SitesBLAST
Comparing GFF56 FitnessBrowser__Marino:GFF56 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)
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
49% identity, 99% coverage: 5:374/374 of query aligns to 5:378/380 of 2pg0A
- active site: M124 (= M124), T125 (≠ S125), E243 (= E239), A364 (≠ G360), R376 (= R372)
- binding flavin-adenine dinucleotide: I122 (= I122), M124 (= M124), T125 (≠ S125), G130 (= G130), S131 (= S131), F155 (= F155), I156 (= I156), T157 (= T157), R269 (= R265), F272 (= F268), F279 (= F275), Q337 (= Q333), L338 (= L334), G340 (= G336), G341 (= G337), V359 (= V355), I362 (= I358), Y363 (= Y359), T366 (= T362), E368 (= E364), M369 (≠ I365)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
49% identity, 100% coverage: 1:374/374 of query aligns to 49:426/430 of P51174
- K318 (= K266) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (= K270) modified: N6-acetyllysine; alternate; mutation to R: Reduces activity by 23%; reduces activity by 80% when associated with R-318.
Sites not aligning to the query:
- 42 modified: N6-acetyllysine; K→R: Reduces activity by 90% when associated with R-318 and R-322.
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
46% identity, 100% coverage: 1:374/374 of query aligns to 49:426/430 of P28330
- E291 (= E239) active site, Proton acceptor; mutation to Q: Loss of long-chain-acyl-CoA dehydrogenase activity. No effect on protein abundance. No effect on solubility. No effect on substrate binding.
- S303 (≠ I251) to T: in dbSNP:rs1801204
- K333 (= K281) to Q: in dbSNP:rs2286963
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
37% identity, 98% coverage: 8:374/374 of query aligns to 8:377/378 of 3r7kA
- active site: V126 (≠ M124), T127 (≠ S125), E242 (= E239), G363 (= G360), K375 (≠ R372)
- binding dihydroflavine-adenine dinucleotide: V126 (≠ M124), T127 (≠ S125), G132 (= G130), S133 (= S131), F157 (= F155), I158 (= I156), T159 (= T157), R268 (= R265), T270 (≠ V267), F271 (= F268), L275 (≠ V272), R278 (≠ F275), I281 (≠ T278), Q336 (= Q333), I337 (≠ L334), G340 (= G337), I358 (≠ V355), T365 (= T362), E367 (= E364)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
37% identity, 97% coverage: 11:374/374 of query aligns to 8:372/374 of 5lnxD
- active site: L122 (≠ M124), T123 (≠ S125), G239 (≠ E239), E358 (≠ G360), K370 (≠ R372)
- binding flavin-adenine dinucleotide: L122 (≠ M124), T123 (≠ S125), G128 (= G130), S129 (= S131), F153 (= F155), T155 (= T157), R265 (= R265), Q267 (≠ V267), F268 (= F268), I272 (≠ V272), N275 (≠ F275), I278 (≠ T278), Q331 (= Q333), I332 (≠ L334), G335 (= G337), Y357 (= Y359), T360 (= T362), E362 (= E364)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
33% identity, 98% coverage: 5:372/374 of query aligns to 12:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S125), G140 (= G130), S141 (= S131), W165 (≠ F155), T167 (= T157), R279 (= R265), F282 (= F268), I286 (≠ V272), F289 (= F275), Q347 (= Q333), C348 (≠ L334), G351 (= G337), L369 (≠ V355), G375 (= G361), T376 (= T362), L382 (≠ E368)
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)
33% identity, 98% coverage: 5:372/374 of query aligns to 45:419/426 of P26440
- 165:174 (vs. 122:131, 70% identical) binding
- S174 (= S131) binding
- WIT 198:200 (≠ FIT 155:157) binding
- SR 222:223 (≠ SK 175:176) binding
- G250 (= G203) to A: in IVA; uncertain significance
- Y277 (≠ G230) binding
- DLER 284:287 (≠ AWER 237:240) binding
- E286 (= E239) 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 (= A244) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R265) binding
- Q323 (= Q276) binding
- I379 (≠ L332) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QLHGG 333:337) binding
- R398 (≠ I351) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ A356) to N: in IVA; uncertain significance
- A407 (≠ G360) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ GG 360:361) binding
- TSE 409:411 (= TSE 362:364) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
33% identity, 98% coverage: 5:372/374 of query aligns to 8:382/387 of 1ivhA
- active site: M130 (= M124), S131 (= S125), E249 (= E239), A370 (≠ G360), R382 (= R372)
- binding coenzyme a persulfide: S137 (= S131), S185 (= S175), R186 (≠ K176), V239 (≠ F229), Y240 (≠ G230), M243 (≠ T233), E249 (= E239), R250 (= R240), G369 (≠ Y359), A370 (≠ G360), G371 (= G361), V375 (≠ I365)
- binding flavin-adenine dinucleotide: L128 (≠ I122), M130 (= M124), S131 (= S125), G136 (= G130), S137 (= S131), W161 (≠ F155), T163 (= T157), R275 (= R265), F278 (= F268), F285 (= F275), M288 (≠ T278), Q343 (= Q333), C344 (≠ L334), G347 (= G337), T372 (= T362), E374 (= E364)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
37% identity, 98% coverage: 9:374/374 of query aligns to 8:376/378 of 5ol2F
- active site: L124 (≠ M124), T125 (≠ S125), G241 (≠ E239), G374 (≠ R372)
- binding calcium ion: E29 (= E30), E33 (≠ S34), R35 (≠ I36)
- binding coenzyme a persulfide: L238 (= L236), R242 (= R240), E362 (≠ G360), G363 (= G361)
- binding flavin-adenine dinucleotide: F122 (≠ I122), L124 (≠ M124), T125 (≠ S125), P127 (= P127), T131 (≠ S131), F155 (= F155), I156 (= I156), T157 (= T157), E198 (≠ L196), R267 (= R265), F270 (= F268), L274 (≠ V272), F277 (= F275), Q335 (= Q333), L336 (= L334), G338 (= G336), G339 (= G337), Y361 (= Y359), T364 (= T362), E366 (= E364)
3p4tA Crystal structure of a putative acyl-coa dehydrogenase from mycobacterium smegmatis (see paper)
35% identity, 98% coverage: 8:374/374 of query aligns to 7:377/381 of 3p4tA
- active site: I125 (≠ M124), T126 (≠ S125), E241 (= E239), G363 (= G360), K375 (≠ R372)
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-[(4aS,10aR)-7,8-dimethyl-2,4-dioxo-1,3,4,4a,5,10a-hexahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate: L123 (≠ I122), I125 (≠ M124), T126 (≠ S125), G130 (≠ I129), G131 (= G130), S132 (= S131), Y156 (≠ F155), I157 (= I156), T158 (= T157), K200 (= K198), R267 (= R265), T269 (≠ V267), L274 (≠ V272), R277 (≠ F275), Q336 (= Q333), L337 (= L334), G340 (= G337), I358 (≠ V355), T365 (= T362)
3oibA Crystal structure of a putative acyl-coa dehydrogenase from mycobacterium smegmatis, iodide soak (see paper)
35% identity, 98% coverage: 8:374/374 of query aligns to 7:377/381 of 3oibA
- active site: I125 (≠ M124), T126 (≠ S125), E241 (= E239), G363 (= G360), K375 (≠ R372)
- binding dihydroflavine-adenine dinucleotide: L123 (≠ I122), I125 (≠ M124), T126 (≠ S125), G131 (= G130), S132 (= S131), Y156 (≠ F155), I157 (= I156), T158 (= T157), K200 (= K198), R267 (= R265), T269 (≠ V267), L274 (≠ V272), R277 (≠ F275), Q336 (= Q333), L337 (= L334), G340 (= G337), I358 (≠ V355), T365 (= T362), E367 (= E364)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
34% identity, 99% coverage: 5:374/374 of query aligns to 3:376/379 of 6fahD
- active site: L124 (≠ M124), T125 (≠ S125), G241 (≠ E239), G374 (≠ R372)
- binding flavin-adenine dinucleotide: F122 (≠ I122), L124 (≠ M124), T125 (≠ S125), R152 (≠ Q152), F155 (= F155), T157 (= T157), E198 (≠ L196), R267 (= R265), Q269 (≠ V267), F270 (= F268), I274 (≠ V272), F277 (= F275), Q335 (= Q333), I336 (≠ L334), G339 (= G337), Y361 (= Y359), T364 (= T362), Q366 (≠ E364)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
32% identity, 100% coverage: 1:374/374 of query aligns to 2:378/378 of 4n5fA
- active site: L126 (≠ M124), T127 (≠ S125), G243 (≠ E239), E364 (≠ G360), R376 (= R372)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M124), T127 (≠ S125), G132 (= G130), S133 (= S131), F157 (= F155), T159 (= T157), T210 (= T206), Y363 (= Y359), T366 (= T362), E368 (= E364), M372 (≠ E368)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
35% identity, 95% coverage: 19:374/374 of query aligns to 16:375/383 of 4iv6B
- active site: L121 (≠ M124), T122 (≠ S125), G240 (≠ E239), E361 (≠ G360), K373 (≠ R372)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ M124), T122 (≠ S125), G126 (≠ I129), G127 (= G130), S128 (= S131), W152 (≠ F155), I153 (= I156), S154 (≠ T157), R266 (= R265), S268 (≠ V267), F269 (= F268), I273 (≠ V272), H276 (≠ F275), V279 (≠ T278), R334 (≠ Q333), V335 (≠ L334), G338 (= G337), L356 (≠ V355), G360 (≠ Y359), T363 (= T362), E365 (= E364), I366 (= I365)
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
34% identity, 98% coverage: 7:374/374 of query aligns to 12:374/377 of 4ktoA
- active site: M130 (= M124), S131 (= S125), E239 (= E239), A360 (≠ G360), R372 (= R372)
- binding flavin-adenine dinucleotide: L128 (≠ I122), M130 (= M124), S131 (= S125), M155 (≠ T154), W156 (≠ F155), T158 (= T157), R265 (= R265), F268 (= F268), I272 (≠ V272), F275 (= F275), M278 (≠ T278), Q333 (= Q333), A334 (≠ L334), G337 (= G337), L355 (≠ V355), G359 (≠ Y359), T362 (= T362), E364 (= E364)
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)
34% identity, 98% coverage: 9:374/374 of query aligns to 1:367/369 of 3pfdC
- active site: L116 (≠ M124), S117 (= S125), T233 (≠ E239), E353 (≠ G360), R365 (= R372)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ I122), L116 (≠ M124), S117 (= S125), G122 (= G130), S123 (= S131), W147 (≠ F155), I148 (= I156), T149 (= T157), R259 (= R265), F262 (= F268), V266 (= V272), N269 (≠ F275), Q326 (= Q333), L327 (= L334), G330 (= G337), I348 (≠ V355), Y352 (= Y359), T355 (= T362), Q357 (≠ E364)
7w0jE Acyl-coa dehydrogenase, tfu_1647
34% identity, 98% coverage: 7:374/374 of query aligns to 9:380/382 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 (= S125), W157 (≠ F155), R270 (= R265), Q272 (≠ V267), F273 (= F268), I277 (≠ V272), F280 (= F275), I283 (≠ T278), Q339 (= Q333), L340 (= L334), G343 (= G337), Y365 (= Y359), E366 (≠ G360), T368 (= T362), Q370 (≠ E364), I371 (= I365)
7szvA Crystal structure of acyl-coa dehydrogenase from mycobacterium marinum in complex with fda
34% identity, 98% coverage: 7:374/374 of query aligns to 4:370/372 of 7szvA
- binding dihydroflavine-adenine dinucleotide: L122 (≠ M124), T123 (≠ S125), F153 (= F155), I154 (= I156), T155 (= T157), K194 (= K198), R261 (= R265), S263 (≠ V267), Y271 (≠ F275), I274 (≠ T278), Q329 (= Q333), V330 (≠ L334), G332 (= G336), G333 (= G337), T358 (= T362), E360 (= E364)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
34% identity, 98% coverage: 7:374/374 of query aligns to 7:376/379 of 1ukwB
- active site: L124 (≠ M124), S125 (= S125), T241 (≠ E239), E362 (≠ G360), R374 (= R372)
- binding cobalt (ii) ion: D145 (= D145), H146 (≠ Q146)
- binding flavin-adenine dinucleotide: F122 (≠ I122), L124 (≠ M124), S125 (= S125), G130 (= G130), S131 (= S131), W155 (≠ F155), S157 (≠ T157), K200 (= K198), L357 (≠ V355), Y361 (= Y359), E362 (≠ G360), T364 (= T362), E366 (= E364), L370 (≠ E368)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
34% identity, 98% coverage: 7:374/374 of query aligns to 7:376/379 of 1ukwA
- active site: L124 (≠ M124), S125 (= S125), T241 (≠ E239), E362 (≠ G360), R374 (= R372)
- binding flavin-adenine dinucleotide: F122 (≠ I122), L124 (≠ M124), S125 (= S125), G130 (= G130), S131 (= S131), W155 (≠ F155), S157 (≠ T157), L357 (≠ V355), Y361 (= Y359), E362 (≠ G360), T364 (= T362), E366 (= E364), L370 (≠ E368)
Query Sequence
>GFF56 FitnessBrowser__Marino:GFF56
MRTVFREDHNMFREQARRFIEREICPHLEEWEKSGIVPKEIWRKAGEMGLLCSTVPEEYG
GAGGDFGHSAVMIEELARVNATAIGFTTHSEIVAPYIVAYGTEEQKQKWLPRMVSGEIIG
VIAMSEPGIGSDLRSMRTQLRRDGDQYIISGQKTFITNGGNADLVVTATKVDPASKDLTL
VCVETDRDGFAKGRLLDKIGLKGQDTAELFFDDVRVPVSNRLGEENEGFGYLTHQLAWER
LIIAIRAAESIDSFLDMTIGYTKERKVFGKTVFDFQNTRFKLAEIKAQATMLRVFVDNCL
ERVMNNDLPADVAAMAKLMGSELQGKLLDEMLQLHGGYGFMSEYRIGQAWIDARVARIYG
GTSEIMKEIISRKL
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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