SitesBLAST
Comparing N515DRAFT_0941 FitnessBrowser__Dyella79:N515DRAFT_0941 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)
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
63% identity, 98% coverage: 4:381/385 of query aligns to 8:375/377 of 4ktoA
- active site: M130 (= M126), S131 (= S127), E239 (= E245), A360 (= A366), R372 (= R378)
- binding flavin-adenine dinucleotide: L128 (= L124), M130 (= M126), S131 (= S127), M155 (= M157), W156 (= W158), T158 (= T160), R265 (= R271), F268 (= F274), I272 (= I278), F275 (= F281), M278 (= M284), Q333 (= Q339), A334 (= A340), G337 (= G343), L355 (= L361), G359 (= G365), T362 (= T368), E364 (= E370)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
61% identity, 97% coverage: 6:378/385 of query aligns to 8:382/387 of 1ivhA
- active site: M130 (= M126), S131 (= S127), E249 (= E245), A370 (= A366), R382 (= R378)
- binding coenzyme a persulfide: S137 (= S133), S185 (= S181), R186 (= R182), V239 (= V235), Y240 (≠ R236), M243 (= M239), E249 (= E245), R250 (= R246), G369 (= G365), A370 (= A366), G371 (= G367), V375 (≠ I371)
- binding flavin-adenine dinucleotide: L128 (= L124), M130 (= M126), S131 (= S127), G136 (= G132), S137 (= S133), W161 (= W158), T163 (= T160), R275 (= R271), F278 (= F274), F285 (= F281), M288 (= M284), Q343 (= Q339), C344 (≠ A340), G347 (= G343), T372 (= T368), E374 (= E370)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
61% identity, 97% coverage: 6:378/385 of query aligns to 12:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S127), G140 (= G132), S141 (= S133), W165 (= W158), T167 (= T160), R279 (= R271), F282 (= F274), I286 (= I278), F289 (= F281), Q347 (= Q339), C348 (≠ A340), G351 (= G343), L369 (= L361), G375 (= G367), T376 (= T368), L382 (≠ M374)
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)
61% identity, 97% coverage: 6:378/385 of query aligns to 45:419/426 of P26440
- 165:174 (vs. 124:133, 90% identical) binding
- S174 (= S133) binding
- WIT 198:200 (= WIT 158:160) binding
- SR 222:223 (= SR 181:182) binding
- G250 (= G209) to A: in IVA; uncertain significance
- Y277 (≠ R236) binding
- DLER 284:287 (≠ DTER 243:246) binding
- E286 (= E245) 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 (≠ S250) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R271) binding
- Q323 (≠ G282) binding
- I379 (= I338) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QALGG 339:343) binding
- R398 (= R357) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (= Y362) to N: in IVA; uncertain significance
- A407 (= A366) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (= AG 366:367) binding
- TSE 409:411 (≠ TNE 368:370) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
39% identity, 97% coverage: 8:380/385 of query aligns to 6:376/378 of 5ol2F
- active site: L124 (≠ M126), T125 (≠ S127), G241 (≠ E245), G374 (≠ R378)
- binding calcium ion: E29 (≠ Q31), E33 (≠ D35), R35 (≠ V37)
- binding coenzyme a persulfide: L238 (= L242), R242 (= R246), E362 (≠ A366), G363 (= G367)
- binding flavin-adenine dinucleotide: F122 (≠ L124), L124 (≠ M126), T125 (≠ S127), P127 (= P129), T131 (≠ S133), F155 (≠ W158), I156 (= I159), T157 (= T160), E198 (≠ L202), R267 (= R271), F270 (= F274), L274 (≠ I278), F277 (= F281), Q335 (= Q339), L336 (≠ A340), G338 (= G342), G339 (= G343), Y361 (≠ G365), T364 (= T368), E366 (= E370)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
39% identity, 97% coverage: 6:380/385 of query aligns to 7:379/384 of 1jqiA
- active site: G377 (≠ R378)
- binding acetoacetyl-coenzyme a: L95 (= L94), F125 (≠ L124), S134 (= S133), F234 (≠ V235), M238 (= M239), Q239 (≠ S240), L241 (= L242), D242 (= D243), R245 (= R246), Y364 (≠ G365), E365 (≠ A366), G366 (= G367)
- binding flavin-adenine dinucleotide: F125 (≠ L124), L127 (≠ M126), S128 (= S127), G133 (= G132), S134 (= S133), W158 (= W158), T160 (= T160), R270 (= R271), F273 (= F274), L280 (≠ F281), Q338 (= Q339), I339 (≠ A340), G342 (= G343), I360 (≠ L361), T367 (= T368), E369 (= E370), I370 (= I371)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
39% identity, 97% coverage: 6:380/385 of query aligns to 34:406/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
40% identity, 97% coverage: 6:380/385 of query aligns to 7:379/385 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 (≠ N344), T347 (≠ N348), E348 (= E349)
- binding flavin-adenine dinucleotide: F125 (≠ L124), L127 (≠ M126), S128 (= S127), G133 (= G132), S134 (= S133), W158 (= W158), T160 (= T160), R270 (= R271), F273 (= F274), L280 (≠ F281), V282 (≠ M283), Q338 (= Q339), I339 (≠ A340), G342 (= G343), I360 (≠ L361), Y364 (≠ G365), T367 (= T368), E369 (= E370), I370 (= I371), L373 (≠ M374)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
40% identity, 97% coverage: 6:380/385 of query aligns to 10:382/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L124), L130 (≠ M126), S131 (= S127), G136 (= G132), S137 (= S133), W161 (= W158), T163 (= T160), T214 (= T212), R273 (= R271), F276 (= F274), L280 (≠ I278), L283 (≠ F281), V285 (≠ M283), Q341 (= Q339), I342 (≠ A340), G345 (= G343), I363 (≠ L361), Y367 (≠ G365), T370 (= T368), E372 (= E370), L376 (≠ M374)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
40% identity, 97% coverage: 6:380/385 of query aligns to 34:406/412 of P16219
- G90 (= G62) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E76) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 124:133, 70% identical) binding in other chain
- R171 (≠ E144) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 158:160) binding in other chain
- A192 (= A165) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ C183) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R271) binding
- Q308 (≠ G282) binding in other chain
- R325 (= R299) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S327) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QALGG 339:343) binding
- R380 (= R354) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TNE 368:370) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
40% identity, 97% coverage: 6:380/385 of query aligns to 4:376/381 of 8sgsA
- binding coenzyme a: S131 (= S133), A133 (≠ V135), N177 (≠ S181), F231 (≠ V235), M235 (= M239), L238 (= L242), I312 (≠ R316), E362 (≠ A366), G363 (= G367)
- binding flavin-adenine dinucleotide: F122 (≠ L124), L124 (≠ M126), S125 (= S127), G130 (= G132), S131 (= S133), W155 (= W158), T157 (= T160), R267 (= R271), F270 (= F274), L274 (≠ I278), L277 (≠ F281), Q335 (= Q339), I336 (≠ A340), G338 (= G342), G339 (= G343), I357 (≠ L361), I360 (= I364), Y361 (≠ G365), T364 (= T368), E366 (= E370)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
39% identity, 97% coverage: 8:380/385 of query aligns to 4:372/374 of 5lnxD
- active site: L122 (≠ M126), T123 (≠ S127), G239 (≠ E245), E358 (≠ A366), K370 (≠ R378)
- binding flavin-adenine dinucleotide: L122 (≠ M126), T123 (≠ S127), G128 (= G132), S129 (= S133), F153 (≠ W158), T155 (= T160), R265 (= R271), Q267 (= Q273), F268 (= F274), I272 (= I278), N275 (≠ F281), I278 (≠ M284), Q331 (= Q339), I332 (≠ A340), G335 (= G343), Y357 (≠ G365), T360 (= T368), E362 (= E370)
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
40% identity, 97% coverage: 6:380/385 of query aligns to 1:366/371 of 2vigB
- active site: L121 (≠ M126), S122 (= S127), G231 (≠ E245), E352 (≠ A366), G364 (≠ R378)
- binding coenzyme a persulfide: S128 (= S133), F221 (≠ V235), M225 (= M239), Q226 (≠ S240), L228 (= L242), D229 (= D243), R232 (= R246), E352 (≠ A366), G353 (= G367), I357 (= I371)
- binding flavin-adenine dinucleotide: L121 (≠ M126), S122 (= S127), G127 (= G132), S128 (= S133), W152 (= W158), T154 (= T160), R257 (= R271), F260 (= F274), L264 (≠ I278), L267 (≠ F281), Q325 (= Q339), I326 (≠ A340), G329 (= G343), I347 (≠ L361), Y351 (≠ G365), T354 (= T368), E356 (= E370)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
36% identity, 98% coverage: 4:380/385 of query aligns to 3:377/380 of 4l1fA
- active site: L125 (≠ M126), T126 (≠ S127), G242 (≠ E245), E363 (≠ A366), R375 (= R378)
- binding coenzyme a persulfide: T132 (≠ S133), H179 (≠ R182), F232 (≠ V235), M236 (= M239), E237 (≠ S240), L239 (= L242), D240 (= D243), R243 (= R246), Y362 (≠ G365), E363 (≠ A366), G364 (= G367), R375 (= R378)
- binding flavin-adenine dinucleotide: F123 (≠ L124), L125 (≠ M126), T126 (≠ S127), G131 (= G132), T132 (≠ S133), F156 (≠ W158), I157 (= I159), T158 (= T160), R268 (= R271), Q270 (= Q273), F271 (= F274), I275 (= I278), F278 (= F281), L281 (≠ M284), Q336 (= Q339), I337 (≠ A340), G340 (= G343), I358 (≠ L361), Y362 (≠ G365), T365 (= T368), Q367 (≠ E370)
- binding 1,3-propandiol: L5 (= L6), Q10 (≠ D11)
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
39% identity, 97% coverage: 4:376/385 of query aligns to 3:377/395 of 3mpiC
- active site: I128 (≠ M126), T129 (≠ S127), T245 (≠ E245), E367 (≠ A366)
- binding flavin-adenine dinucleotide: I128 (≠ M126), T129 (≠ S127), G134 (= G132), S135 (= S133), W159 (= W158), I160 (= I159), S161 (≠ T160), M365 (≠ I364), V366 (≠ G365), S369 (≠ T368), N371 (≠ E370), M375 (= M374)
- binding glutaryl-coenzyme A: R87 (≠ G85), F126 (≠ L124), S135 (= S133), V137 (= V135), S181 (= S181), F239 (≠ M239), R246 (= R246), N315 (≠ K314), V366 (≠ G365), E367 (≠ A366), G368 (= G367), I376 (≠ L375)
Sites not aligning to the query:
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
39% identity, 97% coverage: 4:376/385 of query aligns to 3:377/389 of C3UVB0
- A80 (≠ S78) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ G85) binding
- V88 (≠ L86) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ G89) binding
- FGIT 126:129 (≠ LAMS 124:127) binding
- S135 (= S133) binding ; binding
- WIS 159:161 (≠ WIT 158:160) binding
- S181 (= S181) binding
- R271 (= R271) binding
- FQMN 281:284 (≠ FGMM 281:284) binding
- R340 (≠ Q339) binding
- A344 (≠ G343) binding
- V366 (≠ G365) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ AGTNE 366:370) binding
Sites not aligning to the query:
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
39% identity, 97% coverage: 4:376/385 of query aligns to 3:377/393 of 3mpjB
- active site: I128 (≠ M126), T129 (≠ S127), T245 (≠ E245), E367 (≠ A366)
- binding flavin-adenine dinucleotide: F126 (≠ L124), I128 (≠ M126), T129 (≠ S127), G134 (= G132), S135 (= S133), W159 (= W158), I160 (= I159), S161 (≠ T160), V366 (≠ G365), S369 (≠ T368), N371 (≠ E370), M375 (= M374)
- binding : H36 (≠ V37), F37 (= F38), Y39 (vs. gap), A164 (≠ P163), Q165 (≠ D164), D167 (= D166), N193 (≠ G192)
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)
39% identity, 97% coverage: 6:380/385 of query aligns to 4:377/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (= S133), L133 (≠ V135), K178 (≠ R182), F231 (≠ V235), M235 (= M239), L238 (= L242), N241 (≠ E245), R242 (= R246), Y362 (≠ G365), T363 (≠ A366), G364 (= G367), R375 (= R378)
- binding flavin-adenine dinucleotide: L122 (= L124), A124 (≠ M126), T125 (≠ S127), G130 (= G132), S131 (= S133), F155 (≠ W158), I156 (= I159), T157 (= T160), K200 (= K204), N208 (≠ T212), L358 (= L361), T365 (= T368), Q367 (≠ E370), I368 (= I371)
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
39% identity, 97% coverage: 6:380/385 of query aligns to 2:375/378 of 7p9xA
- binding 1-monoenoyl-CoA: L82 (= L86), D89 (≠ N93), S129 (= S133), L131 (≠ V135), K176 (≠ R182), F229 (≠ V235), M233 (= M239), L236 (= L242), R240 (= R246), Y360 (≠ G365), T361 (≠ A366), G362 (= G367), R373 (= R378)
- binding flavin-adenine dinucleotide: A122 (≠ M126), T123 (≠ S127), G128 (= G132), S129 (= S133), F153 (≠ W158), I154 (= I159), T155 (= T160), N206 (≠ T212), L356 (= L361), Y360 (≠ G365), T363 (= T368), Q365 (≠ E370), I366 (= I371)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
37% identity, 98% coverage: 4:380/385 of query aligns to 3:376/379 of 1ukwB
- active site: L124 (≠ M126), S125 (= S127), T241 (≠ E245), E362 (≠ A366), R374 (= R378)
- binding cobalt (ii) ion: D145 (= D148), H146 (≠ V149)
- binding flavin-adenine dinucleotide: F122 (≠ L124), L124 (≠ M126), S125 (= S127), G130 (= G132), S131 (= S133), W155 (= W158), S157 (≠ T160), K200 (= K204), L357 (= L361), Y361 (≠ G365), E362 (≠ A366), T364 (= T368), E366 (= E370), L370 (≠ M374)
Query Sequence
>N515DRAFT_0941 FitnessBrowser__Dyella79:N515DRAFT_0941
MRPFSLGEELDLLRESVHAFAEKEIAPRATQIDHDNVFPADLWRKFGEMGLLGMTIPEAY
GGTGLGYLAHMVAMEEISRASGSVGLSYGAHSNLCVQNLFHNGNEEQRRKYIPRLCSGEY
VGALAMSEPGAGSDVVGSMSCKAELRGDVWVANGTKMWITNGPDADVLLVYMRTAPRPAG
SRCMTAFIIEKGMKGFSTAQKLDKLGMRGSNTCELVFEDCEIPAANIVGEVNEGVRVLMS
GLDTERLVLSGGPLGLMQAAMDLVLPYVRERKQFNAPIGTFGMMQAKVADMYTALQSSRG
FAYMVAREFDQGSKSRIDPAACLLNASQNAVKVALEAIQALGGNGYINEFPAGRLLRDAK
LYEIGAGTNEIRRMLIGRELYHGKS
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