SitesBLAST
Comparing Ga0059261_0839 FitnessBrowser__Korea:Ga0059261_0839 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)
36% identity, 86% coverage: 54:392/393 of query aligns to 388:710/711 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.
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
32% identity, 99% coverage: 4:392/393 of query aligns to 5:378/380 of 6wy9A
- active site: Y122 (= Y133), T123 (≠ S134), E237 (= E248), T372 (≠ K386)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q131), Y122 (= Y133), T123 (≠ S134), G128 (= G139), T129 (≠ S140), F153 (≠ W164), S155 (= S166), F358 (≠ I372), V362 (≠ T376), E364 (= E378)
6wy8B Tcur3481-tcur3483 steroid acad (see paper)
32% identity, 99% coverage: 4:392/393 of query aligns to 9:382/384 of 6wy8B
- active site: Y126 (= Y133), T127 (≠ S134), E241 (= E248), T376 (≠ K386)
- binding flavin-adenine dinucleotide: I124 (≠ Q131), Y126 (= Y133), T127 (≠ S134), G132 (= G139), T133 (≠ S140), F157 (≠ W164), S159 (= S166), V359 (≠ A369), F362 (≠ I372), G363 (≠ E373), V366 (≠ T376), E368 (= E378)
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
34% identity, 87% coverage: 53:392/393 of query aligns to 44:383/386 of 4x28A
- active site: Y122 (= Y133), S123 (= S134), E240 (= E248), G365 (= G374), M377 (≠ K386)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q131), Y122 (= Y133), S123 (= S134), G128 (= G139), T129 (≠ S140), W153 (= W164), S155 (= S166), F363 (vs. gap), T367 (= T376), E369 (= E378), V370 (= V379)
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)
33% identity, 87% coverage: 51:392/393 of query aligns to 49:396/400 of I6YCA3
- IGYS 127:130 (≠ QGYS 131:134) binding
- T136 (≠ S140) binding
- S162 (= S166) binding
- E247 (= E248) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ TSE 376:378) 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)
39% identity, 54% coverage: 43:256/393 of query aligns to 24:249/387 of P71858
- E241 (= E248) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
8hk0B Crystal structure of fic32-33 complex from streptomyces ficellus nrrl 8067 (see paper)
30% identity, 94% coverage: 16:385/393 of query aligns to 9:370/379 of 8hk0B
- binding flavin-adenine dinucleotide: V126 (≠ Q131), Y128 (= Y133), T129 (≠ S134), G134 (= G139), S135 (= S140), F159 (≠ W164), S160 (≠ T165), L161 (≠ S166), G354 (≠ A369), S358 (≠ E373), T361 (= T376), E363 (= E378)
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
28% identity, 94% coverage: 21:388/393 of query aligns to 14:378/380 of 2pg0A
- active site: M124 (≠ Y133), T125 (≠ S134), E243 (= E248), A364 (≠ G374), R376 (≠ K386)
- binding flavin-adenine dinucleotide: I122 (≠ Q131), M124 (≠ Y133), T125 (≠ S134), G130 (= G139), S131 (= S140), F155 (≠ W164), I156 (≠ T165), T157 (≠ S166), R269 (≠ G263), F272 (≠ I266), F279 (≠ M273), Q337 (≠ E339), L338 (≠ M340), G340 (≠ A342), G341 (= G343), V359 (≠ A369), I362 (= I372), Y363 (≠ E373), T366 (= T376), E368 (= E378), M369 (≠ V379)
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)
29% identity, 87% coverage: 47:388/393 of query aligns to 90:428/432 of P45954
- V137 (≠ L94) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (vs. gap) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 129:140, 50% identical) binding in other chain
- S183 (= S140) binding
- WIS 207:209 (≠ WTS 164:166) binding in other chain
- S210 (≠ Y167) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ Q186) binding
- L255 (≠ S210) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ W238) binding
- NEGR 291:294 (≠ GHER 246:249) binding
- I316 (≠ A269) to V: in dbSNP:rs1131430
- R319 (= R272) binding
- Q330 (≠ L285) binding
- EWMGG 387:391 (≠ EWESA 349:353) binding
- A416 (≠ T376) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TSE 376:378) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
29% identity, 87% coverage: 47:388/393 of query aligns to 39:377/381 of 2jifA
- active site: L125 (≠ Y133), S126 (= S134), G242 (≠ E248), E363 (≠ G374), K375 (= K386)
- binding coenzyme a persulfide: S132 (= S140), S134 (≠ L142), Y178 (≠ Q186), Y232 (≠ W238), I236 (≠ K242), L239 (= L245), N240 (≠ G246), R243 (= R249), Y362 (≠ E373), E363 (≠ G374), G364 (= G375), I368 (≠ V379)
- binding flavin-adenine dinucleotide: F123 (≠ W129), L125 (≠ Y133), S126 (= S134), G131 (= G139), S132 (= S140), W156 (= W164), I157 (≠ T165), S158 (= S166), K201 (≠ L207), T209 (≠ F215), R268 (= R272), F271 (≠ L275), L275 (= L281), F278 (≠ P284), L281 (= L286), E336 (= E349), W337 (= W350), G340 (≠ A353), N367 (≠ E378), I368 (≠ V379)
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)
37% identity, 50% coverage: 65:259/393 of query aligns to 98:297/426 of P26440
- 165:174 (vs. 131:140, 70% identical) binding
- S174 (= S140) binding
- WIT 198:200 (≠ WTS 164:166) binding
- SR 222:223 (vs. gap) binding
- G250 (vs. gap) to A: in IVA; uncertain significance
- Y277 (≠ D239) binding
- DLER 284:287 (≠ GHER 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 (≠ S253) to V: in IVA; uncertain significance; dbSNP:rs886042098
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 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
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
37% identity, 50% coverage: 65:259/393 of query aligns to 61:260/387 of 1ivhA
- active site: M130 (≠ Y133), S131 (= S134), E249 (= E248)
- binding coenzyme a persulfide: S137 (= S140), S185 (vs. gap), R186 (vs. gap), V239 (≠ W238), Y240 (≠ D239), M243 (≠ K242), E249 (= E248), R250 (= R249)
- binding flavin-adenine dinucleotide: L128 (≠ Q131), M130 (≠ Y133), S131 (= S134), G136 (= G139), S137 (= S140), W161 (= W164), T163 (≠ S166)
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)
37% identity, 50% coverage: 65:259/393 of query aligns to 65:264/393 of 8sgrA
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 279, 282, 286, 289, 347, 348, 351, 369, 375, 376, 382
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
36% identity, 50% coverage: 65:260/393 of query aligns to 57:257/393 of 3mpjB
- active site: I128 (≠ Y133), T129 (≠ S134), T245 (≠ E248)
- binding flavin-adenine dinucleotide: F126 (≠ Q131), I128 (≠ Y133), T129 (≠ S134), G134 (= G139), S135 (= S140), W159 (= W164), I160 (≠ T165), S161 (= S166)
- binding : A164 (≠ D169), Q165 (≠ K170), D167 (= D172), N193 (≠ A197)
Sites not aligning to the query:
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
36% identity, 50% coverage: 65:260/393 of query aligns to 57:257/395 of 3mpiC
- active site: I128 (≠ Y133), T129 (≠ S134), T245 (≠ E248)
- binding flavin-adenine dinucleotide: I128 (≠ Y133), T129 (≠ S134), G134 (= G139), S135 (= S140), W159 (= W164), I160 (≠ T165), S161 (= S166)
- binding glutaryl-coenzyme A: R87 (≠ L94), F126 (≠ Q131), S135 (= S140), V137 (≠ L142), S181 (≠ Q186), F239 (≠ K242), R246 (= R249)
Sites not aligning to the query:
- active site: 367, 379
- binding flavin-adenine dinucleotide: 365, 366, 369, 371, 375
- binding glutaryl-coenzyme A: 315, 366, 367, 368, 376, 385, 389
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
36% identity, 50% coverage: 65:260/393 of query aligns to 57:257/389 of C3UVB0
- A80 (= A87) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ L94) binding
- V88 (≠ S95) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ G98) binding
- FGIT 126:129 (≠ QGYS 131:134) binding
- S135 (= S140) binding ; binding
- WIS 159:161 (≠ WTS 164:166) binding
- S181 (≠ Q186) binding
Sites not aligning to the query:
- 271 binding
- 281:284 binding
- 340 binding
- 344 binding
- 366 V→Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- 367:371 binding
- 385 binding
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
28% identity, 87% coverage: 51:390/393 of query aligns to 41:378/378 of 5ol2F
- active site: L124 (≠ Y133), T125 (≠ S134), G241 (≠ E248), G374 (≠ K386)
- binding coenzyme a persulfide: L238 (= L245), R242 (= R249), E362 (≠ G374), G363 (= G375)
- binding flavin-adenine dinucleotide: F122 (≠ Q131), L124 (≠ Y133), T125 (≠ S134), P127 (= P136), T131 (≠ S140), F155 (≠ W164), I156 (≠ T165), T157 (≠ S166), E198 (≠ K204), R267 (= R272), F270 (≠ L275), L274 (vs. gap), F277 (vs. gap), Q335 (≠ E339), L336 (≠ M340), G338 (≠ A342), G339 (= G343), Y361 (≠ E373), T364 (= T376), E366 (= E378)
Sites not aligning to the query:
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
29% identity, 87% coverage: 51:390/393 of query aligns to 41:378/379 of 6fahD
- active site: L124 (≠ Y133), T125 (≠ S134), G241 (≠ E248), G374 (≠ K386)
- binding flavin-adenine dinucleotide: F122 (≠ Q131), L124 (≠ Y133), T125 (≠ S134), R152 (≠ Q161), F155 (≠ W164), T157 (≠ S166), E198 (vs. gap), R267 (= R272), Q269 (≠ G274), F270 (≠ L275), I274 (≠ L281), F277 (vs. gap), Q335 (≠ M340), I336 (≠ A341), G339 (= G344), Y361 (≠ E373), T364 (= T376), Q366 (≠ E378)
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
28% identity, 97% coverage: 10:389/393 of query aligns to 6:377/381 of 8sgsA
- binding coenzyme a: S131 (= S140), A133 (≠ L142), N177 (≠ Q186), F231 (≠ W238), M235 (≠ K242), L238 (= L245), I312 (≠ P318), E362 (≠ G374), G363 (= G375)
- binding flavin-adenine dinucleotide: F122 (≠ Q131), L124 (≠ Y133), S125 (= S134), G130 (= G139), S131 (= S140), W155 (= W164), T157 (≠ S166), R267 (= R272), F270 (≠ L275), L274 (= L285), L277 (≠ G288), Q335 (≠ M340), I336 (≠ A341), G338 (= G343), G339 (= G344), I357 (≠ A369), I360 (= I372), Y361 (≠ E373), T364 (= T376), E366 (= E378)
5iduC Crystal structure of an acyl-coa dehydrogenase domain protein from burkholderia phymatum bound to fad
31% identity, 49% coverage: 68:260/393 of query aligns to 78:272/405 of 5iduC
Sites not aligning to the query:
- active site: 381, 393
- binding flavin-adenine dinucleotide: 286, 288, 296, 354, 355, 358, 376, 380, 383, 385
Query Sequence
>Ga0059261_0839 FitnessBrowser__Korea:Ga0059261_0839
MSDLDTFRAETRAWLEENCPASMREPVRSEKDTVWGGRDQSALTPDQKTWMDRMAARGWT
VPDWPKAYGGGGLSPAESKILREEMRALGCRNPLSSFGISMLGPALLKYGNEEQKLEHLP
RIARGEIRWCQGYSEPNAGSDLAALATSAEDMGDHYLVNGQKVWTSYADKADWIFCLVRT
DKSVKQAGISFLLFDMASPGVSTKPILLISGYSPFCETFFDDVKVPKANLVGELNKGWDV
AKYLLGHEREMISGMGLGLSSGGTLIGNAVARMGLGDDGRLADPLLRGQIALHEVRARAF
AAMSERFLDELKTGRAHPAQPSMMKYYGTELNKARHELEMAAGGSDSLEWESAASNNGAA
PRAWLRTKANSIEGGTSEVQLNIIAKRILELPS
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