SitesBLAST
Comparing H281DRAFT_05560 FitnessBrowser__Burk376:H281DRAFT_05560 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)
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
41% identity, 96% coverage: 21:567/572 of query aligns to 2:536/541 of 5ez3B
- active site: M181 (= M196), T182 (= T197), T295 (= T318), E423 (= E446), R435 (= R458)
- binding flavin-adenine dinucleotide: M181 (= M196), T182 (= T197), G186 (= G201), G187 (= G202), T188 (≠ S203), F213 (= F236), S215 (= S238), R321 (= R344), F324 (= F347), L328 (= L351), Q331 (≠ R354), M334 (= M357), E396 (≠ Q419), C397 (= C420), G399 (= G422), G400 (= G423), W422 (= W445), E423 (= E446), S425 (≠ T448), N427 (= N450), L431 (≠ M454)
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
39% identity, 92% coverage: 19:543/572 of query aligns to 3:520/540 of 3u33A
- active site: M184 (= M196), T185 (= T197), T298 (= T318), E425 (= E446), R437 (= R458)
- binding flavin-adenine dinucleotide: M182 (≠ Y194), M184 (= M196), T185 (= T197), G190 (= G202), S191 (= S203), F216 (= F236), S218 (= S238), R324 (= R344), F327 (= F347), L331 (= L351), Q334 (≠ R354), M337 (= M357), E398 (≠ Q419), V399 (≠ C420), G401 (= G422), G402 (= G423), W424 (= W445), G426 (= G447), S427 (≠ T448), N429 (= N450), L433 (≠ M454)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
39% identity, 92% coverage: 19:543/572 of query aligns to 3:520/541 of P33224
- 182:191 (vs. 194:203, 80% identical) binding
- T185 (= T197) binding
- S191 (= S203) binding
- FFS 216:218 (≠ FCS 236:238) binding
- S218 (= S238) binding
- 423:433 (vs. 444:454, 55% identical) binding
- N429 (= N450) binding
- R437 (= R458) mutation to Q: Does not affect DNA binding affinity.
- R518 (≠ P541) mutation to Q: Reduces DNA binding affinity.
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
26% identity, 87% coverage: 35:530/572 of query aligns to 44:567/617 of Q9XWZ2
- E91 (≠ N78) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ V141) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ Q143) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G202) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G425) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R437) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
26% identity, 87% coverage: 35:530/572 of query aligns to 26:549/593 of 4y9jB
- active site: M190 (= M196), T191 (= T197), T315 (= T318), E446 (= E446), R458 (= R458)
- binding flavin-adenine dinucleotide: Q188 (≠ Y194), M190 (= M196), T191 (= T197), G196 (= G202), S197 (= S203), F223 (= F236), S224 (≠ C237), S225 (= S238), R341 (= R344), V343 (≠ G346), F344 (= F347), Q348 (≠ L351), E419 (≠ Q419), C420 (= C420), G422 (= G422), G423 (= G423), Y426 (≠ F426), W445 (= W445), T448 (= T448), V451 (≠ M451), L454 (≠ M454)
- 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 (≠ G146), A147 (≠ G150), Q188 (≠ Y194), S197 (= S203), S249 (vs. gap), R303 (= R306), V305 (≠ I308), S309 (≠ L312), L312 (≠ A315), N313 (≠ H316), R316 (= R319), A322 (≠ G325), R396 (= R396), W445 (= W445), E446 (= E446), V451 (≠ M451), R458 (= R458)
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
28% identity, 75% coverage: 35:462/572 of query aligns to 11:443/503 of 6sdaB
- active site: M171 (= M196), T172 (= T197), T296 (= T318), R439 (= R458)
- binding flavin-adenine dinucleotide: Q169 (≠ Y194), M171 (= M196), T172 (= T197), G177 (= G202), S178 (= S203), F208 (= F236), T209 (≠ C237), R322 (= R344), F325 (= F347), L329 (= L351), H332 (≠ R354), E400 (≠ Q419), M401 (≠ C420), G404 (= G423), Y407 (≠ F426), W426 (= W445), T429 (= T448), N431 (= N450), L435 (≠ M454)
- binding decanoyl-CoA: C128 (= C147), G177 (= G202), S178 (= S203), S230 (vs. gap), V286 (≠ I308), A290 (≠ L312), L293 (≠ A315), N294 (≠ H316), R297 (= R319), R377 (= R396), W426 (= W445), E427 (= E446)
6sd8X Bd2924 apo-form (see paper)
28% identity, 75% coverage: 35:462/572 of query aligns to 11:443/503 of 6sd8X
- active site: M171 (= M196), T172 (= T197), T296 (= T318), R439 (= R458)
- binding flavin-adenine dinucleotide: Q169 (≠ Y194), M171 (= M196), T172 (= T197), G176 (= G201), G177 (= G202), S178 (= S203), F208 (= F236), T209 (≠ C237), R322 (= R344), F325 (= F347), L329 (= L351), H332 (≠ R354), M401 (≠ C420), G404 (= G423), W426 (= W445), T429 (= T448), V432 (≠ M451), L435 (≠ M454)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
28% identity, 49% coverage: 183:463/572 of query aligns to 107:379/379 of 6fahD
- active site: L124 (≠ M196), T125 (= T197), G241 (≠ T318), G374 (≠ R458)
- binding flavin-adenine dinucleotide: F122 (≠ Y194), L124 (≠ M196), T125 (= T197), R152 (≠ H233), F155 (= F236), T157 (≠ S238), E198 (≠ K278), R267 (= R344), Q269 (≠ G346), F270 (= F347), I274 (≠ L351), F277 (≠ R354), Q335 (= Q419), I336 (≠ C420), G339 (= G423), Y361 (≠ W445), T364 (= T448), Q366 (≠ N450)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
27% identity, 49% coverage: 182:461/572 of query aligns to 111:377/379 of 1ukwB
- active site: L124 (≠ M196), S125 (≠ T197), T241 (= T318), E362 (= E446), R374 (= R458)
- binding cobalt (ii) ion: D145 (≠ Y220), H146 (= H221)
- binding flavin-adenine dinucleotide: F122 (≠ Y194), L124 (≠ M196), S125 (≠ T197), G130 (= G202), S131 (= S203), W155 (= W235), S157 (≠ C237), K200 (= K280), L357 (= L441), Y361 (≠ W445), E362 (= E446), T364 (= T448), E366 (≠ N450), L370 (≠ M454)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
27% identity, 49% coverage: 182:461/572 of query aligns to 111:377/379 of 1ukwA
- active site: L124 (≠ M196), S125 (≠ T197), T241 (= T318), E362 (= E446), R374 (= R458)
- binding flavin-adenine dinucleotide: F122 (≠ Y194), L124 (≠ M196), S125 (≠ T197), G130 (= G202), S131 (= S203), W155 (= W235), S157 (≠ C237), L357 (= L441), Y361 (≠ W445), E362 (= E446), T364 (= T448), E366 (≠ N450), L370 (≠ M454)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
25% identity, 69% coverage: 71:464/572 of query aligns to 17:383/387 of 1ivhA
- active site: M130 (= M196), S131 (≠ T197), E249 (≠ T318), A370 (≠ E446), R382 (≠ Q463)
- binding coenzyme a persulfide: S137 (= S203), S185 (≠ A252), R186 (≠ G253), V239 (≠ I308), Y240 (≠ R309), M243 (≠ L312), E249 (≠ T318), R250 (= R319), G369 (≠ W445), A370 (≠ E446), G371 (= G447), V375 (= V456)
- binding flavin-adenine dinucleotide: L128 (≠ Y194), M130 (= M196), S131 (≠ T197), G136 (= G202), S137 (= S203), W161 (= W235), T163 (≠ C237), R275 (= R344), F278 (= F347), F285 (≠ R354), M288 (= M357), Q343 (= Q419), C344 (= C420), G347 (= G423), T372 (= T448), E374 (≠ D455)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
26% identity, 47% coverage: 194:462/572 of query aligns to 119:368/371 of 2vigB
- active site: L121 (≠ M196), S122 (≠ T197), G231 (≠ T318), E352 (= E446), G364 (≠ R458)
- binding coenzyme a persulfide: S128 (= S203), F221 (≠ I308), M225 (≠ L312), Q226 (≠ S313), L228 (≠ A315), D229 (≠ H316), R232 (= R319), E352 (= E446), G353 (= G447), I357 (≠ M451)
- binding flavin-adenine dinucleotide: L121 (≠ M196), S122 (≠ T197), G127 (= G202), S128 (= S203), W152 (= W235), T154 (≠ C237), R257 (= R344), F260 (= F347), L264 (= L351), L267 (≠ R354), Q325 (= Q419), I326 (≠ C420), G329 (= G423), I347 (≠ L441), Y351 (≠ W445), T354 (= T448), E356 (≠ N450)
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)
25% identity, 69% coverage: 71:464/572 of query aligns to 54:420/426 of P26440
- 165:174 (vs. 194:203, 50% identical) binding
- S174 (= S203) binding
- WIT 198:200 (≠ WFC 235:237) binding
- SR 222:223 (≠ AG 252:253) binding
- G250 (≠ S285) to A: in IVA; uncertain significance
- Y277 (≠ R309) binding
- DLER 284:287 (≠ HLTR 316:319) binding
- E286 (≠ T318) 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 (= A323) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R344) binding
- Q323 (≠ P355) binding
- I379 (≠ L418) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QCHGG 419:423) binding
- R398 (= R437) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ N442) to N: in IVA; uncertain significance
- A407 (≠ E446) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ EG 446:447) binding
- TS-----E 409:411 (≠ TANMMCMD 448:455) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
25% identity, 69% coverage: 71:464/572 of query aligns to 21:387/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T197), G140 (= G202), S141 (= S203), W165 (= W235), T167 (≠ C237), R279 (= R344), F282 (= F347), I286 (≠ L351), F289 (≠ R354), Q347 (= Q419), C348 (= C420), G351 (= G423), L369 (= L441), G375 (= G447), T376 (= T448), L382 (≠ A459)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
25% identity, 58% coverage: 133:462/572 of query aligns to 66:379/380 of 4l1fA
- active site: L125 (≠ M196), T126 (= T197), G242 (≠ T318), E363 (= E446), R375 (= R458)
- binding coenzyme a persulfide: T132 (≠ S203), H179 (vs. gap), F232 (≠ I308), M236 (≠ L312), E237 (≠ S313), L239 (≠ A315), D240 (≠ H316), R243 (= R319), Y362 (≠ W445), E363 (= E446), G364 (= G447), R375 (= R458)
- binding flavin-adenine dinucleotide: F123 (≠ Y194), L125 (≠ M196), T126 (= T197), G131 (= G202), T132 (≠ S203), F156 (= F236), I157 (≠ C237), T158 (≠ S238), R268 (= R344), Q270 (≠ G346), F271 (= F347), I275 (≠ L351), F278 (≠ R354), L281 (≠ M357), Q336 (= Q419), I337 (≠ C420), G340 (= G423), I358 (≠ L441), Y362 (≠ W445), T365 (= T448), Q367 (≠ N450)
Sites not aligning to the query:
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
26% identity, 47% coverage: 194:462/572 of query aligns to 152:408/412 of P16219
- 152:161 (vs. 194:203, 40% identical) binding in other chain
- R171 (≠ H221) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WFC 235:237) binding in other chain
- A192 (≠ S242) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ E254) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R344) binding
- Q308 (≠ P355) binding in other chain
- R325 (≠ T372) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ C407) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QCHGG 419:423) binding
- R380 (= R434) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TAN 448:450) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 90 G → S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- 104 natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
26% identity, 47% coverage: 194:462/572 of query aligns to 125:381/385 of 7y0bA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: M343 (≠ N424), T347 (≠ E428), E348 (= E429)
- binding flavin-adenine dinucleotide: F125 (≠ Y194), L127 (≠ M196), S128 (≠ T197), G133 (= G202), S134 (= S203), W158 (= W235), T160 (≠ C237), R270 (= R344), F273 (= F347), L280 (≠ R354), V282 (≠ M356), Q338 (= Q419), I339 (≠ C420), G342 (= G423), I360 (≠ L441), Y364 (≠ W445), T367 (= T448), E369 (≠ N450), I370 (≠ M451), L373 (≠ M454)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
26% identity, 47% coverage: 194:462/572 of query aligns to 122:378/381 of 8sgsA
- binding coenzyme a: S131 (= S203), A133 (≠ L205), N177 (≠ A252), F231 (≠ I308), M235 (≠ L312), L238 (≠ A315), I312 (≠ A395), E362 (= E446), G363 (= G447)
- binding flavin-adenine dinucleotide: F122 (≠ Y194), L124 (≠ M196), S125 (≠ T197), G130 (= G202), S131 (= S203), W155 (= W235), T157 (≠ C237), R267 (= R344), F270 (= F347), L274 (= L351), L277 (≠ R354), Q335 (= Q419), I336 (≠ C420), G338 (= G422), G339 (= G423), I357 (≠ L441), I360 (≠ V444), Y361 (≠ W445), T364 (= T448), E366 (≠ N450)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
26% identity, 47% coverage: 194:462/572 of query aligns to 128:384/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ Y194), L130 (≠ M196), S131 (≠ T197), G136 (= G202), S137 (= S203), W161 (= W235), T163 (≠ C237), T214 (≠ S288), R273 (= R344), F276 (= F347), L280 (= L351), L283 (≠ R354), V285 (≠ M356), Q341 (= Q419), I342 (≠ C420), G345 (= G423), I363 (≠ L441), Y367 (≠ W445), T370 (= T448), E372 (≠ N450), L376 (≠ M454)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
25% identity, 47% coverage: 194:462/572 of query aligns to 152:408/412 of P15651
- 152:161 (vs. 194:203, 40% identical) binding
- S161 (= S203) binding
- WIT 185:187 (≠ W-- 227) binding
- DMGR 269:272 (≠ HLTR 316:319) binding
- R297 (= R344) binding
- QILGG 365:369 (≠ QCHGG 419:423) binding
- E392 (= E446) active site, Proton acceptor
- TSE 394:396 (≠ TAN 448:450) binding
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
Query Sequence
>H281DRAFT_05560 FitnessBrowser__Burk376:H281DRAFT_05560
MNAPLIAESVAPARAADRYSTHVVKNQAASASGFNAFDGDVILKSAVEREAPWAASRCSA
LGKLAGDEAVQELARLANRNLPELKTHDRYGNRIDWVEFHPSWHELMSLAWRHEVPSLAW
TAKEQQPHFARAVLSYLWNQVEQGTGCPTGMAYASHAGFMAEPALKIWAEKACGTVYEFS
RREVSLKPSVVIGYAMTEKQGGSDLRETQTTAVYSHSAGYHGETAHWYELTGHKWFCSVP
QSDGFFTLAKVAGEVTCFFLPRTLPDGSYNRFFVQRLKDKCGNKSNASSEVEYSGTMAIR
VGEEGRGIREILSHAHLTRLDFAVGSAGLMRQALGLALNHASTRNGFGSSLADRPMMTNV
LADMAVEVEAATLLALRIAKATDHIDTDEQQKAFARVATPMAKFFNCSRAPAVAYEALQC
HGGNGFIEENPMARLYREAPLNSVWEGTANMMCMDVRRAMLKQASCREALIAELQDVRGQ
HAGFDSFIDSMGPLLDRVVKDEFLARPATEAIARAVQGAELLRHSTSEVVDAFMKTRLTG
PSGSWGVMFGSMGAEVTKLQATRIVERARFTA
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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