SitesBLAST
Comparing GFF53 FitnessBrowser__Marino:GFF53 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)
P96855 Acyl-CoA dehydrogenase FadE34; ACAD; 3-oxochol-4-en-24-oyl-CoA dehydrogenase; EC 1.3.99.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
33% identity, 86% coverage: 53:382/383 of query aligns to 388:709/711 of P96855
- E581 (= E250) mutation to Q: Displays less than 1% activity with cholyl-CoA as substrate. Still binds FAD.
Sites not aligning to the query:
- 236 R→A: Displays less than 2% activity with cholyl-CoA as substrate. Cannot bind FAD.
P71858 Acyl-CoA dehydrogenase FadE29; ACAD; 3-oxo-23,24-bisnorchol-4-en-22-oyl-CoA dehydrogenase beta subunit; 3-oxo-4-pregnene-20-carboxyl-CoA dehydrogenase beta subunit; EC 1.3.99.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
32% identity, 85% coverage: 51:377/383 of query aligns to 46:376/387 of P71858
- E241 (= E250) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
8hk0B Crystal structure of fic32-33 complex from streptomyces ficellus nrrl 8067 (see paper)
29% identity, 95% coverage: 13:377/383 of query aligns to 7:370/379 of 8hk0B
- binding flavin-adenine dinucleotide: V126 (≠ I130), Y128 (≠ M132), T129 (≠ S133), G134 (= G138), S135 (= S139), F159 (≠ W163), S160 (≠ T164), L161 (≠ T165), G354 (≠ S361), S358 (≠ R365), T361 (= T368), E363 (= E370)
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
29% identity, 97% coverage: 6:376/383 of query aligns to 1:375/386 of 4x28A
- active site: Y122 (≠ M132), S123 (= S133), E240 (= E250), G365 (= G366)
- binding dihydroflavine-adenine dinucleotide: I120 (= I130), Y122 (≠ M132), S123 (= S133), G128 (= G138), T129 (≠ S139), W153 (= W163), S155 (≠ T165), F363 (≠ L364), T367 (= T368), E369 (= E370), V370 (≠ I371)
Sites not aligning to the query:
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
28% identity, 87% coverage: 48:382/383 of query aligns to 40:377/380 of 6wy9A
- active site: Y122 (≠ M132), T123 (≠ S133), E237 (= E250), T372 (≠ R378)
- binding dihydroflavine-adenine dinucleotide: I120 (= I130), Y122 (≠ M132), T123 (≠ S133), G128 (= G138), T129 (≠ S139), F153 (≠ W163), S155 (≠ T165), F358 (≠ L364), V362 (≠ T368), E364 (= E370)
6wy8B Tcur3481-tcur3483 steroid acad (see paper)
28% identity, 87% coverage: 48:382/383 of query aligns to 44:381/384 of 6wy8B
- active site: Y126 (≠ M132), T127 (≠ S133), E241 (= E250), T376 (≠ R378)
- binding flavin-adenine dinucleotide: I124 (= I130), Y126 (≠ M132), T127 (≠ S133), G132 (= G138), T133 (≠ S139), F157 (≠ W163), S159 (≠ T165), V359 (≠ S361), F362 (≠ L364), G363 (≠ R365), V366 (≠ T368), E368 (= E370)
I6YCA3 Acyl-CoA dehydrogenase FadE26; ACAD; 3-oxocholest-4-en-26-oyl-CoA dehydrogenase alpha subunit; EC 1.3.99.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
28% identity, 97% coverage: 6:376/383 of query aligns to 1:388/400 of I6YCA3
- IGYS 127:130 (≠ IGMS 130:133) binding
- T136 (≠ S139) binding
- S162 (≠ T165) binding
- E247 (= E250) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ TRE 368:370) binding
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
28% identity, 95% coverage: 14:378/383 of query aligns to 56:424/430 of P51174
- K318 (≠ R281) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ R285) 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.
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
31% identity, 63% coverage: 13:253/383 of query aligns to 4:242/374 of 5lnxD
Sites not aligning to the query:
- active site: 358, 370
- binding flavin-adenine dinucleotide: 265, 267, 268, 272, 275, 278, 331, 332, 335, 357, 360, 362
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
26% identity, 97% coverage: 6:377/383 of query aligns to 2:376/385 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 (≠ L352), T347 (= T356), E348 (≠ Q357)
- binding flavin-adenine dinucleotide: F125 (≠ I130), L127 (≠ M132), S128 (= S133), G133 (= G138), S134 (= S139), W158 (= W163), T160 (= T165), R270 (≠ L278), F273 (vs. gap), L280 (≠ I286), V282 (≠ A288), Q338 (= Q341), I339 (= I342), G342 (= G345), I360 (vs. gap), Y364 (vs. gap), T367 (= T368), E369 (= E370), I370 (= I371), L373 (≠ G374)
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, 97% coverage: 6:377/383 of query aligns to 29:403/412 of P16219
- G90 (= G69) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E83) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 130:139, 50% identical) binding in other chain
- R171 (≠ K149) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WTT 163:165) binding in other chain
- A192 (≠ S170) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G190) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (≠ L278) binding
- Q308 (≠ T287) binding in other chain
- R325 (≠ E308) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (vs. gap) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIDGG 341:345) binding
- R380 (≠ F362) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TRE 368:370) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
26% identity, 97% coverage: 6:377/383 of query aligns to 5:379/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ I130), L130 (≠ M132), S131 (= S133), G136 (= G138), S137 (= S139), W161 (= W163), T163 (= T165), T214 (≠ F217), R273 (≠ L278), F276 (vs. gap), L280 (≠ I283), L283 (≠ I286), V285 (≠ A288), Q341 (= Q341), I342 (= I342), G345 (= G345), I363 (vs. gap), Y367 (vs. gap), T370 (= T368), E372 (= E370), L376 (≠ G374)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
30% identity, 68% coverage: 9:269/383 of query aligns to 6:266/387 of 1ivhA
- active site: M130 (= M132), S131 (= S133), E249 (= E250)
- binding coenzyme a persulfide: S137 (= S139), S185 (≠ H188), R186 (≠ G189), V239 (≠ W240), Y240 (≠ Q241), M243 (≠ T244), E249 (= E250), R250 (= R251)
- binding flavin-adenine dinucleotide: L128 (≠ I130), M130 (= M132), S131 (= S133), G136 (= G138), S137 (= S139), W161 (= W163), T163 (= T165)
Sites not aligning to the query:
- active site: 370, 382
- binding coenzyme a persulfide: 369, 370, 371, 375
- binding flavin-adenine dinucleotide: 275, 278, 285, 288, 343, 344, 347, 372, 374
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
30% identity, 68% coverage: 9:269/383 of query aligns to 10:270/393 of 8sgrA
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 279, 282, 286, 289, 347, 348, 351, 369, 375, 376, 382
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
26% identity, 96% coverage: 11:377/383 of query aligns to 4:373/381 of 8sgsA
- binding coenzyme a: S131 (= S139), A133 (≠ L141), N177 (≠ G186), F231 (≠ W240), M235 (≠ T244), L238 (= L247), I312 (≠ E325), E362 (vs. gap), G363 (= G367)
- binding flavin-adenine dinucleotide: F122 (≠ I130), L124 (≠ M132), S125 (= S133), G130 (= G138), S131 (= S139), W155 (= W163), T157 (= T165), R267 (≠ L278), F270 (vs. gap), L274 (≠ I283), L277 (≠ I286), Q335 (= Q341), I336 (= I342), G338 (= G344), G339 (= G345), I357 (vs. gap), I360 (vs. gap), Y361 (vs. gap), T364 (= T368), E366 (= E370)
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)
30% identity, 63% coverage: 9:251/383 of query aligns to 43:287/426 of P26440
- 165:174 (vs. 130:139, 60% identical) binding
- S174 (= S139) binding
- WIT 198:200 (≠ WTT 163:165) binding
- SR 222:223 (≠ HG 188:189) binding
- G250 (= G214) to A: in IVA; uncertain significance
- Y277 (≠ Q241) binding
- DLER 284:287 (≠ AFER 248:251) binding
- E286 (= E250) 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.
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 291 A → V: in IVA; uncertain significance; dbSNP:rs886042098
- 312 binding
- 323 binding
- 379 I → T: in IVA; uncertain significance
- 380:384 binding
- 398 R → Q: in IVA; uncertain significance; dbSNP:rs1477527791
- 403 Y → N: in IVA; uncertain significance
- 407 A→E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- 407:408 binding
- 409:411 binding
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
27% identity, 97% coverage: 13:382/383 of query aligns to 7:380/380 of 2pg0A
- active site: M124 (= M132), T125 (≠ S133), E243 (= E255), A364 (≠ G366), R376 (= R378)
- binding flavin-adenine dinucleotide: I122 (= I130), M124 (= M132), T125 (≠ S133), G130 (= G138), S131 (= S139), F155 (≠ W163), I156 (≠ T164), T157 (= T165), R269 (= R281), F272 (≠ I283), F279 (≠ L290), Q337 (= Q341), L338 (≠ I342), G340 (= G344), G341 (= G345), V359 (≠ S361), I362 (≠ L364), Y363 (≠ R365), T366 (= T368), E368 (= E370), M369 (≠ I371)
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
26% identity, 95% coverage: 14:378/383 of query aligns to 56:424/430 of P28330
- E291 (= E250) 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 (≠ A266) to T: in dbSNP:rs1801204
- K333 (vs. gap) to Q: in dbSNP:rs2286963
3nf4A Crystal structure of acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to flavin adenine dinucleotide (see paper)
34% identity, 62% coverage: 34:269/383 of query aligns to 29:257/369 of 3nf4A
Sites not aligning to the query:
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
25% identity, 97% coverage: 6:377/383 of query aligns to 2:376/384 of 1jqiA
- binding acetoacetyl-coenzyme a: L95 (vs. gap), F125 (≠ I130), S134 (= S139), F234 (≠ W240), M238 (≠ T244), Q239 (≠ A245), L241 (= L247), D242 (≠ A248), R245 (= R251), Y364 (vs. gap), E365 (vs. gap), G366 (= G367)
- binding flavin-adenine dinucleotide: F125 (≠ I130), L127 (≠ M132), S128 (= S133), G133 (= G138), S134 (= S139), W158 (= W163), T160 (= T165), R270 (≠ P275), F273 (≠ L278), L280 (≠ I286), Q338 (= Q341), I339 (= I342), G342 (= G345), I360 (vs. gap), T367 (= T368), E369 (= E370), I370 (= I371)
Sites not aligning to the query:
Query Sequence
>GFF53 FitnessBrowser__Marino:GFF53
MSISQFRQSSIPQEAELLRSEVQSFLKSELTDYPLSDRAHSWMGFDAEFSRKLGAKGWLG
MSLPIQYGGAEASPFARYVVIEELLAAGAPVSAHWIADRQSGPLIQRFGTAEQKEKFLPS
ICKGESFFCIGMSEPDSGSDLASIKTNAKRTDNGWVLNGQKVWTTNAHLSHYMIALVRTG
DREETGRHGGMSQFIIDLSLPGVTVRAIPDLTGGEHFNEVFFDNVALEKDALIGEEGAGW
QQVTAELAFERSGPERFLSSIALVYAALDVIGTNPDALQSRDIGRITARLLTLRDMSLSV
TQQLSDGENPAWAASCVKDLGNAFEQEIPEILQLLIEQQPQIDGGSEYSRVLAYLTQMAP
SFSLRGGTREILRGIIARGLGLR
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