SitesBLAST
Comparing RR42_RS11190 FitnessBrowser__Cup4G11:RR42_RS11190 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
45% identity, 100% coverage: 1:540/540 of query aligns to 5:540/541 of 5ez3B
- active site: M181 (= M175), T182 (= T176), T295 (≠ S293), E423 (= E420), R435 (= R432)
- binding flavin-adenine dinucleotide: M181 (= M175), T182 (= T176), G186 (= G180), G187 (= G181), T188 (≠ S182), F213 (= F211), S215 (= S213), R321 (= R319), F324 (= F322), L328 (= L326), Q331 (= Q329), M334 (= M332), E396 (= E393), C397 (≠ V394), G399 (= G396), G400 (= G397), W422 (= W419), E423 (= E420), S425 (= S422), N427 (= N424), L431 (= L428)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
45% identity, 96% coverage: 3:519/540 of query aligns to 10:521/541 of P33224
- 182:191 (vs. 173:182, 100% identical) binding
- T185 (= T176) binding
- S191 (= S182) binding
- FFS 216:218 (= FFS 211:213) binding
- S218 (= S213) binding
- 423:433 (vs. 418:428, 91% identical) binding
- N429 (= N424) binding
- R437 (= R432) mutation to Q: Does not affect DNA binding affinity.
- R518 (≠ E516) mutation to Q: Reduces DNA binding affinity.
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
45% identity, 96% coverage: 3:519/540 of query aligns to 10:521/540 of 3u33A
- active site: M184 (= M175), T185 (= T176), T298 (≠ S293), E425 (= E420), R437 (= R432)
- binding flavin-adenine dinucleotide: M182 (= M173), M184 (= M175), T185 (= T176), G190 (= G181), S191 (= S182), F216 (= F211), S218 (= S213), R324 (= R319), F327 (= F322), L331 (= L326), Q334 (= Q329), M337 (= M332), E398 (= E393), V399 (= V394), G401 (= G396), G402 (= G397), W424 (= W419), G426 (= G421), S427 (= S422), N429 (= N424), L433 (= L428)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
29% identity, 85% coverage: 11:470/540 of query aligns to 43:518/617 of Q9XWZ2
- E91 (≠ N56) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ I119) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ S121) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G181) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G399) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R411) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
29% identity, 85% coverage: 11:470/540 of query aligns to 25:500/593 of 4y9jB
- active site: M190 (= M175), T191 (= T176), T315 (≠ S293), E446 (= E420), R458 (= R432)
- binding flavin-adenine dinucleotide: Q188 (≠ M173), M190 (= M175), T191 (= T176), G196 (= G181), S197 (= S182), F223 (= F211), S224 (≠ F212), S225 (= S213), R341 (= R319), V343 (≠ A321), F344 (= F322), Q348 (≠ L326), E419 (= E393), C420 (≠ V394), G422 (= G396), G423 (= G397), Y426 (= Y400), W445 (= W419), T448 (≠ S422), V451 (= V425), L454 (= L428)
- binding S-{(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} undecanethioate: S143 (≠ L124), A147 (≠ N128), Q188 (≠ M173), S197 (= S182), S249 (= S230), R303 (= R281), V305 (≠ I283), S309 (≠ L287), L312 (≠ A290), N313 (≠ T291), R316 (= R294), A322 (≠ S300), R396 (= R370), W445 (= W419), E446 (= E420), V451 (= V425), R458 (= R432)
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
32% identity, 76% coverage: 69:481/540 of query aligns to 71:483/503 of 6sdaB
- active site: M171 (= M175), T172 (= T176), T296 (≠ S293), R439 (= R432)
- binding flavin-adenine dinucleotide: Q169 (≠ M173), M171 (= M175), T172 (= T176), G177 (= G181), S178 (= S182), F208 (= F211), T209 (≠ F212), R322 (= R319), F325 (= F322), L329 (= L326), H332 (≠ Q329), E400 (= E393), M401 (≠ V394), G404 (= G397), Y407 (= Y400), W426 (= W419), T429 (≠ S422), N431 (= N424), L435 (= L428)
- binding decanoyl-CoA: C128 (= C125), G177 (= G181), S178 (= S182), S230 (vs. gap), V286 (≠ I283), A290 (≠ L287), L293 (≠ A290), N294 (≠ T291), R297 (= R294), R377 (= R370), W426 (= W419), E427 (= E420)
6sd8X Bd2924 apo-form (see paper)
32% identity, 76% coverage: 69:481/540 of query aligns to 71:483/503 of 6sd8X
- active site: M171 (= M175), T172 (= T176), T296 (≠ S293), R439 (= R432)
- binding flavin-adenine dinucleotide: Q169 (≠ M173), M171 (= M175), T172 (= T176), G176 (= G180), G177 (= G181), S178 (= S182), F208 (= F211), T209 (≠ F212), R322 (= R319), F325 (= F322), L329 (= L326), H332 (≠ Q329), M401 (≠ V394), G404 (= G397), W426 (= W419), T429 (≠ S422), V432 (= V425), L435 (= L428)
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)
30% identity, 48% coverage: 173:431/540 of query aligns to 161:446/591 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 (= F211) mutation to A: Almost completely abolishes the activity.
- S197 (= S213) mutation to A: Retains 3.6% of wild-type activity.
- K223 (vs. gap) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ G280) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ R281) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ P284) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ L287) mutation to A: Retains 76% of wild-type activity.
- Y434 (≠ W419) mutation to A: Retains 51% of wild-type activity.
- E435 (= E420) mutation to A: Loss of activity.
Sites not aligning to the query:
- 448 R→A: Retains 44% of wild-type activity.
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
28% identity, 51% coverage: 162:437/540 of query aligns to 113:380/380 of 4l1fA
- active site: L125 (≠ M175), T126 (= T176), G242 (≠ S293), E363 (= E420), R375 (= R432)
- binding coenzyme a persulfide: T132 (≠ S182), H179 (vs. gap), F232 (≠ I283), M236 (≠ L287), E237 (= E288), L239 (≠ A290), D240 (≠ T291), R243 (= R294), Y362 (≠ W419), E363 (= E420), G364 (= G421), R375 (= R432)
- binding flavin-adenine dinucleotide: F123 (≠ M173), L125 (≠ M175), T126 (= T176), G131 (= G181), T132 (≠ S182), F156 (= F211), I157 (≠ F212), T158 (≠ S213), R268 (= R319), Q270 (≠ A321), F271 (= F322), I275 (≠ L326), F278 (≠ Q329), L281 (≠ M332), Q336 (≠ E393), I337 (≠ V394), G340 (= G397), I358 (≠ V415), Y362 (≠ W419), T365 (≠ S422), Q367 (≠ N424)
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)
27% identity, 57% coverage: 127:436/540 of query aligns to 71:369/369 of 3pfdC
- active site: L116 (≠ M175), S117 (≠ T176), T233 (≠ S293), E353 (= E420), R365 (= R432)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M173), L116 (≠ M175), S117 (≠ T176), G122 (= G181), S123 (= S182), W147 (= W210), I148 (≠ F211), T149 (≠ F212), R259 (= R319), F262 (= F322), V266 (≠ L326), N269 (≠ Q329), Q326 (≠ E393), L327 (≠ V394), G330 (= G397), I348 (≠ V415), Y352 (≠ W419), T355 (≠ S422), Q357 (≠ N424)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
28% identity, 50% coverage: 163:434/540 of query aligns to 112:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S182), L133 (≠ V184), K178 (≠ A228), F231 (≠ I283), M235 (≠ L287), L238 (≠ A290), N241 (≠ S293), R242 (= R294), Y362 (≠ W419), T363 (≠ E420), G364 (= G421), R375 (= R432)
- binding flavin-adenine dinucleotide: L122 (≠ M173), A124 (≠ M175), T125 (= T176), G130 (= G181), S131 (= S182), F155 (= F211), I156 (≠ F212), T157 (≠ S213), K200 (= K255), N208 (≠ S263), L358 (≠ V415), T365 (≠ S422), Q367 (≠ N424), I368 (≠ V425)
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
28% identity, 50% coverage: 163:434/540 of query aligns to 110:375/378 of 7p9xA
- binding 1-monoenoyl-CoA: S129 (= S182), L131 (≠ V184), K176 (≠ A228), F229 (≠ I283), M233 (≠ L287), L236 (≠ A290), R240 (= R294), Y360 (≠ W419), T361 (≠ E420), G362 (= G421), R373 (= R432)
- binding flavin-adenine dinucleotide: A122 (≠ M175), T123 (= T176), G128 (= G181), S129 (= S182), F153 (= F211), I154 (≠ F212), T155 (≠ S213), N206 (≠ S263), L356 (≠ V415), Y360 (≠ W419), T363 (≠ S422), Q365 (≠ N424), I366 (≠ V425)
Sites not aligning to the query:
P26440 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Butyryl-CoA dehydrogenase; EC 1.3.8.4; EC 1.3.8.1 from Homo sapiens (Human) (see 5 papers)
28% identity, 49% coverage: 173:439/540 of query aligns to 165:426/426 of P26440
- 165:174 (vs. 173:182, 40% identical) binding
- S174 (= S182) binding
- WIT 198:200 (≠ WFF 210:212) binding
- SR 222:223 (vs. gap) binding
- G250 (≠ S260) to A: in IVA; uncertain significance
- Y277 (≠ P284) binding
- DLER 284:287 (≠ TYSR 291:294) binding
- E286 (≠ S293) active site, Proton acceptor; mutation to D: Residual isovaleryl-CoA dehydrogenase activity.; mutation to G: Loss of isovaleryl-CoA dehydrogenase activity. Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 407-E.; mutation to Q: Loss of isovaleryl-CoA dehydrogenase activity.
- A291 (≠ S298) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R319) binding
- Q323 (≠ P330) binding
- I379 (≠ M392) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ EVFGG 393:397) binding
- R398 (= R411) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ N416) to N: in IVA; uncertain significance
- A407 (≠ E420) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ EG 420:421) binding
- TSE 409:411 (≠ SGN 422:424) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
28% identity, 49% coverage: 173:439/540 of query aligns to 132:393/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T176), G140 (= G181), S141 (= S182), W165 (= W210), T167 (≠ F212), R279 (= R319), F282 (= F322), I286 (≠ L326), F289 (≠ Q329), Q347 (≠ E393), C348 (≠ V394), G351 (= G397), L369 (≠ V415), G375 (= G421), T376 (≠ S422), L382 (= L428)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
27% identity, 49% coverage: 162:425/540 of query aligns to 112:367/378 of 5ol2F
- active site: L124 (≠ M175), T125 (= T176), G241 (≠ S293)
- binding coenzyme a persulfide: L238 (≠ A290), R242 (= R294), E362 (= E420), G363 (= G421)
- binding flavin-adenine dinucleotide: F122 (≠ M173), L124 (≠ M175), T125 (= T176), P127 (≠ K178), T131 (≠ S182), F155 (= F211), I156 (≠ F212), T157 (≠ S213), E198 (= E248), R267 (= R319), F270 (= F322), L274 (= L326), F277 (≠ Q329), Q335 (≠ E393), L336 (≠ V394), G338 (= G396), G339 (= G397), Y361 (≠ W419), T364 (≠ S422), E366 (≠ N424)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
26% identity, 69% coverage: 61:430/540 of query aligns to 20:368/374 of 5lnxD
- active site: L122 (≠ M175), T123 (= T176), G239 (≠ S293), E358 (= E420)
- binding flavin-adenine dinucleotide: L122 (≠ M175), T123 (= T176), G128 (= G181), S129 (= S182), F153 (= F211), T155 (≠ S213), R265 (= R319), Q267 (≠ A321), F268 (= F322), I272 (≠ L326), N275 (≠ Q329), I278 (≠ M332), Q331 (≠ E393), I332 (≠ V394), G335 (= G397), Y357 (≠ W419), T360 (≠ S422), E362 (≠ N424)
Sites not aligning to the query:
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
29% identity, 47% coverage: 174:425/540 of query aligns to 124:370/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S182), T134 (≠ V184), R180 (vs. gap), R234 (≠ P284), L237 (= L287), R238 (≠ E288), L240 (≠ A290), D241 (≠ T291), R244 (= R294), E365 (= E420), G366 (= G421)
- binding flavin-adenine dinucleotide: L125 (≠ M175), S126 (≠ T176), G131 (= G181), S132 (= S182), W156 (= W210), I157 (≠ F211), T158 (≠ F212), I360 (≠ V415), T367 (≠ S422), Q369 (≠ N424)
Sites not aligning to the query:
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
29% identity, 47% coverage: 174:425/540 of query aligns to 124:370/381 of 8i4pA
- binding flavin-adenine dinucleotide: L125 (≠ M175), S126 (≠ T176), G131 (= G181), S132 (= S182), W156 (= W210), I157 (≠ F211), T158 (≠ F212), I360 (≠ V415), Y364 (≠ W419), T367 (≠ S422), Q369 (≠ N424)
Sites not aligning to the query:
7w0jE Acyl-coa dehydrogenase, tfu_1647
29% identity, 47% coverage: 174:425/540 of query aligns to 125:371/382 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 (= W210), R270 (= R319), Q272 (≠ A321), F273 (= F322), I277 (≠ L326), F280 (≠ Q329), I283 (≠ M332), Q339 (≠ E393), L340 (≠ V394), G343 (= G397), Y365 (≠ W419), E366 (= E420), T368 (≠ S422), Q370 (≠ N424), I371 (≠ V425)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
28% identity, 49% coverage: 173:434/540 of query aligns to 128:384/387 of 1ivhA
- active site: M130 (= M175), S131 (≠ T176), E249 (≠ S293), A370 (≠ E420), R382 (= R432)
- binding coenzyme a persulfide: S137 (= S182), S185 (vs. gap), R186 (vs. gap), V239 (≠ I283), Y240 (≠ P284), M243 (≠ L287), E249 (≠ S293), R250 (= R294), G369 (≠ W419), A370 (≠ E420), G371 (= G421), V375 (= V425)
- binding flavin-adenine dinucleotide: L128 (≠ M173), M130 (= M175), S131 (≠ T176), G136 (= G181), S137 (= S182), W161 (= W210), T163 (≠ F212), R275 (= R319), F278 (= F322), F285 (≠ Q329), M288 (= M332), Q343 (≠ E393), C344 (≠ V394), G347 (= G397), T372 (≠ S422), E374 (≠ N424)
Query Sequence
>RR42_RS11190 FitnessBrowser__Cup4G11:RR42_RS11190
MTNQVPELKDYNLYTSDPGIRRAVARAGAGWNEGELERQGAVLGAEQTIQHAEDANRHHP
ELHTHSRIGERIDQVRFHPAWHELMAMARHSGLANLPFADTRPSAWASYAASLYMHSQIE
SGSLCPTNMTQACIPVLRKEPGLFAQFGDKLLTQAYDPRDLPIAHKRSINVGMGMTEKQG
GSDVRANTTRAVPGRGEGRGAEYLITGHKWFFSAPMSDAHLVLANTEAGSSCFFVPRWRP
DGSKNPIEIQRLKDKVGNRSNSSSEVEFRDAWGIMVGEEGRGIPTILEMATYSRLNCSLS
SAGFLRQALVQALHYARHRSAFGKPLIRQPLMVRLLADMALEAEAAMLLAMDLATAFEAT
DDPARLAWRRILTPASKFWICKRAVEMTGEAMEVFGGNGYVEDGPMGRLFREAPVNSIWE
GSGNVMCLDVLRAIGRNPHDYLRVLEHMSVVGADEPRIQASVAALRAALRLPEEEQQAEA
RRTTTRLVLTAQACLMLQHADTATADAFLASRFDPEWGAVMGISAGQSHAARILEMAWAA
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