SitesBLAST
Comparing BWI76_RS02590 FitnessBrowser__Koxy:BWI76_RS02590 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)
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), M184 (= M184), T185 (= T185), G190 (= G190), S191 (= S191), F216 (= F216), S218 (= S218), R324 (= R324), F327 (= F327), L331 (= L331), Q334 (= Q334), M337 (= M337), E398 (= E398), V399 (= V399), G401 (= G401), G402 (= G402), W424 (= W424), G426 (= G426), S427 (= S427), N429 (= N429), 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: M181 (= M184), T182 (= T185), G186 (= G189), G187 (= G190), T188 (≠ S191), F213 (= F216), S215 (= S218), R321 (= R324), F324 (= F327), L328 (= L331), Q331 (= Q334), M334 (= M337), E396 (= E398), C397 (≠ V399), G399 (= G401), G400 (= G402), W422 (= W424), E423 (= E425), S425 (= S427), N427 (= N429), 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), M171 (= M184), T172 (= T185), G177 (= G190), S178 (= S191), F208 (= F216), T209 (≠ F217), R322 (= R324), F325 (= F327), L329 (= L331), H332 (≠ Q334), E400 (= E398), M401 (≠ V399), G404 (= G402), Y407 (= Y405), W426 (= W424), T429 (≠ S427), N431 (= N429), L435 (= L433)
- binding decanoyl-CoA: C128 (= C133), G177 (= G190), S178 (= S191), S230 (vs. gap), V286 (= V288), A290 (≠ L292), L293 (≠ G295), N294 (≠ G296), R297 (= R299), R377 (= R375), W426 (= W424), E427 (= E425)
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), M171 (= M184), T172 (= T185), G176 (= G189), G177 (= G190), S178 (= S191), F208 (= F216), T209 (≠ F217), R322 (= R324), F325 (= F327), L329 (= L331), H332 (≠ Q334), M401 (≠ V399), G404 (= G402), W426 (= W424), T429 (≠ S427), 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), M190 (= M184), T191 (= T185), G196 (= G190), S197 (= S191), F223 (= F216), S224 (≠ F217), S225 (= S218), R341 (= R324), V343 (≠ A326), F344 (= F327), Q348 (≠ L331), E419 (= E398), C420 (≠ V399), G422 (= G401), G423 (= G402), Y426 (= Y405), W445 (= W424), T448 (≠ S427), 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), A147 (≠ T136), Q188 (≠ M182), S197 (= S191), S249 (≠ P232), R303 (≠ D286), V305 (= V288), S309 (≠ L292), L312 (≠ G295), N313 (≠ G296), R316 (= R299), A322 (≠ G305), R396 (= R375), W445 (= W424), E446 (= E425), V451 (≠ I430), 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.
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, 49% coverage: 182:450/545 of query aligns to 161:460/591 of A3SI50
- M161 (= M182) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S191) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F216) mutation to A: Almost completely abolishes the activity.
- S197 (= S218) mutation to A: Retains 3.6% of wild-type activity.
- K223 (vs. gap) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ G285) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ D286) mutation to A: Retains 54% of wild-type activity.
- R284 (= R289) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ L292) mutation to A: Retains 76% of wild-type activity.
- Y434 (≠ W424) mutation to A: Retains 51% of wild-type activity.
- E435 (= E425) mutation to A: Loss of activity.
- R448 (≠ V438) mutation to A: Retains 44% of wild-type activity.
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
- binding coenzyme a: M162 (= M182), S171 (= S191), V173 (= V193), T224 (≠ P232), K225 (≠ A233), I290 (≠ V288), F294 (≠ L292), E298 (≠ G296), R301 (= R299), A447 (≠ E425), G448 (= G426), I452 (= I430), D456 (= D434), R460 (vs. gap), K461 (≠ R437)
- binding flavin-adenine dinucleotide: L164 (≠ M184), T165 (= T185), G170 (= G190), S171 (= S191), F196 (= F216), I197 (≠ F217), T198 (≠ S218), T266 (≠ S268), R326 (= R324), I345 (≠ L331), H348 (≠ Q334), Q420 (≠ E398), T421 (≠ V399), G423 (= G401), G424 (= G402), I442 (≠ V420), Y446 (≠ W424), T449 (≠ S427), Q455 (≠ L433)
6ksaB Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c18coa (see paper)
27% identity, 52% coverage: 175:460/545 of query aligns to 158:487/611 of 6ksaB
- binding flavin-adenine dinucleotide: M165 (= M182), L167 (≠ M184), T168 (= T185), G173 (= G190), S174 (= S191), F199 (= F216), I200 (≠ F217), T201 (≠ S218), R329 (= R324), I348 (≠ L331), H351 (≠ Q334), Q423 (≠ E398), T424 (≠ V399), G426 (= G401), G427 (= G402), I445 (≠ V420), Y449 (≠ W424), T452 (≠ S427)
- binding magnesium ion: H388 (≠ D363), Y475 (≠ L448), E479 (= E452)
- binding stearoyl-coenzyme a: A163 (≠ I180), M165 (= M182), L167 (≠ M184), S174 (= S191), V176 (= V193), T227 (≠ P232), K228 (≠ A233), I293 (≠ V288), F297 (≠ L292), Q302 (≠ L297), R304 (= R299), Y449 (≠ W424), A450 (≠ E425), I455 (= I430), D459 (= D434), R463 (vs. gap), K464 (≠ R437)
Sites not aligning to the query:
6lq8A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c22coa (see paper)
27% identity, 53% coverage: 175:461/545 of query aligns to 155:485/607 of 6lq8A
- binding coenzyme a: M162 (= M182), L164 (≠ M184), S171 (= S191), V173 (= V193), T224 (≠ P232), K225 (≠ A233), I290 (≠ V288), F294 (≠ L292), R301 (= R299), A447 (≠ E425), G448 (= G426), I452 (= I430), D456 (= D434), R460 (vs. gap), K461 (≠ R437)
- binding docosanoic acid: M162 (= M182), T198 (≠ S218), Q299 (≠ L297), A300 (≠ T298), Y446 (≠ W424), A447 (≠ E425)
- binding flavin-adenine dinucleotide: M162 (= M182), L164 (≠ M184), T165 (= T185), G170 (= G190), S171 (= S191), F196 (= F216), I197 (≠ F217), T198 (≠ S218), R326 (= R324), I345 (≠ L331), H348 (≠ Q334), Q420 (≠ E398), T421 (≠ V399), G423 (= G401), G424 (= G402), I442 (≠ V420), Y446 (≠ W424), T449 (≠ S427)
Sites not aligning to the query:
6lq7A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c17coa (see paper)
27% identity, 53% coverage: 175:461/545 of query aligns to 155:485/607 of 6lq7A
- binding coenzyme a: M162 (= M182), L164 (≠ M184), S171 (= S191), V173 (= V193), T224 (≠ P232), K225 (≠ A233), I290 (≠ V288), F294 (≠ L292), R301 (= R299), A447 (≠ E425), G448 (= G426), I452 (= I430), D456 (= D434), R460 (vs. gap), K461 (≠ R437)
- binding flavin-adenine dinucleotide: M162 (= M182), L164 (≠ M184), T165 (= T185), G170 (= G190), S171 (= S191), F196 (= F216), I197 (≠ F217), T198 (≠ S218), R326 (= R324), I345 (≠ L331), H348 (≠ Q334), Q420 (≠ E398), T421 (≠ V399), G423 (= G401), G424 (= G402), I442 (≠ V420), Y446 (≠ W424), T449 (≠ S427)
- binding heptadecanoic acid: A160 (≠ I180), Q299 (≠ L297), Y446 (≠ W424), A447 (≠ E425)
Sites not aligning to the query:
6lq6A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c20coa (see paper)
27% identity, 53% coverage: 175:461/545 of query aligns to 155:485/607 of 6lq6A
- binding coenzyme a: M162 (= M182), L164 (≠ M184), S171 (= S191), V173 (= V193), T224 (≠ P232), K225 (≠ A233), I290 (≠ V288), F294 (≠ L292), R301 (= R299), A447 (≠ E425), G448 (= G426), I452 (= I430), D456 (= D434), R460 (vs. gap), K461 (≠ R437)
- binding icosanoic acid: A160 (≠ I180), Q299 (≠ L297), M303 (≠ D301), A447 (≠ E425)
- binding flavin-adenine dinucleotide: M162 (= M182), L164 (≠ M184), T165 (= T185), G170 (= G190), S171 (= S191), F196 (= F216), I197 (≠ F217), T198 (≠ S218), T266 (≠ S268), R326 (= R324), H348 (≠ Q334), Q420 (≠ E398), T421 (≠ V399), G423 (= G401), G424 (= G402), I442 (≠ V420), Y446 (≠ W424), T449 (≠ S427)
Sites not aligning to the query:
6lq1A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c8coa (see paper)
27% identity, 53% coverage: 175:461/545 of query aligns to 155:485/607 of 6lq1A
- binding coenzyme a: M162 (= M182), S171 (= S191), V173 (= V193), T224 (≠ P232), I290 (≠ V288), F294 (≠ L292), R301 (= R299), A447 (≠ E425), I452 (= I430), D456 (= D434), R460 (vs. gap), K461 (≠ R437)
- binding flavin-adenine dinucleotide: L164 (≠ M184), T165 (= T185), G170 (= G190), S171 (= S191), F196 (= F216), I197 (≠ F217), T198 (≠ S218), T266 (≠ S268), R326 (= R324), H348 (≠ Q334), Q420 (≠ E398), T421 (≠ V399), G423 (= G401), G424 (= G402), I442 (≠ V420), Y446 (≠ W424), T449 (≠ S427)
- binding octanoic acid (caprylic acid): M162 (= M182), Y446 (≠ W424), A447 (≠ E425)
Sites not aligning to the query:
6lq0A Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c6coa (see paper)
27% identity, 53% coverage: 175:461/545 of query aligns to 155:485/607 of 6lq0A
- binding hexanoic acid: M303 (≠ D301), Y446 (≠ W424), A447 (≠ E425)
- binding coenzyme a: S171 (= S191), V173 (= V193), T224 (≠ P232), K225 (≠ A233), I290 (≠ V288), F294 (≠ L292), R301 (= R299), A447 (≠ E425), G448 (= G426), I452 (= I430), D456 (= D434), R460 (vs. gap), K461 (≠ R437)
- binding flavin-adenine dinucleotide: M162 (= M182), L164 (≠ M184), T165 (= T185), G170 (= G190), S171 (= S191), F196 (= F216), I197 (≠ F217), T198 (≠ S218), R326 (= R324), I345 (≠ L331), H348 (≠ Q334), Q420 (≠ E398), T421 (≠ V399), G423 (= G401), G424 (= G402), I442 (≠ V420), Y446 (≠ W424), T449 (≠ S427), Q455 (≠ L433)
6lpyA Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria smegmatis in complex with c4coa (see paper)
27% identity, 53% coverage: 175:461/545 of query aligns to 155:485/607 of 6lpyA
- binding butanoic acid: Y446 (≠ W424), A447 (≠ E425)
- binding coenzyme a: M162 (= M182), L164 (≠ M184), S171 (= S191), V173 (= V193), T224 (≠ P232), K225 (≠ A233), I290 (≠ V288), F294 (≠ L292), R301 (= R299), A447 (≠ E425), I452 (= I430), D456 (= D434), R460 (vs. gap), K461 (≠ R437), R464 (≠ M440)
- binding flavin-adenine dinucleotide: M162 (= M182), L164 (≠ M184), T165 (= T185), G170 (= G190), S171 (= S191), F196 (= F216), I197 (≠ F217), T198 (≠ S218), R326 (= R324), I345 (≠ L331), H348 (≠ Q334), Q420 (≠ E398), T421 (≠ V399), G423 (= G401), G424 (= G402), I442 (≠ V420), Y446 (≠ W424), T449 (≠ S427)
6kseA Crystal structure of e447a acyl-coa dehydrogenase fade5 mutant from mycobacteria tuberculosisin complex with c18coa (see paper)
28% identity, 54% coverage: 175:468/545 of query aligns to 155:485/607 of 6kseA
- active site: L164 (≠ M184), T165 (= T185), A300 (≠ T298), R460 (vs. gap)
- binding flavin-adenine dinucleotide: M162 (= M182), L164 (≠ M184), T165 (= T185), G170 (= G190), S171 (= S191), F196 (= F216), T198 (≠ S218), R326 (= R324), Q328 (vs. gap), I345 (≠ L331), H348 (≠ Q334), Q420 (≠ E398), T421 (≠ V399), G423 (= G401), G424 (= G402), I442 (≠ V420), Y446 (≠ W424), T449 (≠ S427)
- binding stearoyl-coenzyme a: M162 (= M182), S171 (= S191), T224 (≠ P232), K225 (≠ A233), I290 (≠ V288), F294 (≠ L292), A300 (≠ T298), R301 (= R299), Y446 (≠ W424), A447 (≠ E425), I452 (= I430), D456 (= D434), R460 (vs. gap), K461 (≠ R437)
Sites not aligning to the query:
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
29% identity, 50% coverage: 168:441/545 of query aligns to 106:370/370 of 2dvlA
- active site: L121 (≠ M184), T122 (= T185), G233 (≠ T298), E354 (= E425), R366 (= R437)
- binding flavin-adenine dinucleotide: L121 (≠ M184), T122 (= T185), G127 (= G190), S128 (= S191), W152 (= W215), I153 (≠ F216), T154 (≠ F217), T356 (≠ S427), E358 (≠ N429)
Query Sequence
>BWI76_RS02590 FitnessBrowser__Koxy:BWI76_RS02590
MHWQTHTVFNQPSPLCNSNLFLSDTALREAVVREGAGWDGDLLASIGQQLGTAESLELGR
LANSNPPELLRYDATGSRLDDVRFHPAWHLLMQGLCANRVHNLAWQEDAREGAFVARAAR
FMLHAQVEAGTLCPITMTFAAIPLLQRSLPRPFSDWLSPLLSDRYDPHLIPGNQKRGLLI
GMGMTEKQGGSDVLSNTTRAEKTAEGFYHLIGHKWFFSVPQSDAHLVLAQAPAGLSCFFV
PRLLPDGQRNGVHLERLKDKLGNRANASSEVEFFNACGWLVGEEGDGVRQILKMGGLTRF
DCALGSHALMRRAYSVALYHALQRQAFGKNLVDQPMMRQVLGQMALRLEGQTAFLFRLAR
AWDRRDDAQEALWARLFTPAAKFAICKSGIAFVAEAMEVLGGSGYCEESELPRLYREMPV
NSIWEGSGNIMCLDVMRVLMKQPAALELLAAECAEVKGQNRHFDRAWRQLQQWLRRPLEE
QGREITRLVYLLGVGAQVLRFASPPLAEAWCRMMLDTRGGMRLDEQTLDDLLLRAMGRGR
QAPQA
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