SitesBLAST
Comparing BPHYT_RS18740 FitnessBrowser__BFirm:BPHYT_RS18740 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)
49% identity, 93% coverage: 8:531/561 of query aligns to 4:515/540 of 3u33A
- active site: M184 (= M186), T185 (= T187), T298 (= T306), E425 (= E438), R437 (= R450)
- binding flavin-adenine dinucleotide: M182 (= M184), M184 (= M186), T185 (= T187), G190 (= G192), S191 (= S193), F216 (= F222), S218 (= S224), R324 (= R332), F327 (= F335), L331 (= L339), Q334 (= Q342), M337 (= M345), E398 (= E411), V399 (= V412), G401 (= G414), G402 (= G415), W424 (= W437), G426 (= G439), S427 (= S440), N429 (= N442), L433 (= L446)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
49% identity, 93% coverage: 8:531/561 of query aligns to 4:515/541 of P33224
- 182:191 (vs. 184:193, 100% identical) binding
- T185 (= T187) binding
- S191 (= S193) binding
- FFS 216:218 (= FFS 222:224) binding
- S218 (= S224) binding
- 423:433 (vs. 436:446, 91% identical) binding
- N429 (= N442) binding
- R437 (= R450) mutation to Q: Does not affect DNA binding affinity.
Sites not aligning to the query:
- 518 R→Q: Reduces DNA binding affinity.
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
46% identity, 99% coverage: 8:560/561 of query aligns to 1:539/541 of 5ez3B
- active site: M181 (= M186), T182 (= T187), T295 (= T306), E423 (= E438), R435 (= R450)
- binding flavin-adenine dinucleotide: M181 (= M186), T182 (= T187), G186 (= G191), G187 (= G192), T188 (≠ S193), F213 (= F222), S215 (= S224), R321 (= R332), F324 (= F335), L328 (= L339), Q331 (= Q342), M334 (= M345), E396 (= E411), C397 (≠ V412), G399 (= G414), G400 (= G415), W422 (= W437), E423 (= E438), S425 (= S440), N427 (= N442), L431 (= L446)
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
33% identity, 86% coverage: 23:502/561 of query aligns to 11:486/503 of 6sdaB
- active site: M171 (= M186), T172 (= T187), T296 (= T306), R439 (= R450)
- binding flavin-adenine dinucleotide: Q169 (≠ M184), M171 (= M186), T172 (= T187), G177 (= G192), S178 (= S193), F208 (= F222), T209 (≠ F223), R322 (= R332), F325 (= F335), L329 (= L339), H332 (≠ Q342), E400 (= E411), M401 (≠ V412), G404 (= G415), Y407 (= Y418), W426 (= W437), T429 (≠ S440), N431 (= N442), L435 (= L446)
- binding decanoyl-CoA: C128 (= C136), G177 (= G192), S178 (= S193), S230 (≠ H240), V286 (= V296), A290 (≠ I300), L293 (≠ A303), N294 (= N304), R297 (= R307), R377 (= R388), W426 (= W437), E427 (= E438)
6sd8X Bd2924 apo-form (see paper)
33% identity, 86% coverage: 23:502/561 of query aligns to 11:486/503 of 6sd8X
- active site: M171 (= M186), T172 (= T187), T296 (= T306), R439 (= R450)
- binding flavin-adenine dinucleotide: Q169 (≠ M184), M171 (= M186), T172 (= T187), G176 (= G191), G177 (= G192), S178 (= S193), F208 (= F222), T209 (≠ F223), R322 (= R332), F325 (= F335), L329 (= L339), H332 (≠ Q342), M401 (≠ V412), G404 (= G415), W426 (= W437), T429 (≠ S440), V432 (= V443), L435 (= L446)
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
30% identity, 83% coverage: 56:518/561 of query aligns to 62:544/593 of 4y9jB
- active site: M190 (= M186), T191 (= T187), T315 (= T306), E446 (= E438), R458 (= R450)
- binding flavin-adenine dinucleotide: Q188 (≠ M184), M190 (= M186), T191 (= T187), G196 (= G192), S197 (= S193), F223 (= F222), S224 (≠ F223), S225 (= S224), R341 (= R332), V343 (≠ A334), F344 (= F335), Q348 (≠ L339), E419 (= E411), C420 (≠ V412), G422 (= G414), G423 (= G415), Y426 (= Y418), W445 (= W437), T448 (≠ S440), V451 (= V443), L454 (= L446)
- 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 (≠ L135), A147 (≠ T139), Q188 (≠ M184), S197 (= S193), S249 (vs. gap), R303 (= R294), V305 (= V296), S309 (≠ I300), L312 (≠ A303), N313 (= N304), R316 (= R307), A322 (≠ G313), R396 (= R388), W445 (= W437), E446 (= E438), V451 (= V443), R458 (= R450)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
32% identity, 71% coverage: 56:452/561 of query aligns to 80:478/617 of Q9XWZ2
- E91 (≠ N67) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ I130) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ S132) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G192) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G417) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R429) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
26% identity, 48% coverage: 184:455/561 of query aligns to 123:380/380 of 4l1fA
- active site: L125 (≠ M186), T126 (= T187), G242 (≠ T306), E363 (= E438), R375 (= R450)
- binding coenzyme a persulfide: T132 (≠ S193), H179 (vs. gap), F232 (≠ V296), M236 (≠ I300), E237 (= E301), L239 (≠ A303), D240 (≠ N304), R243 (= R307), Y362 (≠ W437), E363 (= E438), G364 (= G439), R375 (= R450)
- binding flavin-adenine dinucleotide: F123 (≠ M184), L125 (≠ M186), T126 (= T187), G131 (= G192), T132 (≠ S193), F156 (= F222), I157 (≠ F223), T158 (≠ S224), R268 (= R332), Q270 (≠ A334), F271 (= F335), I275 (≠ L339), F278 (≠ Q342), L281 (≠ M345), Q336 (≠ E411), I337 (≠ V412), G340 (= G415), I358 (≠ V433), Y362 (≠ W437), T365 (≠ S440), Q367 (≠ N442)
Sites not aligning to the query:
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
31% identity, 47% coverage: 183:443/561 of query aligns to 125:372/393 of 3mpjB
- active site: I128 (≠ M186), T129 (= T187), T245 (= T306), E367 (= E438)
- binding flavin-adenine dinucleotide: F126 (≠ M184), I128 (≠ M186), T129 (= T187), G134 (= G192), S135 (= S193), W159 (= W221), I160 (≠ F222), S161 (≠ F223), V366 (≠ W437), S369 (= S440), N371 (= N442)
- binding : A164 (≠ P226), Q165 (= Q227), D167 (= D229), N193 (≠ F251)
Sites not aligning to the query:
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
31% identity, 47% coverage: 183:443/561 of query aligns to 125:372/395 of 3mpiC
- active site: I128 (≠ M186), T129 (= T187), T245 (= T306), E367 (= E438)
- binding flavin-adenine dinucleotide: I128 (≠ M186), T129 (= T187), G134 (= G192), S135 (= S193), W159 (= W221), I160 (≠ F222), S161 (≠ F223), M365 (≠ I436), V366 (≠ W437), S369 (= S440), N371 (= N442)
- binding glutaryl-coenzyme A: F126 (≠ M184), S135 (= S193), V137 (= V195), S181 (≠ H240), F239 (≠ I300), R246 (= R307), N315 (≠ T374), V366 (≠ W437), E367 (= E438), G368 (= G439)
Sites not aligning to the query:
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
31% identity, 47% coverage: 183:443/561 of query aligns to 125:372/389 of C3UVB0
- FGIT 126:129 (≠ MGMT 184:187) binding
- S135 (= S193) binding ; binding
- WIS 159:161 (≠ WFF 221:223) binding
- S181 (≠ H240) binding
- R271 (= R332) binding
- FQMN 281:284 (≠ QPLM 342:345) binding
- R340 (≠ E411) binding
- A344 (≠ G415) binding
- V366 (≠ W437) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ EGSGN 438:442) binding
Sites not aligning to the query:
- 80 A→E: Loses the FAD cofactor and dehydrogenase activity.
- 87 binding
- 88 V→S: A residual dehydrogenase activity is observed.
- 91 binding
- 385 binding
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)
26% identity, 55% coverage: 145:454/561 of query aligns to 78:369/369 of 3pfdC
- active site: L116 (≠ M186), S117 (≠ T187), T233 (= T306), E353 (= E438), R365 (= R450)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M184), L116 (≠ M186), S117 (≠ T187), G122 (= G192), S123 (= S193), W147 (= W221), I148 (≠ F222), T149 (≠ F223), R259 (= R332), F262 (= F335), V266 (≠ L339), N269 (≠ Q342), Q326 (≠ E411), L327 (≠ V412), G330 (= G415), I348 (≠ V433), Y352 (≠ W437), T355 (≠ S440), Q357 (≠ N442)
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, 47% coverage: 184:449/561 of query aligns to 161:446/591 of A3SI50
- M161 (= M184) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S193) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F222) mutation to A: Almost completely abolishes the activity.
- S197 (= S224) mutation to A: Retains 3.6% of wild-type activity.
- K223 (≠ E241) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ G293) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ R294) mutation to A: Retains 54% of wild-type activity.
- R284 (≠ P297) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ I300) mutation to A: Retains 76% of wild-type activity.
- Y434 (≠ W437) mutation to A: Retains 51% of wild-type activity.
- E435 (= E438) mutation to A: Loss of activity.
Sites not aligning to the query:
- 448 R→A: Retains 44% of wild-type activity.
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
26% identity, 56% coverage: 132:443/561 of query aligns to 83:370/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S193), T134 (≠ V195), R180 (= R256), R234 (≠ P297), L237 (≠ I300), R238 (≠ E301), L240 (≠ A303), D241 (≠ N304), R244 (= R307), E365 (= E438), G366 (= G439)
- binding flavin-adenine dinucleotide: Y123 (≠ M184), L125 (≠ M186), S126 (≠ T187), G131 (= G192), S132 (= S193), W156 (= W221), I157 (≠ F222), T158 (≠ F223), I360 (≠ V433), T367 (≠ S440), Q369 (≠ N442)
Sites not aligning to the query:
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
26% identity, 56% coverage: 132:443/561 of query aligns to 83:370/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ M184), L125 (≠ M186), S126 (≠ T187), G131 (= G192), S132 (= S193), W156 (= W221), I157 (≠ F222), T158 (≠ F223), I360 (≠ V433), Y364 (≠ W437), T367 (≠ S440), Q369 (≠ N442)
7w0jE Acyl-coa dehydrogenase, tfu_1647
26% identity, 56% coverage: 132:443/561 of query aligns to 84:371/382 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 (≠ T187), W157 (= W221), R270 (= R332), Q272 (≠ A334), F273 (= F335), I277 (≠ L339), F280 (≠ Q342), I283 (≠ M345), Q339 (≠ E411), L340 (≠ V412), G343 (= G415), Y365 (≠ W437), E366 (= E438), T368 (≠ S440), Q370 (≠ N442), I371 (≠ V443)
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: 184:453/561 of query aligns to 165:422/426 of P26440
- 165:174 (vs. 184:193, 40% identical) binding
- S174 (= S193) binding
- WIT 198:200 (≠ WFF 221:223) binding
- SR 222:223 (≠ HE 240:241) binding
- G250 (≠ S273) to A: in IVA; uncertain significance
- Y277 (≠ P297) binding
- DLER 284:287 (≠ NYTR 304:307) binding
- E286 (≠ T306) 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 (≠ V311) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R332) binding
- Q323 (≠ P343) binding
- I379 (≠ M410) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ EVWGG 411:415) binding
- R398 (= R429) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ N434) to N: in IVA; uncertain significance
- A407 (≠ E438) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ EG 438:439) binding
- TSE 409:411 (≠ SGN 440:442) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
27% identity, 48% coverage: 184:453/561 of query aligns to 132:389/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T187), G140 (= G192), S141 (= S193), W165 (= W221), T167 (≠ F223), R279 (= R332), F282 (= F335), I286 (≠ L339), F289 (≠ Q342), Q347 (≠ E411), C348 (≠ V412), G351 (= G415), L369 (≠ V433), G375 (= G439), T376 (≠ S440), L382 (= L446)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
27% identity, 48% coverage: 184:453/561 of query aligns to 128:385/387 of 1ivhA
- active site: M130 (= M186), S131 (≠ T187), E249 (≠ T306), A370 (≠ E438), R382 (= R450)
- binding coenzyme a persulfide: S137 (= S193), S185 (≠ H240), R186 (≠ E241), V239 (= V296), Y240 (≠ P297), M243 (≠ I300), E249 (≠ T306), R250 (= R307), G369 (≠ W437), A370 (≠ E438), G371 (= G439), V375 (= V443)
- binding flavin-adenine dinucleotide: L128 (≠ M184), M130 (= M186), S131 (≠ T187), G136 (= G192), S137 (= S193), W161 (= W221), T163 (≠ F223), R275 (= R332), F278 (= F335), F285 (≠ Q342), M288 (= M345), Q343 (≠ E411), C344 (≠ V412), G347 (= G415), T372 (≠ S440), E374 (≠ N442)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
26% identity, 49% coverage: 172:446/561 of query aligns to 115:375/383 of 1bucA
- active site: L128 (≠ M186), T129 (= T187), G246 (≠ T306), E367 (= E438)
- binding acetoacetyl-coenzyme a: F126 (≠ M184), G134 (= G192), T135 (≠ S193), T162 (≠ S224), N182 (≠ H240), H183 (≠ E241), F236 (≠ V296), M240 (≠ I300), M241 (≠ E301), L243 (≠ A303), D244 (≠ N304), T317 (≠ S373), Y366 (≠ W437), E367 (= E438), G368 (= G439)
- binding flavin-adenine dinucleotide: F126 (≠ M184), L128 (≠ M186), T129 (= T187), G134 (= G192), T135 (≠ S193), F160 (= F222), T162 (≠ S224), Y366 (≠ W437), T369 (≠ S440), E371 (≠ N442), M375 (≠ L446)
Sites not aligning to the query:
Query Sequence
>BPHYT_RS18740 FitnessBrowser__BFirm:BPHYT_RS18740
MERHSFGQTHEVTNQVPPLADYNLFSSDAALSAALERDGAGWHRGALVRHGAALTTPETL
ALAELANRHEPELVTHSPRGERIDALEFHPSWHALLSLLRREGLHALPFSDPQRGAMVAR
CAGYFLHAQIESGSLCPLTMTFASIPVLQREPALFATLRDKLYAREHDSRDLPLKQKTSA
MIGMGMTEKQGGSDVRSNQTRAYSTAGSGRGAAYRLVGHKWFFSAPQCDAHLVLGRTDEH
EGLSCFYVPRFAPDGRKNNVQIQRLKDKLGNRSNASSEVEFLDAFGIMIGDEGRGVPTII
EMANYTRLDCVIGSAALMRAALVQAIHHARHRSAFGRHLADQPLMRNVLADLALESEAAT
VLFMRLARAFEESTDAASTSLAERAWRRIVTPAAKYWVCKRALEFTGEAMEVWGGNGYVE
TGPMARFYREAPVNSIWEGSGNVMCLDVLRAMEREPEAAQALFAAWHADAQAHPALSAAL
GKLAATLNGPAEHREASARRIAQQVVLIAQATLLLKHAPAEVAEAFVATRLAEGCGESGR
VYGTLPATFDHAAIIERAFPV
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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