SitesBLAST
Comparing BWI76_RS02590 FitnessBrowser__Koxy:BWI76_RS02590 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)
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
79% identity, 99% coverage: 1:537/545 of query aligns to 1:537/540 of 3u33A
- active site: M184 (= M184), T185 (= T185), T298 (= T298), E425 (= E425), R437 (= R437)
- binding flavin-adenine dinucleotide: M182 (= M182), G183 (= G183), M184 (= M184), T185 (= T185), G189 (= G189), G190 (= G190), S191 (= S191), F216 (= F216), F217 (= F217), S218 (= S218), K260 (= K260), S268 (= S268), R324 (= R324), V326 (≠ A326), F327 (= F327), L331 (= L331), Q334 (= Q334), M337 (= M337), E398 (= E398), V399 (= V399), G401 (= G401), G402 (= G402), Y405 (= Y405), V420 (= V420), I423 (= I423), W424 (= W424), E425 (= E425), G426 (= G426), S427 (= S427), N429 (= N429), I430 (= I430), L433 (= L433)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
79% identity, 99% coverage: 1:537/545 of query aligns to 1:537/541 of P33224
- 182:191 (vs. 182:191, 100% identical) binding
- T185 (= T185) binding
- S191 (= S191) binding
- FFS 216:218 (= FFS 216:218) binding
- S218 (= S218) binding
- 423:433 (vs. 423:433, 100% identical) binding
- N429 (= N429) binding
- R437 (= R437) mutation to Q: Does not affect DNA binding affinity.
- R518 (= R518) mutation to Q: Reduces DNA binding affinity.
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
48% identity, 81% coverage: 4:447/545 of query aligns to 1:445/541 of 5ez3B
- active site: M181 (= M184), T182 (= T185), T295 (= T298), E423 (= E425), R435 (= R437)
- binding flavin-adenine dinucleotide: M179 (= M182), M181 (= M184), T182 (= T185), G186 (= G189), G187 (= G190), T188 (≠ S191), F213 (= F216), M214 (≠ F217), S215 (= S218), K257 (= K260), S265 (= S268), R321 (= R324), V323 (≠ A326), F324 (= F327), L328 (= L331), Q331 (= Q334), M334 (= M337), E396 (= E398), C397 (≠ V399), G399 (= G401), G400 (= G402), Y403 (= Y405), V418 (= V420), I421 (= I423), W422 (= W424), E423 (= E425), S425 (= S427), N427 (= N429), V428 (≠ I430), L431 (= L433)
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
31% identity, 80% coverage: 9:444/545 of query aligns to 2:446/503 of 6sdaB
- active site: M171 (= M184), T172 (= T185), T296 (= T298), R439 (= R437)
- binding flavin-adenine dinucleotide: Q169 (≠ M182), W170 (≠ G183), M171 (= M184), T172 (= T185), G176 (= G189), G177 (= G190), S178 (= S191), F208 (= F216), T209 (≠ F217), T266 (≠ S268), R322 (= R324), A324 (= A326), F325 (= F327), L329 (= L331), H332 (≠ Q334), H335 (≠ M337), E400 (= E398), M401 (≠ V399), G403 (= G401), G404 (= G402), Y407 (= Y405), W426 (= W424), T429 (≠ S427), N431 (= N429), V432 (≠ I430), L435 (= L433)
- binding decanoyl-CoA: S127 (≠ L132), C128 (= C133), A131 (≠ T136), G177 (= G190), S178 (= S191), S230 (vs. gap), R231 (vs. gap), V286 (= V288), K287 (≠ R289), A290 (≠ L292), L293 (≠ G295), N294 (≠ G296), T296 (= T298), R297 (= R299), N300 (≠ C302), R377 (= R375), W426 (= W424), E427 (= E425), V432 (≠ I430), D436 (= D434), R439 (= R437)
6sd8X Bd2924 apo-form (see paper)
31% identity, 80% coverage: 9:444/545 of query aligns to 2:446/503 of 6sd8X
- active site: M171 (= M184), T172 (= T185), T296 (= T298), R439 (= R437)
- binding flavin-adenine dinucleotide: Q169 (≠ M182), W170 (≠ G183), M171 (= M184), T172 (= T185), G176 (= G189), G177 (= G190), S178 (= S191), F208 (= F216), T209 (≠ F217), K258 (= K260), T266 (≠ S268), R322 (= R324), A324 (= A326), F325 (= F327), L329 (= L331), H332 (≠ Q334), H335 (≠ M337), E400 (= E398), M401 (≠ V399), G403 (= G401), G404 (= G402), Y407 (= Y405), V422 (= V420), I425 (= I423), W426 (= W424), T429 (≠ S427), N431 (= N429), V432 (≠ I430), L435 (= L433)
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
30% identity, 80% coverage: 43:480/545 of query aligns to 54:501/593 of 4y9jB
- active site: M190 (= M184), T191 (= T185), T315 (= T298), E446 (= E425), R458 (= R437)
- binding flavin-adenine dinucleotide: Q188 (≠ M182), W189 (≠ G183), M190 (= M184), T191 (= T185), G195 (= G189), G196 (= G190), S197 (= S191), F223 (= F216), S224 (≠ F217), S225 (= S218), T285 (≠ S268), R341 (= R324), V343 (≠ A326), F344 (= F327), Q348 (≠ L331), W351 (≠ Q334), H354 (≠ M337), E419 (= E398), C420 (≠ V399), F421 (≠ L400), G422 (= G401), G423 (= G402), Y426 (= Y405), I444 (= I423), W445 (= W424), T448 (≠ S427), N450 (= N429), V451 (≠ I430), L454 (= L433)
- 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), C144 (= C133), A147 (≠ T136), M148 (= M137), Q188 (≠ M182), M190 (= M184), G196 (= G190), S197 (= S191), S249 (≠ P232), R303 (≠ D286), V305 (= V288), A306 (≠ R289), S309 (≠ L292), L312 (≠ G295), N313 (≠ G296), R316 (= R299), H318 (≠ D301), N319 (≠ C302), A322 (≠ G305), R396 (= R375), W445 (= W424), E446 (= E425), G447 (= G426), V451 (≠ I430), D455 (= D434), R458 (= R437)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
30% identity, 80% coverage: 43:480/545 of query aligns to 72:519/617 of Q9XWZ2
- E91 (≠ N63) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ V127) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ A129) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G190) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G404) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R416) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
Q3L887 Broad-specificity linear acyl-CoA dehydrogenase FadE5; Long-chain-acyl-CoA dehydrogenase; Medium-chain-acyl-CoA dehydrogenase; Short-chain-acyl-CoA dehydrogenase; EC 1.3.8.8; EC 1.3.8.7; EC 1.3.8.1 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
27% identity, 52% coverage: 175:460/545 of query aligns to 155:485/611 of Q3L887
O53666 Broad-specificity linear acyl-CoA dehydrogenase FadE5; Long-chain-acyl-CoA dehydrogenase; Medium-chain-acyl-CoA dehydrogenase; Short-chain-acyl-CoA dehydrogenase; EC 1.3.8.8; EC 1.3.8.7; EC 1.3.8.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
28% identity, 53% coverage: 175:463/545 of query aligns to 155:480/611 of O53666
- MVLT 162:165 (≠ MGMT 182:185) binding
- S171 (= S191) binding ; binding ; mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- T198 (≠ S218) binding
- TK 224:225 (≠ PA 232:233) binding
- K225 (≠ A233) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- F294 (≠ L292) mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R301 (= R299) binding ; mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R326 (= R324) binding
- K338 (= K329) binding
- QTLGG 420:424 (≠ EVLGG 398:402) binding
- E447 (= E425) binding ; mutation to A: Loss of activity.
- T449 (≠ S427) binding
- D456 (= D434) binding
- R460 (vs. gap) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- RK 460:461 (≠ -R 437) binding
6ksbA Crystal structure of e447a m130g acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c16coa (see paper)
27% identity, 53% coverage: 175:461/545 of query aligns to 155:486/608 of 6ksbA