCF_000744815.1:WP_037575735.1 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)
7w0jE Acyl-coa dehydrogenase, tfu_1647
74% identity, 98% coverage: 6:384/385 of query aligns to 1:380/382 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 (= S132), W157 (= W162), R270 (= R274), Q272 (= Q276), F273 (= F277), I277 (= I281), F280 (= F284), I283 (≠ V287), Q339 (= Q343), L340 (= L344), G343 (= G347), Y365 (= Y369), E366 (= E370), T368 (= T372), Q370 (= Q374), I371 (≠ V375)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
74% identity, 98% coverage: 7:384/385 of query aligns to 1:379/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S138), T134 (≠ A140), R180 (≠ K185), R234 (≠ A239), L237 (≠ M242), R238 (≠ K243), L240 (= L245), D241 (= D246), R244 (= R249), E365 (= E370), G366 (= G371), R377 (= R382)
- binding flavin-adenine dinucleotide: Y123 (= Y129), L125 (= L131), S126 (= S132), G131 (= G137), S132 (= S138), W156 (= W162), I157 (= I163), T158 (= T164), I360 (= I365), T367 (= T372), Q369 (= Q374)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
74% identity, 98% coverage: 7:384/385 of query aligns to 1:379/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (= Y129), L125 (= L131), S126 (= S132), G131 (= G137), S132 (= S138), W156 (= W162), I157 (= I163), T158 (= T164), I360 (= I365), Y364 (= Y369), T367 (= T372), Q369 (= Q374)
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)
69% identity, 96% coverage: 16:384/385 of query aligns to 1:367/369 of 3pfdC
- active site: L116 (= L131), S117 (= S132), T233 (= T248), E353 (= E370), R365 (= R382)
- binding dihydroflavine-adenine dinucleotide: Y114 (= Y129), L116 (= L131), S117 (= S132), G122 (= G137), S123 (= S138), W147 (= W162), I148 (= I163), T149 (= T164), R259 (= R274), F262 (= F277), V266 (≠ I281), N269 (≠ F284), Q326 (= Q343), L327 (= L344), G330 (= G347), I348 (= I365), Y352 (= Y369), T355 (= T372), Q357 (= Q374)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
52% identity, 97% coverage: 13:384/385 of query aligns to 5:376/378 of 5ol2F
- active site: L124 (= L131), T125 (≠ S132), G241 (≠ T248), G374 (≠ R382)
- binding calcium ion: E29 (= E37), E33 (≠ Q41), R35 (= R43)
- binding coenzyme a persulfide: L238 (= L245), R242 (= R249), E362 (= E370), G363 (= G371)
- binding flavin-adenine dinucleotide: F122 (≠ Y129), L124 (= L131), T125 (≠ S132), P127 (= P134), T131 (≠ S138), F155 (≠ W162), I156 (= I163), T157 (= T164), E198 (= E205), R267 (= R274), F270 (= F277), L274 (≠ I281), F277 (= F284), Q335 (= Q343), L336 (= L344), G338 (= G346), G339 (= G347), Y361 (= Y369), T364 (= T372), E366 (≠ Q374)
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
49% identity, 97% coverage: 11:384/385 of query aligns to 1:375/378 of 7p9xA
- binding 1-monoenoyl-CoA: L82 (= L92), D89 (≠ L99), S129 (= S138), L131 (≠ A140), K176 (= K185), F229 (= F238), M233 (= M242), L236 (= L245), R240 (= R249), Y360 (= Y369), T361 (≠ E370), G362 (= G371), R373 (= R382)
- binding flavin-adenine dinucleotide: A122 (vs. gap), T123 (≠ S132), G128 (= G137), S129 (= S138), F153 (≠ W162), I154 (= I163), T155 (= T164), N206 (≠ T215), L356 (≠ I365), Y360 (= Y369), T363 (= T372), Q365 (= Q374), I366 (≠ V375)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
49% identity, 97% coverage: 11:384/385 of query aligns to 3:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S138), L133 (≠ A140), K178 (= K185), F231 (= F238), M235 (= M242), L238 (= L245), N241 (≠ T248), R242 (= R249), Y362 (= Y369), T363 (≠ E370), G364 (= G371), R375 (= R382)
- binding flavin-adenine dinucleotide: L122 (= L131), A124 (vs. gap), T125 (≠ S132), G130 (= G137), S131 (= S138), F155 (≠ W162), I156 (= I163), T157 (= T164), K200 (= K207), N208 (≠ T215), L358 (≠ I365), T365 (= T372), Q367 (= Q374), I368 (≠ V375)
Q39QF5 Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase; CHeneCoA dehydrogenase; EC 1.3.8.10 from Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15) (see paper)
49% identity, 97% coverage: 11:384/385 of query aligns to 3:377/380 of Q39QF5
- D91 (≠ L99) mutation to E: Retains minor activity.; mutation to N: Loss of activity. Gains a low but significant C1,C2-dehydrogenation activity, but the C3,C6- and C3,C4-dehydrogenating activities are largely diminished; when associated with D-241.
- L122 (= L131) binding FAD
- A124 (vs. gap) binding FAD
- T125 (≠ S132) binding FAD
- S131 (= S138) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA; binding FAD
- T157 (= T164) binding FAD
- K178 (= K185) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- N241 (≠ T248) mutation to D: Shows decreased activity, with a shift towards C3,C4- versus C3,C6-dehydrogenation. Gains a low but significant C1,C2-dehydrogenation activity, but the C3,C6- and C3,C4-dehydrogenating activities are largely diminished; when associated with N-91.
- R242 (= R249) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- T363 (≠ E370) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA; mutation to V: Shows decreased activity, with a shift towards C3,C4- versus C3,C6-dehydrogenation.
- T365 (= T372) binding FAD
- Q367 (= Q374) binding FAD
- R375 (= R382) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
48% identity, 97% coverage: 10:384/385 of query aligns to 3:377/380 of 4l1fA
- active site: L125 (= L131), T126 (≠ S132), G242 (≠ T248), E363 (= E370), R375 (= R382)
- binding coenzyme a persulfide: T132 (≠ S138), H179 (≠ K185), F232 (= F238), M236 (= M242), E237 (≠ K243), L239 (= L245), D240 (= D246), R243 (= R249), Y362 (= Y369), E363 (= E370), G364 (= G371), R375 (= R382)
- binding flavin-adenine dinucleotide: F123 (≠ Y129), L125 (= L131), T126 (≠ S132), G131 (= G137), T132 (≠ S138), F156 (≠ W162), I157 (= I163), T158 (= T164), R268 (= R274), Q270 (= Q276), F271 (= F277), I275 (= I281), F278 (= F284), L281 (≠ V287), Q336 (= Q343), I337 (≠ L344), G340 (= G347), I358 (= I365), Y362 (= Y369), T365 (= T372), Q367 (= Q374)
- binding 1,3-propandiol: L5 (≠ I12), Q10 (≠ E17)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
44% identity, 97% coverage: 10:384/385 of query aligns to 3:376/379 of 1ukwB
- active site: L124 (= L131), S125 (= S132), T241 (= T248), E362 (= E370), R374 (= R382)
- binding cobalt (ii) ion: D145 (= D152), H146 (≠ A153)
- binding flavin-adenine dinucleotide: F122 (≠ Y129), L124 (= L131), S125 (= S132), G130 (= G137), S131 (= S138), W155 (= W162), S157 (≠ T164), K200 (= K207), L357 (≠ I365), Y361 (= Y369), E362 (= E370), T364 (= T372), E366 (≠ Q374), L370 (≠ I378)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
44% identity, 97% coverage: 10:384/385 of query aligns to 3:376/379 of 1ukwA
- active site: L124 (= L131), S125 (= S132), T241 (= T248), E362 (= E370), R374 (= R382)
- binding flavin-adenine dinucleotide: F122 (≠ Y129), L124 (= L131), S125 (= S132), G130 (= G137), S131 (= S138), W155 (= W162), S157 (≠ T164), L357 (≠ I365), Y361 (= Y369), E362 (= E370), T364 (= T372), E366 (≠ Q374), L370 (≠ I378)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
44% identity, 96% coverage: 14:384/385 of query aligns to 4:372/374 of 5lnxD