SitesBLAST
Comparing WP_022389822.1 NCBI__GCF_000473955.1:WP_022389822.1 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)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
38% identity, 61% coverage: 100:443/568 of query aligns to 44:364/374 of 5lnxD
- active site: L122 (= L175), T123 (= T176), G239 (≠ A292), E358 (= E437)
- binding flavin-adenine dinucleotide: L122 (= L175), T123 (= T176), G128 (= G181), S129 (= S182), F153 (= F208), T155 (= T210), R265 (= R318), Q267 (= Q320), F268 (= F321), I272 (= I325), N275 (≠ F328), I278 (≠ V331), Q331 (= Q410), I332 (= I411), G335 (= G414), Y357 (= Y436), T360 (= T439), E362 (≠ Q441)
Sites not aligning to the query:
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
35% identity, 64% coverage: 93:457/568 of query aligns to 39:377/378 of 5ol2F
- active site: L124 (= L175), T125 (= T176), G241 (≠ A292), G374 (= G454)
- binding coenzyme a persulfide: L238 (≠ M289), R242 (= R293), E362 (= E437), G363 (= G438)
- binding flavin-adenine dinucleotide: F122 (≠ M173), L124 (= L175), T125 (= T176), P127 (= P178), T131 (≠ S182), F155 (= F208), I156 (= I209), T157 (= T210), E198 (= E251), R267 (= R318), F270 (= F321), L274 (≠ I325), F277 (= F328), Q335 (= Q410), L336 (≠ I411), G338 (= G413), G339 (= G414), Y361 (= Y436), T364 (= T439), E366 (≠ Q441)
Sites not aligning to the query:
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
35% identity, 63% coverage: 93:449/568 of query aligns to 40:375/380 of 4l1fA
- active site: L125 (= L175), T126 (= T176), G242 (≠ A292), E363 (= E437), R375 (= R449)
- binding coenzyme a persulfide: T132 (≠ S182), H179 (≠ R231), F232 (≠ L281), M236 (= M286), E237 (≠ A287), L239 (≠ M289), D240 (≠ N290), R243 (= R293), Y362 (= Y436), E363 (= E437), G364 (= G438), R375 (= R449)
- binding flavin-adenine dinucleotide: F123 (≠ M173), L125 (= L175), T126 (= T176), G131 (= G181), T132 (≠ S182), F156 (= F208), I157 (= I209), T158 (= T210), R268 (= R318), Q270 (= Q320), F271 (= F321), I275 (= I325), F278 (= F328), L281 (≠ V331), Q336 (= Q410), I337 (= I411), G340 (= G414), I358 (= I432), Y362 (= Y436), T365 (= T439), Q367 (= Q441)
Sites not aligning to the query:
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
33% identity, 68% coverage: 64:451/568 of query aligns to 23:378/378 of 4n5fA
- active site: L126 (= L175), T127 (= T176), G243 (≠ A292), E364 (= E437), R376 (= R449)
- binding dihydroflavine-adenine dinucleotide: L126 (= L175), T127 (= T176), G132 (= G181), S133 (= S182), F157 (= F208), T159 (= T210), T210 (= T261), Y363 (= Y436), T366 (= T439), E368 (≠ Q441), M372 (≠ V445)
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
32% identity, 70% coverage: 54:451/568 of query aligns to 11:376/376 of 4m9aB
- active site: L124 (= L175), T125 (= T176), G241 (≠ A292), E362 (= E437), R374 (= R449)
- binding dihydroflavine-adenine dinucleotide: F122 (≠ M173), T125 (= T176), G130 (= G181), S131 (= S182), F155 (= F208), T157 (= T210), T208 (= T261), Y361 (= Y436), T364 (= T439), E366 (≠ Q441), M370 (≠ V445)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
31% identity, 73% coverage: 42:457/568 of query aligns to 1:382/383 of 1bucA
- active site: L128 (= L175), T129 (= T176), G246 (≠ A292), E367 (= E437), G379 (= G454)
- binding acetoacetyl-coenzyme a: L96 (≠ D144), F126 (≠ M173), G134 (= G181), T135 (≠ S182), T162 (= T210), N182 (≠ G230), H183 (≠ R231), F236 (≠ L281), M240 (= M286), M241 (≠ A287), L243 (≠ M289), D244 (≠ N290), T317 (≠ Q383), Y366 (= Y436), E367 (= E437), G368 (= G438)
- binding flavin-adenine dinucleotide: F126 (≠ M173), L128 (= L175), T129 (= T176), G134 (= G181), T135 (≠ S182), F160 (= F208), T162 (= T210), Y366 (= Y436), T369 (= T439), E371 (≠ Q441), M375 (≠ V445)
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
31% identity, 73% coverage: 42:457/568 of query aligns to 1:382/383 of Q06319
- E367 (= E437) active site, Proton acceptor; mutation to Q: Loss of activity.
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
32% identity, 61% coverage: 95:443/568 of query aligns to 41:368/379 of 6fahD
- active site: L124 (= L175), T125 (= T176), G241 (≠ A292)
- binding flavin-adenine dinucleotide: F122 (≠ M173), L124 (= L175), T125 (= T176), R152 (≠ V205), F155 (= F208), T157 (= T210), E198 (= E251), R267 (= R318), Q269 (= Q320), F270 (= F321), I274 (= I325), F277 (= F328), Q335 (= Q410), I336 (= I411), G339 (= G414), Y361 (= Y436), T364 (= T439), Q366 (= Q441)
Sites not aligning to the query:
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
31% identity, 72% coverage: 43:451/568 of query aligns to 2:379/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S182), T134 (≠ L184), R180 (= R231), R234 (≠ K283), L237 (≠ M286), R238 (≠ A287), L240 (≠ M289), D241 (≠ N290), R244 (= R293), E365 (= E437), G366 (= G438), R377 (= R449)
- binding flavin-adenine dinucleotide: Y123 (≠ M173), L125 (= L175), S126 (≠ T176), G131 (= G181), S132 (= S182), W156 (≠ F208), I157 (= I209), T158 (= T210), I360 (= I432), T367 (= T439), Q369 (= Q441)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
31% identity, 72% coverage: 43:451/568 of query aligns to 2:379/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ M173), L125 (= L175), S126 (≠ T176), G131 (= G181), S132 (= S182), W156 (≠ F208), I157 (= I209), T158 (= T210), I360 (= I432), Y364 (= Y436), T367 (= T439), Q369 (= Q441)
7w0jE Acyl-coa dehydrogenase, tfu_1647
31% identity, 72% coverage: 43:451/568 of query aligns to 3:380/382 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 (≠ T176), W157 (≠ F208), R270 (= R318), Q272 (= Q320), F273 (= F321), I277 (= I325), F280 (= F328), I283 (≠ V331), Q339 (= Q410), L340 (≠ I411), G343 (= G414), Y365 (= Y436), E366 (= E437), T368 (= T439), Q370 (= Q441), I371 (≠ L442)
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)
29% identity, 73% coverage: 49:464/568 of query aligns to 35:463/591 of A3SI50
- M161 (= M173) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S182) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F208) mutation to A: Almost completely abolishes the activity.
- S197 (≠ T210) mutation to A: Retains 3.6% of wild-type activity.
- K223 (≠ R231) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ K278) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ M279) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ K283) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ M286) 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 (= R449) mutation to A: Retains 44% of wild-type activity.
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, 68% coverage: 66:449/568 of query aligns to 16:365/369 of 3pfdC
- active site: L116 (= L175), S117 (≠ T176), T233 (≠ A292), E353 (= E437), R365 (= R449)
- binding dihydroflavine-adenine dinucleotide: Y114 (vs. gap), L116 (= L175), S117 (≠ T176), G122 (= G181), S123 (= S182), W147 (≠ F208), I148 (= I209), T149 (= T210), R259 (= R318), F262 (= F321), V266 (≠ I325), N269 (≠ F328), Q326 (= Q410), L327 (≠ I411), G330 (= G414), I348 (= I432), Y352 (= Y436), T355 (= T439), Q357 (= Q441)
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
29% identity, 63% coverage: 95:451/568 of query aligns to 43:377/381 of 2jifA
- active site: L125 (= L175), S126 (≠ T176), G242 (≠ A292), E363 (= E437), K375 (≠ R449)
- binding coenzyme a persulfide: S132 (= S182), S134 (≠ L184), Y178 (vs. gap), Y232 (≠ L281), I236 (≠ M286), L239 (≠ M289), N240 (= N290), R243 (= R293), Y362 (= Y436), E363 (= E437), G364 (= G438), I368 (≠ L442)
- binding flavin-adenine dinucleotide: F123 (≠ M173), L125 (= L175), S126 (≠ T176), G131 (= G181), S132 (= S182), W156 (≠ F208), I157 (= I209), S158 (≠ T210), K201 (= K253), T209 (= T261), R268 (= R318), F271 (= F321), L275 (≠ I325), F278 (= F328), L281 (≠ V331), E336 (≠ Q410), W337 (≠ I411), G340 (= G414), N367 (≠ Q441), I368 (≠ L442)
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)
29% identity, 63% coverage: 95:451/568 of query aligns to 94:428/432 of P45954
- V137 (≠ N138) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ I139) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 173:182, 50% identical) binding in other chain
- S183 (= S182) binding substrate
- WIS 207:209 (≠ FIT 208:210) binding in other chain
- S210 (≠ N211) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (vs. gap) binding substrate
- L255 (≠ I256) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ L281) binding substrate
- NEGR 291:294 (≠ NGAR 290:293) binding substrate
- I316 (≠ A315) to V: in dbSNP:rs1131430
- R319 (= R318) binding FAD
- Q330 (≠ P329) binding FAD
- EWMGG 387:391 (≠ QIHGG 410:414) binding FAD
- A416 (≠ T439) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TTQ 439:441) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
8pnsA Crystal structure of the acyl-coa dehydrogenase pa0506 (fade1) from pseudomonas aeruginosa
31% identity, 71% coverage: 45:445/568 of query aligns to 31:448/600 of 8pnsA
- binding octanoyl-coenzyme a: M162 (= M173), T171 (≠ S182), L173 (= L184), T223 (≠ G230), L284 (= L281), F288 (≠ M286), M291 (= M289), Y439 (= Y436), E440 (= E437)
- binding flavin-adenine dinucleotide: L164 (= L175), T165 (= T176), G170 (= G181), T171 (≠ S182), F196 (= F208), S198 (≠ T210), R320 (= R318), Q322 (= Q320), M323 (≠ F321), I339 (= I325), H342 (≠ F328), Q413 (= Q410), I414 (= I411), G417 (= G414), I435 (= I432), Y439 (= Y436), T442 (= T439)
Sites not aligning to the query:
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
34% identity, 62% coverage: 92:443/568 of query aligns to 36:367/383 of 4iv6B
- active site: L121 (= L175), T122 (= T176), G240 (≠ A292), E361 (= E437)
- binding dihydroflavine-adenine dinucleotide: L121 (= L175), T122 (= T176), G126 (≠ A180), G127 (= G181), S128 (= S182), W152 (≠ F208), I153 (= I209), S154 (≠ T210), R266 (= R318), S268 (≠ Q320), F269 (= F321), I273 (= I325), H276 (≠ F328), V279 (= V331), R334 (≠ Q410), V335 (≠ I411), G338 (= G414), L356 (≠ I432), G360 (≠ Y436), T363 (= T439), E365 (≠ Q441), I366 (≠ L442)
Sites not aligning to the query:
8phfA Cryo-em structure of human acad9-s191a (see paper)
31% identity, 71% coverage: 92:494/568 of query aligns to 58:442/547 of 8phfA
- binding flavin-adenine dinucleotide: T144 (= T176), W176 (≠ F208), K225 (= K253), R292 (= R318), Q294 (= Q320), F295 (= F321), F302 (= F328), L304 (≠ A330), I305 (≠ V331), I363 (= I411), G365 (= G413), G366 (= G414), F388 (≠ Y436), E393 (≠ Q441), M397 (≠ V445)
Sites not aligning to the query:
8pu5B Crystal structure of the acyl-coa dehydrogenase fade1(pa0506) e441a from pseudomonas aeruginosa complexed with c16coa
31% identity, 71% coverage: 45:445/568 of query aligns to 30:447/599 of 8pu5B
- binding Palmitoyl-CoA: L109 (≠ I123), G127 (= G141), M161 (= M173), T170 (≠ S182), L172 (= L184), T222 (≠ G230), L283 (= L281), F287 (≠ M286), M290 (= M289), N291 (= N290), R294 (= R293), Y438 (= Y436), A439 (≠ E437)
Sites not aligning to the query:
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
32% identity, 63% coverage: 94:451/568 of query aligns to 37:368/370 of 2dvlA
- active site: L121 (= L175), T122 (= T176), G233 (≠ A292), E354 (= E437), R366 (= R449)
- binding flavin-adenine dinucleotide: L121 (= L175), T122 (= T176), G127 (= G181), S128 (= S182), W152 (≠ F208), I153 (= I209), T154 (= T210), T356 (= T439), E358 (≠ Q441)
Query Sequence
>WP_022389822.1 NCBI__GCF_000473955.1:WP_022389822.1
MANFYLDNSDLKHHLNHPLMKRLVALKERNYTDAEKYDYAPIDFEDAMDSYEKVLEIAGE
ICGDIVAPNAESVDHEGPQVINGRVKYASGTEKNLDALVKAGLMGISIPRRYNGLNFSLV
PYIMAADMVSRADAGFVNIWGLQDCAETIYEFASEEQKQKYLPRVCAGETMAMDLTEPDA
GSDLQAVMLKATYSEKDGCWYLNGVKRFITNGDGHIALVLARSEEGTKDGRGLSMFIYDK
NDGGVTVRRIENKMGIKGSPTCELVFKNAKAELCGDRKMGLIKYVMALMNGARLGIAAQS
VGVSEAAYREALTYAQERRQFGKAIIEFPAVYEMLSLMKAKLDASRSLLYETTRFVDMYK
VYEDISKERKLEKEERDEMKKYQRQADAFTPLAKGMSSEFCNQNAYDCVQIHGGSGFMKD
YACERIYRDARITSIYEGTTQLQVVAAIRHVTTGTFLNMMKFYEQETICPELVPLQNRLK
AMTEIYEKTVASVVETKDNEYIDFHARRMVEMAGHIIMGHLLLLDTTRCDSFRNSAEVYI
HFGEAEVKKQAEFISKFNVEDLEFYRKG
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