SitesBLAST
Comparing H281DRAFT_05793 FitnessBrowser__Burk376:H281DRAFT_05793 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)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
48% identity, 94% coverage: 8:536/561 of query aligns to 4:520/541 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.
- R518 (≠ G534) mutation to Q: Reduces DNA binding affinity.
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
48% identity, 94% coverage: 8:536/561 of query aligns to 4:520/540 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)
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
45% identity, 99% coverage: 8:561/561 of query aligns to 1:540/541 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)
32% 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 (vs. gap), V286 (= V296), A290 (≠ I300), L293 (≠ A303), N294 (= N304), R297 (= R307), R377 (= R388), W426 (= W437), E427 (= E438)
6sd8X Bd2924 apo-form (see paper)
32% 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)
29% 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)
29% identity, 83% coverage: 56:518/561 of query aligns to 80:562/617 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.
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 (≠ A241) 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.
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
25% 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:
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)
24% identity, 65% coverage: 93:454/561 of query aligns to 31:369/369 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)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
27% identity, 47% coverage: 184:446/561 of query aligns to 126:375/383 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 (≠ A241), 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:
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
27% identity, 47% coverage: 184:446/561 of query aligns to 126:375/383 of Q06319
- E367 (= E438) active site, Proton acceptor; mutation to Q: Loss of activity.
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
28% identity, 48% coverage: 186:454/561 of query aligns to 121:370/370 of 2dvlA
- active site: L121 (≠ M186), T122 (= T187), G233 (≠ T306), E354 (= E438), R366 (= R450)
- binding flavin-adenine dinucleotide: L121 (≠ M186), T122 (= T187), G127 (= G192), S128 (= S193), W152 (= W221), I153 (≠ F222), T154 (≠ F223), T356 (≠ S440), E358 (≠ N442)
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
30% 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 (vs. gap) 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
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
30% 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)
30% 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 (vs. gap), F239 (≠ I300), R246 (= R307), N315 (≠ W386), V366 (≠ W437), E367 (= E438), G368 (= G439)
Sites not aligning to the query:
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
24% identity, 63% coverage: 93:443/561 of query aligns to 36:366/383 of 4iv6B
- active site: L121 (≠ M186), T122 (= T187), G240 (≠ T306), E361 (= E438)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ M186), T122 (= T187), G126 (= G191), G127 (= G192), S128 (= S193), W152 (= W221), I153 (≠ F222), S154 (≠ F223), R266 (= R332), S268 (≠ A334), F269 (= F335), I273 (≠ L339), H276 (≠ Q342), V279 (≠ M345), R334 (≠ E411), V335 (= V412), G338 (= G415), L356 (≠ V433), G360 (≠ W437), T363 (≠ S440), E365 (≠ N442), I366 (≠ V443)
Sites not aligning to the query:
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, 51% coverage: 167:453/561 of query aligns to 148:422/426 of P26440
- 165:174 (vs. 184:193, 40% identical) binding
- S174 (= S193) binding
- WIT 198:200 (≠ WFF 221:223) binding
- SR 222:223 (vs. gap) 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, 51% coverage: 167:453/561 of query aligns to 115:389/393 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, 51% coverage: 167:453/561 of query aligns to 111:385/387 of 1ivhA
- active site: M130 (= M186), S131 (≠ T187), E249 (≠ T306), A370 (≠ E438), R382 (= R450)
- binding coenzyme a persulfide: S137 (= S193), S185 (vs. gap), R186 (vs. gap), 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)
Query Sequence
>H281DRAFT_05793 FitnessBrowser__Burk376:H281DRAFT_05793
MQRHSFGQTHEVTNQVPPLADYNLFSSDAALSAALERDGAAWHRDALLRHGAALTTPETL
ALAELANRHTPELSTHSPTGERIDALEFHPAWHELLSLLRRKGLHALPFSDPQPGAMAAR
CAGYFLHAQIESGSLCPLTMTFASIPVLQREPQLFETLRDKLYAREQDPRDLPLTQKISA
MIGMGMTEKQGGSDVRSNQTQARAIAAGGRGGAYELVGHKWFFSAPQCDAHLVLARTHDH
AGLSCFFVPRFAPDGSKNAVQIQRLKDKLGNRSNASSEVEFLDAFGIMIGDEGRGVPTII
EMANYTRLDCVIGSAALMRAALVQAIHHARHRSAFGRNLVDQPLMRNVLADLSLESEAAT
VLFMRLAHAFEQSVDADSATSAERAWRRIVTPAAKYWICKRTLEFTGEAMEVWGGNGYVE
TGPMARFYREAPVNSIWEGSGNVMCLDVLRAMEREPEAAQALFAQWQADAAAHAALSAAL
GKLAATLNGPAEDREASARRIAQQIVLIAQATLLIKHAPAAVAEAFIATRLGSGCGESGR
VYGTLPATFDHAAIVERAFPA
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