SitesBLAST
Comparing HSERO_RS04905 FitnessBrowser__HerbieS:HSERO_RS04905 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)
51% identity, 95% coverage: 2:525/550 of query aligns to 4:520/540 of 3u33A
- active site: M184 (= M180), T185 (= T181), T298 (= T300), E425 (= E427), R437 (= R439)
- binding flavin-adenine dinucleotide: M182 (= M178), M184 (= M180), T185 (= T181), G190 (= G186), S191 (= S187), F216 (= F218), S218 (= S220), R324 (= R326), F327 (= F329), L331 (= L333), Q334 (= Q336), M337 (= M339), E398 (= E400), V399 (= V401), G401 (= G403), G402 (= G404), W424 (= W426), G426 (= G428), S427 (= S429), N429 (= N431), L433 (= L435)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
51% identity, 95% coverage: 2:525/550 of query aligns to 4:520/541 of P33224
- 182:191 (vs. 178:187, 100% identical) binding
- T185 (= T181) binding
- S191 (= S187) binding
- FFS 216:218 (= FFS 218:220) binding
- S218 (= S220) binding
- 423:433 (vs. 425:435, 91% identical) binding
- N429 (= N431) binding
- R437 (= R439) mutation to Q: Does not affect DNA binding affinity.
- R518 (≠ D523) mutation to Q: Reduces DNA binding affinity.
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
46% identity, 96% coverage: 3:531/550 of query aligns to 2:524/541 of 5ez3B
- active site: M181 (= M180), T182 (= T181), T295 (= T300), E423 (= E427), R435 (= R439)
- binding flavin-adenine dinucleotide: M181 (= M180), T182 (= T181), G186 (= G185), G187 (= G186), T188 (≠ S187), F213 (= F218), S215 (= S220), R321 (= R326), F324 (= F329), L328 (= L333), Q331 (= Q336), M334 (= M339), E396 (= E400), C397 (≠ V401), G399 (= G403), G400 (= G404), W422 (= W426), E423 (= E427), S425 (= S429), N427 (= N431), L431 (= L435)
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
30% identity, 87% coverage: 11:490/550 of query aligns to 7:485/503 of 6sdaB
- active site: M171 (= M180), T172 (= T181), T296 (= T300), R439 (= R439)
- binding flavin-adenine dinucleotide: Q169 (≠ M178), M171 (= M180), T172 (= T181), G177 (= G186), S178 (= S187), F208 (= F218), T209 (≠ F219), R322 (= R326), F325 (= F329), L329 (= L333), H332 (≠ Q336), E400 (= E400), M401 (≠ V401), G404 (= G404), Y407 (= Y407), W426 (= W426), T429 (≠ S429), N431 (= N431), L435 (= L435)
- binding decanoyl-CoA: C128 (= C130), G177 (= G186), S178 (= S187), S230 (vs. gap), V286 (≠ I290), A290 (≠ I294), L293 (≠ A297), N294 (= N298), R297 (= R301), R377 (= R377), W426 (= W426), E427 (= E427)
6sd8X Bd2924 apo-form (see paper)
30% identity, 87% coverage: 11:490/550 of query aligns to 7:485/503 of 6sd8X
- active site: M171 (= M180), T172 (= T181), T296 (= T300), R439 (= R439)
- binding flavin-adenine dinucleotide: Q169 (≠ M178), M171 (= M180), T172 (= T181), G176 (= G185), G177 (= G186), S178 (= S187), F208 (= F218), T209 (≠ F219), R322 (= R326), F325 (= F329), L329 (= L333), H332 (≠ Q336), M401 (≠ V401), G404 (= G404), W426 (= W426), T429 (≠ S429), V432 (= V432), L435 (= L435)
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
29% identity, 71% coverage: 51:442/550 of query aligns to 63:461/593 of 4y9jB
- active site: M190 (= M180), T191 (= T181), T315 (= T300), E446 (= E427), R458 (= R439)
- binding flavin-adenine dinucleotide: Q188 (≠ M178), M190 (= M180), T191 (= T181), G196 (= G186), S197 (= S187), F223 (= F218), S224 (≠ F219), S225 (= S220), R341 (= R326), V343 (≠ A328), F344 (= F329), Q348 (≠ L333), E419 (= E400), C420 (≠ V401), G422 (= G403), G423 (= G404), Y426 (= Y407), W445 (= W426), T448 (≠ S429), V451 (= V432), L454 (= L435)
- 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 (≠ L129), A147 (≠ T133), Q188 (≠ M178), S197 (= S187), S249 (vs. gap), R303 (= R288), V305 (≠ I290), S309 (≠ I294), L312 (≠ A297), N313 (= N298), R316 (= R301), A322 (≠ G307), R396 (= R377), W445 (= W426), E446 (= E427), V451 (= V432), R458 (= R439)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
29% identity, 71% coverage: 51:442/550 of query aligns to 81:479/617 of Q9XWZ2
- E91 (≠ N61) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ I124) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ A126) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G186) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G406) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R418) 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, 51% coverage: 178:455/550 of query aligns to 161:464/591 of A3SI50
- M161 (= M178) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S187) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F218) mutation to A: Almost completely abolishes the activity.
- S197 (= S220) mutation to A: Retains 3.6% of wild-type activity.
- K223 (≠ N235) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ G287) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ R288) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ P291) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ I294) mutation to A: Retains 76% of wild-type activity.
- Y434 (≠ W426) mutation to A: Retains 51% of wild-type activity.
- E435 (= E427) mutation to A: Loss of activity.
- R448 (= R439) mutation to A: Retains 44% of wild-type activity.
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
25% identity, 53% coverage: 156:444/550 of query aligns to 100:380/380 of 4l1fA
- active site: L125 (≠ M180), T126 (= T181), G242 (≠ T300), E363 (= E427), R375 (= R439)
- binding coenzyme a persulfide: T132 (≠ S187), H179 (vs. gap), F232 (≠ I290), M236 (≠ I294), E237 (= E295), L239 (≠ A297), D240 (≠ N298), R243 (= R301), Y362 (≠ W426), E363 (= E427), G364 (= G428), R375 (= R439)
- binding flavin-adenine dinucleotide: F123 (≠ M178), L125 (≠ M180), T126 (= T181), G131 (= G186), T132 (≠ S187), F156 (= F218), I157 (≠ F219), T158 (≠ S220), R268 (= R326), Q270 (≠ A328), F271 (= F329), I275 (≠ L333), F278 (≠ Q336), L281 (≠ M339), Q336 (≠ E400), I337 (≠ V401), G340 (= G404), I358 (≠ V422), Y362 (≠ W426), T365 (≠ S429), Q367 (≠ N431)
Sites not aligning to the query:
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
28% identity, 52% coverage: 157:443/550 of query aligns to 97:370/370 of 2dvlA
- active site: L121 (≠ M180), T122 (= T181), G233 (≠ T300), E354 (= E427), R366 (= R439)
- binding flavin-adenine dinucleotide: L121 (≠ M180), T122 (= T181), G127 (= G186), S128 (= S187), W152 (= W217), I153 (≠ F218), T154 (≠ F219), T356 (≠ S429), E358 (≠ N431)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
25% identity, 46% coverage: 180:432/550 of query aligns to 124:367/379 of 6fahD
- active site: L124 (≠ M180), T125 (= T181), G241 (≠ T300)
- binding flavin-adenine dinucleotide: L124 (≠ M180), T125 (= T181), R152 (≠ H215), F155 (= F218), T157 (≠ S220), E198 (≠ K260), R267 (= R326), Q269 (≠ A328), F270 (= F329), I274 (≠ L333), F277 (≠ Q336), Q335 (≠ E400), I336 (≠ V401), G339 (= G404), Y361 (≠ W426), T364 (≠ S429), Q366 (≠ N431)
Sites not aligning to the query:
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
25% identity, 52% coverage: 158:441/550 of query aligns to 102:378/380 of 2pg0A
- active site: M124 (= M180), T125 (= T181), E243 (≠ T300), A364 (≠ E427), R376 (= R439)
- binding flavin-adenine dinucleotide: I122 (≠ M178), M124 (= M180), T125 (= T181), G130 (= G186), S131 (= S187), F155 (= F218), I156 (≠ F219), T157 (≠ S220), R269 (= R326), F272 (= F329), F279 (≠ Q336), Q337 (≠ E400), L338 (≠ V401), G340 (= G403), G341 (= G404), V359 (= V422), I362 (= I425), Y363 (≠ W426), T366 (≠ S429), E368 (≠ N431), M369 (≠ V432)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
27% identity, 48% coverage: 178:441/550 of query aligns to 132:388/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T181), G140 (= G186), S141 (= S187), W165 (= W217), T167 (≠ F219), R279 (= R326), F282 (= F329), I286 (≠ L333), F289 (≠ Q336), Q347 (≠ E400), C348 (≠ V401), G351 (= G404), L369 (≠ V422), G375 (= G428), T376 (≠ S429), L382 (= L435)
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)
25% identity, 52% coverage: 158:443/550 of query aligns to 94:369/369 of 3pfdC
- active site: L116 (≠ M180), S117 (≠ T181), T233 (= T300), E353 (= E427), R365 (= R439)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M178), L116 (≠ M180), S117 (≠ T181), G122 (= G186), S123 (= S187), W147 (= W217), I148 (≠ F218), T149 (≠ F219), R259 (= R326), F262 (= F329), V266 (≠ L333), N269 (≠ Q336), Q326 (≠ E400), L327 (≠ V401), G330 (= G404), I348 (≠ V422), Y352 (≠ W426), T355 (≠ S429), Q357 (≠ N431)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
27% identity, 48% coverage: 178:441/550 of query aligns to 128:384/387 of 1ivhA
- active site: M130 (= M180), S131 (≠ T181), E249 (≠ T300), A370 (≠ E427), R382 (= R439)
- binding coenzyme a persulfide: S137 (= S187), S185 (vs. gap), R186 (≠ N235), V239 (≠ I290), Y240 (≠ P291), M243 (≠ I294), E249 (≠ T300), R250 (= R301), G369 (≠ W426), A370 (≠ E427), G371 (= G428), V375 (= V432)
- binding flavin-adenine dinucleotide: L128 (≠ M178), M130 (= M180), S131 (≠ T181), G136 (= G186), S137 (= S187), W161 (= W217), T163 (≠ F219), R275 (= R326), F278 (= F329), F285 (≠ Q336), M288 (= M339), Q343 (≠ E400), C344 (≠ V401), G347 (= G404), T372 (≠ S429), E374 (≠ N431)
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)
27% identity, 48% coverage: 178:441/550 of query aligns to 165:421/426 of P26440
- 165:174 (vs. 178:187, 40% identical) binding
- S174 (= S187) binding
- WIT 198:200 (≠ WFF 217:219) binding
- SR 222:223 (≠ -N 235) binding
- G250 (≠ S267) to A: in IVA; uncertain significance
- Y277 (≠ P291) binding
- DLER 284:287 (≠ NHTR 298:301) binding
- E286 (≠ T300) 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 (≠ I305) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R326) binding
- Q323 (≠ P337) binding
- I379 (≠ M399) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ EVWGG 400:404) binding
- R398 (= R418) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ N423) to N: in IVA; uncertain significance
- A407 (≠ E427) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ EG 427:428) binding
- TSE 409:411 (≠ SGN 429:431) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
25% identity, 52% coverage: 157:443/550 of query aligns to 104:383/383 of 1bucA
- active site: L128 (≠ M180), T129 (= T181), G246 (≠ T300), E367 (= E427), G379 (≠ R439)
- binding acetoacetyl-coenzyme a: F126 (≠ M178), G134 (= G186), T135 (≠ S187), T162 (≠ S220), N182 (vs. gap), H183 (vs. gap), F236 (≠ I290), M240 (≠ I294), M241 (≠ E295), L243 (≠ A297), D244 (≠ N298), T317 (≠ I379), Y366 (≠ W426), E367 (= E427), G368 (= G428)
- binding flavin-adenine dinucleotide: F126 (≠ M178), L128 (≠ M180), T129 (= T181), G134 (= G186), T135 (≠ S187), F160 (= F218), T162 (≠ S220), Y366 (≠ W426), T369 (≠ S429), E371 (≠ N431), M375 (≠ L435)
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)
25% identity, 52% coverage: 157:443/550 of query aligns to 104:383/383 of Q06319
- E367 (= E427) active site, Proton acceptor; mutation to Q: Loss of activity.
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
23% identity, 63% coverage: 87:432/550 of query aligns to 38:367/378 of 5ol2F
- active site: L124 (≠ M180), T125 (= T181), G241 (≠ T300)
- binding coenzyme a persulfide: L238 (≠ A297), R242 (= R301), E362 (= E427), G363 (= G428)
- binding flavin-adenine dinucleotide: F122 (≠ M178), L124 (≠ M180), T125 (= T181), P127 (≠ K183), T131 (≠ S187), F155 (= F218), I156 (≠ F219), T157 (≠ S220), E198 (≠ K260), R267 (= R326), F270 (= F329), L274 (= L333), F277 (≠ Q336), Q335 (≠ E400), L336 (≠ V401), G338 (= G403), G339 (= G404), Y361 (≠ W426), T364 (≠ S429), E366 (≠ N431)
Sites not aligning to the query:
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
25% identity, 49% coverage: 173:441/550 of query aligns to 117:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S187), L133 (≠ V189), K178 (≠ N235), F231 (≠ I290), M235 (≠ I294), L238 (≠ A297), N241 (≠ T300), R242 (= R301), Y362 (≠ W426), T363 (≠ E427), G364 (= G428), R375 (= R439)
- binding flavin-adenine dinucleotide: L122 (≠ M178), A124 (≠ M180), T125 (= T181), G130 (= G186), S131 (= S187), F155 (= F218), I156 (≠ F219), T157 (≠ S220), K200 (= K262), N208 (≠ S270), L358 (≠ V422), T365 (≠ S429), Q367 (≠ N431), I368 (≠ V432)
Query Sequence
>HSERO_RS04905 FitnessBrowser__HerbieS:HSERO_RS04905
MHTHEITNQVPDLSGYNLYRSDAALAEAVQREGAHWHDCTLASQGELLGGAEMREMAELA
NRHTPVLHTHDRCGRRIDVVEFHPAWHTLLDQLRRAGLHALPWMQPGDGAHAARAAGYFL
HAQIEAGSLCPTTMTFAAIAVLQQEPALFEQLRTRLFSREHDARDLPIPQKRSILIGMGM
TEKQGGSDVRSNASIAMPVDPLNDGRGAAYLLSGHKWFFSAPMCDAHLMLARTENGLSCF
FVPRWLPDGTRNPILIQRLKDKLGNRSNSSSEVEFEEAMGIMVGDEGRGIPTIIEMANHT
RLDCIIGSAALMRQALVQAIHHARHRSAFGRRLAEQPLMRAVLADLALESEAATMLMLRV
AHAFDAPDDPLQRAWKRIITPAAKFWICKRTLEFTGECMEVWGGNGYVETAPMARLYREA
PVNSIWEGSGNVMCLDVLRAMARETQGLALLLLELDDAAAGHPALRQQVDALKQMLAAPE
EEREAGARRLVQQLVLALQGMLMLRHAPAGSAQAFLESRSQADGGRVYGTLGSASLAAQE
AILQRAWPEA
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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