SitesBLAST
Comparing 3609216 FitnessBrowser__Dino:3609216 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)
3nf4A Crystal structure of acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to flavin adenine dinucleotide (see paper)
33% identity, 89% coverage: 16:372/401 of query aligns to 23:368/369 of 3nf4A
- active site: L127 (= L120), S128 (≠ T121), G240 (≠ A238), E354 (≠ D358), R366 (= R370)
- binding flavin-adenine dinucleotide: Y125 (≠ F118), L127 (= L120), S128 (≠ T121), G133 (= G126), S134 (= S127), W158 (= W152), T160 (≠ S154), I349 (≠ M353), T356 (= T360), Q358 (≠ E362), I359 (= I363)
1rx0C Crystal structure of isobutyryl-coa dehydrogenase complexed with substrate/ligand. (see paper)
30% identity, 93% coverage: 1:372/401 of query aligns to 9:380/383 of 1rx0C
- active site: L128 (= L120), T129 (= T121), G244 (≠ A238), E366 (≠ D358), R378 (= R370)
- binding methacrylyl-coenzyme a: I93 (≠ M85), Y126 (≠ F118), S135 (= S127), V238 (≠ L232), L241 (≠ I235), N242 (≠ D236), R245 (= R239), V316 (≠ P308), E366 (≠ D358), G367 (= G359), L375 (≠ V367), R378 (= R370)
- binding flavin-adenine dinucleotide: Y126 (≠ F118), L128 (= L120), T129 (= T121), G134 (= G126), S135 (= S127), F159 (≠ W152), I160 (≠ V153), S161 (= S154), R270 (= R264), F273 (= F267), N280 (≠ L274), L283 (≠ I277), Q339 (= Q331), M340 (≠ V332), G342 (= G334), G343 (= G335), Y344 (≠ M336), L365 (≠ V357), S368 (≠ T360), E370 (= E362)
1rx0A Crystal structure of isobutyryl-coa dehydrogenase complexed with substrate/ligand. (see paper)
30% identity, 93% coverage: 1:372/401 of query aligns to 10:381/384 of 1rx0A
- active site: L129 (= L120), T130 (= T121), G245 (≠ A238), E367 (≠ D358), R379 (= R370)
- binding flavin-adenine dinucleotide: Y127 (≠ F118), L129 (= L120), T130 (= T121), G135 (= G126), S136 (= S127), F160 (≠ W152), I161 (≠ V153), S162 (= S154), W207 (≠ Y200), R271 (= R264), F274 (= F267), L278 (≠ N271), N281 (≠ L274), L284 (≠ I277), Q340 (= Q331), M341 (≠ V332), G343 (= G334), G344 (= G335), Y345 (≠ M336), L366 (≠ V357), S369 (≠ T360), E371 (= E362)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
31% identity, 93% coverage: 2:372/401 of query aligns to 7:378/378 of 4n5fA
- active site: L126 (= L120), T127 (= T121), G243 (≠ A238), E364 (≠ D358), R376 (= R370)
- binding dihydroflavine-adenine dinucleotide: L126 (= L120), T127 (= T121), G132 (= G126), S133 (= S127), F157 (≠ W152), T159 (≠ S154), T210 (≠ M205), Y363 (≠ V357), T366 (= T360), E368 (= E362), M372 (≠ V366)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
30% identity, 93% coverage: 2:374/401 of query aligns to 7:381/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S127), T134 (≠ P129), R180 (≠ K175), R234 (≠ Q229), L237 (= L232), R238 (≠ M233), L240 (≠ I235), D241 (= D236), R244 (= R239), E365 (≠ D358), G366 (= G359), R377 (= R370)
- binding flavin-adenine dinucleotide: Y123 (≠ F118), L125 (= L120), S126 (≠ T121), G131 (= G126), S132 (= S127), W156 (= W152), I157 (≠ V153), T158 (≠ S154), I360 (≠ M353), T367 (= T360), Q369 (≠ E362)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
30% identity, 93% coverage: 2:374/401 of query aligns to 7:381/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ F118), L125 (= L120), S126 (≠ T121), G131 (= G126), S132 (= S127), W156 (= W152), I157 (≠ V153), T158 (≠ S154), I360 (≠ M353), Y364 (≠ V357), T367 (= T360), Q369 (≠ E362)
7w0jE Acyl-coa dehydrogenase, tfu_1647
30% identity, 93% coverage: 2:374/401 of query aligns to 8:382/382 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 (≠ T121), W157 (= W152), R270 (= R264), Q272 (≠ M266), F273 (= F267), I277 (≠ N271), F280 (≠ L274), I283 (= I277), Q339 (= Q331), L340 (≠ V332), G343 (= G335), Y365 (≠ V357), E366 (≠ D358), T368 (= T360), Q370 (≠ E362), I371 (= I363)
Q9UKU7 Isobutyryl-CoA dehydrogenase, mitochondrial; IBDH; Activator-recruited cofactor 42 kDa component; ARC42; Acyl-CoA dehydrogenase family member 8; ACAD-8; EC 1.3.8.5 from Homo sapiens (Human) (see 3 papers)
30% identity, 93% coverage: 1:372/401 of query aligns to 41:412/415 of Q9UKU7
- G137 (= G97) to R: in IBDD; loss of protein solubility; complete loss of isobutyryl-CoA dehydrogenase activity; dbSNP:rs371449613
- 158:167 (vs. 118:127, 70% identical) binding in other chain
- S167 (= S127) binding
- FIS 191:193 (≠ WVS 152:154) binding in other chain
- NGGR 274:277 (≠ DIAR 236:239) binding
- R302 (= R264) binding ; to Q: in IBDD; no effect on localization to the mitochondrion; complete loss of isobutyryl-CoA dehydrogenase activity; loss of protein expression in patient cells; dbSNP:rs121908422
- NQ 312:313 (≠ LD 274:275) binding
- A320 (≠ G282) to T: in IBDD; decreased isobutyryl-CoA dehydrogenase activity; less than 20% of wild-type; dbSNP:rs200620279
- QMHGG 371:375 (≠ QVLGG 331:335) binding
- SNE 400:402 (≠ TTE 360:362) binding in other chain
- R410 (= R370) 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)
29% identity, 92% coverage: 7:374/401 of query aligns to 3:369/369 of 3pfdC
- active site: L116 (= L120), S117 (≠ T121), T233 (≠ A238), E353 (≠ D358), R365 (= R370)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ F118), L116 (= L120), S117 (≠ T121), G122 (= G126), S123 (= S127), W147 (= W152), I148 (≠ V153), T149 (≠ S154), R259 (= R264), F262 (= F267), V266 (≠ N271), N269 (≠ L274), Q326 (= Q331), L327 (≠ V332), G330 (= G335), I348 (≠ M353), Y352 (≠ V357), T355 (= T360), Q357 (≠ E362)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
29% identity, 93% coverage: 1:372/401 of query aligns to 5:377/380 of 4l1fA
- active site: L125 (= L120), T126 (= T121), G242 (≠ A238), E363 (≠ D358), R375 (= R370)
- binding coenzyme a persulfide: T132 (≠ S127), H179 (≠ K175), F232 (≠ L228), M236 (≠ L232), E237 (≠ M233), L239 (≠ I235), D240 (= D236), R243 (= R239), Y362 (≠ V357), E363 (≠ D358), G364 (= G359), R375 (= R370)
- binding flavin-adenine dinucleotide: F123 (= F118), L125 (= L120), T126 (= T121), G131 (= G126), T132 (≠ S127), F156 (≠ W152), I157 (≠ V153), T158 (≠ S154), R268 (= R264), Q270 (≠ M266), F271 (= F267), I275 (≠ N271), F278 (≠ L274), L281 (≠ I277), Q336 (= Q331), I337 (≠ V332), G340 (= G335), I358 (≠ M353), Y362 (≠ V357), T365 (= T360), Q367 (≠ E362)
- binding 1,3-propandiol: L5 (≠ M1), Q10 (≠ D6)
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
31% identity, 93% coverage: 2:372/401 of query aligns to 5:376/376 of 4m9aB
- active site: L124 (= L120), T125 (= T121), G241 (≠ A238), E362 (≠ D358), R374 (= R370)
- binding dihydroflavine-adenine dinucleotide: F122 (= F118), T125 (= T121), G130 (= G126), S131 (= S127), F155 (≠ W152), T157 (≠ S154), T208 (≠ M205), Y361 (≠ V357), T364 (= T360), E366 (= E362), M370 (≠ V366)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
29% identity, 93% coverage: 2:374/401 of query aligns to 5:378/378 of 5ol2F
- active site: L124 (= L120), T125 (= T121), G241 (≠ A238), G374 (≠ R370)
- binding calcium ion: E29 (≠ A26), E33 (≠ A30), R35 (≠ A32)
- binding coenzyme a persulfide: L238 (≠ I235), R242 (= R239), E362 (≠ D358), G363 (= G359)
- binding flavin-adenine dinucleotide: F122 (= F118), L124 (= L120), T125 (= T121), P127 (= P123), T131 (≠ S127), F155 (≠ W152), I156 (≠ V153), T157 (≠ S154), E198 (≠ Y195), R267 (= R264), F270 (= F267), L274 (≠ N271), F277 (≠ L274), Q335 (= Q331), L336 (≠ V332), G338 (= G334), G339 (= G335), Y361 (≠ V357), T364 (= T360), E366 (= E362)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
31% identity, 89% coverage: 16:372/401 of query aligns to 17:372/374 of 5lnxD
- active site: L122 (= L120), T123 (= T121), G239 (≠ A238), E358 (≠ D358), K370 (≠ R370)
- binding flavin-adenine dinucleotide: L122 (= L120), T123 (= T121), G128 (= G126), S129 (= S127), F153 (≠ W152), T155 (≠ S154), R265 (= R264), Q267 (≠ M266), F268 (= F267), I272 (≠ N271), N275 (≠ L274), I278 (= I277), Q331 (= Q331), I332 (≠ V332), G335 (= G335), Y357 (≠ V357), T360 (= T360), E362 (= E362)
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
31% identity, 92% coverage: 1:368/401 of query aligns to 5:377/393 of 3mpjB
- active site: I128 (≠ L120), T129 (= T121), T245 (≠ A238), E367 (≠ D358)
- binding flavin-adenine dinucleotide: F126 (= F118), I128 (≠ L120), T129 (= T121), G134 (= G126), S135 (= S127), W159 (= W152), I160 (≠ V153), S161 (= S154), V366 (= V357), S369 (≠ T360), N371 (≠ E362), M375 (≠ V366)
- binding : H36 (≠ A32), F37 (≠ W33), Y39 (vs. gap), A164 (≠ T157), Q165 (≠ E158), D167 (= D160), N193 (≠ D185)
Sites not aligning to the query:
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
31% identity, 92% coverage: 1:368/401 of query aligns to 5:377/395 of 3mpiC
- active site: I128 (≠ L120), T129 (= T121), T245 (≠ A238), E367 (≠ D358)
- binding flavin-adenine dinucleotide: I128 (≠ L120), T129 (= T121), G134 (= G126), S135 (= S127), W159 (= W152), I160 (≠ V153), S161 (= S154), M365 (≠ I356), V366 (= V357), S369 (≠ T360), N371 (≠ E362), M375 (≠ V366)
- binding glutaryl-coenzyme A: R87 (≠ A80), F126 (= F118), S135 (= S127), V137 (≠ P129), S181 (≠ H174), F239 (≠ L232), R246 (= R239), N315 (≠ D306), V366 (= V357), E367 (≠ D358), G368 (= G359), I376 (≠ V367)
Sites not aligning to the query:
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
31% identity, 92% coverage: 1:368/401 of query aligns to 5:377/389 of C3UVB0
- A80 (≠ G73) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ A80) binding
- V88 (≠ F81) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ S84) binding
- FGIT 126:129 (≠ FALT 118:121) binding
- S135 (= S127) binding ; binding
- WIS 159:161 (≠ WVS 152:154) binding
- S181 (≠ H174) binding
- R271 (= R264) binding
- FQMN 281:284 (≠ LDGI 274:277) binding
- R340 (≠ Q331) binding
- A344 (≠ G335) binding
- V366 (= V357) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ DGTTE 358:362) binding
Sites not aligning to the query:
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
29% identity, 92% coverage: 1:370/401 of query aligns to 8:380/388 of 2a1tC
- active site: V127 (≠ L120), T128 (= T121), T247 (≠ A238), E368 (≠ D358), R380 (= R370)
- binding flavin-adenine dinucleotide: Y125 (≠ F118), V127 (≠ L120), T128 (= T121), G133 (= G126), S134 (= S127), Q155 (≠ S149), W158 (= W152), W158 (= W152), I159 (≠ V153), T160 (≠ S154), R273 (= R264), T275 (≠ M266), F276 (= F267), L280 (≠ N271), H283 (≠ L274), I286 (= I277), Q341 (= Q331), I342 (≠ V332), G345 (= G335), I363 (≠ M353), T370 (= T360), Q372 (≠ E362)
P11310 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; Medium chain acyl-CoA dehydrogenase; MCADH; EC 1.3.8.7 from Homo sapiens (Human) (see 16 papers)
29% identity, 92% coverage: 1:370/401 of query aligns to 41:413/421 of P11310
- Y67 (≠ W27) to H: in ACADMD; mild; dbSNP:rs121434280
- L86 (= L46) mutation to M: Strongly reduced rate of electron transfer to ETF.
- L98 (≠ Q58) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (= L60) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (≠ V68) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (≠ A92) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 118:127, 50% identical) binding in other chain
- S167 (= S127) binding
- W191 (= W152) mutation to A: Loss of electron transfer to ETF.; mutation to F: Reduces rate of electron transfer to ETF about six-fold.
- WIT 191:193 (≠ WVS 152:154) binding in other chain
- T193 (≠ S154) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (≠ Y195) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (= D236) binding
- T280 (≠ A238) mutation to E: Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410.
- R281 (= R239) binding ; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ RKM 264:266) binding
- HQ 316:317 (≠ LD 274:275) binding in other chain
- K329 (≠ D287) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ QVLGG 331:335) binding
- E384 (≠ P341) mutation to A: Reduces rate of electron transfer to ETF three-fold.; mutation to Q: Reduces rate of electron transfer to ETF two-fold.
- E401 (≠ D358) active site, Proton acceptor; binding ; mutation to G: Changed substrate specificity towards longer acyl chains; when associated with E-280.; mutation to Q: Loss of acyl-CoA dehydrogenase activity.; mutation to T: Loss of acyl-CoA dehydrogenase activity; when associated with E-280.
- EGTSQ 401:405 (≠ DGTTE 358:362) binding in other chain
1egcA Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa (see paper)
29% identity, 92% coverage: 1:370/401 of query aligns to 7:379/387 of 1egcA
- active site: V126 (≠ L120), T127 (= T121), E246 (≠ A238), G367 (≠ D358), R379 (= R370)
- binding octanoyl-coenzyme a: E90 (≠ S84), L94 (≠ I88), Y124 (≠ F118), S133 (= S127), V135 (≠ P129), N182 (≠ H174), F236 (≠ L228), M240 (≠ L232), F243 (≠ I235), D244 (= D236), R247 (= R239), Y366 (≠ V357), G367 (≠ D358), G368 (= G359)
- binding flavin-adenine dinucleotide: Y124 (≠ F118), V126 (≠ L120), T127 (= T121), G132 (= G126), S133 (= S127), W157 (= W152), T159 (≠ S154), R272 (= R264), T274 (≠ M266), F275 (= F267), L279 (≠ N271), H282 (≠ L274), I285 (= I277), Q340 (= Q331), I341 (≠ V332), G344 (= G335), I362 (≠ M353), I365 (= I356), Y366 (≠ V357), T369 (= T360), Q371 (≠ E362)
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
29% identity, 91% coverage: 8:372/401 of query aligns to 12:381/383 of 1bucA
- active site: L128 (= L120), T129 (= T121), G246 (≠ A238), E367 (≠ D358), G379 (≠ R370)
- binding acetoacetyl-coenzyme a: L96 (≠ I88), F126 (= F118), G134 (= G126), T135 (≠ S127), T162 (≠ S154), N182 (≠ H174), H183 (≠ K175), F236 (≠ L228), M240 (≠ L232), M241 (= M233), L243 (≠ I235), D244 (= D236), T317 (≠ P308), Y366 (≠ V357), E367 (≠ D358), G368 (= G359)
- binding flavin-adenine dinucleotide: F126 (= F118), L128 (= L120), T129 (= T121), G134 (= G126), T135 (≠ S127), F160 (≠ W152), T162 (≠ S154), Y366 (≠ V357), T369 (= T360), E371 (= E362), M375 (≠ V366)
Query Sequence
>3609216 FitnessBrowser__Dino:3609216
MSEKLDAILAAAHTHATEVVAPNVDAWNAAKAWPRDASDKAGAAGLTGLYAPEDWGGQGL
PLSEGIQVYEQLGLGDGAYAFALSMHNICTFAGCGYGTDAFKKKWARDLTAGRKLANFAL
TEPQSGSDPMKMYTRAMINGDGTWTISGSKAWVSLATEADIYFTVVKTSDAPGHKDMAMI
AIPADAPGISFGPLYETPSYNFLPMSEMYLDNVVVSEENIILPIGQGLQGSLMAIDIARV
SIASGCCGLMQAALDTALSYSKSRKMFGGKNLDLDGIQWMLGEVATDLEASKLLYRRAAE
ALGTPDGPLMAAHAKRFVPDAAVKAANTCTQVLGGMGLLQPYGLDGLSRLAQMLRIVDGT
TEISRVVIGRALQKRAAGLPDLPVPKGFGERDEEASSIAAQ
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