SitesBLAST
Comparing GFF1029 FitnessBrowser__Marino:GFF1029 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
50% identity, 97% coverage: 7:379/383 of query aligns to 6:378/380 of 2pg0A
- active site: M124 (= M127), T125 (= T128), E243 (= E244), A364 (≠ G365), R376 (= R377)
- binding flavin-adenine dinucleotide: I122 (= I125), M124 (= M127), T125 (= T128), G130 (= G133), S131 (= S134), F155 (= F158), I156 (= I159), T157 (= T160), R269 (= R270), F272 (= F273), F279 (≠ L280), Q337 (= Q338), L338 (= L339), G340 (= G341), G341 (= G342), V359 (= V360), I362 (= I363), Y363 (= Y364), T366 (= T367), E368 (= E369), M369 (≠ V370)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
49% identity, 97% coverage: 9:380/383 of query aligns to 56:427/430 of P51174
- K318 (≠ E271) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ Q275) 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)
49% identity, 97% coverage: 9:380/383 of query aligns to 56:427/430 of P28330
- E291 (= E244) 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 (≠ A256) to T: in dbSNP:rs1801204
- K333 (≠ E286) to Q: in dbSNP:rs2286963
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
40% identity, 99% coverage: 3:380/383 of query aligns to 1:377/378 of 5ol2F
- active site: L124 (≠ M127), T125 (= T128), G241 (≠ E244), G374 (≠ R377)
- binding calcium ion: E29 (≠ A31), E33 (≠ S35), R35 (≠ L37)
- binding coenzyme a persulfide: L238 (= L241), R242 (= R245), E362 (≠ G365), G363 (= G366)
- binding flavin-adenine dinucleotide: F122 (≠ I125), L124 (≠ M127), T125 (= T128), P127 (= P130), T131 (≠ S134), F155 (= F158), I156 (= I159), T157 (= T160), E198 (≠ L201), R267 (= R270), F270 (= F273), L274 (= L277), F277 (≠ L280), Q335 (= Q338), L336 (= L339), G338 (= G341), G339 (= G342), Y361 (= Y364), T364 (= T367), E366 (= E369)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
38% identity, 97% coverage: 8:378/383 of query aligns to 14:387/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T128), G140 (= G133), S141 (= S134), W165 (≠ F158), T167 (= T160), R279 (= R270), F282 (= F273), I286 (≠ L277), F289 (≠ L280), Q347 (= Q338), C348 (≠ L339), G351 (= G342), L369 (≠ V360), G375 (= G366), T376 (= T367), L382 (≠ E373)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
38% identity, 97% coverage: 8:378/383 of query aligns to 10:383/387 of 1ivhA
- active site: M130 (= M127), S131 (≠ T128), E249 (= E244), A370 (≠ G365), R382 (= R377)
- binding coenzyme a persulfide: S137 (= S134), S185 (≠ A180), R186 (= R181), V239 (≠ F234), Y240 (≠ V235), M243 (= M238), E249 (= E244), R250 (= R245), G369 (≠ Y364), A370 (≠ G365), G371 (= G366), V375 (= V370)
- binding flavin-adenine dinucleotide: L128 (≠ I125), M130 (= M127), S131 (≠ T128), G136 (= G133), S137 (= S134), W161 (≠ F158), T163 (= T160), R275 (= R270), F278 (= F273), F285 (≠ L280), M288 (≠ T283), Q343 (= Q338), C344 (≠ L339), G347 (= G342), T372 (= T367), E374 (= E369)
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)
38% identity, 97% coverage: 8:378/383 of query aligns to 47:420/426 of P26440
- 165:174 (vs. 125:134, 70% identical) binding
- S174 (= S134) binding
- WIT 198:200 (≠ FIT 158:160) binding
- SR 222:223 (≠ AR 180:181) binding
- G250 (≠ S208) to A: in IVA; uncertain significance
- Y277 (≠ V235) binding
- DLER 284:287 (≠ PRER 242:245) binding
- E286 (= E244) 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 (≠ G249) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R270) binding
- Q323 (= Q281) binding
- I379 (≠ L337) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QLFGG 338:342) binding
- R398 (≠ I356) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ Q361) to N: in IVA; uncertain significance
- A407 (≠ G365) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ GG 365:366) binding
- TSE 409:411 (= TSE 367:369) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
37% identity, 97% coverage: 8:380/383 of query aligns to 7:378/380 of 4l1fA
- active site: L125 (≠ M127), T126 (= T128), G242 (≠ E244), E363 (≠ G365), R375 (= R377)
- binding coenzyme a persulfide: T132 (≠ S134), H179 (≠ R181), F232 (= F234), M236 (= M238), E237 (≠ K239), L239 (= L241), D240 (≠ P242), R243 (= R245), Y362 (= Y364), E363 (≠ G365), G364 (= G366), R375 (= R377)
- binding flavin-adenine dinucleotide: F123 (≠ I125), L125 (≠ M127), T126 (= T128), G131 (= G133), T132 (≠ S134), F156 (= F158), I157 (= I159), T158 (= T160), R268 (= R270), Q270 (≠ L272), F271 (= F273), I275 (≠ L277), F278 (≠ L280), L281 (≠ T283), Q336 (= Q338), I337 (≠ L339), G340 (= G342), I358 (≠ V360), Y362 (= Y364), T365 (= T367), Q367 (≠ E369)
- binding 1,3-propandiol: Q10 (≠ A11)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
37% identity, 98% coverage: 8:381/383 of query aligns to 4:374/374 of 5lnxD
- active site: L122 (≠ M127), T123 (= T128), G239 (≠ E244), E358 (≠ G365), K370 (≠ R377)
- binding flavin-adenine dinucleotide: L122 (≠ M127), T123 (= T128), G128 (= G133), S129 (= S134), F153 (= F158), T155 (= T160), R265 (= R270), Q267 (≠ L272), F268 (= F273), I272 (≠ L277), N275 (≠ L280), I278 (≠ T283), Q331 (= Q338), I332 (≠ L339), G335 (= G342), Y357 (= Y364), T360 (= T367), E362 (= E369)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
37% identity, 96% coverage: 16:382/383 of query aligns to 12:378/383 of 4iv6B
- active site: L121 (≠ M127), T122 (= T128), G240 (≠ E244), E361 (≠ G365), K373 (≠ R377)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ M127), T122 (= T128), G126 (≠ A132), G127 (= G133), S128 (= S134), W152 (≠ F158), I153 (= I159), S154 (≠ T160), R266 (= R270), S268 (≠ L272), F269 (= F273), I273 (≠ L277), H276 (≠ L280), V279 (≠ T283), R334 (≠ Q338), V335 (≠ L339), G338 (= G342), L356 (≠ V360), G360 (≠ Y364), T363 (= T367), E365 (= E369), I366 (≠ V370)
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
36% identity, 94% coverage: 21:379/383 of query aligns to 20:377/378 of 3r7kA
- active site: V126 (≠ M127), T127 (= T128), E242 (= E244), G363 (= G365), K375 (≠ R377)
- binding dihydroflavine-adenine dinucleotide: V126 (≠ M127), T127 (= T128), G132 (= G133), S133 (= S134), F157 (= F158), I158 (= I159), T159 (= T160), R268 (= R270), T270 (≠ L272), F271 (= F273), L275 (= L277), R278 (≠ L280), I281 (≠ T283), Q336 (= Q338), I337 (≠ L339), G340 (= G342), I358 (≠ V360), T365 (= T367), E367 (= E369)
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)
36% identity, 96% coverage: 13:380/383 of query aligns to 4:368/369 of 3pfdC
- active site: L116 (≠ M127), S117 (≠ T128), T233 (≠ E244), E353 (≠ G365), R365 (= R377)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ I125), L116 (≠ M127), S117 (≠ T128), G122 (= G133), S123 (= S134), W147 (≠ F158), I148 (= I159), T149 (= T160), R259 (= R270), F262 (= F273), V266 (≠ L277), N269 (≠ L280), Q326 (= Q338), L327 (= L339), G330 (= G342), I348 (≠ V360), Y352 (= Y364), T355 (= T367), Q357 (≠ E369)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
36% identity, 96% coverage: 12:380/383 of query aligns to 13:380/384 of 1jqiA
- active site: G377 (≠ R377)
- binding acetoacetyl-coenzyme a: L95 (≠ D94), F125 (≠ I125), S134 (= S134), F234 (= F234), M238 (= M238), Q239 (≠ K239), L241 (= L241), D242 (≠ P242), R245 (= R245), Y364 (= Y364), E365 (≠ G365), G366 (= G366)
- binding flavin-adenine dinucleotide: F125 (≠ I125), L127 (≠ M127), S128 (≠ T128), G133 (= G133), S134 (= S134), W158 (≠ F158), T160 (= T160), R270 (= R270), F273 (= F273), L280 (= L280), Q338 (= Q338), I339 (≠ L339), G342 (= G342), I360 (≠ V360), T367 (= T367), E369 (= E369), I370 (≠ V370)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
36% identity, 96% coverage: 12:380/383 of query aligns to 40:407/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
37% identity, 97% coverage: 8:380/383 of query aligns to 12:375/377 of 4ktoA
- active site: M130 (= M127), S131 (≠ T128), E239 (= E244), A360 (≠ G365), R372 (= R377)
- binding flavin-adenine dinucleotide: L128 (≠ I125), M130 (= M127), S131 (≠ T128), M155 (≠ T157), W156 (≠ F158), T158 (= T160), R265 (= R270), F268 (= F273), I272 (≠ L277), F275 (≠ L280), M278 (≠ T283), Q333 (= Q338), A334 (≠ L339), G337 (= G342), L355 (≠ V360), G359 (≠ Y364), T362 (= T367), E364 (= E369)
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
33% identity, 97% coverage: 8:379/383 of query aligns to 8:377/381 of 2jifA
- active site: L125 (≠ M127), S126 (≠ T128), G242 (≠ E244), E363 (≠ G365), K375 (≠ R377)
- binding coenzyme a persulfide: S132 (= S134), S134 (≠ L136), Y178 (≠ A180), Y232 (≠ F234), I236 (≠ M238), L239 (= L241), N240 (≠ P242), R243 (= R245), Y362 (= Y364), E363 (≠ G365), G364 (= G366), I368 (≠ V370)
- binding flavin-adenine dinucleotide: F123 (≠ I125), L125 (≠ M127), S126 (≠ T128), G131 (= G133), S132 (= S134), W156 (≠ F158), I157 (= I159), S158 (≠ T160), K201 (= K203), T209 (= T211), R268 (= R270), F271 (= F273), L275 (= L277), F278 (≠ L280), L281 (≠ T283), E336 (≠ Q338), W337 (≠ L339), G340 (= G342), N367 (≠ E369), I368 (≠ V370)
P45954 Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial; SBCAD; 2-methyl branched chain acyl-CoA dehydrogenase; 2-MEBCAD; 2-methylbutyryl-coenzyme A dehydrogenase; 2-methylbutyryl-CoA dehydrogenase; EC 1.3.8.5 from Homo sapiens (Human) (see 6 papers)
33% identity, 97% coverage: 8:379/383 of query aligns to 59:428/432 of P45954
- V137 (≠ T87) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ N88) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 125:134, 50% identical) binding in other chain
- S183 (= S134) binding
- WIS 207:209 (≠ FIT 158:160) binding in other chain
- S210 (≠ N161) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ A180) binding
- L255 (≠ Q206) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ F234) binding
- NEGR 291:294 (≠ PRER 242:245) binding
- I316 (≠ A267) to V: in dbSNP:rs1131430
- R319 (= R270) binding
- Q330 (= Q281) binding
- EWMGG 387:391 (≠ QLFGG 338:342) binding
- A416 (≠ T367) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TSE 367:369) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
35% identity, 93% coverage: 25:381/383 of query aligns to 24:378/379 of 1ukwB
- active site: L124 (≠ M127), S125 (≠ T128), T241 (≠ E244), E362 (≠ G365), R374 (= R377)
- binding cobalt (ii) ion: D145 (= D148), H146 (≠ E149)
- binding flavin-adenine dinucleotide: F122 (≠ I125), L124 (≠ M127), S125 (≠ T128), G130 (= G133), S131 (= S134), W155 (≠ F158), S157 (≠ T160), K200 (= K203), L357 (≠ V360), Y361 (= Y364), E362 (≠ G365), T364 (= T367), E366 (= E369), L370 (≠ E373)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
35% identity, 93% coverage: 25:381/383 of query aligns to 24:378/379 of 1ukwA
- active site: L124 (≠ M127), S125 (≠ T128), T241 (≠ E244), E362 (≠ G365), R374 (= R377)
- binding flavin-adenine dinucleotide: F122 (≠ I125), L124 (≠ M127), S125 (≠ T128), G130 (= G133), S131 (= S134), W155 (≠ F158), S157 (≠ T160), L357 (≠ V360), Y361 (= Y364), E362 (≠ G365), T364 (= T367), E366 (= E369), L370 (≠ E373)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
36% identity, 98% coverage: 8:382/383 of query aligns to 5:379/379 of 6fahD
- active site: L124 (≠ M127), T125 (= T128), G241 (≠ E244), G374 (≠ R377)
- binding flavin-adenine dinucleotide: F122 (≠ I125), L124 (≠ M127), T125 (= T128), R152 (≠ S155), F155 (= F158), T157 (= T160), E198 (≠ L201), R267 (= R270), Q269 (≠ L272), F270 (= F273), I274 (≠ L277), F277 (≠ L280), Q335 (= Q338), I336 (≠ L339), G339 (= G342), Y361 (= Y364), T364 (= T367), Q366 (≠ E369)
Query Sequence
>GFF1029 FitnessBrowser__Marino:GFF1029
MTVSVDKEELAMFRDSVIKVLEKEVTPHYEAWEKSGLVPRELWNTLGNAGMLCVDVPEEW
GGIGAPFQFSVVVGEELARMGFGALSTNVMVHSDIVAPYLSHMGNEEQRQQWLPKLVSGE
AVGAIAMTEPGAGSDLQAIRTSAVKDGDEYILNGSKTFITNGQHADMVIVAAKTDPKAGA
RGISLFLVDTSLPGFSKGRNLDKIGQHSGDTSELFFSDMRIPASALLGEEGQGFVYLMKE
LPRERLVIGALGVAAARGSLDLTIAYAQERELFGQKLAQLQNTRFEIARMETDYRVNKAF
VDQCIDQYDLGELDAPTASMAKYSATEMQCRVADGCLQLFGGYGYTTEYPISRAFIDARV
QRIYGGTSEVMKEIIARSVLGKA
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