SitesBLAST
Comparing Ga0059261_2859 FitnessBrowser__Korea:Ga0059261_2859 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)
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, 98% coverage: 1:385/392 of query aligns to 1:388/400 of I6YCA3
- IGYS 127:130 (≠ QGFS 126:129) binding
- T136 (≠ S135) binding
- S162 (= S161) binding
- E247 (= E244) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ SSE 377:379) binding
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
34% identity, 98% coverage: 1:385/392 of query aligns to 1:375/386 of 4x28A
- active site: Y122 (≠ F128), S123 (= S129), E240 (= E244), G365 (= G375)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (≠ F128), S123 (= S129), G128 (= G134), T129 (≠ S135), W153 (= W159), S155 (= S161), F363 (≠ I373), T367 (≠ S377), E369 (= E379), V370 (≠ I380)
Sites not aligning to the query:
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)
37% identity, 65% coverage: 1:254/392 of query aligns to 1:248/387 of P71858
- E241 (= E244) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
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, 89% coverage: 43:392/392 of query aligns to 381:709/711 of P96855
- E581 (= E244) 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.
6wy8B Tcur3481-tcur3483 steroid acad (see paper)
32% identity, 98% coverage: 1:386/392 of query aligns to 1:375/384 of 6wy8B
- active site: Y126 (≠ F128), T127 (≠ S129), E241 (= E244)
- binding flavin-adenine dinucleotide: I124 (≠ Q126), Y126 (≠ F128), T127 (≠ S129), G132 (= G134), T133 (≠ S135), F157 (≠ W159), S159 (= S161), V359 (vs. gap), F362 (≠ I373), G363 (≠ Y374), V366 (≠ S377), E368 (= E379)
Sites not aligning to the query:
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
32% identity, 97% coverage: 6:386/392 of query aligns to 2:371/380 of 6wy9A
- active site: Y122 (≠ F128), T123 (≠ S129), E237 (= E244)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (≠ F128), T123 (≠ S129), G128 (= G134), T129 (≠ S135), F153 (≠ W159), S155 (= S161), F358 (≠ I373), V362 (≠ S377), E364 (= E379)
Sites not aligning to the query:
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
30% identity, 97% coverage: 8:389/392 of query aligns to 8:378/380 of 2pg0A
- active site: M124 (≠ F128), T125 (≠ S129), E243 (= E244), A364 (≠ G375), R376 (= R387)
- binding flavin-adenine dinucleotide: I122 (≠ Q126), M124 (≠ F128), T125 (≠ S129), G130 (= G134), S131 (= S135), F155 (≠ W159), I156 (≠ T160), T157 (≠ S161), R269 (= R262), F272 (≠ L265), F279 (≠ D278), Q337 (≠ T348), L338 (≠ V349), G340 (≠ E351), G341 (= G352), V359 (≠ K370), I362 (= I373), Y363 (= Y374), T366 (≠ S377), E368 (= E379), M369 (≠ I380)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
28% identity, 100% coverage: 1:391/392 of query aligns to 1:381/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S135), T134 (≠ L137), R180 (≠ A183), R234 (≠ T235), L237 (≠ K238), R238 (≠ F239), L240 (= L241), D241 (≠ G242), R244 (= R245), E365 (≠ G375), G366 (= G376), R377 (= R387)
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), L125 (≠ F128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), T158 (≠ S161), I360 (≠ K370), T367 (≠ S377), Q369 (≠ E379)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
28% identity, 100% coverage: 1:391/392 of query aligns to 1:381/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), L125 (≠ F128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), T158 (≠ S161), I360 (≠ K370), Y364 (= Y374), T367 (≠ S377), Q369 (≠ E379)
7w0jE Acyl-coa dehydrogenase, tfu_1647
28% identity, 100% coverage: 1:391/392 of query aligns to 2:382/382 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 (= S129), W157 (= W159), R270 (≠ I268), Q272 (≠ P270), F273 (≠ G271), I277 (≠ L275), F280 (≠ D278), I283 (≠ L281), Q339 (≠ T348), L340 (≠ V349), G343 (= G352), Y365 (= Y374), E366 (≠ G375), T368 (≠ S377), Q370 (≠ E379), I371 (= I380)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
30% identity, 76% coverage: 5:302/392 of query aligns to 12:313/393 of 8sgrA
Sites not aligning to the query:
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
30% identity, 76% coverage: 5:302/392 of query aligns to 8:309/387 of 1ivhA
- active site: M130 (≠ F128), S131 (= S129), E249 (= E244)
- binding coenzyme a persulfide: S137 (= S135), S185 (≠ Q182), R186 (≠ A183), V239 (≠ W234), Y240 (≠ T235), M243 (≠ K238), E249 (= E244), R250 (= R245)
- binding flavin-adenine dinucleotide: L128 (≠ Q126), M130 (≠ F128), S131 (= S129), G136 (= G134), S137 (= S135), W161 (= W159), T163 (≠ S161), R275 (≠ I268), F278 (≠ G271), F285 (≠ D278), M288 (≠ L281)
Sites not aligning to the query:
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, 76% coverage: 5:302/392 of query aligns to 45:346/426 of P26440
- 165:174 (vs. 126:135, 60% identical) binding
- S174 (= S135) binding
- WIT 198:200 (≠ WTS 159:161) binding
- SR 222:223 (≠ QA 182:183) binding
- G250 (≠ A210) to A: in IVA; uncertain significance
- Y277 (≠ T235) binding
- DLER 284:287 (≠ GHER 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 (= A249) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (≠ I268) binding
- Q323 (≠ P279) binding
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 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
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
29% identity, 98% coverage: 7:389/392 of query aligns to 7:377/378 of 3r7kA
- active site: V126 (≠ F128), T127 (≠ S129), E242 (= E244), G363 (= G375), K375 (≠ R387)
- binding dihydroflavine-adenine dinucleotide: V126 (≠ F128), T127 (≠ S129), G132 (= G134), S133 (= S135), F157 (≠ W159), I158 (≠ T160), T159 (≠ S161), R268 (= R262), T270 (≠ A264), F271 (≠ L265), L275 (= L275), R278 (≠ D278), I281 (≠ L281), Q336 (≠ S342), I337 (≠ L343), G340 (= G352), I358 (≠ K370), T365 (≠ S377), E367 (= E379)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
27% identity, 98% coverage: 5:390/392 of query aligns to 2:376/383 of 4iv6B
- active site: L121 (≠ F128), T122 (≠ S129), G240 (= G242), E361 (vs. gap), K373 (≠ R387)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ F128), T122 (≠ S129), G126 (≠ A133), G127 (= G134), S128 (= S135), W152 (= W159), I153 (≠ T160), S154 (= S161), R266 (= R267), S268 (≠ P270), F269 (≠ G271), I273 (≠ L275), H276 (≠ D278), V279 (≠ L281), R334 (≠ L343), V335 (≠ T344), G338 (≠ V353), L356 (= L371), G360 (= G375), T363 (≠ S377), E365 (= E379), I366 (= I380)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
27% identity, 87% coverage: 50:391/392 of query aligns to 44:378/378 of 5ol2F
- active site: L124 (≠ F128), T125 (≠ S129), G241 (≠ E244), G374 (≠ R387)
- binding coenzyme a persulfide: L238 (= L241), R242 (= R245), E362 (≠ G375), G363 (= G376)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ F128), T125 (≠ S129), P127 (= P131), T131 (≠ S135), F155 (≠ W159), I156 (≠ T160), T157 (≠ S161), E198 (≠ L203), R267 (= R267), F270 (≠ G271), L274 (= L275), F277 (≠ D278), Q335 (≠ E336), L336 (≠ V337), G338 (≠ E339), G339 (≠ I340), Y361 (= Y374), T364 (≠ S377), E366 (= E379)
Sites not aligning to the query:
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, 98% coverage: 4:389/392 of query aligns to 56:428/432 of P45954
- V137 (≠ N90) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ I91) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 126:135, 50% identical) binding in other chain
- S183 (= S135) binding
- WIS 207:209 (≠ WTS 159:161) binding in other chain
- S210 (≠ W162) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ Q182) binding
- L255 (≠ M208) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ W234) binding
- NEGR 291:294 (≠ VGAG 247:250) binding
- I316 (vs. gap) to V: in dbSNP:rs1131430
- R319 (vs. gap) binding
- Q330 (≠ P279) binding
- EW-------------MGG 387:391 (≠ EVGEIVSLTHPLTVSEGV 336:353) binding
- A416 (≠ S377) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ SSE 377:379) 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, 98% coverage: 4:389/392 of query aligns to 5:377/381 of 2jifA
- active site: L125 (≠ F128), S126 (= S129), G242 (≠ A249), E363 (≠ G375), K375 (≠ R387)
- binding coenzyme a persulfide: S132 (= S135), S134 (≠ L137), Y178 (≠ Q182), Y232 (≠ W234), I236 (≠ L241), L239 (= L246), N240 (≠ V247), R243 (≠ G250), Y362 (= Y374), E363 (≠ G375), G364 (= G376), I368 (= I380)
- binding flavin-adenine dinucleotide: F123 (≠ Q126), L125 (≠ F128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), S158 (= S161), K201 (≠ L205), T209 (≠ E213), R268 (vs. gap), F271 (vs. gap), L275 (= L275), F278 (≠ D278), L281 (= L281), E336 (= E336), W337 (≠ V337), G340 (≠ V353), N367 (≠ E379), I368 (= I380)
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
24% identity, 98% coverage: 5:390/392 of query aligns to 53:427/430 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 (= S254) to T: in dbSNP:rs1801204
- K333 (≠ R284) to Q: in dbSNP:rs2286963
2z1qB Crystal structure of acyl coa dehydrogenase
31% identity, 86% coverage: 54:390/392 of query aligns to 69:409/549 of 2z1qB
- active site: L144 (≠ F128), T145 (≠ S129), G259 (≠ E244), E394 (≠ G375), G406 (≠ R387)
- binding flavin-adenine dinucleotide: Y142 (≠ Q126), L144 (≠ F128), T145 (≠ S129), G150 (= G134), S151 (= S135), W177 (= W159), S179 (= S161), R285 (= R267), F288 (≠ G271), I292 (≠ L275), F295 (≠ D278), I298 (≠ L281), H369 (vs. gap), G370 (vs. gap), F393 (≠ Y374), I399 (= I380)
Sites not aligning to the query:
Query Sequence
>Ga0059261_2859 FitnessBrowser__Korea:Ga0059261_2859
MDLTIPPEAEALRQAMRGFLRDQLPPELAEATLYGRKLSKGDHQRWQRILERQGWLAPSW
PTQWGGTGWGPLERFIWDEESALAGAPRANIPSLDLLGPVIVEFGTEAQKRELLPRILSG
EDWWCQGFSEPQAGSDLAALQMRAVRDGDDYIVNGTKLWTSWAHMANKIFCLVRTSADGP
KQAGISFLLIDMEQPGVTISPILTLGGMHAVNEVQITDVRVPVANLLGQEGDAWTITKFL
LGHERLVGAGIGPSMALSRQLRGALGRIGPGGAPLGDDPVLAQRVAEVETDLLALRYTAY
RVLADELSGKAPGPEVSVLKIRGGEVQQALTELLMEVGEIVSLTHPLTVSEGVVPIESAY
MAQQHFDRRKLTIYGGSSEIQRNIIARRLLNV
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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