SitesBLAST
Comparing WP_047215817.1 NCBI__GCF_001931675.1:WP_047215817.1 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)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
34% identity, 98% coverage: 3:381/387 of query aligns to 2:376/383 of 4iv6B
- active site: L121 (≠ V124), T122 (= T125), G240 (≠ E245), E361 (≠ P366), K373 (≠ E378)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ V124), T122 (= T125), G126 (≠ T129), G127 (= G130), S128 (≠ T131), W152 (= W155), I153 (= I156), S154 (= S157), R266 (= R271), S268 (≠ V273), F269 (= F274), I273 (= I278), H276 (≠ N281), V279 (= V284), R334 (≠ Q339), V335 (≠ T340), G338 (= G343), L356 (= L361), G360 (≠ A365), T363 (≠ S368), E365 (≠ N370), I366 (≠ L371)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
31% identity, 92% coverage: 8:364/387 of query aligns to 7:360/378 of 5ol2F
- active site: L124 (≠ V124), T125 (= T125), G241 (≠ E245)
- binding calcium ion: E29 (= E30), E33 (≠ A34), R35 (≠ D36)
- binding coenzyme a persulfide: L238 (= L242), R242 (= R246)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), T125 (= T125), P127 (= P127), T131 (= T131), F155 (≠ W155), I156 (= I156), T157 (≠ S157), E198 (vs. gap), R267 (= R271), F270 (= F274), L274 (≠ I278), F277 (≠ N281), Q335 (= Q339), L336 (≠ T340), G338 (= G342), G339 (= G343)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
31% identity, 96% coverage: 12:382/387 of query aligns to 9:374/374 of 5lnxD
- active site: L122 (≠ V124), T123 (= T125), G239 (≠ E245), E358 (≠ P366), K370 (≠ E378)
- binding flavin-adenine dinucleotide: L122 (≠ V124), T123 (= T125), G128 (= G130), S129 (≠ T131), F153 (≠ W155), T155 (≠ S157), R265 (= R271), Q267 (≠ V273), F268 (= F274), I272 (= I278), N275 (= N281), I278 (≠ V284), Q331 (= Q339), I332 (≠ T340), G335 (= G343), Y357 (≠ A365), T360 (≠ S368), E362 (≠ N370)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
32% identity, 96% coverage: 14:384/387 of query aligns to 13:380/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (≠ T131), L133 (≠ T133), K178 (≠ E182), F231 (= F235), M235 (≠ L239), L238 (= L242), N241 (≠ E245), R242 (= R246), Y362 (≠ A365), T363 (≠ I367), G364 (≠ S368), R375 (≠ H379)
- binding flavin-adenine dinucleotide: L122 (≠ M122), A124 (≠ V124), T125 (= T125), G130 (= G130), S131 (≠ T131), F155 (≠ W155), I156 (= I156), T157 (≠ S157), K200 (≠ V201), N208 (= N209), L358 (= L361), T365 (= T369), Q367 (≠ L371), I368 (= I372)
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)
32% identity, 96% coverage: 14:384/387 of query aligns to 13:380/380 of Q39QF5
- D91 (≠ Y91) 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 (≠ M122) binding FAD
- A124 (≠ V124) binding FAD
- T125 (= T125) binding FAD
- S131 (≠ T131) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA; binding FAD
- T157 (≠ S157) binding FAD
- K178 (≠ E182) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- N241 (≠ E245) 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 (= R246) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- T363 (≠ I367) 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 (= T369) binding FAD
- Q367 (≠ L371) binding FAD
- R375 (≠ H379) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
32% identity, 96% coverage: 14:384/387 of query aligns to 11:378/378 of 7p9xA
- binding 1-monoenoyl-CoA: L82 (≠ G84), D89 (≠ Y91), S129 (≠ T131), L131 (≠ T133), K176 (≠ E182), F229 (= F235), M233 (≠ L239), L236 (= L242), R240 (= R246), Y360 (≠ A365), T361 (≠ I367), G362 (≠ S368), R373 (≠ H379)
- binding flavin-adenine dinucleotide: A122 (≠ V124), T123 (= T125), G128 (= G130), S129 (≠ T131), F153 (≠ W155), I154 (= I156), T155 (≠ S157), N206 (= N209), L356 (= L361), Y360 (≠ A365), T363 (= T369), Q365 (≠ L371), I366 (= I372)
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)
32% identity, 91% coverage: 12:364/387 of query aligns to 4:351/369 of 3pfdC
- active site: L116 (≠ V124), S117 (≠ T125), T233 (≠ E245)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M122), L116 (≠ V124), S117 (≠ T125), G122 (= G130), S123 (≠ T131), W147 (= W155), I148 (= I156), T149 (≠ S157), R259 (= R271), F262 (= F274), V266 (≠ I278), N269 (= N281), Q326 (= Q339), L327 (≠ T340), G330 (= G343), I348 (≠ L361)
Sites not aligning to the query:
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
31% identity, 91% coverage: 29:381/387 of query aligns to 29:377/379 of 1ukwB
- active site: L124 (≠ V124), S125 (≠ T125), T241 (≠ E245), E362 (≠ P366), R374 (≠ E378)
- binding cobalt (ii) ion: D145 (= D145), H146 (≠ R146)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), S125 (≠ T125), G130 (= G130), S131 (≠ T131), W155 (= W155), S157 (= S157), K200 (≠ A194), L357 (= L361), Y361 (≠ A365), E362 (≠ P366), T364 (≠ S368), E366 (≠ N370), L370 (≠ S374)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
31% identity, 91% coverage: 29:381/387 of query aligns to 29:377/379 of 1ukwA
- active site: L124 (≠ V124), S125 (≠ T125), T241 (≠ E245), E362 (≠ P366), R374 (≠ E378)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), S125 (≠ T125), G130 (= G130), S131 (≠ T131), W155 (= W155), S157 (= S157), L357 (= L361), Y361 (≠ A365), E362 (≠ P366), T364 (≠ S368), E366 (≠ N370), L370 (≠ S374)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
31% identity, 91% coverage: 12:364/387 of query aligns to 10:360/379 of 6fahD
- active site: L124 (≠ V124), T125 (= T125), G241 (≠ E245)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), T125 (= T125), R152 (≠ Q152), F155 (≠ W155), T157 (≠ S157), E198 (≠ V201), R267 (= R271), Q269 (≠ V273), F270 (= F274), I274 (= I278), F277 (≠ N281), Q335 (= Q339), I336 (≠ T340), G339 (= G343)
Sites not aligning to the query:
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
30% identity, 97% coverage: 7:380/387 of query aligns to 8:377/381 of 2jifA
- active site: L125 (≠ V124), S126 (≠ T125), G242 (≠ E245), E363 (≠ P366), K375 (≠ E378)
- binding coenzyme a persulfide: S132 (≠ T131), S134 (≠ T133), Y178 (≠ V177), Y232 (≠ F235), I236 (≠ L239), L239 (= L242), N240 (= N243), R243 (= R246), Y362 (≠ A365), E363 (≠ P366), G364 (≠ I367), I368 (≠ L371)
- binding flavin-adenine dinucleotide: F123 (≠ M122), L125 (≠ V124), S126 (≠ T125), G131 (= G130), S132 (≠ T131), W156 (= W155), I157 (= I156), S158 (= S157), K201 (≠ I204), T209 (= T212), R268 (= R271), F271 (= F274), L275 (≠ I278), F278 (≠ N281), L281 (≠ V284), E336 (≠ Q339), W337 (≠ T340), G340 (= G343), N367 (= N370), I368 (≠ L371)
P45954 Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial; SBCAD; 2-methyl branched chain acyl-CoA dehydrogenase; 2-MEBCAD; 2-methylbutyryl-coenzyme A dehydrogenase; 2-methylbutyryl-CoA dehydrogenase; EC 1.3.8.5 from Homo sapiens (Human) (see 6 papers)
30% identity, 97% coverage: 7:380/387 of query aligns to 59:428/432 of P45954