SitesBLAST
Comparing AZOBR_RS29205 AZOBR_RS29205 acyl-CoA dehydrogenase 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)
35% identity, 86% coverage: 53:380/381 of query aligns to 388:709/711 of P96855
- E581 (= E248) 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.
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
31% identity, 95% coverage: 13:374/381 of query aligns to 7:375/386 of 4x28A
- active site: Y122 (≠ M132), S123 (= S133), E240 (= E248), G365 (= G364)
- binding dihydroflavine-adenine dinucleotide: I120 (= I130), Y122 (≠ M132), S123 (= S133), G128 (= G138), T129 (≠ S139), W153 (= W163), S155 (≠ T165), F363 (≠ L362), T367 (= T366), E369 (= E368), V370 (≠ I369)
Sites not aligning to the query:
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)
31% identity, 95% coverage: 13:374/381 of query aligns to 7:388/400 of I6YCA3
- IGYS 127:130 (≠ IGMS 130:133) binding
- T136 (≠ S139) binding
- S162 (≠ T165) binding
- E247 (= E248) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ TRE 366:368) binding
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)
36% identity, 65% coverage: 12:259/381 of query aligns to 6:255/387 of P71858
- E241 (= E248) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
30% identity, 96% coverage: 16:380/381 of query aligns to 6:377/380 of 6wy9A
- active site: Y122 (≠ M132), T123 (≠ S133), E237 (= E248), T372 (≠ R376)
- binding dihydroflavine-adenine dinucleotide: I120 (= I130), Y122 (≠ M132), T123 (≠ S133), G128 (= G138), T129 (≠ S139), F153 (≠ W163), S155 (≠ T165), F358 (≠ L362), V362 (≠ T366), E364 (= E368)
6wy8B Tcur3481-tcur3483 steroid acad (see paper)
30% identity, 96% coverage: 16:380/381 of query aligns to 10:381/384 of 6wy8B
- active site: Y126 (≠ M132), T127 (≠ S133), E241 (= E248), T376 (≠ R376)
- binding flavin-adenine dinucleotide: I124 (= I130), Y126 (≠ M132), T127 (≠ S133), G132 (= G138), T133 (≠ S139), F157 (≠ W163), S159 (≠ T165), V359 (≠ L355), F362 (≠ L362), G363 (≠ R363), V366 (≠ T366), E368 (= E368)
8hk0B Crystal structure of fic32-33 complex from streptomyces ficellus nrrl 8067 (see paper)
33% identity, 85% coverage: 51:375/381 of query aligns to 47:370/379 of 8hk0B
- binding flavin-adenine dinucleotide: V126 (≠ I130), Y128 (≠ M132), T129 (≠ S133), G134 (= G138), S135 (= S139), F159 (≠ W163), S160 (≠ T164), L161 (≠ T165), G354 (≠ A359), S358 (≠ R363), T361 (= T366), E363 (= E368)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
27% identity, 94% coverage: 17:376/381 of query aligns to 18:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S133), G140 (= G138), S141 (= S139), W165 (= W163), T167 (= T165), R279 (≠ V266), F282 (≠ L269), I286 (≠ M273), F289 (vs. gap), Q347 (= Q332), C348 (≠ L333), G351 (≠ M336), L369 (≠ A359), G375 (= G365), T376 (= T366), L382 (≠ G372)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
27% identity, 94% coverage: 17:376/381 of query aligns to 14:382/387 of 1ivhA
- active site: M130 (= M132), S131 (= S133), E249 (= E248), A370 (≠ G364), R382 (= R376)
- binding coenzyme a persulfide: S137 (= S139), S185 (≠ H186), R186 (≠ G187), V239 (≠ W238), Y240 (≠ N239), M243 (= M242), E249 (= E248), R250 (= R249), G369 (≠ R363), A370 (≠ G364), G371 (= G365), V375 (≠ I369)
- binding flavin-adenine dinucleotide: L128 (≠ I130), M130 (= M132), S131 (= S133), G136 (= G138), S137 (= S139), W161 (= W163), T163 (= T165), R275 (≠ V266), F278 (≠ L269), F285 (vs. gap), M288 (≠ A277), Q343 (= Q332), C344 (≠ L333), G347 (≠ M336), T372 (= T366), E374 (= 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)
27% identity, 95% coverage: 17:378/381 of query aligns to 51:421/426 of P26440
- 165:174 (vs. 130:139, 60% identical) binding
- S174 (= S139) binding
- WIT 198:200 (≠ WTT 163:165) binding
- SR 222:223 (≠ HG 186:187) binding
- G250 (≠ H214) to A: in IVA; uncertain significance
- Y277 (≠ N239) binding
- DLER 284:287 (≠ AYER 246:249) binding
- E286 (= E248) 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 (vs. gap) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (≠ V266) binding
- Q323 (≠ P275) binding
- I379 (≠ R331) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QLMAM 332:336) binding
- R398 (≠ L355) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ F360) to N: in IVA; uncertain significance
- A407 (≠ G364) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ GG 364:365) binding
- TSE 409:411 (≠ TRE 366:368) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
31% identity, 61% coverage: 18:251/381 of query aligns to 9:242/374 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
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
27% identity, 95% coverage: 18:380/381 of query aligns to 12:380/380 of 2pg0A
- active site: M124 (= M132), T125 (≠ S133), E243 (= E248), A364 (≠ G364), R376 (= R376)
- binding flavin-adenine dinucleotide: I122 (= I130), M124 (= M132), T125 (≠ S133), G130 (= G138), S131 (= S139), F155 (≠ W163), I156 (≠ T164), T157 (= T165), R269 (≠ V266), F272 (≠ L269), F279 (vs. gap), Q337 (≠ R341), L338 (≠ S342), G340 (≠ D344), G341 (≠ A345), V359 (≠ A359), I362 (≠ L362), Y363 (≠ R363), T366 (= T366), E368 (= E368), M369 (≠ I369)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
28% identity, 81% coverage: 13:320/381 of query aligns to 5:322/381 of 8sgsA
- binding coenzyme a: S131 (= S139), A133 (≠ L141), N177 (≠ H186), F231 (≠ W238), M235 (= M242), L238 (= L245), I312 (≠ L310)
- binding flavin-adenine dinucleotide: F122 (≠ I130), L124 (≠ M132), S125 (= S133), G130 (= G138), S131 (= S139), W155 (= W163), T157 (= T165), R267 (≠ V266), F270 (≠ L269), L274 (≠ M273), L277 (≠ D276)
Sites not aligning to the query:
2d29A Structural study on project id tt0172 from thermus thermophilus hb8
34% identity, 60% coverage: 23:251/381 of query aligns to 18:250/386 of 2d29A
Sites not aligning to the query:
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
28% identity, 81% coverage: 13:320/381 of query aligns to 8:325/385 of 7y0bA
- binding flavin-adenine dinucleotide: F125 (≠ I130), L127 (≠ M132), S128 (= S133), G133 (= G138), S134 (= S139), W158 (= W163), T160 (= T165), R270 (≠ V266), F273 (≠ L269), L280 (≠ D276), V282 (≠ A278)
Sites not aligning to the query:
- 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: 343, 347, 348
- binding flavin-adenine dinucleotide: 338, 339, 342, 360, 364, 367, 369, 370, 373
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
28% identity, 81% coverage: 13:320/381 of query aligns to 11:328/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ I130), L130 (≠ M132), S131 (= S133), G136 (= G138), S137 (= S139), W161 (= W163), T163 (= T165), T214 (vs. gap), R273 (≠ V266), F276 (≠ L269), L280 (≠ M273), L283 (≠ D276), V285 (≠ A278)
Sites not aligning to the query:
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
28% identity, 81% coverage: 13:320/381 of query aligns to 35:352/412 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 (≠ V149) 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 (= A170) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G188) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (≠ V266) binding
- Q308 (≠ A277) binding in other chain
- R325 (= R292) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 353 S → L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- 365:369 binding
- 380 R → W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- 394:396 binding in other chain
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
28% identity, 81% coverage: 13:320/381 of query aligns to 35:352/412 of P15651
- 152:161 (vs. 130:139, 50% identical) binding
- S161 (= S139) binding
- WIT 185:187 (≠ WTT 163:165) binding
- DMGR 269:272 (≠ AYER 246:249) binding
- R297 (≠ V266) binding
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 365:369 binding
- 392 active site, Proton acceptor
- 394:396 binding
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
28% identity, 81% coverage: 13:320/381 of query aligns to 8:325/384 of 1jqiA
- binding acetoacetyl-coenzyme a: L95 (≠ S101), F125 (≠ I130), S134 (= S139), F234 (≠ W238), M238 (= M242), Q239 (≠ S243), L241 (= L245), D242 (≠ A246), R245 (= R249)
- binding flavin-adenine dinucleotide: F125 (≠ I130), L127 (≠ M132), S128 (= S133), G133 (= G138), S134 (= S139), W158 (= W163), T160 (= T165), R270 (≠ V266), F273 (≠ L269), L280 (vs. gap)
Sites not aligning to the query:
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
30% identity, 52% coverage: 46:245/381 of query aligns to 38:239/380 of 4l1fA
- active site: L125 (≠ M132), T126 (≠ S133)
- binding coenzyme a persulfide: T132 (≠ S139), H179 (= H186), F232 (≠ W238), M236 (= M242), E237 (≠ S243), L239 (= L245)
- binding flavin-adenine dinucleotide: F123 (≠ I130), L125 (≠ M132), T126 (≠ S133), G131 (= G138), T132 (≠ S139), F156 (≠ W163), I157 (≠ T164), T158 (= T165)
Sites not aligning to the query:
- active site: 242, 363, 375
- binding coenzyme a persulfide: 240, 243, 362, 363, 364, 375
- binding flavin-adenine dinucleotide: 268, 270, 271, 275, 278, 281, 336, 337, 340, 358, 362, 365, 367
- binding 1,3-propandiol: 5, 10
Query Sequence
>AZOBR_RS29205 AZOBR_RS29205 acyl-CoA dehydrogenase
MQDFSFPAPPTAPDTAELRAEVRAFLAAELAGYPAAKRIRSWSGFDAEFSRKLGQRGWIG
MAWPKQYGGHERSALERYVVLEELLAAGAPVAAHWIADRQSGPLLLKVGTEEQKRSILPR
IAAGEFFFCIGMSEPDSGSDLAAVRTRAVPVEGGWRVNGTKLWTTYAHHAHAMILYCRTG
AADDRHGGTSQFLVDLTLPGITIRPIADLSGARHFNEVVFEDVLLPHSALIGQEGDGWNQ
VMSELAYERSGPERFMSTFVLFVELVRALGSQMTPDAAGALGRLGVHLVVLRRLSRSVAG
MLQDGRNPALQASVVKDLGALVEQEIPEIARQLMAMEPDLRSHDALSAVLGYSILNAPAF
SLRGGTREILRGIIARGLGLR
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