SitesBLAST
Comparing RR42_RS01285 FitnessBrowser__Cup4G11:RR42_RS01285 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)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
47% identity, 92% coverage: 6:512/553 of query aligns to 5:502/541 of P33224
- 182:191 (vs. 181:190, 100% identical) binding
- T185 (= T184) binding
- S191 (= S190) binding
- FFS 216:218 (= FFS 219:221) binding
- S218 (= S221) binding
- 423:433 (vs. 430:440, 100% identical) binding
- N429 (= N436) binding
- R437 (= R444) mutation to Q: Does not affect DNA binding affinity.
Sites not aligning to the query:
- 518 R→Q: Reduces DNA binding affinity.
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
47% identity, 92% coverage: 6:512/553 of query aligns to 5:502/540 of 3u33A
- active site: M184 (= M183), T185 (= T184), T298 (= T304), E425 (= E432), R437 (= R444)
- binding flavin-adenine dinucleotide: M182 (= M181), M184 (= M183), T185 (= T184), G190 (= G189), S191 (= S190), F216 (= F219), S218 (= S221), R324 (= R330), F327 (= F333), L331 (= L337), Q334 (= Q340), M337 (= M343), E398 (= E405), V399 (= V406), G401 (= G408), G402 (= G409), W424 (= W431), G426 (= G433), S427 (= S434), N429 (= N436), L433 (= L440)
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
45% identity, 99% coverage: 6:553/553 of query aligns to 2:540/541 of 5ez3B
- active site: M181 (= M183), T182 (= T184), T295 (= T304), E423 (= E432), R435 (= R444)
- binding flavin-adenine dinucleotide: M181 (= M183), T182 (= T184), G186 (= G188), G187 (= G189), T188 (≠ S190), F213 (= F219), S215 (= S221), R321 (= R330), F324 (= F333), L328 (= L337), Q331 (= Q340), M334 (= M343), E396 (= E405), C397 (≠ V406), G399 (= G408), G400 (= G409), W422 (= W431), E423 (= E432), S425 (= S434), N427 (= N436), L431 (= L440)
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
31% identity, 86% coverage: 20:496/553 of query aligns to 11:486/503 of 6sdaB
- active site: M171 (= M183), T172 (= T184), T296 (= T304), R439 (= R444)
- binding flavin-adenine dinucleotide: Q169 (≠ M181), M171 (= M183), T172 (= T184), G177 (= G189), S178 (= S190), F208 (= F219), T209 (≠ F220), R322 (= R330), F325 (= F333), L329 (= L337), H332 (≠ Q340), E400 (= E405), M401 (≠ V406), G404 (= G409), Y407 (= Y412), W426 (= W431), T429 (≠ S434), N431 (= N436), L435 (= L440)
- binding decanoyl-CoA: C128 (= C133), G177 (= G189), S178 (= S190), S230 (≠ P240), V286 (≠ I294), A290 (≠ I298), L293 (≠ A301), N294 (≠ T302), R297 (= R305), R377 (= R382), W426 (= W431), E427 (= E432)
6sd8X Bd2924 apo-form (see paper)
31% identity, 86% coverage: 20:496/553 of query aligns to 11:486/503 of 6sd8X
- active site: M171 (= M183), T172 (= T184), T296 (= T304), R439 (= R444)
- binding flavin-adenine dinucleotide: Q169 (≠ M181), M171 (= M183), T172 (= T184), G176 (= G188), G177 (= G189), S178 (= S190), F208 (= F219), T209 (≠ F220), R322 (= R330), F325 (= F333), L329 (= L337), H332 (≠ Q340), M401 (≠ V406), G404 (= G409), W426 (= W431), T429 (≠ S434), V432 (≠ I437), L435 (= L440)
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
28% identity, 90% coverage: 17:512/553 of query aligns to 23:544/593 of 4y9jB
- active site: M190 (= M183), T191 (= T184), T315 (= T304), E446 (= E432), R458 (= R444)
- binding flavin-adenine dinucleotide: Q188 (≠ M181), M190 (= M183), T191 (= T184), G196 (= G189), S197 (= S190), F223 (= F219), S224 (≠ F220), S225 (= S221), R341 (= R330), V343 (≠ A332), F344 (= F333), Q348 (≠ L337), E419 (= E405), C420 (≠ V406), G422 (= G408), G423 (= G409), Y426 (= Y412), W445 (= W431), T448 (≠ S434), V451 (≠ I437), L454 (= L440)
- 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 (≠ L132), A147 (≠ T136), Q188 (≠ M181), S197 (= S190), S249 (vs. gap), R303 (= R292), V305 (≠ I294), S309 (≠ I298), L312 (≠ A301), N313 (≠ T302), R316 (= R305), A322 (≠ G311), R396 (= R382), W445 (= W431), E446 (= E432), V451 (≠ I437), R458 (= R444)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
28% identity, 90% coverage: 17:512/553 of query aligns to 41:562/617 of Q9XWZ2
- E91 (≠ N64) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ A127) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ S129) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G189) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G411) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R423) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
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)
27% identity, 59% coverage: 181:507/553 of query aligns to 161:511/591 of A3SI50
- M161 (= M181) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S190) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F219) mutation to A: Almost completely abolishes the activity.
- S197 (= S221) mutation to A: Retains 3.6% of wild-type activity.
- K223 (vs. gap) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ G291) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ R292) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ P295) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ I298) mutation to A: Retains 76% of wild-type activity.
- Y434 (≠ W431) mutation to A: Retains 51% of wild-type activity.
- E435 (= E432) mutation to A: Loss of activity.
- R448 (≠ Q447) mutation to A: Retains 44% of wild-type activity.
7w0jE Acyl-coa dehydrogenase, tfu_1647
28% identity, 58% coverage: 129:446/553 of query aligns to 84:380/382 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 (≠ T184), W157 (= W218), R270 (= R330), Q272 (≠ A332), F273 (= F333), I277 (≠ L337), F280 (≠ Q340), I283 (≠ M343), Q339 (≠ E405), L340 (≠ V406), G343 (= G409), Y365 (≠ W431), E366 (= E432), T368 (≠ S434), Q370 (≠ N436), I371 (= I437)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
28% identity, 58% coverage: 129:446/553 of query aligns to 83:379/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S190), T134 (≠ V192), R180 (vs. gap), R234 (≠ P295), L237 (≠ I298), R238 (≠ E299), L240 (≠ A301), D241 (≠ T302), R244 (= R305), E365 (= E432), G366 (= G433), R377 (= R444)
- binding flavin-adenine dinucleotide: Y123 (≠ M181), L125 (≠ M183), S126 (≠ T184), G131 (= G189), S132 (= S190), W156 (= W218), I157 (≠ F219), T158 (≠ F220), I360 (≠ V427), T367 (≠ S434), Q369 (≠ N436)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
28% identity, 58% coverage: 129:446/553 of query aligns to 83:379/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ M181), L125 (≠ M183), S126 (≠ T184), G131 (= G189), S132 (= S190), W156 (= W218), I157 (≠ F219), T158 (≠ F220), I360 (≠ V427), Y364 (≠ W431), T367 (≠ S434), Q369 (≠ N436)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
26% identity, 49% coverage: 181:449/553 of query aligns to 123:380/380 of 4l1fA
- active site: L125 (≠ M183), T126 (= T184), G242 (≠ T304), E363 (= E432), R375 (= R444)
- binding coenzyme a persulfide: T132 (≠ S190), H179 (vs. gap), F232 (≠ I294), M236 (≠ I298), E237 (= E299), L239 (≠ A301), D240 (≠ T302), R243 (= R305), Y362 (≠ W431), E363 (= E432), G364 (= G433), R375 (= R444)
- binding flavin-adenine dinucleotide: F123 (≠ M181), L125 (≠ M183), T126 (= T184), G131 (= G189), T132 (≠ S190), F156 (= F219), I157 (≠ F220), T158 (≠ S221), R268 (= R330), Q270 (≠ A332), F271 (= F333), I275 (≠ L337), F278 (≠ Q340), L281 (≠ M343), Q336 (≠ E405), I337 (≠ V406), G340 (= G409), I358 (≠ V427), Y362 (≠ W431), T365 (≠ S434), Q367 (≠ N436)
Sites not aligning to the query:
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
28% identity, 49% coverage: 174:446/553 of query aligns to 113:375/378 of 7p9xA
- binding 1-monoenoyl-CoA: S129 (= S190), L131 (≠ V192), K176 (vs. gap), F229 (≠ I294), M233 (≠ I298), L236 (≠ A301), R240 (= R305), Y360 (≠ W431), T361 (≠ E432), G362 (= G433), R373 (= R444)
- binding flavin-adenine dinucleotide: A122 (≠ M183), T123 (= T184), G128 (= G189), S129 (= S190), F153 (= F219), I154 (≠ F220), T155 (≠ S221), N206 (≠ S274), L356 (≠ V427), Y360 (≠ W431), T363 (≠ S434), Q365 (≠ N436), I366 (= I437)
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)
28% identity, 51% coverage: 169:448/553 of query aligns to 102:369/369 of 3pfdC
- active site: L116 (≠ M183), S117 (≠ T184), T233 (= T304), E353 (= E432), R365 (= R444)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M181), L116 (≠ M183), S117 (≠ T184), G122 (= G189), S123 (= S190), W147 (= W218), I148 (≠ F219), T149 (≠ F220), R259 (= R330), F262 (= F333), V266 (≠ L337), N269 (≠ Q340), Q326 (≠ E405), L327 (≠ V406), G330 (= G409), I348 (≠ V427), Y352 (≠ W431), T355 (≠ S434), Q357 (≠ N436)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
28% identity, 49% coverage: 174:446/553 of query aligns to 115:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S190), L133 (≠ V192), K178 (vs. gap), F231 (≠ I294), M235 (≠ I298), L238 (≠ A301), N241 (≠ T304), R242 (= R305), Y362 (≠ W431), T363 (≠ E432), G364 (= G433), R375 (= R444)
- binding flavin-adenine dinucleotide: L122 (≠ M181), A124 (≠ M183), T125 (= T184), G130 (= G189), S131 (= S190), F155 (= F219), I156 (≠ F220), T157 (≠ S221), K200 (= K266), N208 (≠ S274), L358 (≠ V427), T365 (≠ S434), Q367 (≠ N436), I368 (= I437)
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
31% identity, 48% coverage: 183:448/553 of query aligns to 121:370/370 of 2dvlA
- active site: L121 (≠ M183), T122 (= T184), G233 (≠ T304), E354 (= E432), R366 (= R444)
- binding flavin-adenine dinucleotide: L121 (≠ M183), T122 (= T184), G127 (= G189), S128 (= S190), W152 (= W218), I153 (≠ F219), T154 (≠ F220), T356 (≠ S434), E358 (≠ N436)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
26% identity, 48% coverage: 181:448/553 of query aligns to 126:383/383 of 1bucA
- active site: L128 (≠ M183), T129 (= T184), G246 (≠ T304), E367 (= E432), G379 (≠ R444)
- binding acetoacetyl-coenzyme a: F126 (≠ M181), G134 (= G189), T135 (≠ S190), T162 (≠ S221), N182 (≠ P240), H183 (vs. gap), F236 (≠ I294), M240 (≠ I298), M241 (≠ E299), L243 (≠ A301), D244 (≠ T302), T317 (vs. gap), Y366 (≠ W431), E367 (= E432), G368 (= G433)
- binding flavin-adenine dinucleotide: F126 (≠ M181), L128 (≠ M183), T129 (= T184), G134 (= G189), T135 (≠ S190), F160 (= F219), T162 (≠ S221), Y366 (≠ W431), T369 (≠ S434), E371 (≠ N436), M375 (≠ L440)
Sites not aligning to the query:
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
26% identity, 48% coverage: 181:448/553 of query aligns to 126:383/383 of Q06319
- E367 (= E432) active site, Proton acceptor; mutation to Q: Loss of activity.
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
28% identity, 49% coverage: 177:446/553 of query aligns to 118:378/380 of 2pg0A
- active site: M124 (= M183), T125 (= T184), E243 (≠ T304), A364 (≠ E432), R376 (= R444)
- binding flavin-adenine dinucleotide: I122 (≠ M181), M124 (= M183), T125 (= T184), G130 (= G189), S131 (= S190), F155 (= F219), I156 (≠ F220), T157 (≠ S221), R269 (= R330), F272 (= F333), F279 (≠ Q340), Q337 (≠ E405), L338 (≠ V406), G340 (= G408), G341 (= G409), V359 (= V427), I362 (= I430), Y363 (≠ W431), T366 (≠ S434), E368 (≠ N436), M369 (≠ I437)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
27% identity, 46% coverage: 181:437/553 of query aligns to 119:366/383 of 4iv6B
- active site: L121 (≠ M183), T122 (= T184), G240 (≠ T304), E361 (= E432)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ M183), T122 (= T184), G126 (= G188), G127 (= G189), S128 (= S190), W152 (= W218), I153 (≠ F219), S154 (≠ F220), R266 (= R330), S268 (≠ A332), F269 (= F333), I273 (≠ L337), H276 (≠ Q340), V279 (≠ M343), R334 (≠ E405), V335 (= V406), G338 (= G409), L356 (≠ V427), G360 (≠ W431), T363 (≠ S434), E365 (≠ N436), I366 (= I437)
Sites not aligning to the query:
Query Sequence
>RR42_RS01285 FitnessBrowser__Cup4G11:RR42_RS01285
MTEAATHRVFNQVPDLTGYNLFTGDPALRAALERLGGGWHASALDIFGARLGKPDVQQWA
AEANRHAPELHTHSRTGERIDEVEFPPAWHALLALLRSQQLQALPFAQPREGAWVARAAG
YFLQAQAESGSLCPPTMTFASIPVLQKEATLFAELGPKLFATLHDPRDLPWRDKHAVMIG
MGMTEKQGGSDVRSNTTVARAVRGGGRGAEYAITGHKWFFSAPMCDAHMVVARMGAQDGP
LSCFFVPRFRDDGSKNPVQIQRLKDKLGNRSNASSEVEFREATGILIGEEGRGIPTIIEM
ATYTRLDCVIGSAAIIRAALVQAIHHARHRMAFGRLLVEQPLMRNVLADLALESQAATLL
MMELAHAFERADADPLAAAWKRIVTPAAKFWVCKRAIEVTGEAMEVWGGNGYVEEGPMAR
LYREAPVNSIWEGSGNIMCLDVLRALQRNPEDAGRLLQDLSRRAGGHPAVRAALASLQAM
LRDAPDLLEAGARRFAQGLVLTAQAALMLAHADADDAERFVASRLGHQHGRVFGTLEGGD
AALARVVARAWPA
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